Cysteine. Medical search

A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.

ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.

A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.

An enzyme that catalyzes the conversion of L-CYSTEINE to 3-sulfinoalanine (3-sulfino-L-alanine) in the CYSTEINE metabolism and TAURINE and hypotaurine metabolic pathways.

Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.

An enzyme that catalyzes the biosynthesis of cysteine in microorganisms and plants from O-acetyl-L-serine and hydrogen sulfide. This enzyme was formerly listed as EC 4.2.99.8.

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.

Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.

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.

Compounds containing the -SH radical.

A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.

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

A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.

A homologous group of endogenous CYSTEINE PROTEINASE INHIBITORS. The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN, and other peptidases which have a sulfhydryl group at the active site.

A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).

A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.

A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.

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

A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.

Chemical agents that react with SH groups. This is a chemically diverse group that is used for a variety of purposes. Among these are enzyme inhibition, enzyme reactivation or protection, and labelling.

A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.

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

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

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

Proteins prepared by recombinant DNA technology.

The rate dynamics in chemical or physical systems.

Enzymes that catalyze the cleavage of a carbon-sulfur bond by means other than hydrolysis or oxidation. EC 4.4.

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).

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.

A sulfhydryl reagent that is widely used in experimental biochemical studies.

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.

An enzyme that catalyzes the conversion of L-SERINE to COENZYME A and O-acetyl-L-serine, using ACETYL-COA as a donor.

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.

An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.

A reagent commonly used in biochemical studies as a protective agent to prevent the oxidation of SH (thiol) groups and for reducing disulphides to dithiols.

Organic salts or esters of methanesulfonic acid.

A standard reagent for the determination of reactive sulfhydryl groups by absorbance measurements. It is used primarily for the determination of sulfhydryl and disulfide groups in proteins. The color produced is due to the formation of a thio anion, 3-carboxyl-4-nitrothiophenolate.

The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.

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.

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.

An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate.

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.

Materials that add an electron to an element or compound, that is, decrease the positiveness of its valence. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)

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.

Any of the monobasic inorganic or organic acids of sulfur with the general formula RSO(OH). (From McGraw Hill Dictionary of Scientific and Technical Terms, 4th ed)

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

A sulfur-containing essential L-amino acid that is important in many body functions.

A derivative of ACETIC ACID that contains one IODINE atom attached to its methyl group.

Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.

A multifunctional pyridoxal phosphate enzyme. In the final step in the biosynthesis of cysteine it catalyzes the cleavage of cystathionine to yield cysteine, ammonia, and 2-ketobutyrate. EC 4.4.1.1.

A class of enzymes that catalyze the cleavage of C-C, C-O, and C-N, and other bonds by other means than by hydrolysis or oxidation. (Enzyme Nomenclature, 1992) EC 4.

The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.

The covalent bonding of an alkyl group to an organic compound. It can occur by a simple addition reaction or by substitution of another functional group.

Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.

Oxy acids of sulfur with the general formula RSOH, where R is an alkyl or aryl group such as CH3. They are often encountered as esters and halides. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

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

Proteins found in any species of bacterium.

The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.

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

Established cell cultures that have the potential to propagate indefinitely.

A cytotoxic sulfhydryl reagent that inhibits several subcellular metabolic systems and is used as a tool in cellular physiology.

The N-acetyl derivative of CYSTEINE. It is used as a mucolytic agent to reduce the viscosity of mucous secretions. It has also been shown to have antiviral effects in patients with HIV due to inhibition of viral stimulation by reactive oxygen intermediates.

Non-collagenous, calcium-binding glycoprotein of developing bone. It links collagen to mineral in the bone matrix. In the synonym SPARC glycoprotein, the acronym stands for Secreted Protein, Acidic and Rich in Cysteine.

Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.

Covalent attachment of LIPIDS and FATTY ACIDS to other compounds and PROTEINS.

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.

One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of gamma-glutamylcysteine from glutamate and cysteine in the presence of ATP with the formation of ADP and orthophosphate. EC 6.3.2.2.

Oxidoreductases with specificity for oxidation or reduction of SULFUR COMPOUNDS.

Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).

An antineoplastic agent with alkylating properties. It also acts as a mutagen by damaging DNA and is used experimentally for that effect.

Iodinated derivatives of acetic acid. Iodoacetates are commonly used as alkylating sulfhydryl reagents and enzyme inhibitors in biochemical research.

A conditionally essential nutrient, important during mammalian development. It is present in milk but is isolated mostly from ox bile and strongly conjugates bile acids.

An intracellular cystatin subtype that is found in a broad variety of cell types. It is a cytosolic enzyme inhibitor that protects the cell against the proteolytic action of lysosomal enzymes such as CATHEPSINS.

Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.

Peptides composed of two amino acid units.

An essential amino acid that is required for the production of HISTAMINE.

An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.

Chemical groups containing the covalent sulfur bonds -S-. The sulfur atom can be bound to inorganic or organic moieties.

A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.

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

A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.

A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.

Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.

