Endonucleases. Medical search

Enzymes that catalyze the hydrolysis of the internal bonds and thereby the formation of polynucleotides or oligonucleotides from ribo- or deoxyribonucleotide chains. EC 3.1.-.

Enzyme systems containing a single subunit and requiring only magnesium for endonucleolytic activity. The corresponding modification methylases are separate enzymes. The systems recognize specific short DNA sequences and cleave either within, or at a short specific distance from, the recognition sequence to give specific double-stranded fragments with terminal 5'-phosphates. Enzymes from different microorganisms with the same specificity are called isoschizomers. EC 3.1.21.4.

Enzymes that are part of the restriction-modification systems. They catalyze the endonucleolytic cleavage of DNA sequences which lack the species-specific methylation pattern in the host cell's DNA. Cleavage yields random or specific double-stranded fragments with terminal 5'-phosphates. The function of restriction enzymes is to destroy any foreign DNA that invades the host cell. Most have been studied in bacterial systems, but a few have been found in eukaryotic organisms. They are also used as tools for the systematic dissection and mapping of chromosomes, in the determination of base sequences of DNAs, and have made it possible to splice and recombine genes from one organism into the genome of another. EC 3.21.1.

A group of enzymes catalyzing the endonucleolytic cleavage of DNA. They include members of EC 3.1.21.-, EC 3.1.22.-, EC 3.1.23.- (DNA RESTRICTION ENZYMES), EC 3.1.24.- (DNA RESTRICTION ENZYMES), and EC 3.1.25.-.

An enzyme which catalyzes the endonucleolytic cleavage of phosphodiester bonds at purinic or apyrimidinic sites (AP-sites) to produce 5'-Phosphooligonucleotide end products. The enzyme prefers single-stranded DNA (ssDNA) and was formerly classified as EC 3.1.4.30.

A reaction that severs one of the covalent sugar-phosphate linkages between NUCLEOTIDES that compose the sugar phosphate backbone of DNA. It is catalyzed enzymatically, chemically or by radiation. Cleavage may be exonucleolytic - removing the end nucleotide, or endonucleolytic - splitting the strand in two.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).

A DNA repair enzyme that catalyses the excision of ribose residues at apurinic and apyrimidinic DNA sites that can result from the action of DNA GLYCOSYLASES. The enzyme catalyzes a beta-elimination reaction in which the C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. This enzyme was previously listed under EC 3.1.25.2.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

Deoxyribonucleic acid that makes up the genetic material of viruses.

One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence G/AATTC at the slash. EcoRI is from E coliRY13. Several isoschizomers have been identified. EC 3.1.21.-.

One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence G/GATCC at the slash. BamHI is from Bacillus amyloliquefaciens N. Numerous isoschizomers have been identified. EC 3.1.21.-.

Enzymes which catalyze the hydrolases of ester bonds within DNA. EC 3.1.-.

Deoxyribonucleic acid that makes up the genetic material of bacteria.

Enzyme systems containing three different subunits and requiring ATP, S-adenosylmethionine, and magnesium for endonucleolytic activity to give random double-stranded fragments with terminal 5'-phosphates. They function also as DNA-dependent ATPases and modification methylases, catalyzing the reactions of EC 2.1.1.72 and EC 2.1.1.73 with similar site-specificity. The systems recognize specific short DNA sequences and cleave at sites remote from the recognition sequence. Enzymes from different microorganisms with the same specificity are called isoschizomers. EC 3.1.21.3.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

Electrophoresis in which agar or agarose gel is used as the diffusion medium.

Endonucleases that remove 5' DNA sequences from a DNA structure called a DNA flap. The DNA flap structure occurs in double-stranded DNA containing a single-stranded break where the 5' portion of the downstream strand is too long and overlaps the 3' end of the upstream strand. Flap endonucleases cleave the downstream strand of the overlap flap structure precisely after the first base-paired nucleotide, creating a ligatable nick.

Variation occurring within a species in the presence or length of DNA fragment generated by a specific endonuclease at a specific site in the genome. Such variations are generated by mutations that create or abolish recognition sites for these enzymes or change the length of the fragment.

Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.

Widely used technique which exploits the ability of complementary sequences in single-stranded DNAs or RNAs to pair with each other to form a double helix. Hybridization can take place between two complimentary DNA sequences, between a single-stranded DNA and a complementary RNA, or between two RNA sequences. The technique is used to detect and isolate specific sequences, measure homology, or define other characteristics of one or both strands. (Kendrew, Encyclopedia of Molecular Biology, 1994, p503)

One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequences C/CGG and GGC/C at the slash. HpaII is from Haemophilus parainfluenzae. Several isoschizomers have been identified. EC 3.1.21.-.

A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.

The excision of in-frame internal protein sequences (INTEINS) of a precursor protein, coupled with ligation of the flanking sequences (EXTEINS). Protein splicing is an autocatalytic reaction and results in the production of two proteins from a single primary translation product: the intein and the mature protein.

Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.

Enzymes that recognize CRUCIFORM DNA structures and introduce paired incisions that help to resolve the structure into two DNA helices.

Any of the covalently closed DNA molecules found in bacteria, many viruses, mitochondria, plastids, and plasmids. Small, polydisperse circular DNA's have also been observed in a number of eukaryotic organisms and are suggested to have homology with chromosomal DNA and the capacity to be inserted into, and excised from, chromosomal DNA. It is a fragment of DNA formed by a process of looping out and deletion, containing a constant region of the mu heavy chain and the 3'-part of the mu switch region. Circular DNA is a normal product of rearrangement among gene segments encoding the variable regions of immunoglobulin light and heavy chains, as well as the T-cell receptor. (Riger et al., Glossary of Genetics, 5th ed & Segen, Dictionary of Modern Medicine, 1992)

A free-living soil amoeba pathogenic to humans and animals. It occurs also in water and sewage. The most commonly found species in man is NAEGLERIA FOWLERI which is the pathogen for primary amebic meningoencephalitis in primates.

Viruses whose hosts are bacterial cells.

The reconstruction of a continuous two-stranded DNA molecule without mismatch from a molecule which contained damaged regions. The major repair mechanisms are excision repair, in which defective regions in one strand are excised and resynthesized using the complementary base pairing information in the intact strand; photoreactivation repair, in which the lethal and mutagenic effects of ultraviolet light are eliminated; and post-replication repair, in which the primary lesions are not repaired, but the gaps in one daughter duplex are filled in by incorporation of portions of the other (undamaged) daughter duplex. Excision repair and post-replication repair are sometimes referred to as "dark repair" because they do not require light.

Interruptions in one of the strands of the sugar-phosphate backbone of double-stranded DNA.

The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

Hydrolysate of DNA in which purine bases have been removed.

Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes.

The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.

A reaction that severs one of the sugar-phosphate linkages of the phosphodiester backbone of RNA. It is catalyzed enzymatically, chemically, or by radiation. Cleavage may be exonucleolytic, or endonucleolytic.

Sequences of DNA in the genes that are located between the EXONS. They are transcribed along with the exons but are removed from the primary gene transcript by RNA SPLICING to leave mature RNA. Some introns code for separate genes.

One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence A/AGCTT at the slash. HindIII is from Haemophilus influenzae R(d). Numerous isoschizomers have been identified. EC 3.1.21.-.

A family of enzymes that catalyze the endonucleolytic cleavage of RNA. It includes EC 3.1.26.-, EC 3.1.27.-, EC 3.1.30.-, and EC 3.1.31.-.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

The functional hereditary units of VIRUSES.

Systems consisting of two enzymes, a modification methylase and a restriction endonuclease. They are closely related in their specificity and protect the DNA of a given bacterial species. The methylase adds methyl groups to adenine or cytosine residues in the same target sequence that constitutes the restriction enzyme binding site. The methylation renders the target site resistant to restriction, thereby protecting DNA against cleavage.

Biologically active DNA which has been formed by the in vitro joining of segments of DNA from different sources. It includes the recombination joint or edge of a heteroduplex region where two recombining DNA molecules are connected.

The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.

Enzymes that catalyze the cleavage of a carbon-oxygen bond by means other than hydrolysis or oxidation. EC 4.2.

The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.

Circular duplex DNA isolated from viruses, bacteria and mitochondria in supercoiled or supertwisted form. This superhelical DNA is endowed with free energy. During transcription, the magnitude of RNA initiation is proportional to the DNA superhelicity.

Any method used for determining the location of and relative distances between genes on a chromosome.

Enzyme systems composed of two subunits and requiring ATP and magnesium for endonucleolytic activity; they do not function as ATPases. They exist as complexes with modification methylases of similar specificity listed under EC 2.1.1.72 or EC 2.1.1.73. The systems recognize specific short DNA sequences and cleave a short distance, about 24 to 27 bases, away from the recognition sequence to give specific double-stranded fragments with terminal 5'-phosphates. Enzymes from different microorganisms with the same specificity are called isoschizomers. EC 3.1.21.5.

Enzymes that catalyze the release of mononucleotides by the hydrolysis of the terminal bond of deoxyribonucleotide or ribonucleotide chains.

Protein components of the CRISPR-CAS SYSTEMS for anti-viral defense in ARCHAEA and BACTERIA. These are proteins that carry out a variety of functions during the creation and expansion of the CRISPR ARRAYS, the capture of new CRISPR SPACERS, biogenesis of SMALL INTERFERING RNA (CRISPR or crRNAs), and the targeting and silencing of invading viruses and plasmids. They include DNA HELICASES; RNA-BINDING PROTEINS; ENDONUCLEASES; and RNA and DNA POLYMERASES.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

The sum of the weight of all the atoms in a molecule.

An enzyme which catalyzes an endonucleolytic cleavage near PYRIMIDINE DIMERS to produce a 5'-phosphate product. The enzyme acts on the damaged DNA strand, from the 5' side of the damaged site.

Enzymes that are part of the restriction-modification systems. They are responsible for producing a species-characteristic methylation pattern, on either adenine or cytosine residues, in a specific short base sequence in the host cell's own DNA. This methylated sequence will occur many times in the host-cell DNA and remain intact for the lifetime of the cell. Any DNA from another species which gains entry into a living cell and lacks the characteristic methylation pattern will be recognized by the restriction endonucleases of similar specificity and destroyed by cleavage. Most have been studied in bacterial systems, but a few have been found in eukaryotic organisms.

Gel electrophoresis in which the direction of the electric field is changed periodically. This technique is similar to other electrophoretic methods normally used to separate double-stranded DNA molecules ranging in size up to tens of thousands of base-pairs. However, by alternating the electric field direction one is able to separate DNA molecules up to several million base-pairs in length.

Viruses whose host is Escherichia coli.

A family of enzymes that catalyze the exonucleolytic cleavage of DNA. It includes members of the class EC 3.1.11 that produce 5'-phosphomonoesters as cleavage products.

Production of new arrangements of DNA by various mechanisms such as assortment and segregation, CROSSING OVER; GENE CONVERSION; GENETIC TRANSFORMATION; GENETIC CONJUGATION; GENETIC TRANSDUCTION; or mixed infection of viruses.

Physiological processes and properties of microorganisms, including ARCHAEA; BACTERIA; RICKETTSIA; VIRUSES; FUNGI; and others.

A series of 7 virulent phages which infect E. coli. The T-even phages T2, T4; (BACTERIOPHAGE T4), and T6, and the phage T5 are called "autonomously virulent" because they cause cessation of all bacterial metabolism on infection. Phages T1, T3; (BACTERIOPHAGE T3), and T7; (BACTERIOPHAGE T7) are called "dependent virulent" because they depend on continued bacterial metabolism during the lytic cycle. The T-even phages contain 5-hydroxymethylcytosine in place of ordinary cytosine in their DNA.

A temperate inducible phage and type species of the genus lambda-like viruses, in the family SIPHOVIRIDAE. Its natural host is E. coli K12. Its VIRION contains linear double-stranded DNA with single-stranded 12-base 5' sticky ends. The DNA circularizes on infection.

A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.

An enzyme responsible for producing a species-characteristic methylation pattern on adenine residues in a specific short base sequence in the host cell DNA. The enzyme catalyzes the methylation of DNA adenine in the presence of S-adenosyl-L-methionine to form DNA containing 6-methylaminopurine and S-adenosyl-L-homocysteine. EC 2.1.1.72.

The internal fragments of precursor proteins (INternal proTEINS) that are autocatalytically removed by PROTEIN SPLICING. The flanking fragments (EXTEINS) are ligated forming mature proteins. The nucleic acid sequences coding for inteins are considered to be MOBILE GENETIC ELEMENTS. Inteins are composed of self-splicing domains and an endonuclease domain which plays a role in the spread of the intein's genomic sequence. Mini-inteins are composed of the self-splicing domains only.

Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

The rate dynamics in chemical or physical systems.

In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.

A cross-shaped DNA structure that can be observed under the electron microscope. It is formed by the incomplete exchange of strands between two double-stranded helices or by complementary INVERTED REPEAT SEQUENCES that refold into hairpin loops on opposite strands across from each other.

A genus of gram-positive, spherical bacteria found in soils and fresh water, and frequently on the skin of man and other animals.

The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.

An enzyme capable of hydrolyzing highly polymerized DNA by splitting phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide. This catalyzes endonucleolytic cleavage of DNA yielding 5'-phosphodi- and oligonucleotide end-products. The enzyme has a preference for double-stranded DNA.

Addition of methyl groups. In histo-chemistry methylation is used to esterify carboxyl groups and remove sulfate groups by treating tissue sections with hot methanol in the presence of hydrochloric acid. (From Stedman, 25th ed)

Virulent bacteriophage and type species of the genus T4-like phages, in the family MYOVIRIDAE. It infects E. coli and is the best known of the T-even phages. Its virion contains linear double-stranded DNA, terminally redundant and circularly permuted.

Enzymes that catalyze the endonucleolytic cleavage of single-stranded regions of DNA or RNA molecules while leaving the double-stranded regions intact. They are particularly useful in the laboratory for producing "blunt-ended" DNA molecules from DNA with single-stranded ends and for sensitive GENETIC TECHNIQUES such as NUCLEASE PROTECTION ASSAYS that involve the detection of single-stranded DNA and RNA.

A pyrimidine base that is a fundamental unit of nucleic acids.

Structures within the nucleus of bacterial cells consisting of or containing DNA, which carry genetic information essential to the cell.

A group of deoxyribonucleotides (up to 12) in which the phosphate residues of each deoxyribonucleotide act as bridges in forming diester linkages between the deoxyribose moieties.

Ribonucleic acid in archaea having regulatory and catalytic roles as well as involvement in protein synthesis.

Proteins obtained from ESCHERICHIA COLI.

DNA sequences encoding RIBOSOMAL RNA and the segments of DNA separating the individual ribosomal RNA genes, referred to as RIBOSOMAL SPACER DNA.

The functional hereditary units of BACTERIA.

The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

Defective viruses which can multiply only by association with a helper virus which complements the defective gene. Satellite viruses may be associated with certain plant viruses, animal viruses, or bacteriophages. They differ from satellite RNA; (RNA, SATELLITE) in that satellite viruses encode their own coat protein.

Injuries to DNA that introduce deviations from its normal, intact structure and which may, if left unrepaired, result in a MUTATION or a block of DNA REPLICATION. These deviations may be caused by physical or chemical agents and occur by natural or unnatural, introduced circumstances. They include the introduction of illegitimate bases during replication or by deamination or other modification of bases; the loss of a base from the DNA backbone leaving an abasic site; single-strand breaks; double strand breaks; and intrastrand (PYRIMIDINE DIMERS) or interstrand crosslinking. Damage can often be repaired (DNA REPAIR). If the damage is extensive, it can induce APOPTOSIS.

Polymers made up of a few (2-20) nucleotides. In molecular genetics, they refer to a short sequence synthesized to match a region where a mutation is known to occur, and then used as a probe (OLIGONUCLEOTIDE PROBES). (Dorland, 28th ed)

A genus of PASTEURELLACEAE that consists of several species occurring in animals and humans. Its organisms are described as gram-negative, facultatively anaerobic, coccobacillus or rod-shaped, and nonmotile.

The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.

A method (first developed by E.M. Southern) for detection of DNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.

Discrete segments of DNA which can excise and reintegrate to another site in the genome. Most are inactive, i.e., have not been found to exist outside the integrated state. DNA transposable elements include bacterial IS (insertion sequence) elements, Tn elements, the maize controlling elements Ac and Ds, Drosophila P, gypsy, and pogo elements, the human Tigger elements and the Tc and mariner elements which are found throughout the animal kingdom.

A technique for identifying individuals of a species that is based on the uniqueness of their DNA sequence. Uniqueness is determined by identifying which combination of allelic variations occur in the individual at a statistically relevant number of different loci. In forensic studies, RESTRICTION FRAGMENT LENGTH POLYMORPHISM of multiple, highly polymorphic VNTR LOCI or MICROSATELLITE REPEAT loci are analyzed. The number of loci used for the profile depends on the ALLELE FREQUENCY in the population.

The most abundant form of RNA. Together with proteins, it forms the ribosomes, playing a structural role and also a role in ribosomal binding of mRNA and tRNAs. Individual chains are conventionally designated by their sedimentation coefficients. In eukaryotes, four large chains exist, synthesized in the nucleolus and constituting about 50% of the ribosome. (Dorland, 28th ed)

Adaptive antiviral defense mechanisms, in archaea and bacteria, based on DNA repeat arrays called CLUSTERED REGULARLY INTERSPACED SHORT PALINDROMIC REPEATS (CRISPR elements) that function in conjunction with CRISPR-ASSOCIATED PROTEINS (Cas proteins). Several types have been distinguished, including Type I, Type II, and Type III, based on signature motifs of CRISPR-ASSOCIATED PROTEINS.

The relationships of groups of organisms as reflected by their genetic makeup.

5-Bromo-2,4(1H,3H)-pyrimidinedione. Brominated derivative of uracil that acts as an antimetabolite, substituting for thymine in DNA. It is used mainly as an experimental mutagen, but its deoxyriboside (BROMODEOXYURIDINE) is used to treat neoplasms.

Disruption of the secondary structure of nucleic acids by heat, extreme pH or chemical treatment. Double strand DNA is "melted" by dissociation of the non-covalent hydrogen bonds and hydrophobic interactions. Denatured DNA appears to be a single-stranded flexible structure. The effects of denaturation on RNA are similar though less pronounced and largely reversible.

The relative amounts of the PURINES and PYRIMIDINES in a nucleic acid.

Proteins found in any species of bacterium.

The heritable modification of the properties of a competent bacterium by naked DNA from another source. The uptake of naked DNA is a naturally occuring phenomenon in some bacteria. It is often used as a GENE TRANSFER TECHNIQUE.

Catalyze the joining of preformed ribonucleotides or deoxyribonucleotides in phosphodiester linkage during genetic processes. EC 6.5.1.

Directed modification of the gene complement of a living organism by such techniques as altering the DNA, substituting genetic material by means of a virus, transplanting whole nuclei, transplanting cell hybrids, etc.

Vertical transmission of hereditary characters by DNA from cytoplasmic organelles such as MITOCHONDRIA; CHLOROPLASTS; and PLASTIDS, or from PLASMIDS or viral episomal DNA.

Small kinetoplastid mitochondrial RNA that plays a major role in RNA EDITING. These molecules form perfect hybrids with edited mRNA sequences and possess nucleotide sequences at their 5'-ends that are complementary to the sequences of the mRNA's immediately downstream of the pre-edited regions.

A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic.

Double-stranded nucleic acid molecules (DNA-DNA or DNA-RNA) which contain regions of nucleotide mismatches (non-complementary). In vivo, these heteroduplexes can result from mutation or genetic recombination; in vitro, they are formed by nucleic acid hybridization. Electron microscopic analysis of the resulting heteroduplexes facilitates the mapping of regions of base sequence homology of nucleic acids.

A class of enzymes involved in the hydrolysis of the N-glycosidic bond of nitrogen-linked sugars.

A single chain of deoxyribonucleotides that occurs in some bacteria and viruses. It usually exists as a covalently closed circle.

A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.

Positively charged atoms, radicals or groups of atoms with a valence of plus 2, which travel to the cathode or negative pole during electrolysis.

A genus of strictly anaerobic ultrathermophilic archaea, in the family THERMOCOCCACEAE, occurring in heated seawaters. They exhibit heterotrophic growth at an optimum temperature of 100 degrees C.

A species of strictly anaerobic, hyperthermophilic archaea which lives in geothermally-heated marine sediments. It exhibits heterotropic growth by fermentation or sulfur respiration.

Species- or subspecies-specific DNA (including COMPLEMENTARY DNA; conserved genes, whole chromosomes, or whole genomes) used in hybridization studies in order to identify microorganisms, to measure DNA-DNA homologies, to group subspecies, etc. The DNA probe hybridizes with a specific mRNA, if present. Conventional techniques used for testing for the hybridization product include dot blot assays, Southern blot assays, and DNA:RNA hybrid-specific antibody tests. Conventional labels for the DNA probe include the radioisotope labels 32P and 125I and the chemical label biotin. The use of DNA probes provides a specific, sensitive, rapid, and inexpensive replacement for cell culture techniques for diagnosing infections.

Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.

A methylated nucleotide base found in eukaryotic DNA. In ANIMALS, the DNA METHYLATION of CYTOSINE to form 5-methylcytosine is found primarily in the palindromic sequence CpG. In PLANTS, the methylated sequence is CpNpGp, where N can be any base.

A family of BACTERIOPHAGES and ARCHAEAL VIRUSES which are characterized by complex contractile tails.

Enzymes that are involved in the reconstruction of a continuous two-stranded DNA molecule without mismatch from a molecule, which contained damaged regions.

Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.

Sequences of DNA or RNA that occur in multiple copies. There are several types: INTERSPERSED REPETITIVE SEQUENCES are copies of transposable elements (DNA TRANSPOSABLE ELEMENTS or RETROELEMENTS) dispersed throughout the genome. TERMINAL REPEAT SEQUENCES flank both ends of another sequence, for example, the long terminal repeats (LTRs) on RETROVIRUSES. Variations may be direct repeats, those occurring in the same direction, or inverted repeats, those opposite to each other in direction. TANDEM REPEAT SEQUENCES are copies which lie adjacent to each other, direct or inverted (INVERTED REPEAT SEQUENCES).

A species of POLYOMAVIRUS originally isolated from Rhesus monkey kidney tissue. It produces malignancy in human and newborn hamster kidney cell cultures.

Interruptions in the sugar-phosphate backbone of DNA, across both strands adjacently.

A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.

Double-stranded DNA of MITOCHONDRIA. In eukaryotes, the mitochondrial GENOME is circular and codes for ribosomal RNAs, transfer RNAs, and about 10 proteins.

A purine that is an isomer of ADENINE (6-aminopurine).

Deoxyribonucleic acid that makes up the genetic material of fungi.

A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.

The process by which two molecules of the same chemical composition form a condensation product or polymer.

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

A broad category of enzymes that are involved in the process of GENETIC RECOMBINATION.

Gram-negative aerobic rods found in warm water (40-79 degrees C) such as hot springs, hot water tanks, and thermally polluted rivers.

Emission or propagation of acoustic waves (SOUND), ELECTROMAGNETIC ENERGY waves (such as LIGHT; RADIO WAVES; GAMMA RAYS; or X-RAYS), or a stream of subatomic particles (such as ELECTRONS; NEUTRONS; PROTONS; or ALPHA PARTICLES).

The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

A genus of gram-negative, rod-shaped to ellipsoidal bacteria occurring singly or in pairs and found in flowers, soil, honey bees, fruits, cider, beer, wine, and vinegar. (From Bergey's Manual of Determinative Bacteriology, 9th ed)

A genus of tree shrews of the family TUPAIIDAE which consists of about 12 species. One of the most frequently encountered species is T. glis. Members of this genus inhabit rain forests and secondary growth areas in southeast Asia.

Electropositive chemical elements characterized by ductility, malleability, luster, and conductance of heat and electricity. They can replace the hydrogen of an acid and form bases with hydroxyl radicals. (Grant & Hackh's Chemical Dictionary, 5th ed)

Methylases that are specific for CYTOSINE residues found on DNA.

The genetic complement of a BACTERIA as represented in its DNA.

Simultaneous inflammation of the cornea and conjunctiva.

Polynucleotides are long chains of nucleotides that make up DNA and RNA, which carry genetic information in cells.

The integration of exogenous DNA into the genome of an organism at sites where its expression can be suitably controlled. This integration occurs as a result of homologous recombination.

The effects on gene expression that depend on the location of a gene with respect to its neighboring genes and region of chromosome. Stable position effects are sequence dependent. Variegated position effects depend on whether the gene is located in or adjacent to HETEROCHROMATIN or EUCHROMATIN.

A class of enzymes that catalyze the hydrolysis of one of the two ester bonds in a phosphodiester compound. EC 3.1.4.

Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.

The ultimate exclusion of nonsense sequences or intervening sequences (introns) before the final RNA transcript is sent to the cytoplasm.

The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.

A family of DNA repair enzymes that recognize damaged nucleotide bases and remove them by hydrolyzing the N-glycosidic bond that attaches them to the sugar backbone of the DNA molecule. The process called BASE EXCISION REPAIR can be completed by a DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE which excises the remaining RIBOSE sugar from the DNA.

Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.

Genes involved in activating the enzyme VDJ recombinase. RAG-1 is located on chromosome 11 in humans (chromosome 2 in mice) and is expressed exclusively in maturing lymphocytes.

A sequence of successive nucleotide triplets that are read as CODONS specifying AMINO ACIDS and begin with an INITIATOR CODON and end with a stop codon (CODON, TERMINATOR).

Poly(deoxyribonucleotide):poly(deoxyribonucleotide)ligases. Enzymes that catalyze the joining of preformed deoxyribonucleotides in phosphodiester linkage during genetic processes during repair of a single-stranded break in duplex DNA. The class includes both EC 6.5.1.1 (ATP) and EC 6.5.1.2 (NAD).

Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.

A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.

The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.

Proteins found in any species of archaeon.

Dimers found in DNA chains damaged by ULTRAVIOLET RAYS. They consist of two adjacent PYRIMIDINE NUCLEOTIDES, usually THYMINE nucleotides, in which the pyrimidine residues are covalently joined by a cyclobutane ring. These dimers block DNA REPLICATION.

Two-dimensional separation and analysis of nucleotides.

A family of gram-negative, gliding bacteria in the order Cytophagales, class Cytophagia. They are found in SOIL and SEA WATER.

Species of the genus MASTADENOVIRUS, causing a wide range of diseases in humans. Infections are mostly asymptomatic, but can be associated with diseases of the respiratory, ocular, and gastrointestinal systems. Serotypes (named with Arabic numbers) have been grouped into species designated Human adenovirus A-F.

Genotypic differences observed among individuals in a population.

The reformation of all, or part of, the native conformation of a nucleic acid molecule after the molecule has undergone denaturation.

A DNA-dependent DNA polymerase characterized in prokaryotes and may be present in higher organisms. It has both 3'-5' and 5'-3' exonuclease activity, but cannot use native double-stranded DNA as template-primer. It is not inhibited by sulfhydryl reagents and is active in both DNA synthesis and repair. EC 2.7.7.7.

A class of plasmids that transfer antibiotic resistance from one bacterium to another by conjugation.

A DNA repair enzyme that is an N-glycosyl hydrolase with specificity for DNA-containing ring-opened N(7)-methylguanine residues.

One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.

The techniques used to produce molecules exhibiting properties that conform to the demands of the experimenter. These techniques combine methods of generating structural changes with methods of selection. They are also used to examine proposed mechanisms of evolution under in vitro selection conditions.

Bacteriocins elaborated by strains of Escherichia coli and related species. They are proteins or protein-lipopolysaccharide complexes lethal to other strains of the same species.

A dye which inhibits protein biosynthesis at the initial stages. The ammonium salt (aluminon) is a reagent for the colorimetric estimation of aluminum in water, foods, and tissues.

Pairing of purine and pyrimidine bases by HYDROGEN BONDING in double-stranded DNA or RNA.

Ribonucleic acid in bacteria having regulatory and catalytic roles as well as involvement in protein synthesis.

Established cell cultures that have the potential to propagate indefinitely.

The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.

A family of double-stranded DNA viruses infecting mammals (including humans), birds and insects. There are two subfamilies: CHORDOPOXVIRINAE, poxviruses of vertebrates, and ENTOMOPOXVIRINAE, poxviruses of insects.

The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

Procedures for identifying types and strains of bacteria. The most frequently employed typing systems are BACTERIOPHAGE TYPING and SEROTYPING as well as bacteriocin typing and biotyping.

Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.

A species of gram-positive bacteria that is a common soil and water saprophyte.

Copies of transposable elements interspersed throughout the genome, some of which are still active and often referred to as "jumping genes". There are two classes of interspersed repetitive elements. Class I elements (or RETROELEMENTS - such as retrotransposons, retroviruses, LONG INTERSPERSED NUCLEOTIDE ELEMENTS and SHORT INTERSPERSED NUCLEOTIDE ELEMENTS) transpose via reverse transcription of an RNA intermediate. Class II elements (or DNA TRANSPOSABLE ELEMENTS - such as transposons, Tn elements, insertion sequence elements and mobile gene cassettes of bacterial integrons) transpose directly from one site in the DNA to another.

A species of gram-negative, facultatively anaerobic, rod-shaped bacteria that occurs in soil, fecal matter, and sewage. It is an opportunistic pathogen and causes cystitis and pyelonephritis.

The process by which a DNA molecule is duplicated.

A group of 13 or more deoxyribonucleotides in which the phosphate residues of each deoxyribonucleotide act as bridges in forming diester linkages between the deoxyribose moieties.

A subclass of enzymes of the transferase class that catalyze the transfer of a methyl group from one compound to another. (Dorland, 28th ed) EC 2.1.1.

A purine or pyrimidine base bonded to a DEOXYRIBOSE containing a bond to a phosphate group.

The monomeric units from which DNA or RNA polymers are constructed. They consist of a purine or pyrimidine base, a pentose sugar, and a phosphate group. (From King & Stansfield, A Dictionary of Genetics, 4th ed)

DNA-dependent DNA polymerases found in bacteria, animal and plant cells. During the replication process, these enzymes catalyze the addition of deoxyribonucleotide residues to the end of a DNA strand in the presence of DNA as template-primer. They also possess exonuclease activity and therefore function in DNA repair.

The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.

Proteins found in any species of virus.

A purine base and a fundamental unit of ADENINE NUCLEOTIDES.

A species of ALPHARETROVIRUS causing anemia in fowl.

Constituent of 30S subunit prokaryotic ribosomes containing 1600 nucleotides and 21 proteins. 16S rRNA is involved in initiation of polypeptide synthesis.

A trace element with atomic symbol Mn, atomic number 25, and atomic weight 54.94. It is concentrated in cell mitochondria, mostly in the pituitary gland, liver, pancreas, kidney, and bone, influences the synthesis of mucopolysaccharides, stimulates hepatic synthesis of cholesterol and fatty acids, and is a cofactor in many enzymes, including arginase and alkaline phosphatase in the liver. (From AMA Drug Evaluations Annual 1992, p2035)

The process of cleaving a chemical compound by the addition of a molecule of water.

Motifs in DNA- and RNA-binding proteins whose amino acids are folded into a single structural unit around a zinc atom. In the classic zinc finger, one zinc atom is bound to two cysteines and two histidines. In between the cysteines and histidines are 12 residues which form a DNA binding fingertip. By variations in the composition of the sequences in the fingertip and the number and spacing of tandem repeats of the motif, zinc fingers can form a large number of different sequence specific binding sites.

Plasmids containing at least one cos (cohesive-end site) of PHAGE LAMBDA. They are used as cloning vehicles.

The material of CHROMOSOMES. It is a complex of DNA; HISTONES; and nonhistone proteins (CHROMOSOMAL PROTEINS, NON-HISTONE) found within the nucleus of a cell.

The process of cumulative change over successive generations through which organisms acquire their distinguishing morphological and physiological characteristics.

The type species of the genus MICROVIRUS. A prototype of the small virulent DNA coliphages, it is composed of a single strand of supercoiled circular DNA, which on infection, is converted to a double-stranded replicative form by a host enzyme.

The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.

A genus of potentially oncogenic viruses of the family POLYOMAVIRIDAE. These viruses are normally present in their natural hosts as latent infections. The virus is oncogenic in hosts different from the species of origin.

The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.

The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.

Postnatal growth failure, short life span, and early onset of cellular senescence and subsequent immortalization in mice lacking the xeroderma pigmentosum group G gene. (1/2984)

The xeroderma pigmentosum group G (XP-G) gene (XPG) encodes a structure-specific DNA endonuclease that functions in nucleotide excision repair (NER). XP-G patients show various symptoms, ranging from mild cutaneous abnormalities to severe dermatological impairments. In some cases, patients exhibit growth failure and life-shortening and neurological dysfunctions, which are characteristics of Cockayne syndrome (CS). The known XPG protein function as the 3' nuclease in NER, however, cannot explain the development of CS in certain XP-G patients. To gain an insight into the functions of the XPG protein, we have generated and examined mice lacking xpg (the mouse counterpart of the human XPG gene) alleles. The xpg-deficient mice exhibited postnatal growth failure and underwent premature death. Since XPA-deficient mice, which are totally defective in NER, do not show such symptoms, our data indicate that XPG performs an additional function(s) besides its role in NER. Our in vitro studies showed that primary embryonic fibroblasts isolated from the xpg-deficient mice underwent premature senescence and exhibited the early onset of immortalization and accumulation of p53. (+info)

A novel nucleotide incorporation activity implicated in the editing of mitochondrial transfer RNAs in Acanthamoeba castellanii. (2/2984)

In Acanthamoeba castellanii, most of the mtDNA-encoded tRNAs are edited by a process that replaces one or more of the first three nucleotides at their 5' ends. As a result, base pairing potential is restored at acceptor stem positions (1:72, 2:71, and/or 3:70, in standard tRNA nomenclature) that are mismatched according to the corresponding tRNA gene sequence. Here we describe a novel nucleotide incorporation activity, partially purified from A. castellanii mitochondria, that has properties implicating it in mitochondrial tRNA editing in this organism. This activity is able to replace nucleotides at the first three positions of a tRNA (positions 1, 2, and 3), matching the newly incorporated residues through canonical base pairing to the respective partner nucleotide in the 3' half of the acceptor stem. Labeling experiments with natural (Escherichia coli tRNATyr) and synthetic (run-off transcripts corresponding to A. castellanii mitochondrial tRNALeu1) substrates suggest that the nucleotide incorporation activity consists of at least two components, a 5' exonuclease or endonuclease and a template-directed 3'-to-5' nucleotidyltransferase. The nucleotidyltransferase component displays an ATP requirement and generates 5' pppN... termini in vitro. The development of an accurate and efficient in vitro system opens the way for detailed studies of the biochemical properties of this novel activity and its relationship to mitochondrial tRNA editing in A. castellanii. In addition, the system will allow delineation of the structural features in a tRNA that identify it as a substrate for the labeling activity. (+info)

Base excision repair of oxidative DNA damage activated by XPG protein. (3/2984)

Oxidized pyrimidines in DNA are removed by a distinct base excision repair pathway initiated by the DNA glycosylase--AP lyase hNth1 in human cells. We have reconstituted this single-residue replacement pathway with recombinant proteins, including the AP endonuclease HAP1/APE, DNA polymerase beta, and DNA ligase III-XRCC1 heterodimer. With these proteins, the nucleotide excision repair enzyme XPG serves as a cofactor for the efficient function of hNth1. XPG protein promotes binding of hNth1 to damaged DNA. The stimulation of hNth1 activity is retained in XPG catalytic site mutants inactive in nucleotide excision repair. The data support the model that development of Cockayne syndrome in XP-G patients is related to inefficient excision of endogenous oxidative DNA damage. (+info)

Conserved residues of human XPG protein important for nuclease activity and function in nucleotide excision repair. (4/2984)

The human XPG endonuclease cuts on the 3' side of a DNA lesion during nucleotide excision repair. Mutations in XPG can lead to the disorders xeroderma pigmentosum (XP) and Cockayne syndrome. XPG shares sequence similarities in two regions with a family of structure-specific nucleases and exonucleases. To begin defining its catalytic mechanism, we changed highly conserved residues and determined the effects on the endonuclease activity of isolated XPG, its function in open complex formation and dual incision reconstituted with purified proteins, and its ability to restore cellular resistance to UV light. The substitution A792V present in two XP complementation group G (XP-G) individuals reduced but did not abolish endonuclease activity, explaining their mild clinical phenotype. Isolated XPG proteins with Asp-77 or Glu-791 substitutions did not cleave DNA. In the reconstituted repair system, alanine substitutions at these positions permitted open complex formation but were inactive for 3' cleavage, whereas D77E and E791D proteins retained considerable activity. The function of each mutant protein in the reconstituted system was mirrored by its ability to restore UV resistance to XP-G cell lines. Hydrodynamic measurements indicated that XPG exists as a monomer in high salt conditions, but immunoprecipitation of intact and truncated XPG proteins showed that XPG polypeptides can interact with each other, suggesting dimerization as an element of XPG function. The mutation results define critical residues in the catalytic center of XPG and strongly suggest that key features of the strand cleavage mechanism and active site structure are shared by members of the nuclease family. (+info)

A restriction endonuclease from Staphylococcus aureus. (5/2984)

A specific endonuclease, Sau 3AI, has been partially purified from Staphylococcus aureus strain 3A by DEAE-cellulose chromatography. The enzyme cleaves adenovirus type 5 DNA many times, SV40 DNA eight times but does not cleave double-stranded phi X174 DNA. It recognizes the sequence (see article) and cleaves as indicated by the arrows. Evidence is presented that this enzyme plays a role in the biological restriction-modification system of Staphylococcus aureus strain 3A. (+info)

Chromatin structure: a property of the higher structures of chromatin and in the time course of its formation during chromatin replication. (6/2984)

The action of a number of enzymes and metals on one nuclear preparation were interpreted in terms of the existence of a fragile but highly DNAase-I resistant feature of chromatin superstructure. The generation of this DNAase-I resistance feature of chromatin was then followed during normal DNA synthesis in the regenerating rat liver by following the disappearance of a transitory DNAase-I susceptible state. This transitory, DNAase-I susceptible state appears to be extremely similar to the post-synthetic, DNAase-I susceptible state that has been described in He La32. (+info)

'Saccharomyces cerevisiae MSH2/6 complex interacts with Holliday junctions and facilitates their cleavage by phage resolution enzymes. (7/2984)

Genetic and biochemical studies have indicated that mismatch repair proteins can interact with recombination intermediates. In this study, gel shift assays and electron microscopic analysis were used to show that the Saccharomyces cerevisiae MSH2/6 complex binds to Holliday junctions and has an affinity and specificity for them that is at least as high as it has as for mispaired bases. Under equilibrium binding conditions, the MSH2/6 complex had a Kd of binding to Holliday junctions of 0.5 nM. The MSH2/6 complex enhanced the cleavage of Holliday junctions by T4 endonuclease VII and T7 endonuclease I. This is consistent with the view that the MSH2/6 complex can function in both mismatch repair and the resolution of recombination intermediates as predicted by genetic studies. (+info)

Defective repair of cisplatin-induced DNA damage caused by reduced XPA protein in testicular germ cell tumours. (8/2984)

Metastatic cancer in adults usually has a fatal outcome. In contrast, advanced testicular germ cell tumours are cured in over 80% of patients using cisplatin-based combination chemotherapy [1]. An understanding of why these cells are sensitive to chemotherapeutic drugs is likely to have implications for the treatment of other types of cancer. Earlier measurements indicate that testis tumour cells are hypersensitive to cisplatin and have a low capacity to remove cisplatin-induced DNA damage from the genome [2] [3]. We have investigated the nucleotide excision repair (NER) capacity of extracts from the well-defined 833K and GCT27 human testis tumour cell lines. Both had a reduced ability to carry out the incision steps of NER in comparison with extracts from known repair-proficient cells. Immunoblotting revealed that the testis tumour cells had normal amounts of most NER proteins, but low levels of the xeroderma pigmentosum group A protein (XPA) and the ERCC1-XPF endonuclease complex. Addition of XPA specifically conferred full NER capacity on the testis tumour extracts. These results show that a low XPA level in the testis tumour cell lines is sufficient to explain their poor ability to remove cisplatin adducts from DNA and might be a major reason for the high cisplatin sensitivity of testis tumours. Targeted inhibition of XPA could sensitise other types of cells and tumours to cisplatin and broaden the usefulness of this chemotherapeutic agent. (+info)

Endonucleases are a class of enzymes that cleave DNA or RNA at specific sites within the molecule. They are important in various biological processes, including DNA replication, repair, and gene expression. In the medical field, endonucleases are used in a variety of applications, such as gene therapy, where they are used to target and modify specific genes, and in the treatment of genetic disorders, where they are used to correct mutations in DNA. They are also used in molecular biology research to manipulate and analyze DNA and RNA molecules.

Deoxyribonucleases, Type II Site-Specific are a group of enzymes that specifically target and cleave DNA at specific sites within the molecule. These enzymes are also known as restriction enzymes or restriction endonucleases. They are commonly used in molecular biology for a variety of applications, including DNA cloning, genetic engineering, and the study of gene expression. These enzymes recognize specific DNA sequences and cut the DNA at specific locations, releasing short DNA fragments that can be used for further analysis or manipulation. They are important tools in the field of molecular biology and have a wide range of applications in research and medicine.

DNA restriction enzymes are a class of enzymes that are naturally produced by bacteria and archaea to protect their DNA from foreign invaders. These enzymes recognize specific sequences of DNA and cut the strands at specific points, creating a double-stranded break. This allows the bacteria or archaea to destroy the foreign DNA and prevent it from replicating within their cells. In the medical field, DNA restriction enzymes are commonly used in molecular biology techniques such as DNA cloning, genetic engineering, and DNA fingerprinting. They are also used in the diagnosis and treatment of genetic diseases, as well as in the study of viral infections and cancer. By cutting DNA at specific sites, researchers can manipulate and analyze the genetic material to gain insights into the function and regulation of genes, and to develop new therapies for genetic diseases.

Endodeoxyribonucleases are a class of enzymes that cleave DNA strands by hydrolyzing the phosphodiester bonds between the nucleotides. These enzymes are capable of cutting DNA at specific recognition sites, and are often used in molecular biology techniques such as restriction digestion, ligation, and cloning. In the medical field, endodeoxyribonucleases have potential applications in gene therapy, where they can be used to target and cleave specific DNA sequences, or in the treatment of genetic disorders, where they can be used to correct mutations in the genome.

DNA, or deoxyribonucleic acid, is a molecule that carries genetic information in living organisms. It is composed of four types of nitrogen-containing molecules called nucleotides, which are arranged in a specific sequence to form the genetic code. In the medical field, DNA is often studied as a tool for understanding and diagnosing genetic disorders. Genetic disorders are caused by changes in the DNA sequence that can affect the function of genes, leading to a variety of health problems. By analyzing DNA, doctors and researchers can identify specific genetic mutations that may be responsible for a particular disorder, and develop targeted treatments or therapies to address the underlying cause of the condition. DNA is also used in forensic science to identify individuals based on their unique genetic fingerprint. This is because each person's DNA sequence is unique, and can be used to distinguish one individual from another. DNA analysis is also used in criminal investigations to help solve crimes by linking DNA evidence to suspects or victims.

In the medical field, "DNA, Viral" refers to the genetic material of viruses, which is composed of deoxyribonucleic acid (DNA). Viruses are infectious agents that can only replicate inside living cells of organisms, including humans. The genetic material of viruses is different from that of cells, as viruses do not have a cellular structure and cannot carry out metabolic processes on their own. Instead, they rely on the host cell's machinery to replicate and produce new viral particles. Understanding the genetic material of viruses is important for developing treatments and vaccines against viral infections. By studying the DNA or RNA (ribonucleic acid) of viruses, researchers can identify potential targets for antiviral drugs and design vaccines that stimulate the immune system to recognize and fight off viral infections.

Deoxyribonuclease EcoRI (DNase EcoRI) is a type of restriction enzyme that is commonly used in molecular biology to cut DNA at specific sequences. It is named after the bacterium Escherichia coli strain RY13, from which it was first isolated. DNase EcoRI recognizes and cuts DNA at a specific sequence of four nucleotides: GAATTC. This sequence is also known as the EcoRI recognition site. When the enzyme binds to this sequence, it cleaves the phosphodiester bond between the second and third nucleotides, resulting in two fragments of DNA. DNase EcoRI is widely used in molecular biology for a variety of applications, including gene cloning, DNA fingerprinting, and the study of gene expression. It is also used in genetic engineering to cut DNA at specific sites, allowing researchers to insert, delete, or modify genes in living organisms.

Deoxyribonuclease BamHI is a type of restriction enzyme that is commonly used in molecular biology to cut DNA at specific sequences. It is named after the bacterium Bacillus amyloliquefaciens, which produces the enzyme. BamHI recognizes and cuts DNA at a specific sequence of four nucleotides: GATC. This sequence is not found in the human genome, which makes BamHI a useful tool for manipulating DNA in the laboratory. When BamHI cuts DNA, it creates a staggered cut with a 4-base pair overhang on one side and a 3-base pair overhang on the other side. BamHI is often used in combination with other restriction enzymes to create recombinant DNA molecules, which can be used to study gene function or to create genetically modified organisms. It is also used in the process of DNA cloning, where a fragment of DNA is inserted into a plasmid vector and then transformed into a bacterial host for amplification. In the medical field, BamHI and other restriction enzymes are used in a variety of applications, including gene therapy, genetic testing, and the development of new drugs. For example, researchers may use BamHI to cut and insert a new gene into a patient's cells in order to treat a genetic disorder. They may also use it to analyze a patient's DNA to identify genetic mutations that may be causing a disease.

Deoxyribonucleases (DNases) are enzymes that break down DNA molecules into smaller fragments. In the medical field, DNases are used to treat a variety of conditions, including: 1. Pulmonary fibrosis: DNases are used to break down excess DNA in the lungs, which can accumulate in people with pulmonary fibrosis and contribute to the scarring of lung tissue. 2. Cystic fibrosis: DNases are used to break down excess DNA in the airways of people with cystic fibrosis, which can help to reduce the buildup of mucus and improve lung function. 3. Inflammatory bowel disease: DNases are used to break down DNA in the gut, which can help to reduce inflammation and improve symptoms in people with inflammatory bowel disease. 4. Cancer: DNases are being studied as a potential treatment for cancer, as they may be able to help to break down DNA in cancer cells and kill them. DNases are typically administered as a medication, either by inhalation or injection. They are generally considered safe and well-tolerated, although they can cause side effects such as fever, chills, and nausea.

DNA, Bacterial refers to the genetic material of bacteria, which is a type of single-celled microorganism that can be found in various environments, including soil, water, and the human body. Bacterial DNA is typically circular in shape and contains genes that encode for the proteins necessary for the bacteria to survive and reproduce. In the medical field, bacterial DNA is often studied as a means of identifying and diagnosing bacterial infections. Bacterial DNA can be extracted from samples such as blood, urine, or sputum and analyzed using techniques such as polymerase chain reaction (PCR) or DNA sequencing. This information can be used to identify the specific type of bacteria causing an infection and to determine the most effective treatment. Bacterial DNA can also be used in research to study the evolution and diversity of bacteria, as well as their interactions with other organisms and the environment. Additionally, bacterial DNA can be modified or manipulated to create genetically engineered bacteria with specific properties, such as the ability to produce certain drugs or to degrade pollutants.

Deoxyribonucleases, Type I Site-Specific are a class of enzymes that specifically cleave DNA at specific recognition sites within the molecule. These enzymes are also known as restriction enzymes or restriction endonucleases. They are commonly used in molecular biology for a variety of applications, including DNA cloning, genetic engineering, and the study of gene expression. These enzymes recognize specific sequences of DNA bases and cleave the phosphodiester bonds between the nucleotides, resulting in the production of DNA fragments. The specificity of these enzymes allows for the precise manipulation of DNA sequences, making them a valuable tool in the field of molecular biology.

Flap endonucleases are a class of enzymes that play a crucial role in DNA replication and repair. They are responsible for cleaving the phosphodiester bond at the 5' end of a flap structure that forms during DNA replication or repair. This allows the DNA polymerase to continue synthesizing the new strand of DNA without interference from the flap structure. Flap endonucleases are found in all organisms and are essential for maintaining the integrity of the genome. Mutations in the genes encoding flap endonucleases can lead to various genetic disorders, including Cockayne syndrome, which is a rare inherited disorder characterized by sensitivity to sunlight and developmental delays. In addition to their role in DNA replication and repair, flap endonucleases have also been implicated in various cellular processes, including transcription, recombination, and telomere maintenance.

Deoxyribonuclease HpaII (DNase HpaII) is an enzyme that cleaves the phosphodiester bond between the 5-carbon sugar and the adenine base in the DNA molecule. It is a type of restriction enzyme, which are enzymes that recognize specific DNA sequences and cut them in a predictable manner. DNase HpaII is commonly used in molecular biology research to study DNA methylation patterns. Methylation is a chemical modification of DNA that plays a role in gene expression and is associated with various diseases, including cancer. DNase HpaII recognizes and cleaves DNA that contains the cytosine base methylated at the 5-carbon position, which is a common modification in mammalian DNA. By digesting DNA with DNase HpaII, researchers can identify regions of the genome that are methylated and study their function in gene regulation.

Holliday junction resolvases are a class of enzymes that play a crucial role in DNA repair and genetic recombination. These enzymes are responsible for resolving Holliday junctions, which are intermediate structures that form during DNA double-strand break repair and meiotic recombination. Holliday junctions are formed when two DNA double-strand breaks are repaired by a process called homologous recombination. During this process, the two broken DNA strands are repaired by using a homologous template, which is a DNA sequence that is similar to one of the broken strands. The repair process results in the formation of a Holliday junction, which is a four-way DNA structure that contains two double-stranded arms and two single-stranded arms. Holliday junction resolvases recognize and cleave the Holliday junction, resulting in the separation of the two double-stranded arms and the formation of two new DNA molecules. This process is essential for the proper repair of DNA double-strand breaks and the accurate segregation of genetic material during meiosis. In the medical field, Holliday junction resolvases are of particular interest because they are involved in the development of cancer and other genetic diseases. Mutations in genes encoding Holliday junction resolvases can lead to defects in DNA repair and an increased risk of cancer. Additionally, these enzymes are being studied as potential targets for the development of new cancer therapies.

In the medical field, DNA, Circular refers to a type of DNA molecule that is shaped like a circle, rather than the typical linear shape of most DNA molecules. Circular DNA molecules are often found in bacteria and viruses, and they can also be artificially created in the laboratory. Circular DNA molecules are unique in that they do not have a 5' and 3' end, as all linear DNA molecules do. Instead, they have a single continuous strand of nucleotides that forms a loop. This structure makes circular DNA molecules more stable and resistant to degradation than linear DNA molecules. In the context of medical research, circular DNA molecules have been used as vectors for gene therapy, where they are used to deliver genetic material into cells to treat or prevent diseases. They have also been used as tools for studying gene expression and regulation, as well as for developing new drugs and vaccines.

Apurinic acid is a DNA or RNA base that lacks a purine or pyrimidine ring. It is also known as deoxyadenosine or deoxythymidine, depending on whether it is found in DNA or RNA. In DNA, apurinic acid is formed when a purine base is removed or damaged, leaving behind an abasic site. In RNA, it can be formed during transcription when a ribonucleotide is incorporated in place of a deoxyribonucleotide. Apurinic acid can be repaired by the base excision repair pathway, which removes the damaged base and replaces it with the correct nucleotide. However, if the repair is not successful, it can lead to mutations and genomic instability.

Deoxyribonuclease HindIII (DNase HindIII) is a type of restriction enzyme that is commonly used in molecular biology to cut DNA at specific sequences. It is named after the bacterium "Haemophilus influenzae" strain Rd, which produces this enzyme. DNase HindIII recognizes and cuts DNA at a specific sequence of four nucleotides: AAGCT. The enzyme cleaves the phosphodiester bond between the second and third nucleotides in this sequence, producing two fragments of DNA with a 4-base pair overhang on each end. DNase HindIII is widely used in molecular biology for a variety of applications, including DNA cloning, gene expression analysis, and genome sequencing. It is also used in the study of gene regulation and the identification of genetic mutations.

Endoribonucleases are a class of enzymes that cleave RNA molecules within their strands. They are involved in various cellular processes, including gene expression, RNA processing, and degradation of unwanted or damaged RNA molecules. In the medical field, endoribonucleases have been studied for their potential therapeutic applications. For example, some endoribonucleases have been developed as gene therapy tools to target and degrade specific RNA molecules involved in diseases such as cancer, viral infections, and genetic disorders. Additionally, endoribonucleases have been used as research tools to study RNA biology and to develop new methods for RNA analysis and manipulation. For example, they can be used to selectively label or modify RNA molecules for visualization or manipulation in vitro or in vivo. Overall, endoribonucleases play important roles in RNA biology and have potential applications in both basic research and medical therapy.

DNA restriction-modification enzymes are a class of enzymes that are naturally produced by bacteria and archaea to protect their DNA from foreign invaders. These enzymes recognize specific DNA sequences and cleave the DNA at specific sites, thereby preventing the foreign DNA from being incorporated into the bacterial genome. In the medical field, these enzymes are widely used in molecular biology techniques such as DNA cloning, genetic engineering, and DNA fingerprinting. They are also used in the diagnosis and treatment of genetic diseases, as well as in the development of new drugs and vaccines. One of the most well-known applications of DNA restriction-modification enzymes is in the process of DNA fingerprinting, which is used to identify individuals based on the unique sequence of their DNA. This technique is also used in forensic science to identify suspects in criminal investigations. Overall, DNA restriction-modification enzymes play a crucial role in the field of molecular biology and have numerous applications in medicine and other fields.

In the medical field, "DNA, Recombinant" refers to a type of DNA that has been artificially synthesized or modified to contain specific genes or genetic sequences. This is achieved through a process called genetic engineering, which involves inserting foreign DNA into a host organism's genome. Recombinant DNA technology has revolutionized the field of medicine, allowing scientists to create new drugs, vaccines, and other therapeutic agents. For example, recombinant DNA technology has been used to create insulin for the treatment of diabetes, human growth hormone for the treatment of growth disorders, and vaccines for a variety of infectious diseases. Recombinant DNA technology also has important applications in basic research, allowing scientists to study the function of specific genes and genetic sequences, and to investigate the mechanisms of diseases.

In the medical field, Carbon-Oxygen Lyases are a class of enzymes that catalyze the cleavage of carbon-oxygen bonds in organic molecules. These enzymes are involved in various metabolic pathways, including the breakdown of fatty acids, amino acids, and carbohydrates. One example of a carbon-oxygen lyase is acyl-CoA dehydrogenase, which is involved in the breakdown of fatty acids. This enzyme catalyzes the removal of a hydrogen atom from the fatty acid molecule, resulting in the formation of a double bond and the release of a molecule of carbon dioxide. Carbon-oxygen lyases are also involved in the metabolism of amino acids, such as the conversion of pyruvate to acetyl-CoA, which is an important step in the production of energy in the body. Overall, carbon-oxygen lyases play a crucial role in the metabolism of organic molecules in the body and are involved in many important physiological processes.

In the medical field, "DNA, Superhelical" refers to a type of DNA molecule that has a twisted or coiled structure, known as a double helix. The double helix is composed of two strands of nucleotides that are held together by hydrogen bonds between the nitrogenous bases. Superhelical DNA is characterized by an additional level of twist or winding around its axis, which is known as supercoiling. This supercoiling can occur in either a left-handed or right-handed direction, and it is thought to play a role in regulating gene expression and other cellular processes. Supercoiling can be induced by a variety of factors, including changes in temperature, pH, or the presence of certain enzymes. It can also be influenced by the presence of proteins that bind to the DNA and help to stabilize the superhelical structure. In medical research, supercoiled DNA is often used as a model system for studying the behavior of DNA under different conditions, as well as for developing new techniques for manipulating and analyzing DNA. It is also an important component of many genetic engineering and biotechnology applications.

Deoxyribonucleases, Type III Site-Specific are a group of enzymes that specifically recognize and cleave double-stranded DNA at specific sites within the genome. These enzymes are also known as restriction enzymes or restriction endonucleases. They are commonly used in molecular biology for a variety of applications, including DNA cloning, genetic engineering, and the study of gene expression and regulation. Type III site-specific deoxyribonucleases are characterized by their ability to cleave DNA at specific sequences, which are typically four to six nucleotides long. They are also known for their high specificity and efficiency, which makes them valuable tools in the field of molecular biology.

Exonucleases are a class of enzymes that degrade nucleic acids by removing nucleotides from the ends of DNA or RNA strands. In the medical field, exonucleases are used in a variety of applications, including: 1. DNA sequencing: Exonucleases are used to generate single-stranded DNA templates for sequencing by removing the complementary strand of DNA. 2. Gene editing: Exonucleases are used in gene editing technologies such as CRISPR-Cas9 to remove specific DNA sequences. 3. DNA repair: Exonucleases are involved in the repair of DNA damage by removing damaged or incorrect nucleotides. 4. Cancer therapy: Exonucleases are being investigated as potential cancer therapies, as they can selectively target and degrade cancer cells. 5. Drug discovery: Exonucleases are used in drug discovery to identify potential drug targets by degrading specific DNA or RNA sequences. Overall, exonucleases play important roles in many areas of medical research and have the potential to be used in a variety of therapeutic applications.

CRISPR-associated proteins (Cas proteins) are a group of enzymes that are involved in the CRISPR-Cas immune system, which is found in bacteria and archaea. In this system, the Cas proteins work together to recognize and destroy foreign DNA, such as viruses or plasmids, that have invaded the cell. There are several different types of Cas proteins, each with its own specific function in the CRISPR-Cas system. Some Cas proteins are responsible for recognizing and binding to foreign DNA, while others are responsible for cutting the DNA and destroying it. In recent years, scientists have discovered that some of these Cas proteins can be harnessed for use in gene editing. For example, the Cas9 protein has been used to create targeted double-stranded breaks in DNA, which can then be repaired by the cell's own repair mechanisms. This has led to the development of a new class of gene editing tools known as CRISPR-Cas9, which has revolutionized the field of genetics and has the potential to be used to treat a wide range of diseases.

DNA modification methylases are enzymes that add or remove methyl groups to DNA molecules. These enzymes play important roles in regulating gene expression and maintaining genome stability. In the medical field, DNA modification methylases are often studied in the context of diseases such as cancer, where changes in DNA methylation patterns can contribute to the development and progression of the disease. Additionally, DNA modification methylases are being investigated as potential therapeutic targets for cancer treatment.

Exodeoxyribonucleases (EDNs) are a group of enzymes that degrade DNA by cleaving the phosphodiester bonds between the sugar-phosphate backbone of the DNA molecule. These enzymes are involved in various biological processes, including DNA repair, replication, and transcription. In the medical field, EDNs are often used as tools for studying DNA structure and function, as well as for developing new diagnostic and therapeutic strategies. For example, some EDNs have been used to selectively degrade specific regions of DNA, allowing researchers to study the function of specific genes or regulatory elements. Additionally, some EDNs have been developed as potential cancer therapies, as they can selectively target and degrade cancer cells' DNA, leading to cell death. Overall, EDNs play a critical role in many biological processes and have important applications in the medical field.

In the medical field, "DNA, Cruciform" refers to a specific type of DNA structure that is formed when two DNA strands cross over each other and form an X-shape. This structure is also known as a "Holliday junction" or a "crossing-over intermediate." Cruciform DNA structures are important in the process of DNA replication and repair, as they can form during the process of DNA replication when the two strands of DNA must be separated and then reassembled. They can also form during DNA repair when damaged or mismatched bases need to be corrected. The presence of cruciform DNA structures can have important implications for the function and stability of DNA, and they have been studied extensively in the field of molecular biology.

Deoxyribonuclease I (DNase I) is an enzyme that breaks down DNA molecules into smaller fragments. It is commonly used in molecular biology research to digest DNA samples for various applications such as DNA sequencing, Southern blotting, and restriction enzyme digestion. In the medical field, DNase I is used to treat certain lung diseases such as cystic fibrosis and acute respiratory distress syndrome (ARDS), where the lungs become inflamed and produce excess mucus that can obstruct airways. DNase I can help break down the excess mucus, making it easier to clear from the lungs. It is also used in some laboratory tests to detect the presence of DNA in biological samples.

Single-strand specific DNA and RNA endonucleases are enzymes that cleave DNA or RNA strands at specific sites within the molecule. These enzymes are capable of recognizing and binding to single-stranded regions of DNA or RNA, and then cleaving the strand at a specific nucleotide sequence. Single-strand specific endonucleases are important tools in molecular biology and genetics, as they can be used to manipulate DNA or RNA molecules for a variety of purposes. For example, they can be used to generate specific cuts in DNA or RNA molecules for use in genetic engineering, or to study the structure and function of DNA or RNA. There are several different types of single-strand specific endonucleases, including restriction enzymes, exonucleases, and endonucleases that cleave both DNA and RNA. Each type of enzyme has its own specific characteristics and uses, and researchers can choose the appropriate enzyme for their particular application based on the desired outcome.

Cytosine is a nitrogenous base that is one of the four main building blocks of DNA and RNA. It is a pyrimidine base, meaning it has a six-membered ring structure with two nitrogen atoms and four carbon atoms. In DNA, cytosine is always paired with thymine, while in RNA, it is paired with uracil. Cytosine plays a crucial role in the storage and transmission of genetic information, as it is involved in the formation of the genetic code. In the medical field, cytosine is often studied in the context of genetics and molecular biology, as well as in the development of new drugs and therapies.

Oligodeoxyribonucleotides (ODNs) are short chains of DNA or RNA that are synthesized in the laboratory. They are typically used as tools in molecular biology research, as well as in therapeutic applications such as gene therapy. ODNs can be designed to bind to specific DNA or RNA sequences, and can be used to modulate gene expression or to introduce genetic changes into cells. They can also be used as primers in PCR (polymerase chain reaction) to amplify specific DNA sequences. In the medical field, ODNs are being studied for their potential use in treating a variety of diseases, including cancer, viral infections, and genetic disorders. For example, ODNs can be used to silence specific genes that are involved in disease progression, or to stimulate the immune system to attack cancer cells.

RNA, Archaeal refers to ribonucleic acid (RNA) molecules that are found in archaea, which are a group of single-celled microorganisms that are distinct from bacteria and eukaryotes. Archaeal RNA molecules play important roles in various cellular processes, including gene expression, protein synthesis, and regulation of gene expression. They are characterized by their unique structural features and their ability to function under extreme environmental conditions, such as high temperatures and acidic pH levels. Understanding the structure and function of archaeal RNA molecules is important for understanding the biology of these microorganisms and for developing new strategies for treating diseases caused by archaeal infections.

Escherichia coli (E. coli) is a type of bacteria that is commonly found in the human gut. E. coli proteins are proteins that are produced by E. coli bacteria. These proteins can have a variety of functions, including helping the bacteria to survive and thrive in the gut, as well as potentially causing illness in humans. In the medical field, E. coli proteins are often studied as potential targets for the development of new treatments for bacterial infections. For example, some E. coli proteins are involved in the bacteria's ability to produce toxins that can cause illness in humans, and researchers are working to develop drugs that can block the activity of these proteins in order to prevent or treat E. coli infections. E. coli proteins are also used in research to study the biology of the bacteria and to understand how it interacts with the human body. For example, researchers may use E. coli proteins as markers to track the growth and spread of the bacteria in the gut, or they may use them to study the mechanisms by which the bacteria causes illness. Overall, E. coli proteins are an important area of study in the medical field, as they can provide valuable insights into the biology of this important bacterium and may have potential applications in the treatment of bacterial infections.

DNA, ribosomal, refers to the specific type of DNA found within ribosomes, which are the cellular structures responsible for protein synthesis. Ribosomal DNA (rDNA) is transcribed into ribosomal RNA (rRNA), which then forms the core of the ribosome. The rRNA molecules are essential for the assembly and function of the ribosome, and the rDNA sequences that code for these molecules are highly conserved across different species. Mutations in rDNA can lead to defects in ribosome function and can be associated with various medical conditions, including some forms of cancer and inherited disorders.

Oligonucleotides are short chains of nucleotides, which are the building blocks of DNA and RNA. In the medical field, oligonucleotides are often used as therapeutic agents to target specific genes or genetic mutations that are associated with various diseases. There are several types of oligonucleotides, including antisense oligonucleotides, siRNA (small interfering RNA), miRNA (microRNA), and aptamers. Antisense oligonucleotides are designed to bind to specific messenger RNA (mRNA) molecules and prevent them from being translated into proteins. siRNA and miRNA are designed to degrade specific mRNA molecules, while aptamers are designed to bind to specific proteins and modulate their activity. Oligonucleotides have been used to treat a variety of diseases, including genetic disorders such as spinal muscular atrophy, Duchenne muscular dystrophy, and Huntington's disease, as well as non-genetic diseases such as cancer, viral infections, and autoimmune disorders. They are also being studied as potential treatments for COVID-19. However, oligonucleotides can also have potential side effects, such as immune responses and off-target effects, which can limit their effectiveness and safety. Therefore, careful design and testing are necessary to ensure the optimal therapeutic benefits of oligonucleotides.

DNA transposable elements, also known as transposons, are segments of DNA that can move or transpose from one location in the genome to another. They are found in the genomes of many organisms, including plants, animals, and bacteria. In the medical field, DNA transposable elements are of interest because they can play a role in the evolution of genomes and the development of diseases. For example, some transposable elements can cause mutations in genes, which can lead to genetic disorders or cancer. Additionally, transposable elements can contribute to the evolution of new genes and the adaptation of organisms to changing environments. Transposable elements can also be used as tools in genetic research and biotechnology. For example, scientists can use transposable elements to insert genes into cells or organisms, allowing them to study the function of those genes or to create genetically modified organisms for various purposes.

RNA, Ribosomal (rRNA) is a type of RNA that is essential for protein synthesis in cells. It is a major component of ribosomes, which are the cellular structures responsible for translating the genetic information stored in messenger RNA (mRNA) into proteins. rRNA is synthesized in the nucleolus of the cell and is composed of several distinct regions, including the 18S, 5.8S, and 28S subunits in eukaryotic cells, and the 16S and 23S subunits in prokaryotic cells. These subunits come together to form the ribosomal subunits, which then assemble into a complete ribosome. The rRNA molecules within the ribosome serve several important functions during protein synthesis. They provide a platform for the mRNA molecule to bind and serve as a template for the assembly of the ribosome's protein synthesis machinery. They also participate in the catalytic steps of protein synthesis, including the formation of peptide bonds between amino acids. In summary, RNA, Ribosomal (rRNA) is a critical component of ribosomes and plays a central role in the process of protein synthesis in cells.

Bromouracil is a medication that is used to treat certain types of cancer, including leukemia and lymphoma. It works by interfering with the production of DNA and RNA, which are essential for the growth and reproduction of cancer cells. Bromouracil is usually given as a pill or a liquid, and it is usually taken in combination with other medications. It can cause side effects such as nausea, vomiting, and a decrease in the number of white blood cells.

Bacterial proteins are proteins that are synthesized by bacteria. They are essential for the survival and function of bacteria, and play a variety of roles in bacterial metabolism, growth, and pathogenicity. Bacterial proteins can be classified into several categories based on their function, including structural proteins, metabolic enzymes, regulatory proteins, and toxins. Structural proteins provide support and shape to the bacterial cell, while metabolic enzymes are involved in the breakdown of nutrients and the synthesis of new molecules. Regulatory proteins control the expression of other genes, and toxins can cause damage to host cells and tissues. Bacterial proteins are of interest in the medical field because they can be used as targets for the development of antibiotics and other antimicrobial agents. They can also be used as diagnostic markers for bacterial infections, and as vaccines to prevent bacterial diseases. Additionally, some bacterial proteins have been shown to have therapeutic potential, such as enzymes that can break down harmful substances in the body or proteins that can stimulate the immune system.

Polynucleotide ligases are enzymes that play a crucial role in DNA repair and replication. They catalyze the joining of two DNA strands by forming a phosphodiester bond between the 3'-hydroxyl group of one strand and the 5'-phosphate group of the other strand. This process is known as ligation. There are several types of polynucleotide ligases, including DNA ligase I, DNA ligase II, and DNA ligase III. DNA ligase I is the most abundant and versatile ligase in cells and is involved in DNA replication, repair, and recombination. DNA ligase II is primarily involved in non-homologous end joining (NHEJ), a mechanism for repairing double-strand breaks in DNA. DNA ligase III is involved in both NHEJ and homologous recombination (HR), another mechanism for repairing double-strand breaks. Polynucleotide ligases are important for maintaining the integrity of the genome and preventing mutations that can lead to diseases such as cancer. Mutations in the genes encoding these enzymes can lead to defects in DNA repair and replication, which can result in various genetic disorders.

RNA, Guide, also known as guide RNA or gRNA, is a type of RNA molecule that plays a crucial role in the process of gene editing. Specifically, gRNA is used in a technique called CRISPR-Cas9, which allows scientists to make precise changes to the DNA sequence of an organism. In CRISPR-Cas9, the gRNA molecule is designed to bind to a specific sequence of DNA. Once bound, the Cas9 enzyme is recruited to the site, where it can cut the DNA at that location. This allows scientists to insert, delete, or replace specific genes in an organism's genome. Overall, RNA, Guide is a powerful tool in the field of genetics and has the potential to revolutionize the way we treat genetic diseases and develop new therapies.

In the medical field, nucleic acid heteroduplexes refer to a type of double-stranded DNA molecule that is composed of two different strands, each with a different sequence of nucleotides. These heteroduplexes are formed when a single-stranded DNA molecule, called a probe, is hybridized with a complementary strand of DNA. The probe and the complementary strand form a double-stranded molecule, with the probe strand on one side and the complementary strand on the other. Heteroduplexes are often used in molecular biology and genetic testing to detect specific DNA sequences or to study the structure and function of DNA.

N-Glycosyl Hydrolases (NGHs) are a group of enzymes that hydrolyze (break down) the glycosidic bonds in complex carbohydrates, also known as glycans. These enzymes play important roles in various biological processes, including cell signaling, protein folding, and immune response. In the medical field, NGHs are of particular interest due to their involvement in diseases such as cancer, diabetes, and infectious diseases. For example, some NGHs are overexpressed in cancer cells, leading to increased cell proliferation and invasion. In diabetes, NGHs are involved in the breakdown of glycans in the body, which can lead to hyperglycemia (high blood sugar levels). In infectious diseases, NGHs are produced by pathogens to evade the host immune system. NGHs are also being studied as potential therapeutic targets for various diseases. For example, inhibitors of NGHs have been developed as potential treatments for cancer and diabetes. Additionally, NGHs are being investigated as potential biomarkers for disease diagnosis and prognosis.

DNA, single-stranded refers to a molecule of DNA that is not paired with its complementary strand. In contrast, double-stranded DNA is composed of two complementary strands that are held together by hydrogen bonds between base pairs. Single-stranded DNA can exist in cells under certain conditions, such as during DNA replication or repair, or in certain viruses. It can also be artificially produced in the laboratory for various purposes, such as in the process of DNA sequencing. In the medical field, single-stranded DNA is often used in diagnostic tests and as a tool for genetic research.

Magnesium is a mineral that is essential for many bodily functions. It is involved in over 300 enzymatic reactions in the body, including the production of energy, the synthesis of proteins and DNA, and the regulation of muscle and nerve function. In the medical field, magnesium is used to treat a variety of conditions, including: 1. Hypomagnesemia: A deficiency of magnesium in the blood. This can cause symptoms such as muscle cramps, spasms, and seizures. 2. Cardiac arrhythmias: Abnormal heart rhythms that can be caused by low levels of magnesium. 3. Pre-eclampsia: A condition that can occur during pregnancy and is characterized by high blood pressure and protein in the urine. Magnesium supplementation may be used to treat this condition. 4. Chronic kidney disease: Magnesium is often lost in the urine of people with chronic kidney disease, and supplementation may be necessary to maintain adequate levels. 5. Alcohol withdrawal: Magnesium supplementation may be used to treat symptoms of alcohol withdrawal, such as tremors and seizures. 6. Muscle spasms: Magnesium can help to relax muscles and relieve spasms. 7. Anxiety and depression: Some studies have suggested that magnesium supplementation may help to reduce symptoms of anxiety and depression. Magnesium is available in various forms, including oral tablets, capsules, and intravenous solutions. It is important to note that high levels of magnesium can also be toxic, so it is important to use magnesium supplements under the guidance of a healthcare provider.

In the medical field, "Cations, Divalent" refers to positively charged ions that have a charge of +2. These ions are typically metal ions, such as calcium, magnesium, and zinc, and are important for various physiological processes in the body. Divalent cations play a crucial role in maintaining the balance of electrolytes in the body, which is essential for proper nerve and muscle function. They are also involved in bone health, as calcium and magnesium are important components of bone tissue. Imbalances in the levels of divalent cations can lead to a variety of health problems, including muscle cramps, seizures, and heart arrhythmias. In some cases, medications may be prescribed to help regulate the levels of these ions in the body.

DNA probes are a specific segment of DNA that is labeled with a fluorescent or radioactive marker. They are used in medical research and diagnostics to detect and identify specific DNA sequences in a sample. DNA probes are commonly used in genetic testing to diagnose genetic disorders, such as cystic fibrosis, sickle cell anemia, and Huntington's disease. They can also be used to detect the presence of specific genes or genetic mutations in cancer cells, to identify bacteria or viruses in a sample, and to study the evolution and diversity of different species. DNA probes are created by isolating a specific DNA sequence of interest and attaching a fluorescent or radioactive label to it. The labeled probe is then hybridized to a sample of DNA, and the presence of the probe can be detected by fluorescence or radioactivity. The specificity of DNA probes allows for accurate and sensitive detection of specific DNA sequences, making them a valuable tool in medical research and diagnostics.

DNA-binding proteins are a class of proteins that interact with DNA molecules to regulate gene expression. These proteins recognize specific DNA sequences and bind to them, thereby affecting the transcription of genes into messenger RNA (mRNA) and ultimately the production of proteins. DNA-binding proteins play a crucial role in many biological processes, including cell division, differentiation, and development. They can act as activators or repressors of gene expression, depending on the specific DNA sequence they bind to and the cellular context in which they are expressed. Examples of DNA-binding proteins include transcription factors, histones, and non-histone chromosomal proteins. Transcription factors are proteins that bind to specific DNA sequences and regulate the transcription of genes by recruiting RNA polymerase and other factors to the promoter region of a gene. Histones are proteins that package DNA into chromatin, and non-histone chromosomal proteins help to organize and regulate chromatin structure. DNA-binding proteins are important targets for drug discovery and development, as they play a central role in many diseases, including cancer, genetic disorders, and infectious diseases.

5-Methylcytosine (5mC) is a modified form of the DNA nucleotide cytosine, in which one of the hydrogen atoms in the cytosine ring is replaced by a methyl group (-CH3). This modification is a common epigenetic modification that plays a crucial role in regulating gene expression and maintaining genome stability. In the medical field, 5mC is often studied in the context of cancer, where it is frequently found to be dysregulated. For example, in many types of cancer, the levels of 5mC are reduced, leading to increased expression of oncogenes and decreased expression of tumor suppressor genes. This can contribute to the development and progression of cancer. In addition to its role in cancer, 5mC is also involved in a variety of other biological processes, including embryonic development, aging, and neurological function. As such, it is an important target for research in the fields of genetics, epigenetics, and medicine.

DNA repair enzymes are a group of proteins that play a crucial role in maintaining the integrity of an organism's DNA. These enzymes are responsible for recognizing and repairing damage to DNA that can occur due to various factors, such as exposure to radiation, chemicals, or errors during DNA replication. There are several types of DNA repair enzymes, each with a specific function in repairing different types of DNA damage. Some examples of DNA repair enzymes include: 1. Base excision repair enzymes: These enzymes remove damaged or incorrect bases from DNA and replace them with the correct base. 2. Nucleotide excision repair enzymes: These enzymes remove larger sections of damaged DNA and replace them with the correct sequence. 3. Mismatch repair enzymes: These enzymes recognize and correct errors that occur during DNA replication. 4. Double-strand break repair enzymes: These enzymes repair double-strand breaks in DNA, which can be caused by radiation or other types of DNA damage. DNA repair enzymes are essential for maintaining the stability and integrity of an organism's DNA, and defects in these enzymes can lead to various diseases, including cancer.

DNA, Mitochondrial refers to the genetic material found within the mitochondria, which are small organelles found in the cells of most eukaryotic organisms. Mitochondrial DNA (mtDNA) is a small circular molecule that is separate from the nuclear DNA found in the cell nucleus. Mitochondrial DNA is maternally inherited, meaning that a person inherits their mtDNA from their mother. Unlike nuclear DNA, which is diploid (contains two copies of each gene), mtDNA is haploid (contains only one copy of each gene). Mutations in mitochondrial DNA can lead to a variety of inherited disorders, including mitochondrial disorders, which are a group of conditions that affect the mitochondria and can cause a range of symptoms, including muscle weakness, fatigue, and neurological problems.

2-Aminopurine is a nucleobase that is structurally similar to adenine, but with an amino group (-NH2) replacing the hydrogen atom at the 2-position of the pyrimidine ring. It is not a naturally occurring nucleobase in DNA or RNA, but it can be incorporated into nucleic acids by chemical modification or enzymatic incorporation. In the medical field, 2-aminopurine has been used as a fluorescent probe for studying DNA and RNA structure and dynamics. It can also be used as a substitute for adenine in DNA synthesis, which can be useful for studying the effects of different nucleobases on DNA replication and repair. Additionally, 2-aminopurine has been used as a mutagen in genetic studies, as it can cause mutations when incorporated into DNA during replication.

DNA, Fungal refers to the genetic material of fungi, which is a type of eukaryotic microorganism that includes yeasts, molds, and mushrooms. Fungal DNA is composed of four types of nucleotides: adenine (A), thymine (T), cytosine (C), and guanine (G), which are arranged in a specific sequence to form the genetic code that determines the characteristics and functions of the fungus. In the medical field, fungal DNA is often studied in the context of infections caused by fungi, such as candidiasis, aspergillosis, and cryptococcosis. Fungal DNA can be detected in clinical samples, such as blood, sputum, or tissue, using molecular diagnostic techniques such as polymerase chain reaction (PCR) or DNA sequencing. These tests can help diagnose fungal infections and guide treatment decisions. Additionally, fungal DNA can be used in research to study the evolution and diversity of fungi, as well as their interactions with other organisms and the environment.

Recombinases are a class of enzymes that play a crucial role in the process of genetic recombination, which is the exchange of genetic material between two different DNA molecules. In the medical field, recombinases are often used in genetic engineering and gene therapy to manipulate DNA sequences and create new genetic constructs. There are several different types of recombinases, including homologous recombinases, site-specific recombinases, and transposable recombinases. Homologous recombinases, such as the bacterial enzyme RecA, are involved in the repair of DNA double-strand breaks and the exchange of genetic material between homologous chromosomes during meiosis. Site-specific recombinases, such as the bacterial enzyme Cre, recognize specific DNA sequences and catalyze the exchange of genetic material between two DNA molecules that contain complementary sequences. Transposable recombinases, such as the bacterial enzyme Tn5, are involved in the movement of genetic elements, such as transposons, within the genome. Recombinases are also used in the development of gene therapy, where they are used to insert new genes into a patient's genome in order to treat genetic diseases or to enhance the expression of therapeutic genes. For example, the use of recombinases has been shown to be effective in the treatment of certain types of inherited blindness, where the enzyme is used to insert a functional copy of the affected gene into the patient's genome.

In the medical field, metals are materials that are commonly used in medical devices, implants, and other medical applications. These metals can include stainless steel, titanium, cobalt-chromium alloys, and other materials that are known for their strength, durability, and biocompatibility. Metals are often used in medical devices because they can withstand the rigors of the human body and provide long-lasting support and stability. For example, metal implants are commonly used in orthopedic surgery to replace damaged or diseased joints, while metal stents are used to keep blood vessels open and prevent blockages. However, metals can also have potential risks and complications. For example, some people may be allergic to certain metals, which can cause skin irritation, inflammation, or other adverse reactions. Additionally, metal implants can sometimes cause tissue damage or infection, which may require additional medical treatment. Overall, the use of metals in the medical field is a complex and multifaceted issue that requires careful consideration of the benefits and risks involved.

DNA-cytosine methylases are enzymes that add a methyl group to the cytosine base in DNA. This modification, known as DNA methylation, plays an important role in regulating gene expression and maintaining genome stability. There are several types of DNA-cytosine methylases, including maintenance methylases and de novo methylases. Maintenance methylases are responsible for maintaining DNA methylation patterns that have been established during development, while de novo methylases are responsible for establishing new methylation patterns during early development. DNA methylation is an important mechanism for regulating gene expression and is involved in many biological processes, including cell differentiation, genomic imprinting, and cancer development.

Keratoconjunctivitis is a medical condition that affects the cornea and conjunctiva, which are the clear outer layer of the eye and the thin, moist membrane that covers the white part of the eye and lines the inside of the eyelids. Keratoconjunctivitis is characterized by inflammation and irritation of the cornea and conjunctiva, which can cause redness, swelling, itching, discharge, and sensitivity to light. There are several types of keratoconjunctivitis, including viral keratoconjunctivitis, bacterial keratoconjunctivitis, and allergic keratoconjunctivitis. Treatment for keratoconjunctivitis depends on the underlying cause and may include antihistamines, antibiotics, or antiviral medications, as well as eye drops or ointments to relieve symptoms. In severe cases, hospitalization may be necessary.

In the medical field, polynucleotides are large molecules composed of repeating units of nucleotides. Nucleotides are the building blocks of DNA and RNA, which are the genetic material of all living organisms. Polynucleotides can be either DNA or RNA, and they play a crucial role in the storage and transmission of genetic information. DNA is typically double-stranded and serves as the blueprint for the development and function of all living organisms. RNA, on the other hand, is typically single-stranded and plays a variety of roles in gene expression, including the synthesis of proteins. Polynucleotides can also be used in medical research and therapy. For example, antisense oligonucleotides are short, synthetic polynucleotides that can bind to specific RNA molecules and prevent their function. This approach has been used to treat a variety of genetic disorders, such as spinal muscular atrophy and Duchenne muscular dystrophy. Additionally, polynucleotides are being studied as potential vaccines against viral infections, as they can stimulate an immune response against specific viral targets.

Phosphoric diester hydrolases are a group of enzymes that catalyze the hydrolysis of phosphoric diesters, which are esters of phosphoric acid. These enzymes are involved in a variety of biological processes, including the breakdown of nucleic acids, the metabolism of lipids, and the regulation of signaling pathways. In the medical field, phosphoric diester hydrolases are important for the proper functioning of the body. For example, they are involved in the breakdown of nucleic acids, which are the building blocks of DNA and RNA. This process is essential for the replication and repair of DNA, as well as the production of proteins from genetic information. Phosphoric diester hydrolases are also involved in the metabolism of lipids, which are a type of fat that is stored in the body. These enzymes help to break down lipids into smaller molecules that can be used for energy or stored for later use. In addition, phosphoric diester hydrolases play a role in the regulation of signaling pathways, which are the communication networks that allow cells to respond to changes in their environment. These enzymes help to control the activity of signaling molecules, which can affect a wide range of cellular processes, including cell growth, differentiation, and death. Overall, phosphoric diester hydrolases are important enzymes that play a variety of roles in the body. They are involved in the breakdown of nucleic acids, the metabolism of lipids, and the regulation of signaling pathways, and are essential for the proper functioning of the body.

DNA glycosylases are a class of enzymes that play a crucial role in the repair of damaged DNA. These enzymes recognize and remove damaged or inappropriate nucleotides from the DNA strand, creating an abasic site (also known as an AP site) that can be further processed by other DNA repair enzymes. There are several types of DNA glycosylases, each with a specific substrate specificity. For example, some DNA glycosylases recognize and remove damaged bases such as thymine glycol, 8-oxoguanine, and uracil, while others recognize and remove bulky adducts such as benzo[a]pyrene diol epoxide. DNA glycosylases are important for maintaining the integrity of the genome and preventing mutations that can lead to cancer and other diseases. Mutations in DNA glycosylase genes have been linked to an increased risk of certain types of cancer, such as colon cancer and lung cancer.

Saccharomyces cerevisiae proteins are proteins that are produced by the yeast species Saccharomyces cerevisiae. This yeast is commonly used in the production of bread, beer, and wine, as well as in scientific research. In the medical field, S. cerevisiae proteins have been studied for their potential use in the treatment of various diseases, including cancer, diabetes, and neurodegenerative disorders. Some S. cerevisiae proteins have also been shown to have anti-inflammatory and immunomodulatory effects, making them of interest for the development of new therapies.

DNA ligases are enzymes that play a crucial role in DNA replication and repair. They are responsible for joining together DNA strands by catalyzing a phosphodiester bond between the 3' hydroxyl group of one DNA strand and the 5' phosphate group of another strand. This process is essential for maintaining the integrity of the DNA molecule and ensuring that genetic information is accurately passed on from one generation to the next. There are several types of DNA ligases, each with its own specific function and substrate specificity. For example, DNA ligase I is involved in the joining of Okazaki fragments during DNA replication, while DNA ligase III is involved in non-homologous end joining (NHEJ), a mechanism for repairing double-strand breaks in DNA. Mutations in genes encoding DNA ligases can lead to various genetic disorders, including Cockayne syndrome, Xeroderma pigmentosum, and Nijmegen breakage syndrome. These disorders are characterized by increased sensitivity to UV radiation, developmental abnormalities, and an increased risk of cancer.

DNA primers are short, single-stranded DNA molecules that are used in a variety of molecular biology techniques, including polymerase chain reaction (PCR) and DNA sequencing. They are designed to bind to specific regions of a DNA molecule, and are used to initiate the synthesis of new DNA strands. In PCR, DNA primers are used to amplify specific regions of DNA by providing a starting point for the polymerase enzyme to begin synthesizing new DNA strands. The primers are complementary to the target DNA sequence, and are added to the reaction mixture along with the DNA template, nucleotides, and polymerase enzyme. The polymerase enzyme uses the primers as a template to synthesize new DNA strands, which are then extended by the addition of more nucleotides. This process is repeated multiple times, resulting in the amplification of the target DNA sequence. DNA primers are also used in DNA sequencing to identify the order of nucleotides in a DNA molecule. In this application, the primers are designed to bind to specific regions of the DNA molecule, and are used to initiate the synthesis of short DNA fragments. The fragments are then sequenced using a variety of techniques, such as Sanger sequencing or next-generation sequencing. Overall, DNA primers are an important tool in molecular biology, and are used in a wide range of applications to study and manipulate DNA.

Archaeal proteins are proteins that are encoded by the genes of archaea, a group of single-celled microorganisms that are distinct from bacteria and eukaryotes. Archaeal proteins are characterized by their unique amino acid sequences and structures, which have been the subject of extensive research in the field of biochemistry and molecular biology. In the medical field, archaeal proteins have been studied for their potential applications in various areas, including drug discovery, biotechnology, and medical diagnostics. For example, archaeal enzymes have been used as biocatalysts in the production of biofuels and other valuable chemicals, and archaeal proteins have been explored as potential targets for the development of new antibiotics and other therapeutic agents. In addition, archaeal proteins have been used as diagnostic markers for various diseases, including cancer and infectious diseases. For example, certain archaeal proteins have been found to be overexpressed in certain types of cancer cells, and they have been proposed as potential biomarkers for the early detection and diagnosis of these diseases. Overall, archaeal proteins represent a rich source of novel biological molecules with potential applications in a wide range of fields, including medicine.

Pyrimidine dimers are DNA lesions that occur when two adjacent pyrimidine bases (thymine or cytosine) in the DNA double helix are covalently linked by a cyclobutane ring. This type of DNA damage is primarily caused by exposure to ultraviolet (UV) radiation, particularly UV-B radiation, which has a wavelength of 280-320 nm. Pyrimidine dimers can interfere with normal DNA replication and transcription, leading to mutations and potentially causing cancer or other diseases. The body has mechanisms to repair pyrimidine dimers, including nucleotide excision repair (NER), which involves the removal of the damaged DNA segment and replacement with new nucleotides. However, if the damage is not repaired, it can persist and lead to long-term health effects.

DNA Polymerase I is an enzyme that plays a crucial role in DNA replication in cells. It is responsible for adding nucleotides to the growing DNA strand, using the original DNA strand as a template. During DNA replication, the double-stranded DNA molecule is unwound and separated into two single strands. Each strand then serves as a template for the synthesis of a new complementary strand. DNA Polymerase I is responsible for adding the correct nucleotides to the growing strand, using the template strand as a guide. DNA Polymerase I is also involved in DNA repair processes, such as the removal of damaged or incorrect nucleotides from the DNA strand. It can recognize and remove uracil residues from the DNA strand, which can occur as a result of DNA damage or errors during replication. In the medical field, DNA Polymerase I is often studied as a target for the development of new drugs and therapies for diseases such as cancer, where DNA replication and repair processes are often disrupted. Additionally, DNA Polymerase I is used as a tool in molecular biology research, such as in the construction of recombinant DNA molecules and the analysis of DNA sequences.

DNA-formamidopyrimidine glycosylase (FPG) is an enzyme that plays a role in the repair of DNA damage. It is a member of the base excision repair pathway, which is a mechanism that removes damaged or incorrect bases from DNA. FPG recognizes and removes damaged bases that have been modified by certain types of chemical agents, such as formamidopyrimidines, which are formed when DNA is exposed to certain types of radiation or chemicals. The removal of these damaged bases by FPG is an important step in maintaining the integrity of the DNA molecule and preventing mutations that can lead to cancer and other diseases.

Colicins are a group of protein toxins produced by some strains of the bacterium Escherichia coli (E. coli). They are known to be toxic to other strains of E. coli and some other Gram-negative bacteria. Colicins are typically produced by E. coli as a defense mechanism against competing bacteria in the gut. There are several different types of colicins, each with its own specific mechanism of action. Some colicins act by disrupting the cell membrane of the target bacterium, causing it to leak and eventually die. Others act by inhibiting the synthesis of essential proteins in the target bacterium, leading to its death. Colicins have been studied extensively in the medical field, particularly in the context of infectious diseases. They have been shown to have potential as antimicrobial agents, and researchers are exploring the possibility of using colicins as a new class of antibiotics to treat bacterial infections. However, more research is needed to fully understand the potential of colicins as a therapeutic agent and to develop safe and effective ways to use them in medicine.

Aurintricarboxylic acid (ATA) is a synthetic compound that has been studied for its potential therapeutic effects in various medical conditions. It is a tricarboxylic acid with a gold complex attached to it, and it has been shown to have anti-inflammatory, anti-oxidant, and anti-cancer properties. In the medical field, ATA has been investigated for its potential use in treating a variety of conditions, including cancer, inflammatory diseases, and neurodegenerative disorders. Some studies have suggested that ATA may have anti-tumor effects by inhibiting the growth and proliferation of cancer cells, as well as by inducing apoptosis (cell death) in cancer cells. ATA has also been shown to have anti-inflammatory effects by reducing the production of pro-inflammatory cytokines and by inhibiting the activation of immune cells. Additionally, ATA has been found to have anti-oxidant properties by scavenging free radicals and reducing oxidative stress. While ATA has shown promise in preclinical studies, more research is needed to fully understand its potential therapeutic effects and to determine the optimal dosing and administration for various medical conditions.

RNA, Bacterial refers to the ribonucleic acid molecules that are produced by bacteria. These molecules play a crucial role in the functioning of bacterial cells, including the synthesis of proteins, the regulation of gene expression, and the metabolism of nutrients. Bacterial RNA can be classified into several types, including messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA), which all have specific functions within the bacterial cell. Understanding the structure and function of bacterial RNA is important for the development of new antibiotics and other treatments for bacterial infections.

Polydeoxyribonucleotides, also known as poly(dNTPs), are polymers of deoxyribonucleotides, which are the building blocks of DNA. They are composed of a sugar molecule (deoxyribose), a phosphate group, and a nitrogenous base (adenine, thymine, cytosine, or guanine). In the medical field, poly(dNTPs) are commonly used as a substrate in DNA polymerase reactions, which are essential for DNA replication and repair. They are also used in various molecular biology techniques, such as polymerase chain reaction (PCR), DNA sequencing, and DNA synthesis. Poly(dNTPs) are available in different concentrations and purities, and their selection depends on the specific application and experimental requirements.

Methyltransferases are a group of enzymes that transfer a methyl group (a carbon atom bonded to three hydrogen atoms) from one molecule to another. In the medical field, methyltransferases play important roles in various biological processes, including DNA methylation, RNA methylation, and protein methylation. DNA methylation is a process in which a methyl group is added to the cytosine base of DNA, which can affect gene expression. Methyltransferases that are involved in DNA methylation are called DNA methyltransferases (DNMTs). Abnormalities in DNA methylation have been linked to various diseases, including cancer, neurological disorders, and developmental disorders. RNA methylation is a process in which a methyl group is added to the ribose sugar or the nitrogenous base of RNA. Methyltransferases that are involved in RNA methylation are called RNA methyltransferases (RNMTs). RNA methylation can affect the stability, localization, and translation of RNA molecules. Protein methylation is a process in which a methyl group is added to the amino acid residues of proteins. Methyltransferases that are involved in protein methylation are called protein methyltransferases (PMTs). Protein methylation can affect protein-protein interactions, protein stability, and protein function. Overall, methyltransferases play important roles in regulating gene expression, RNA stability, and protein function, and their dysfunction can contribute to the development of various diseases.

Deoxyribonucleotides (dNTPs) are the building blocks of DNA. They are composed of a deoxyribose sugar, a nitrogenous base (adenine, thymine, cytosine, or guanine), and a phosphate group. In DNA replication, dNTPs are used to synthesize new DNA strands by adding complementary nucleotides to the growing strand. The correct selection of dNTPs is critical for accurate DNA replication and repair. Abnormalities in dNTP metabolism or levels can lead to various genetic disorders and diseases.

In the medical field, nucleotides are the building blocks of nucleic acids, which are the genetic material of cells. Nucleotides are composed of three components: a nitrogenous base, a pentose sugar, and a phosphate group. There are four nitrogenous bases in DNA: adenine (A), thymine (T), cytosine (C), and guanine (G). There are also four nitrogenous bases in RNA: adenine (A), uracil (U), cytosine (C), and guanine (G). The sequence of these nitrogenous bases determines the genetic information encoded in DNA and RNA.

DNA-directed DNA polymerase, also known as DNA polymerase, is an enzyme that plays a crucial role in DNA replication. It is responsible for synthesizing new DNA strands by adding nucleotides to the growing chain, using the original DNA strand as a template. In the medical field, DNA-directed DNA polymerase is often studied in the context of genetic diseases and cancer. Mutations in the genes encoding DNA polymerases can lead to errors in DNA replication, which can result in genetic disorders such as xeroderma pigmentosum and Cockayne syndrome. Additionally, DNA polymerase is a target for some anti-cancer drugs, which work by inhibiting its activity and preventing the replication of cancer cells. Overall, DNA-directed DNA polymerase is a critical enzyme in the process of DNA replication and plays a significant role in both normal cellular function and disease.

Viral proteins are proteins that are synthesized by viruses during their replication cycle within a host cell. These proteins play a crucial role in the viral life cycle, including attachment to host cells, entry into the cell, replication of the viral genome, assembly of new viral particles, and release of the virus from the host cell. Viral proteins can be classified into several categories based on their function, including structural proteins, non-structural proteins, and regulatory proteins. Structural proteins are the building blocks of the viral particle, such as capsid proteins that form the viral coat. Non-structural proteins are proteins that are not part of the viral particle but are essential for viral replication, such as proteases that cleave viral polyproteins into individual proteins. Regulatory proteins are proteins that control the expression of viral genes or the activity of viral enzymes. Viral proteins are important targets for antiviral drugs and vaccines, as they are essential for viral replication and survival. Understanding the structure and function of viral proteins is crucial for the development of effective antiviral therapies and vaccines.

Adenine is a nitrogenous base that is found in DNA and RNA. It is one of the four nitrogenous bases that make up the genetic code, along with guanine, cytosine, and thymine (in DNA) or uracil (in RNA). Adenine is a purine base, which means it has a double ring structure with a six-membered ring fused to a five-membered ring. It is one of the two purine bases found in DNA and RNA, the other being guanine. Adenine is important in the function of DNA and RNA because it forms hydrogen bonds with thymine (in DNA) or uracil (in RNA) to form the base pairs that make up the genetic code.

RNA, Ribosomal, 16S is a type of ribosomal RNA (rRNA) that is found in bacteria and archaea. It is a small subunit of the ribosome, which is the cellular machinery responsible for protein synthesis. The 16S rRNA is located in the 30S subunit of the ribosome and is essential for the binding and decoding of messenger RNA (mRNA) during translation. The sequence of the 16S rRNA is highly conserved among bacteria and archaea, making it a useful target for the identification and classification of these organisms. In the medical field, the 16S rRNA is often used in molecular biology techniques such as polymerase chain reaction (PCR) and DNA sequencing to study the diversity and evolution of bacterial and archaeal populations. It is also used in the development of diagnostic tests for bacterial infections and in the identification of antibiotic-resistant strains of bacteria.

Manganese is a chemical element with the symbol Mn and atomic number 25. It is a trace element that is essential for human health, but only in small amounts. In the medical field, manganese is primarily used to treat manganese toxicity, which is a condition that occurs when the body is exposed to high levels of manganese. Symptoms of manganese toxicity can include tremors, muscle weakness, and cognitive impairment. Treatment typically involves removing the source of exposure and providing supportive care to manage symptoms. Manganese is also used in some medical treatments, such as in the treatment of osteoporosis and in the production of certain medications.

Chromatin is a complex of DNA, RNA, and proteins that makes up the chromosomes in the nucleus of a cell. It plays a crucial role in regulating gene expression and maintaining the structure of the genome. In the medical field, chromatin is studied in relation to various diseases, including cancer, genetic disorders, and neurological conditions. For example, chromatin remodeling is a process that can alter the structure of chromatin and affect gene expression, and it has been implicated in the development of certain types of cancer. Additionally, chromatin-based therapies are being explored as potential treatments for diseases such as Alzheimer's and Parkinson's.

Deoxyribonucleoproteins (DNPs) are complexes of DNA and proteins that play important roles in the storage, replication, and expression of genetic information in cells. In the medical field, DNPs are often studied in the context of diseases such as cancer, where changes in the structure or function of DNPs can lead to the development or progression of the disease. DNPs are also important in the development of new treatments, such as gene therapies, which aim to correct or replace faulty DNA in order to treat or prevent disease.

RNA precursors, also known as ribonucleotides or ribonucleosides, are the building blocks of RNA molecules. They are composed of a nitrogenous base, a five-carbon sugar (ribose), and a phosphate group. In the medical field, RNA precursors are important because they are the starting point for the synthesis of RNA molecules, which play a crucial role in many cellular processes, including protein synthesis, gene expression, and regulation of cellular metabolism. RNA precursors can be synthesized in the cell from nucleotides, which are the building blocks of DNA and RNA. They can also be obtained from dietary sources, such as nucleotides found in meat, fish, and dairy products. Deficiencies in RNA precursors can lead to various health problems, including anemia, fatigue, and impaired immune function. In some cases, supplementation with RNA precursors may be recommended to treat or prevent these conditions.

Micrococcal nuclease (MNase) is a type of enzyme that is commonly used in molecular biology research to study the structure and function of DNA. It is derived from the bacterium Staphylococcus aureus and is a member of the DNase family of enzymes. MNase is a highly specific enzyme that cleaves DNA at the phosphodiester bond between the phosphate group and the sugar-phosphate backbone, leaving a 3' hydroxyl group and a 5' phosphate group. This enzyme is particularly useful for studying the structure of DNA, as it can be used to generate single-stranded DNA fragments that can be analyzed using a variety of molecular biology techniques. In the medical field, MNase is used in a variety of applications, including the study of chromatin structure, the analysis of DNA-protein interactions, and the development of new DNA-based therapies. It is also used in diagnostic tests to detect and identify bacterial infections, as well as in the treatment of certain types of cancer.

Lyases are a class of enzymes that catalyze the cleavage of chemical bonds in a molecule, often resulting in the formation of two smaller molecules. They are involved in a variety of metabolic pathways, including the breakdown of amino acids, carbohydrates, and fatty acids. There are several types of lyases, including oxidoreductases, transferases, hydrolases, and ligases. Each type of lyase has a specific mechanism of action and is involved in different metabolic processes. In the medical field, lyases are often studied in the context of disease and drug development. For example, certain lyases are involved in the metabolism of drugs, and changes in the activity of these enzymes can affect the efficacy and toxicity of drugs. Additionally, some lyases are involved in the metabolism of harmful substances, such as toxins and carcinogens, and their activity can be targeted for therapeutic purposes.

Uracil is a nitrogenous base that is found in RNA, but not in DNA. It is one of the four nitrogenous bases that make up the RNA molecule, along with adenine, guanine, and cytosine. Uracil is a pyrimidine base, which means that it has a six-membered ring structure with two nitrogen atoms and two carbon atoms. It is important for the function of RNA because it is involved in the process of transcription, in which the genetic information in DNA is copied into RNA. In addition, uracil is also involved in the process of translation, in which the information in RNA is used to synthesize proteins.

RNA, Ribosomal, 23S is a type of ribosomal RNA (rRNA) that is found in the large subunit of the ribosome in bacteria and archaea. It is one of the three main types of rRNA, along with 16S rRNA and 5S rRNA, that make up the ribosome and are essential for protein synthesis. The 23S rRNA molecule is approximately 2,300 nucleotides in length and is located in the large subunit of the ribosome. It plays a critical role in the binding and catalysis of the peptide bond formation reaction during protein synthesis. In addition, the 23S rRNA molecule is also involved in the binding of tRNA molecules to the ribosome, which is necessary for the proper translation of mRNA into protein. In the medical field, the 23S rRNA gene is often targeted by antibiotics, such as erythromycin and clarithromycin, which inhibit protein synthesis by binding to the 23S rRNA molecule and preventing the formation of the peptide bond. Mutations in the 23S rRNA gene can also lead to antibiotic resistance, making it important for the development of new antibiotics that target this molecule.

Ribonuclease III (RNase III) is an enzyme that plays a crucial role in the regulation of gene expression and the maintenance of cellular RNA homeostasis. It is a member of the endoribonuclease family and is found in all eukaryotic cells, including humans. RNase III is a double-stranded RNA-specific endonuclease that cleaves RNA molecules at specific sites, usually within hairpin loops or other secondary structures. It is involved in the processing of small interfering RNAs (siRNAs) and microRNAs (miRNAs), which are important regulators of gene expression. RNase III also plays a role in the degradation of messenger RNA (mRNA) and other RNA molecules that are no longer needed by the cell. In addition to its role in RNA metabolism, RNase III has been implicated in a number of cellular processes, including immune response, viral infection, and cancer. Dysregulation of RNase III activity has been linked to a variety of diseases, including cancer, viral infections, and neurological disorders.

Ribonucleases (RNases) are enzymes that catalyze the hydrolysis of RNA molecules. They are found in all living organisms and play important roles in various biological processes, including gene expression, RNA processing, and cellular signaling. In the medical field, RNases are used as research tools to study RNA biology and as therapeutic agents to treat various diseases. For example, RNases have been used to degrade viral RNA, which can help to prevent viral replication and infection. They have also been used to degrade abnormal RNA molecules that are associated with certain diseases, such as cancer and neurological disorders. In addition, RNases have been developed as diagnostic tools for detecting and monitoring various diseases. For example, some RNases can bind specifically to RNA molecules that are associated with certain diseases, allowing for the detection of these molecules in biological samples. Overall, RNases are important tools in the medical field, with applications in research, diagnosis, and therapy.

RNA, Transfer (tRNA) is a type of ribonucleic acid (RNA) that plays a crucial role in protein synthesis. It acts as an adapter molecule that carries specific amino acids to the ribosome, where they are assembled into proteins. Each tRNA molecule has a specific sequence of nucleotides that corresponds to a particular amino acid. The sequence of nucleotides is called the anticodon, and it is complementary to the codon on the messenger RNA (mRNA) molecule that specifies the amino acid. During protein synthesis, the ribosome reads the codons on the mRNA molecule and matches them with the appropriate tRNA molecules carrying the corresponding amino acids. The tRNA molecules then transfer the amino acids to the growing polypeptide chain, which is assembled into a protein. In summary, tRNA is a critical component of the protein synthesis machinery and plays a vital role in translating the genetic information stored in DNA into functional proteins.

RNA, or ribonucleic acid, is a type of nucleic acid that is involved in the process of protein synthesis in cells. It is composed of a chain of nucleotides, which are made up of a sugar molecule, a phosphate group, and a nitrogenous base. There are three types of RNA: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). In the medical field, RNA is often studied as a potential target for the development of new drugs and therapies. For example, some researchers are exploring the use of RNA interference (RNAi) to silence specific genes and treat diseases such as cancer and viral infections. Additionally, RNA is being studied as a potential biomarker for various diseases, as changes in the levels or structure of certain RNA molecules can indicate the presence of a particular condition.

In the medical field, DNA satellites are small DNA sequences that are associated with larger DNA molecules, such as chromosomes. These satellites are typically repetitive in nature and are found in the non-coding regions of DNA. DNA satellites can play a role in the regulation of gene expression and can also be used as markers for genetic disorders or diseases. In some cases, changes in the structure or composition of DNA satellites can be associated with certain medical conditions, such as cancer or neurological disorders. DNA satellites are also important for the stability and organization of chromosomes within the nucleus of a cell. They can help to hold chromosomes together and prevent them from becoming tangled or misaligned.

Cell transformation by viruses refers to the process by which viruses alter the normal functioning of host cells, leading to uncontrolled cell growth and division. This can result in the development of cancerous tumors. Viruses can cause cell transformation by introducing genetic material into the host cell, which can disrupt normal cellular processes and lead to the activation of oncogenes (genes that promote cell growth) or the inactivation of tumor suppressor genes (genes that prevent uncontrolled cell growth). There are several types of viruses that can cause cell transformation, including retroviruses (such as HIV), oncoviruses (such as hepatitis B and C viruses), and papillomaviruses (such as the human papillomavirus, which can cause cervical cancer). Cell transformation by viruses is an important area of research in the field of cancer biology, as it helps to identify the molecular mechanisms underlying cancer development and can lead to the development of new treatments for cancer.

Adenoviridae infections are a group of viral infections caused by members of the Adenoviridae family. These viruses are common and can infect a wide range of hosts, including humans, animals, and plants. In humans, adenoviruses can cause a variety of illnesses, ranging from mild respiratory infections to more severe diseases such as conjunctivitis, pneumonia, and hemorrhagic cystitis. Adenoviruses are characterized by their icosahedral capsid, which is composed of protein subunits arranged in a double-layered structure. The viral genome is a linear double-stranded DNA molecule that is enclosed within the capsid. There are currently more than 100 different serotypes of adenoviruses, each of which is associated with a specific disease. Adenovirus infections are typically transmitted through respiratory droplets, direct contact with infected individuals or surfaces, or through the fecal-oral route. Symptoms of adenovirus infections can vary depending on the specific serotype and the infected individual's immune status. Common symptoms include fever, cough, sore throat, runny nose, and red eyes. In more severe cases, adenovirus infections can cause pneumonia, bronchitis, and other respiratory complications. Treatment for adenovirus infections typically involves supportive care to manage symptoms and prevent complications. In some cases, antiviral medications may be used to help control the infection. Vaccines are currently available for some serotypes of adenoviruses, but they are not effective against all strains. Prevention of adenovirus infections involves good hygiene practices, such as washing hands frequently and avoiding close contact with infected individuals.

Methyl Methanesulfonate (MMS) is a chemical compound that is used in various industries, including the medical field. In medicine, MMS is primarily used as a chemotherapy agent to treat certain types of cancer. It works by interfering with the growth and division of cancer cells, ultimately leading to their death. MMS is typically administered intravenously or orally, and its effectiveness depends on the type and stage of cancer being treated. However, it is important to note that MMS is a potent and toxic substance, and its use is closely monitored by medical professionals to minimize the risk of side effects and complications. In addition to its use as a chemotherapy agent, MMS has also been studied for its potential use in other medical applications, such as the treatment of viral infections and the prevention of certain types of cancer. However, more research is needed to fully understand the potential benefits and risks of MMS in these contexts.

RNA probes are molecules that are used to detect and identify specific RNA sequences in cells or tissues. They are typically composed of a single-stranded RNA molecule that is labeled with a fluorescent or radioactive tag, allowing it to be easily detected and visualized. RNA probes are commonly used in molecular biology and medical research to study gene expression, identify specific RNA transcripts, and detect the presence of specific RNA molecules in cells or tissues. They can also be used in diagnostic tests to detect the presence of specific RNA sequences in clinical samples, such as blood, urine, or tissue biopsies. RNA probes are often used in conjunction with other molecular techniques, such as in situ hybridization, to visualize the localization of specific RNA molecules within cells or tissues. They are also used in conjunction with polymerase chain reaction (PCR) to amplify specific RNA sequences for further analysis.

Recombinant fusion proteins are proteins that are produced by combining two or more genes in a single molecule. These proteins are typically created using genetic engineering techniques, such as recombinant DNA technology, to insert one or more genes into a host organism, such as bacteria or yeast, which then produces the fusion protein. Fusion proteins are often used in medical research and drug development because they can have unique properties that are not present in the individual proteins that make up the fusion. For example, a fusion protein might be designed to have increased stability, improved solubility, or enhanced targeting to specific cells or tissues. Recombinant fusion proteins have a wide range of applications in medicine, including as therapeutic agents, diagnostic tools, and research reagents. Some examples of recombinant fusion proteins used in medicine include antibodies, growth factors, and cytokines.

DNA, ribosomal spacer refers to a region of non-coding DNA that is located between the 16S and 23S ribosomal RNA genes in the bacterial genome. This region is also known as the intergenic spacer (IGS) region. The length and sequence of the ribosomal spacer can vary among different bacterial species and strains, and it has been used as a molecular marker for bacterial identification and classification. In addition, the ribosomal spacer region can also contain genes that are involved in bacterial metabolism and pathogenesis.

DNA helicases are a class of enzymes that unwind or separate the two strands of DNA double helix, allowing access to the genetic information encoded within. They play a crucial role in various cellular processes, including DNA replication, DNA repair, and transcription. During DNA replication, helicases unwind the double-stranded DNA helix, creating a replication fork where new strands of DNA can be synthesized. In DNA repair, helicases are involved in unwinding damaged DNA to allow for the repair machinery to access and fix the damage. During transcription, helicases unwind the DNA double helix ahead of the RNA polymerase enzyme, allowing it to transcribe the genetic information into RNA. DNA helicases are a diverse group of enzymes, with different families and subfamilies having distinct functions and mechanisms of action. Some helicases are ATP-dependent, meaning they use the energy from ATP hydrolysis to unwind the DNA helix, while others are ATP-independent. Some helicases are also processive, meaning they can unwind the entire length of a DNA helix without dissociating from it, while others are non-processive and require the assistance of other proteins to unwind the DNA. In the medical field, DNA helicases are of interest for their potential as therapeutic targets in various diseases, including cancer, viral infections, and neurodegenerative disorders. For example, some viruses, such as HIV and herpes simplex virus, encode their own DNA helicases that are essential for their replication. Targeting these viral helicases with small molecules or antibodies could potentially be used to treat viral infections. Additionally, some DNA helicases have been implicated in the development of certain types of cancer, and targeting these enzymes may be a promising strategy for cancer therapy.

In the medical field, RecA recombinases are a type of enzyme that play a crucial role in DNA repair and recombination. RecA proteins are involved in the process of homologous recombination, which is a mechanism for repairing DNA damage or creating genetic diversity. During homologous recombination, RecA proteins bind to single-stranded DNA and recruit other proteins to form a complex called a nucleoprotein filament. This filament searches for a homologous double-stranded DNA molecule, which is used as a template for repairing the damaged or mutated DNA. RecA recombinases are also involved in the process of genetic recombination, which is the exchange of genetic material between two different DNA molecules. This process can lead to the creation of new genetic combinations and is an important mechanism for evolution. In addition to their role in DNA repair and recombination, RecA recombinases have also been implicated in various diseases, including cancer and bacterial infections. For example, mutations in the RecA gene have been associated with increased susceptibility to certain types of cancer, and some bacteria have evolved mechanisms to evade the immune system by using RecA proteins to manipulate their own DNA.

Thymine is a nitrogenous base that is one of the four nucleobases found in DNA and RNA. It is a pyrimidine base, meaning it has a six-membered ring structure with two nitrogen atoms and four carbon atoms. Thymine is essential for the proper functioning of DNA and RNA, as it is involved in the storage and transmission of genetic information. In the medical field, thymine is often studied in the context of DNA replication and repair, as well as in the development of antiviral and anticancer drugs.

In the medical field, RNA, Messenger (mRNA) refers to a type of RNA molecule that carries genetic information from DNA in the nucleus of a cell to the ribosomes, where proteins are synthesized. During the process of transcription, the DNA sequence of a gene is copied into a complementary RNA sequence called messenger RNA (mRNA). This mRNA molecule then leaves the nucleus and travels to the cytoplasm of the cell, where it binds to ribosomes and serves as a template for the synthesis of a specific protein. The sequence of nucleotides in the mRNA molecule determines the sequence of amino acids in the protein that is synthesized. Therefore, changes in the sequence of nucleotides in the mRNA molecule can result in changes in the amino acid sequence of the protein, which can affect the function of the protein and potentially lead to disease. mRNA molecules are often used in medical research and therapy as a way to introduce new genetic information into cells. For example, mRNA vaccines work by introducing a small piece of mRNA that encodes for a specific protein, which triggers an immune response in the body.

DNA-directed RNA polymerases are a group of enzymes that synthesize RNA molecules from a DNA template. These enzymes are responsible for the transcription process, which is the first step in gene expression. During transcription, the DNA sequence of a gene is copied into a complementary RNA sequence, which can then be translated into a protein. There are several different types of DNA-directed RNA polymerases, each with its own specific function and characteristics. For example, RNA polymerase I is primarily responsible for synthesizing ribosomal RNA (rRNA), which is a key component of ribosomes. RNA polymerase II is responsible for synthesizing messenger RNA (mRNA), which carries the genetic information from the DNA to the ribosomes for protein synthesis. RNA polymerase III is responsible for synthesizing small nuclear RNA (snRNA) and small Cajal body RNA (scaRNA), which play important roles in gene regulation and splicing. DNA-directed RNA polymerases are essential for the proper functioning of cells and are involved in many different biological processes, including growth, development, and response to environmental stimuli. Mutations in the genes that encode these enzymes can lead to a variety of genetic disorders and diseases.

Histidine is an amino acid that is naturally occurring in the human body. It is a building block of proteins and is essential for the proper functioning of many bodily processes. In the medical field, histidine is often used as a diagnostic tool to help diagnose certain medical conditions. For example, high levels of histidine in the blood can be a sign of a genetic disorder called histidinemia, which can cause a range of symptoms including intellectual disability, seizures, and liver problems. Histidine is also used in the treatment of certain medical conditions, such as acidosis, which is a condition in which the body's pH balance is disrupted.

Zinc is a chemical element that is essential for human health. In the medical field, zinc is used in a variety of ways, including as a supplement to treat and prevent certain health conditions. Zinc is involved in many important bodily functions, including immune system function, wound healing, and DNA synthesis. It is also important for the proper functioning of the senses of taste and smell. Zinc deficiency can lead to a range of health problems, including impaired immune function, delayed wound healing, and impaired growth and development in children. Zinc supplements are often recommended for people who are at risk of zinc deficiency, such as pregnant and breastfeeding women, people with certain medical conditions, and people who follow a vegetarian or vegan diet. In addition to its use as a supplement, zinc is also used in some medications, such as those used to treat acne and the common cold. It is also used in some over-the-counter products, such as antacids and nasal sprays. Overall, zinc is an important nutrient that plays a vital role in maintaining good health.

Oligonucleotide probes are short, synthetic DNA or RNA molecules that are designed to bind specifically to a target sequence of DNA or RNA. They are commonly used in medical research and diagnostic applications to detect and identify specific genetic sequences or to study gene expression. In medical research, oligonucleotide probes are often used in techniques such as polymerase chain reaction (PCR) and in situ hybridization (ISH) to amplify and visualize specific DNA or RNA sequences. They can also be used in gene expression studies to measure the levels of specific mRNAs in cells or tissues. In diagnostic applications, oligonucleotide probes are used in a variety of tests, including DNA sequencing, genetic testing, and infectious disease diagnosis. For example, oligonucleotide probes can be used in PCR-based tests to detect the presence of specific pathogens in clinical samples, or in microarray-based tests to measure the expression levels of thousands of genes at once. Overall, oligonucleotide probes are a powerful tool in medical research and diagnostic applications, allowing researchers and clinicians to study and understand the genetic basis of disease and to develop new treatments and diagnostic tests.

RNA-directed DNA polymerase (RDDP) is an enzyme that synthesizes DNA using RNA as a template. It is also known as reverse transcriptase. This enzyme is primarily associated with retroviruses, which are viruses that have RNA genomes that are reverse transcribed into DNA before being integrated into the host cell's genome. In the medical field, RDDP is important because it plays a key role in the replication of retroviruses, such as HIV. HIV uses RDDP to convert its RNA genome into DNA, which is then integrated into the host cell's genome. This integration can lead to the development of AIDS, a life-threatening condition. RDDP is also used in medical research and diagnostics. For example, it is used in the development of antiretroviral drugs, which are used to treat HIV infection. It is also used in the detection of retroviral infections, such as HIV, by detecting the presence of RDDP activity in patient samples.

Recombinant proteins are proteins that are produced by genetically engineering bacteria, yeast, or other organisms to express a specific gene. These proteins are typically used in medical research and drug development because they can be produced in large quantities and are often more pure and consistent than proteins that are extracted from natural sources. Recombinant proteins can be used for a variety of purposes in medicine, including as diagnostic tools, therapeutic agents, and research tools. For example, recombinant versions of human proteins such as insulin, growth hormones, and clotting factors are used to treat a variety of medical conditions. Recombinant proteins can also be used to study the function of specific genes and proteins, which can help researchers understand the underlying causes of diseases and develop new treatments.

Chromosome deletion is a genetic disorder that occurs when a portion of a chromosome is missing or deleted. This can happen during the formation of sperm or egg cells, or during early development of an embryo. Chromosome deletions can be inherited from a parent, or they can occur spontaneously. Chromosome deletions can have a wide range of effects on an individual, depending on which genes are affected and how much of the chromosome is deleted. Some chromosome deletions may cause no symptoms or only mild effects, while others can be more severe and lead to developmental delays, intellectual disabilities, and other health problems. Diagnosis of chromosome deletion typically involves genetic testing, such as karyotyping, which involves analyzing a sample of cells to look for abnormalities in the number or structure of chromosomes. Treatment for chromosome deletion depends on the specific effects it is causing and may include supportive care, therapy, and other interventions to help manage symptoms and improve quality of life.

In the medical field, a protein subunit refers to a smaller, functional unit of a larger protein complex. Proteins are made up of chains of amino acids, and these chains can fold into complex three-dimensional structures that perform a wide range of functions in the body. Protein subunits are often formed when two or more protein chains come together to form a larger complex. These subunits can be identical or different, and they can interact with each other in various ways to perform specific functions. For example, the protein hemoglobin, which carries oxygen in red blood cells, is made up of four subunits: two alpha chains and two beta chains. Each of these subunits has a specific structure and function, and they work together to form a functional hemoglobin molecule. In the medical field, understanding the structure and function of protein subunits is important for developing treatments for a wide range of diseases and conditions, including cancer, neurological disorders, and infectious diseases.

In the medical field, a codon is a sequence of three nucleotides (adenine, cytosine, guanine, thymine, or uracil) that codes for a specific amino acid in a protein. There are 64 possible codons, and each one corresponds to one of the 20 amino acids used to build proteins. The sequence of codons in a gene determines the sequence of amino acids in the resulting protein, which ultimately determines the protein's structure and function. Mutations in a gene can change the codon sequence, which can lead to changes in the amino acid sequence and potentially affect the function of the protein.

Globins are a family of proteins that are found in red blood cells and are responsible for carrying oxygen throughout the body. There are several different types of globins, including hemoglobin, myoglobin, and cytoglobin. Hemoglobin is the most well-known globin and is responsible for binding to oxygen in the lungs and transporting it to the body's tissues. Myoglobin is found in muscle tissue and is responsible for storing oxygen for use during periods of high physical activity. Cytoglobin is found in the cytoplasm of cells and is thought to play a role in the regulation of cellular respiration. Abnormalities in globin levels or function can lead to a variety of medical conditions, including anemia, sickle cell disease, and thalassemia.

Fungal proteins are proteins that are produced by fungi. They can be found in various forms, including extracellular proteins, secreted proteins, and intracellular proteins. Fungal proteins have a wide range of functions, including roles in metabolism, cell wall synthesis, and virulence. In the medical field, fungal proteins are of interest because some of them have potential therapeutic applications, such as in the treatment of fungal infections or as vaccines against fungal diseases. Additionally, some fungal proteins have been shown to have anti-cancer properties, making them potential targets for the development of new cancer treatments.

RNA, Viral refers to the genetic material of viruses that are composed of RNA instead of DNA. Viral RNA is typically single-stranded and can be either positive-sense or negative-sense. Positive-sense RNA viruses can be directly translated into proteins by the host cell's ribosomes, while negative-sense RNA viruses require a complementary positive-sense RNA intermediate before protein synthesis can occur. Viral RNA is often encapsidated within a viral capsid and can be further protected by an envelope made of lipids and proteins derived from the host cell. RNA viruses include a wide range of pathogens that can cause diseases in humans and other organisms, such as influenza, hepatitis C, and SARS-CoV-2 (the virus responsible for COVID-19).

Cell transformation, neoplastic refers to the process by which normal cells in the body undergo genetic changes that cause them to become cancerous or malignant. This process involves the accumulation of mutations in genes that regulate cell growth, division, and death, leading to uncontrolled cell proliferation and the formation of tumors. Neoplastic transformation can occur in any type of cell in the body, and it can be caused by a variety of factors, including exposure to carcinogens, radiation, viruses, and inherited genetic mutations. Once a cell has undergone neoplastic transformation, it can continue to divide and grow uncontrollably, invading nearby tissues and spreading to other parts of the body through the bloodstream or lymphatic system. The diagnosis of neoplastic transformation typically involves a combination of clinical examination, imaging studies, and biopsy. Treatment options for neoplastic transformation depend on the type and stage of cancer, as well as the patient's overall health and preferences. Common treatments include surgery, radiation therapy, chemotherapy, targeted therapy, and immunotherapy.

An example of a Type I restriction endonuclease.: 64 Furthermore, there exist DNA/RNA non-specific endonucleases, such as those ... E. coli cells contain two AP endonucleases: endonuclease IV (endoIV) and exonuclease III (exoIII) while in eukaryotes, there is ... Exonuclease Restriction endonuclease Nuclease Ribonuclease AP endonuclease HUH-tag "Properties of Exonucleases and ... One of the more famous endonucleases is Cas9. Ultimately, there are three categories of restriction endonucleases that ...

https://en.wikipedia.org/wiki/Endonuclease

Flap endonucleases (FENs, also known as 5' durgs in older references) are a class of nucleolytic enzymes that act as both 5'-3 ... The endonuclease activity of FENs was initially identified as acting on a DNA duplex which has a single-stranded 5' overhang on ... Flap endonucleases have been used in biotechnology, for example the Taqman PCR assay and the Invader Assay for mutation and ... Flap endonucleases have been identified in eukaryotes, prokaryotes, archaea, and some viruses. Organisms can have more than one ...

https://en.wikipedia.org/wiki/Flap_endonuclease

... (EC 3.1.27.10, alpha-sarcin) is an enzyme that catalyses the hydrolysis of the phosphodiester linkage between ... RRNA+endonuclease at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Enzymes, Ribosome- ...

https://en.wikipedia.org/wiki/RRNA_endonuclease

DNA repair endonuclease Nucleotide excision repair DNA Grossman L, Yeung AT (1990). "The UvrABC endonuclease system of ... uvrABC+endonuclease at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e v t e ( ... UvrABC endonuclease is a multienzyme complex in bacteria involved in DNA repair by nucleotide excision repair, and it is, ...

https://en.wikipedia.org/wiki/UvrABC_endonuclease

... (endoV) is a highly conserved endonuclease enzyme family. The primary function of endoV differs significantly in ... Vik ES, Nawaz MS, Strøm Andersen P, Fladeby C, Bjørås M, Dalhus B, Alseth I (2013). "Endonuclease V cleaves at inosines in RNA ... Morita Y, Shibutani T, Nakanishi N, Nishikura K, Iwai S, Kuraoka I (2013). "Human endonuclease V is a ribonuclease specific for ... "Structures of endonuclease V with DNA reveal initiation of deaminated adenine repair". Nature Structural & Molecular Biology. ...

https://en.wikipedia.org/wiki/Endonuclease_V

... and APE1 is considered to be the major AP endonuclease in human cells. Human AP endonuclease (APE1), like most AP endonucleases ... Human AP Endonuclease 2 (APE2), like most AP endonucleases, is also of class II. The exonuclease activity of APE2 is strongly ... Humans have two AP endonucleases, APE1 and APE2. APE1 exhibits robust AP-endonuclease activity, which accounts for >95% of the ... Basic Definition of AP endonuclease Archived 2010-06-20 at the Wayback Machine AP endonucleases family 1 in PROSITE AP ...

https://en.wikipedia.org/wiki/AP_endonuclease

The yeast homing endonuclease PI-Sce is a LAGLIDADG-type endonuclease encoded as an intein that splices itself out of another ... The homing endonucleases are a collection of endonucleases encoded either as freestanding genes within introns, as fusions with ... List of homing endonuclease cutting sites I-CreI homing endonuclease Meganucleases Restriction enzyme Introns and inteins ... Generally, owing to the homing mechanism, the gene encoding the endonuclease (the HEG, "homing endonuclease gene") is located ...

https://en.wikipedia.org/wiki/Homing_endonuclease

... tRNA splicing endonuclease, splicing endonuclease, tRNATRPintron endonuclease, transfer splicing endonuclease; systematic name ... The endonuclease relies on exons in pre-tRNA to determine splice sites. Endonuclease enzymes recognize mature domains in ... Eukaryotic tRNA-intron endonucleases are hypothesized to evolve from archaeal tRNA-intron endonucleases. Various structures of ... Eukaryotic tRNA-intron endonucleases are considered to have evolved from Archaeal tRNA-intron endonucleases, more specifically ...

https://en.wikipedia.org/wiki/TRNA-intron_endonuclease

In molecular biology, the DpnII restriction endonuclease family is a family of restriction endonucleases which includes DpnII ...

https://en.wikipedia.org/wiki/DpnII_restriction_endonuclease_family

... is a protein that in humans is encoded by the ENDOU gene. This gene encodes a protein with ... "Entrez Gene: Endonuclease, poly(U) specific". Retrieved 2018-08-17. Laneve P, Gioia U, Ragno R, Altieri F, Di Franco C, Santini ...

https://en.wikipedia.org/wiki/Endonuclease,_poly(u)_specific

... (PEAR) is a DNA amplification technology for the amplification of ... Wang, Xiaolong; Deming Gou; Shuang-yong Xu (January 1, 2010). "Polymerase-Endonuclease Amplification Reaction (PEAR) for Large- ... and thermostable endonuclease (PspGI) cleavage releases monomeric duplex oligonucleotides. PEAR has the potential to be a ... Modified Oligonucleotides Using Polymerase-Endonuclease Amplification Reaction (PEAR)". PLOS ONE. 8 (7): e67558. Bibcode: ...

https://en.wikipedia.org/wiki/Polymerase-endonuclease_amplification_reaction

"Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch ... Flap endonuclease 1 is an enzyme that in humans is encoded by the FEN1 gene. The protein encoded by this gene removes 5' ... Flap structure-specific endonuclease 1 has been shown to interact with: APEX1, BLM CDK2, CCNA2, EP300, HNRNPA1, PCNA, and WRN. ... August 2006). "Flap endonuclease 1 is overexpressed in prostate cancer and is associated with a high Gleason score". BJU ...

https://en.wikipedia.org/wiki/Flap_structure-specific_endonuclease_1

Intron-encoded endonuclease I-Sce I is a homing endonuclease. The enzyme is used in biotechnology as a meganuclease. It ... It is a rare cutting endonuclease. Statistically an 18-bp sequence will occur once in every 6.9*1010 base pairs (a frequency of ...

https://en.wikipedia.org/wiki/Intron-encoded_endonuclease_I-SceI

Homing endonuclease. Restriction enzyme. Introns and inteins. Intragenomic conflict: Homing endonuclease genes. I-CreI homing ... The homing endonucleases are a special type of restriction enzymes encoded by introns or inteins. They act on the cellular DNA ... Further reading: Homing endonuclease § Structural families.) PDB code: Code used to identify the structure of a protein in the ... Turmel M, Mercier JP, Côté V, Otis C, Lemieux C (July 1995). "The site-specific DNA endonuclease encoded by a group I intron in ...

https://en.wikipedia.org/wiki/List_of_homing_endonuclease_cutting_sites

... is a protein that in humans is encoded by the GEN1 gene. This gene encodes a ... "Entrez Gene: GEN1, Holliday junction 5' flap endonuclease". Retrieved 2017-10-16. Wang X, Wang H, Guo B, Zhang Y, Gong Y, Zhang ... provided by RefSeq, Jul 2016]. The GEN1 endonuclease shares redundancy with the EME1/MUS81 protein complex for DNA damage ...

https://en.wikipedia.org/wiki/GEN1,_Holliday_junction_5'_flap_endonuclease

... is a protein in humans that is encoded by the SLX1B gene ... The protein represents the catalytic subunit of the SLX1-SLX4 structure-specific endonuclease, which can resolve DNA secondary ... "Entrez Gene: SLX1 structure-specific endonuclease subunit homolog B (S. cerevisiae)". Retrieved 2013-05-19. v t e (Articles ...

https://en.wikipedia.org/wiki/Slx1_structure-specific_endonuclease_subunit_homolog_b_(s._cerevisiae)

... a restriction enzyme Homing endonuclease List of homing endonuclease cutting sites List of restriction enzyme cutting sites ... and the DNA-free endonuclease". In Alfred M. Pingoud (ed.). Restriction Endonucleases (Nucleic Acids and Molecular Biology, ... Type IIG restriction endonucleases (e.g., RM.Eco57I) do have a single subunit, like classical Type II restriction enzymes, but ... Naturally occurring restriction endonucleases are categorized into five groups (Types I, II, III, IV, and V) based on their ...

https://en.wikipedia.org/wiki/Restriction_enzyme

Homing Endonucleases and Inteins. Nucleic Acids and Molecular Biology. Vol. 16. pp. 345-364. doi:10.1007/3-540-29474-0_20. ISBN ...

https://en.wikipedia.org/wiki/David_W._Wood

Chirikjian, Jack G. (1987). Restriction Endonucleases and Methylases. Elsevier. ISBN 978-0-444-01285-2. "Michael McClelland - ...

https://en.wikipedia.org/wiki/Michael_McClelland_(academic)

Digest with appropriate restriction endonucleases. The region can be digested to remove elements which are thought to not be ...

https://en.wikipedia.org/wiki/Promoter_bashing

Homing endonuclease genes (HEG) convert their rival allele into a copy of themselves, and are thus inherited by nearly all ... They achieve this by encoding an endonuclease which breaks the rival allele. This break is repaired by using the sequence of ... The allele without the HEGs are cleaved by the homing endonuclease and the double-strand break are repaired by homologous ... HEGs encode sequence-specific endonucleases. The recognition sequence (RS) is 15-30 bp long and usually occurs once in the ...

https://en.wikipedia.org/wiki/Intragenomic_conflict

Homing endonuclease. Introns and inteins. Intragenomic conflict: Homing endonuclease genes. I-CreI homing endonuclease. ... One special kind of restriction enzymes is the class of "homing endonucleases", these being present in all three domains of ... A restriction enzyme or restriction endonuclease is a special type of biological macromolecule that functions as part of the " ... Wikidata has the property: cutting site of restriction enzyme (P4864) (see uses) Biology portal List of homing endonuclease ...

https://en.wikipedia.org/wiki/List_of_restriction_enzyme_cutting_sites

... are both endonucleases and deoxyribonucleases. They catalyze cleavage of the phosphodiester bonds in DNA ... Examples include: DNA restriction enzymes micrococcal nuclease Ribonuclease UvrABC endonuclease Endodeoxyribonucleases at the U ...

https://en.wikipedia.org/wiki/Endodeoxyribonuclease

Restriction endonucleases, also known as restriction enzymes are enzymes that cleave the sugar-phosphate backbone of the DNA at ... In 2006, Horton and colleagues, x-ray crystallography evidence was presented showing that the restriction endonuclease HinP1I ... "Biology and Activity of Restriction Endonucleases". Archived from the original on 2014-04-18. Retrieved 2014-04-03. Horton, ... "DNA Nicking by HinP1I Endonuclease: Bending, Base Flipping and Minor Groove Expansion". Nucleic Acids Research. 34 (3): 939-948 ...

https://en.wikipedia.org/wiki/DNA_base_flipping

To achieve this behavior, endonuclease gene drives consist of two nested elements: either a homing endonuclease or a RNA-guided ... At the molecular level, an endonuclease gene drive works by cutting a chromosome at a specific site that does not encode the ... However, homing endonucleases are sequence-specific. Altering their specificity to target other sequences of interest remains a ... Chan YS, Naujoks DA, Huen DS, Russell S (May 2011). "Insect population control by homing endonuclease-based gene drive: an ...

https://en.wikipedia.org/wiki/Gene_drive

... contains the PD..D/EXK motif within its active site like many restriction endonucleases. The enzyme is a homodimer of a ... EcoRI (pronounced "eco R one") is a restriction endonuclease enzyme isolated from species E. coli. It is a restriction enzyme ... Kim YC, Grable JC, Love R, Greene PJ, Rosenberg JM (September 1990). "Refinement of Eco RI endonuclease crystal structure: a ... "FAQs for EcoRI, Restriction Endonucleases, NEB". Archived from the original on 2012-10-15. Retrieved 2010-01-21. Eco-RI at the ...

https://en.wikipedia.org/wiki/EcoRI

Specific restriction endonucleases are used to digest DNA. The RFLP molecular marker is specific to a single fragment. Along ... DNA is first digested with endonucleases. The restriction fragments are then ligated together. A molecular marker is then ... Minisatellites Similar to RFLP, this technique also uses restriction endonucleases to digest the genomic DNA. Minisatellites ...

https://en.wikipedia.org/wiki/Molecular-weight_size_marker

Although both DNase I and II are glycoprotein endonucleases, DNase I has a monomeric sandwich-type structure with a ... Deoxyribonuclease (DNase, for short) refers to a group of glycoprotein endonucleases which are enzymes that catalyze the ... Others cleave anywhere along the chain, known as endodeoxyribonucleases (a subset of endonucleases.) Some DNases are fairly ... Bowen RA, Austgen L, Rouge M (20 February 2000). "Restriction Endonucleases and DNA Modifying Enzymes". Nucleases: DNase and ...

https://en.wikipedia.org/wiki/Deoxyribonuclease

Nei, M; Tajima, F (January 1981). "DNA polymorphism detectable by restriction endonucleases". Genetics. 97 (1): 145-63. doi: ... "Mathematical Model for Studying Genetic Variation in Terms of Restriction Endonucleases". PNAS. 76 (10): 5269-73. Bibcode: ...

https://en.wikipedia.org/wiki/Nucleotide_diversity

Soon after the discovery of restriction endonucleases and ligases, the field of genetics began using these molecular tools to ... Davis, Leonard G.; Dibner, Mark D.; Battey, James F. (1986-01-01). "Restriction Endonucleases (REs) and Their Use". Basic ...

https://en.wikipedia.org/wiki/Synthetic_genomes

... Nature. 2009 May 14;459(7244):278-81 ...

https://pubmed.ncbi.nlm.nih.gov/19369939/

The simplest way to do this is to use the Benzonase,sup,®,/sup, endonuclease. ... Benzonase® endonuclease options. For biomanufacturing, we offer two versions of our ICH Q7 Benzonase® endonuclease to meet your ... Benzonase endonuclease is an endonuclease thats normally expressed in the bacterium Serratia marcescens. Benzonase® ... To learn more about switching from the standard Benzonase® endonuclease to the Benzonase® endonuclease Safety Plus Emprove® ...

https://www.sigmaaldrich.com/GB/en/technical-documents/technical-article/pharmaceutical-and-biopharmaceutical-manufacturing/gene-therapy-manufacturing/removing-dna-and-rna-using-benzonase-endonuclease-during-viral-production

6OZF: Crystal structure of Thermotoga maritima (Tm) Endonuclease V (D110N) in complex with a 12mer DNA containing an inosine ...

https://www.ncbi.nlm.nih.gov/Structure/pdb/6OZF

Cap-dependent Endonuclease Inhibitor. An endonuclease inhibitor has a different mechanism of action than a neuraminidase ... Endonuclease inhibitors interfere with viral RNA transcription and block virus replication in both influenza A and B viruses. ... There is only one approved cap-dependent endonuclease inhibitor:. *Baloxavir marboxil (trade name Xofluza®) for oral ...

https://www.cdc.gov/flu/professionals/antivirals/links.htm

"Cpf1 is a single RNA-guided endonuclease of a Class 2 CRISPR-Cas system" 163, no. 3 (2015). Zetsche, Bernd et al. "Cpf1 is a ... Amino Acid Sequence Article CRISPR-Cas Systems Endonucleases Francisella Genetic Engineering HEK293 Cells Humans Molecular ... 2015). Cpf1 is a single RNA-guided endonuclease of a Class 2 CRISPR-Cas system. 163(3). Zetsche, Bernd et al. " ... Title : Cpf1 is a single RNA-guided endonuclease of a Class 2 CRISPR-Cas system Personal Author(s) : Zetsche, Bernd;Gootenberg ...

https://stacks.cdc.gov/view/cdc/37605

Specified endonuclease or exonuclease can recognize the antibody-stabilized mismatch-like structure and mark the exact modified ... 2: Development of endonuclease facilitated MM-seq method for 6mA mapping in C. reinhardtii and E. coli.. ... b A schematic diagram of MM-seq using T7E1 and MBN endonucleases. c Cleavage signals of reads mapped to the known 6mA sites in ... e High number of overlapping 6mA sites detected between T7E1 endonuclease and Lambda exonuclease in C. reinhardtii and E. coli ...

https://www.nature.com/articles/s41421-022-00484-1?error=cookies_not_supported

AP endonuclease. journals in this list are indexed in OA.mg. If you spot any mistakes in this table of AP endonuclease. OA ... Open Access AP endonuclease Journals. A list of Open Access AP endonuclease. journals for you to publish your manuscript in. AP ... Where can I publish my AP endonuclease paper?. You can publish your AP endonuclease paper in the Open Access journals in this ... We hope this list of AP endonuclease OA journals will be helpful for you in deciding where to publish your AP endonuclease ...

https://oa.mg/journals/open-access-ap-endonuclease-journals

... Auteurs. Coulon S, Noguchi E, Noguchi ... Slx1 and Slx4 are subunits of a structure-specific DNA endonuclease that is found in Saccharomyces cerevisiae, ... Rad22Rad52-dependent repair of ribosomal DNA repeats cleaved by Slx1-Slx4 endonuclease.. ...

https://www.crcm-marseille.fr/publication/rad22rad52-dependent-repair-of-ribosomal-dna-repeats-cleaved-by-slx1-slx4-endonuclease-2/

... of an enzyme called the tRNA splicing endonuclease complex. Learn about this gene and related health conditions. ... The tRNA splicing endonuclease complex is particularly important for the normal processing of a form of RNA known as transfer ... The tRNA splicing endonuclease complex recognizes and then removes introns to help produce mature tRNA molecules. ... The TSEN34 gene provides instructions for making one part (subunit) of an enzyme called the tRNA splicing endonuclease complex ...

https://medlineplus.gov/genetics/gene/tsen34/

3 endonuclease. *. Missense mutations lead to xeroderma pigmentosum without neurological symptoms while mutations that result ...

https://emedicine.medscape.com/article/951148-overview

Analysis of endonuclease R-EcoRI fragments of DNA from lambdoid bacteriophages and other viruses by agarose-gel electrophoresis ... The isolation and partial characterization of a new restriction endonuclease from Providencia stuartii. scientific article ... The isolation and partial characterization of a new restriction endonuclease from Providencia stuartii (English) ...

https://m.wikidata.org/wiki/Q40577420

Colicin endonucleases (DNases) are bound and inactivated by immunity (Im) proteins. Im proteins are broadly cross-reactive yet ... Colicin endonucleases (DNases) are bound and inactivated by immunity (Im) proteins. Im proteins are broadly cross-reactive yet ... Amino Acid Sequence, Amino Acid Substitution, Binding Sites, Colicins, Endonucleases, Escherichia coli, Escherichia coli ... and computational analyses of the energetic basis for dual recognition of immunity proteins by colicin endonucleases. ...

https://www.neuroscience.ox.ac.uk/publications/310203?ae90304a-5f47-11ee-b087-061ab7f93640

Endonuclease EEPD1 Is a gatekeeper for repair of stressed replication forks. Hyun Suk Kim, Jac A. Nickoloff, Yuehan Wu, ... Dive into the research topics of Endonuclease EEPD1 Is a gatekeeper for repair of stressed replication forks. Together they ...

https://scholars.uthscsa.edu/en/publications/endonuclease-eepd1-is-a-gatekeeper-for-repair-of-stressed-replica/fingerprints/

A restriction endonuclease that recognizes the sequence GCG_AT^CGC. ... Restriction Endonucleases: A This product can be used in the following applications: Restriction Enzyme Digestion * Reagents ...

https://www.neb.com/en-us/products/r0630-asisi

... replicative intermediates into linear minichromosomes with hairpin termini by a virally induced Holliday junction endonuclease. ... replicative intermediates into linear minichromosomes with hairpin termini by a virally induced Holliday junction endonuclease. ...

https://www.camsoxford.ox.ac.uk/coi-publications/publications/976595?d544fe38-5eb0-11ee-8a7f-061b866677b4

View mouse Scap Chr9:110162356-110214017 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression

https://www.informatics.jax.org/marker/MGI:2135958

Double-stranded endonuclease activity was determined in a 50 μL reaction containing 0.5 μg of pBR322 DNA and 10 μL of enzyme ...

https://www.qiagen.com/br/products/discovery-and-translational-research/enzymes-for-molecular-biology/rnase-inhibitor

Double-stranded endonuclease activity in Klenow Fragment (3→5 exo-) enzyme was determined in a 50 μL reaction containing 0.5 ...

https://www.qiagen.com/lu/products/discovery-and-translational-research/enzymes-for-molecular-biology/klenow-exo-minus

Apurinic/apyrimidinic endonuclease (APE); comet assay; fungicides; glutathione; malondialdehyde (MDA); organophosphate ...

http://www2a.cdc.gov/nioshtic-2/BuildQyr.asp?s1=pesticide+or+pesticides+or+insecticide+or+insecticides+or+herbicide+or+herbicides+or+fungicide+or+fungicides&f1=TI&Startyear=&t1=1&s2=pesticide+or+pesticides+or+insecticide+or+insecticides+or+herbicide+or+herbicides+or+fungicide+or+fungicides&B1=Search&terms=4&Adv=1&f2=KW&Limit=500&Sort=DP+DESC&EndYear=&D1=10&PageNo=61&RecNo=604&View=f&

... unconventional splicing of XBP1 mRNA in the nucleus that also requires inositol-requiring transmembrane kinase and endonuclease ... inositol-requiring transmembrane kinase and endonuclease 1α (IRE1α), protein kinase-like ER kinase (PERK), and activation of ... unconventional splicing of XBP1 mRNA predominantly occurs in the cytoplasm and is mediated by the ER-located endonuclease IRE1α ... unconventional splicing of XBP1 mRNA in the nucleus that also requires inositol-requiring transmembrane kinase and endonuclease ...

https://www.mdpi.com/1422-0067/16/6/13302

Light blue boxes, conserved group 2 sequence motif; orange, group I intron endonuclease domain; light orange, GIY-YIG excision ... DNA-binding motif found in homing endonucleases and related proteins (NUMOD); red arrows, individual CxxC motifs. Sb, ...

https://www.frontiersin.org/articles/10.3389/fmicb.2020.607182/full

MLH1-MLH3 endonuclease complex. Phenotype Details Phenotype Phenotype annotations for a gene are curated single mutant ...

https://www.yeastgenome.org/locus/S000006085

Name: endonuclease V. Synonyms: A730011L01Rik. Type: Gene. Species: Mus musculus (mouse). Chromosome: 11 ...

https://www.mmrrc.org/catalog/sds.php?mmrrc_id=40182

Structure of the mini-RNA-guided endonuclease CRISPR-Cas12j3. Carabias del Rey, Arturo, Fuglsang, Anders, Temperini, Piero, ... Structure of the mini-RNA-guided endonuclease CRISPR-Cas12j3. Research output: Contribution to journal › Journal article › peer ...

https://www.cpr.ku.dk/staff/?pure=en%2Fpersons%2Fpiero-temperini

108091007521 restriction endonucleases Proteins 0.000 description 1 * 238000005070 sampling Methods 0.000 description 1 ...

https://patents.google.com/patent/WO2021050634A1/en

1. Specific Cleavage of Simian Virus 40 DNA by Restriction Endonuclease of Hemophilus Influenzae Format: Text ...

https://profiles.nlm.nih.gov/spotlight/pd/catalog?f%5Bexhibit_tags%5D%5B%5D=biographical&f%5Bexhibit_tags%5D%5B%5D=enzymes&f%5Breadonly_format_ssim%5D%5B%5D=Text&f%5Breadonly_story-section_ssim%5D%5B%5D=Biographical+Information&f%5Breadonly_subject_ssim%5D%5B%5D=Haemophilus+influenzae&f%5Breadonly_subject_ssim%5D%5B%5D=Simian+virus+40&per_page=100&search_field=all_fields&sort=readonly_date-yyyymmdd_ssim+desc&view=masonry

PDB Compounds: (B:) mismatch repair endonuclease pms2. SCOPe Domain Sequences for d1h7ub1:. Sequence, based on SEQRES records ...

http://scop.berkeley.edu/sunid=65711&ver=2.06

After incubation, the reaction mixture is transferred to the Amplification Microwell, which contains two enzymes (a DNA polymerase and a restriction endonuclease) necessary for SDA. (cdc.gov)

PAM-Dependent Target DNA Recognition and Cleavage by C2c1 CRISPR-Cas Endonuclease. (anl.gov)
C2c1 is a newly identified guide RNA-mediated type V-B CRISPR-Cas endonuclease that site-specifically targets and cleaves both strands of target DNA. (anl.gov)
Componentes proteicos de los SISTEMAS CRISPR-CAS, de defensa antiviral en ARCHAEA y BACTERIAS. (bvsalud.org)

The holoenzyme possesses three activities: 5'→3' DNA-dependent DNA polymerase, 3'→5' proofreading and 3'→5' exonuclease (also known as flap endonuclease). (qiagen.com)

Specified endonuclease or exonuclease can recognize the antibody-stabilized mismatch-like structure and mark the exact modified sites for sequencing readout. (nature.com)

Experimental and computational analyses of the energetic basis for dual recognition of immunity proteins by colicin endonucleases. (ox.ac.uk)
Colicin endonucleases (DNases) are bound and inactivated by immunity (Im) proteins. (ox.ac.uk)
This mutation impairs the function of the tRNA splicing endonuclease complex, which likely disrupts the processing of RNA molecules and affects the production of many types of proteins. (medlineplus.gov)

Whether for developing viral vaccines, viral vectors for vaccine, cell and gene therapy, or oncolytic viruses, Benzonase ® endonuclease removes nucleic acid contamination from the final product to meet regulatory standards. (sigmaaldrich.com)
To learn more about optimizing Benzonase ® endonuclease for your process, see our application note " Optimization Strategy and Process Economics of DNA Digestion in Viral Vector Production for Gene Therapy " and data sheet " Optimization of Benzonase ® endonuclease use in virus purification . (sigmaaldrich.com)
The TSEN34 gene provides instructions for making one part (subunit) of an enzyme called the tRNA splicing endonuclease complex. (medlineplus.gov)

Benzonase ® endonuclease intensifies downstream processes by increasing efficiency of these steps and results in higher recovery of viral particles. (sigmaaldrich.com)
Endonuclease inhibitors interfere with viral RNA transcription and block virus replication in both influenza A and B viruses. (cdc.gov)

Mutations in the tRNA splicing endonuclease complex cause pontocerebellar hypoplasia. (medlineplus.gov)

Researchers suspect that the tRNA splicing endonuclease complex cuts (cleaves) one end of mRNA molecules so a string of adenines (one of the building blocks of RNA) can be added. (medlineplus.gov)

An endonuclease inhibitor has a different mechanism of action than a neuraminidase inhibitor. (cdc.gov)

Benzonase ® endonuclease is expressed in E. coli W3110, a mutant strain of K12. (sigmaaldrich.com)

Once these nucleic acids become broken down, Benzonase ® endonuclease and small DNA fragments can be easily removed by tangential flow filtration. (sigmaaldrich.com)

Double-stranded endonuclease activity was determined in a 50 μL reaction containing 0.5 μg of pBR322 DNA and 10 μL of enzyme solution incubated for 4 hours at 37°C. (qiagen.com)

The slide, entitled, "Ricin Molecule", describes the molecule as a 66kDa heterodimer, bonded by a disulfide bridge, the B-chain (34kDa) binds to cell surface receptors, while the toxin-receptor complex is taken into the cell, the A-chain ((32kDa) has endonuclease activity, and inhibits DNA replication and protein synthesis at low levels (cytotoxin). (cdc.gov)

The tRNA splicing endonuclease complex is particularly important for the normal processing of a form of RNA known as transfer RNA (tRNA). (medlineplus.gov)
The tRNA splicing endonuclease complex recognizes and then removes introns to help produce mature tRNA molecules. (medlineplus.gov)
Studies suggest that the tRNA splicing endonuclease complex may also be involved in processing another form of RNA known as messenger RNA (mRNA). (medlineplus.gov)
However, it is unknown exactly how reduced function of the tRNA splicing endonuclease complex leads to abnormal brain development in people with this condition. (medlineplus.gov)

In this minireview, we describe recent efforts made to overcome these problems by using target-specific endonucleases, including CRISPR. (molcells.org)
Slx1 and Slx4 are subunits of a structure-specific DNA endonuclease that is found in Saccharomyces cerevisiae, Schizosaccharomyces pombe, and other eukaryotic species. (crcm-marseille.fr)
Plasmid identification using specific endonucleases. (wikidata.org)

Actualización sobre el virus la influenza aviar A (H5N1) en los seres humanos. (cdc.gov)

Rad22Rad52-dependent repair of ribosomal DNA repeats cleaved by Slx1-Slx4 endonuclease. (crcm-marseille.fr)

We made this list which includes all the high-impact factor AP endonuclease journals that might be relevant to your field of study. (oa.mg)
Rather than just the top hits AP endonuclease journals, we have made an exhaustive list of open accesss AP endonuclease journals. (oa.mg)

The structures showed that HindIII belongs to the EcoRI-like (alpha-class) subfamily of type II restriction endonucleases. (nih.gov)
Restriction endonuclease approaches were developed to recognize specific DNA sequences, produce double-stranded DNA breaks, and thereby initiate target molecule degradation. (medscape.com)
Unlike other gene therapy approaches, restriction endonucleases are not contingent on stable vector integration into the nuclear genome. (medscape.com)
2014). Restriction endonucleases recognize a broad repertoire of mtDNA sequences ('restriction sites') and some pathogenic mtDNA mutations add restriction sites that restriction endonucleases specifically target. (medscape.com)
Unfortunately, a key limitation of restriction endonucleases is that very few human pathogenic mutations create restriction sites amenable to this form of targeted destruction. (medscape.com)
This can in part be overcome by restriction endonucleases custom designed to bind specific DNA sequences (Klug, 2010). (medscape.com)
Varmus and other scientists use restriction endonucleases extensively for sequencing DNA, for finding individual genes (including oncogenes), and for genetic recombination. (nih.gov)

In two subtypes, PCH2 and PCH4, we identified mutations in three of the four different subunits of the tRNA-splicing endonuclease complex. (nih.gov)
Impairment of the tRNA-splicing endonuclease subunit 54 (tsen54) gene causes neurological abnormalities and larval death in zebrafish models of pontocerebellar hypoplasia. (nih.gov)
The TSEN34 gene provides instructions for making one part (subunit) of an enzyme called the tRNA splicing endonuclease complex. (medlineplus.gov)
The tRNA splicing endonuclease complex is particularly important for the normal processing of a form of RNA known as transfer RNA (tRNA). (medlineplus.gov)
The tRNA splicing endonuclease complex recognizes and then removes introns to help produce mature tRNA molecules. (medlineplus.gov)
Studies suggest that the tRNA splicing endonuclease complex may also be involved in processing another form of RNA known as messenger RNA (mRNA). (medlineplus.gov)
This mutation impairs the function of the tRNA splicing endonuclease complex, which likely disrupts the processing of RNA molecules and affects the production of many types of proteins. (medlineplus.gov)
However, it is unknown exactly how reduced function of the tRNA splicing endonuclease complex leads to abnormal brain development in people with this condition. (medlineplus.gov)

Endonuclease inhibitors interfere with viral RNA transcription and block virus replication in both influenza A and B viruses. (cdc.gov)

A zinc finger nuclease (ZFN) consists of tandem repeat zinc fingers, each binding approximately three DNA bases, combined with a FokI endonuclease domain functioning as the DNA cleavage module (Klug, 2010). (medscape.com)
In traditional TILLING, mutation discovery is accomplished through mismatch cleavage of mutant and wild-type DNA heteroduplexes using endonucleases. (usda.gov)

Non-cognate enzyme-DNA complex: structural and kinetic analysis of EcoRV endonuclease bound to the EcoRI recognition site GAATTC. (nih.gov)

Mm19, a Mycoplasma meleagridis Major Surface Nuclease that Is Related to the RE_AlwI Superfamily of Endonucleases. (uni-bielefeld.de)

LpnPI, an EpiMark ® validated product, is a modification-dependent endonuclease which recognizes C m CDG sites and generates a double-stranded DNA break on the 3´ side of the modified cytosine at N 10 /N 14 . (neb.com)

Endonuclease Buffer & Diluent_DNA Endonuclease_Tool Enzymes, Molecular Markers_Leading Biology Inc. (leadingbiology.com)

Endonucleases are used to target specific sequences in mtDNA causing double-strand breaks and degradation of mtDNA. (medscape.com)

Regulation of eukaryotic abasic endonucleases and their role in genetic stability. (nih.gov)

The endonuclease domain of Bunyavirals is therefore a promising antiviral target. (nih.gov)
A virus-like particle system identifies the endonuclease domain of Crimean-Congo hemorrhagic fever virus. (bvsalud.org)
The utility of the VLP system was demonstrated by showing that the endonuclease domain of L is located around amino acid D693, as was predicted in silico by B. Morin et al. (bvsalud.org)

Real-time observation of DNA recognition and rejection by the RNA-guided endonuclease Cas9. (uchicago.edu)

Isolation and characterization of new homing endonuclease specificities at individual target site positions. (expasy.org)

This graph shows the total number of publications written about "Endonucleases" by people in this website by year, and whether "Endonucleases" was a major or minor topic of these publications. (uchicago.edu)

The XPF-ERCC1 endonuclease and homologous recombination contribute to the repair of minor groove DNA interstrand crosslinks in mammalian cells produced by the pyrrolo[2,1-c][1,4]benzodiazepine dimer SJG-136. (ox.ac.uk)

Anatomy5

Organisms38

Diseases3

Chemicals and Drugs99

Analytical, Diagnostic and Therapeutic Techniques and Equipment28

Phenomena and Processes92

Anthropology, Education, Sociology and Social Phenomena1

Information Science5

Health Care3

Postnatal growth failure, short life span, and early onset of cellular senescence and subsequent immortalization in mice lacking the xeroderma pigmentosum group G gene. (1/2984)

A novel nucleotide incorporation activity implicated in the editing of mitochondrial transfer RNAs in Acanthamoeba castellanii. (2/2984)

Base excision repair of oxidative DNA damage activated by XPG protein. (3/2984)

Conserved residues of human XPG protein important for nuclease activity and function in nucleotide excision repair. (4/2984)

A restriction endonuclease from Staphylococcus aureus. (5/2984)

Chromatin structure: a property of the higher structures of chromatin and in the time course of its formation during chromatin replication. (6/2984)

'Saccharomyces cerevisiae MSH2/6 complex interacts with Holliday junctions and facilitates their cleavage by phage resolution enzymes. (7/2984)

Defective repair of cisplatin-induced DNA damage caused by reduced XPA protein in testicular germ cell tumours. (8/2984)

Endonucleases

Deoxyribonucleases, Type II Site-Specific

DNA Restriction Enzymes

Endodeoxyribonucleases

Deoxyribonuclease IV (Phage T4-Induced)

DNA Cleavage

Base Sequence

DNA

DNA-(Apurinic or Apyrimidinic Site) Lyase

Substrate Specificity

DNA, Viral

Deoxyribonuclease EcoRI

Deoxyribonuclease BamHI

Deoxyribonucleases

DNA, Bacterial

Deoxyribonucleases, Type I Site-Specific

Molecular Sequence Data

Electrophoresis, Agar Gel

Flap Endonucleases

Polymorphism, Restriction Fragment Length

Plasmids

Nucleic Acid Hybridization

Deoxyribonuclease HpaII

Escherichia coli

Protein Splicing

Restriction Mapping

Holliday Junction Resolvases

DNA, Circular

Naegleria

Bacteriophages

DNA Repair

DNA Breaks, Single-Stranded

Nucleic Acid Conformation

Amino Acid Sequence

Apurinic Acid

Protein Engineering

Cloning, Molecular

RNA Cleavage

Introns

Deoxyribonuclease HindIII

Endoribonucleases

Binding Sites

Genes, Viral

DNA Restriction-Modification Enzymes

DNA, Recombinant

Sequence Alignment

Carbon-Oxygen Lyases

Catalytic Domain

DNA, Superhelical

Chromosome Mapping

Deoxyribonucleases, Type III Site-Specific

Exonucleases

CRISPR-Associated Proteins

Models, Molecular

Molecular Weight

Deoxyribonuclease (Pyrimidine Dimer)

DNA Modification Methylases

Electrophoresis, Gel, Pulsed-Field

Coliphages

Exodeoxyribonucleases

Recombination, Genetic

Microbiological Phenomena

T-Phages

Bacteriophage lambda

Genes

Site-Specific DNA-Methyltransferase (Adenine-Specific)

Inteins

Mutation

Kinetics

Polymerase Chain Reaction

DNA, Cruciform

Micrococcus

Species Specificity

Deoxyribonuclease I

Methylation

Bacteriophage T4

Single-Strand Specific DNA and RNA Endonucleases

Cytosine

Chromosomes, Bacterial

Oligodeoxyribonucleotides