A family of ubiquitously-expressed peroxidases that play a role in the reduction of a broad spectrum of PEROXIDES like HYDROGEN PEROXIDE; LIPID PEROXIDES and peroxinitrite. They are found in a wide range of organisms, such as BACTERIA; PLANTS; and MAMMALS. The enzyme requires the presence of a thiol-containing intermediate such as THIOREDOXIN as a reducing cofactor.

Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.

Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.

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

A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.

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

Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.

A cytastin subtype found at high levels in the SKIN and in BLOOD CELLS. Cystatin A incorporates into the cornified cell envelope of stratified squamous epithelial cells and may play a role in bacteriostatic properties of skin.

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 serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.

Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.

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

Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.

The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)

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

Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.

Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including NEUROPEPTIDES; CYTOSKELETAL PROTEINS; proteins from SMOOTH MUSCLE; CARDIAC MUSCLE; liver; platelets; and erythrocytes. Two subclasses having high and low calcium sensitivity are known. Removes Z-discs and M-lines from myofibrils. Activates phosphorylase kinase and cyclic nucleotide-independent protein kinase. This enzyme was formerly listed as EC 3.4.22.4.

Substances used for the detection, identification, analysis, etc. of chemical, biological, or pathologic processes or conditions. Indicators are substances that change in physical appearance, e.g., color, at or approaching the endpoint of a chemical titration, e.g., on the passage between acidity and alkalinity. Reagents are substances used for the detection or determination of another substance by chemical or microscopical means, especially analysis. Types of reagents are precipitants, solvents, oxidizers, reducers, fluxes, and colorimetric reagents. (From Grant & Hackh's Chemical Dictionary, 5th ed, p301, p499)

A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.

The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.

A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.

A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.

Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.

A sulfhydryl proteinase with cysteine at the active site from ficus latex. Preferential cleavage is at tyrosine and phenylalanine residues. EC 3.4.22.3.

The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.

A common saturated fatty acid found in fats and waxes including olive oil, palm oil, and body lipids.

A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials.

Enzymes which transfer sulfur atoms to various acceptor molecules. EC 2.8.1.

A multifunctional pyridoxal phosphate enzyme. In the second stage of cysteine biosynthesis it catalyzes the reaction of homocysteine with serine to form cystathionine with the elimination of water. Deficiency of this enzyme leads to HYPERHOMOCYSTEINEMIA and HOMOCYSTINURIA. EC 4.2.1.22.

Inorganic salts of sulfuric acid.

Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.

A cyclized derivative of L-GLUTAMIC ACID. Elevated blood levels may be associated with problems of GLUTAMINE or GLUTATHIONE metabolism.

A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

A mercaptoethylamine compound that is endogenously derived from the COENZYME A degradative pathway. The fact that cysteamine is readily transported into LYSOSOMES where it reacts with CYSTINE to form cysteine-cysteamine disulfide and CYSTEINE has led to its use in CYSTINE DEPLETING AGENTS for the treatment of CYSTINOSIS.

Proteins obtained from ESCHERICHIA COLI.

A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.

An essential branched-chain amino acid important for hemoglobin formation.

A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.

A sulfur-containing alkyl thionitrite that is one of the NITRIC OXIDE DONORS.

The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.

Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.

A GLUTATHIONE dimer formed by a disulfide bond between the cysteine sulfhydryl side chains during the course of being oxidized.

Conversion into nitroso compounds. An example is the reaction of nitrites with amino compounds to form carcinogenic N-nitrosamines.

A mass spectrometric technique that is used for the analysis of large biomolecules. Analyte molecules are embedded in an excess matrix of small organic molecules that show a high resonant absorption at the laser wavelength used. The matrix absorbs the laser energy, thus inducing a soft disintegration of the sample-matrix mixture into free (gas phase) matrix and analyte molecules and molecular ions. In general, only molecular ions of the analyte molecules are produced, and almost no fragmentation occurs. This makes the method well suited for molecular weight determinations and mixture analysis.

A disturbance in the prooxidant-antioxidant balance in favor of the former, leading to potential damage. Indicators of oxidative stress include damaged DNA bases, protein oxidation products, and lipid peroxidation products (Sies, Oxidative Stress, 1991, pxv-xvi).

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.

Transport proteins that carry specific substances in the blood or across cell membranes.

Inorganic or organic compounds that contain sulfur as an integral part of the molecule.

The addition of an organic acid radical into a molecule.

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.

An element with atomic symbol Cd, atomic number 48, and atomic weight 114. It is a metal and ingestion will lead to CADMIUM POISONING.

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

Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.

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.

A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.

CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)

An antiviral mechanism of nitric oxide: inhibition of a viral protease. (1/10540)

Although nitric oxide (NO) kills or inhibits the replication of a variety of intracellular pathogens, the antimicrobial mechanisms of NO are unknown. Here, we identify a viral protease as a target of NO. The life cycle of many viruses depends upon viral proteases that cleave viral polyproteins into individual polypeptides. NO inactivates the Coxsackievirus protease 3C, an enzyme necessary for the replication of Coxsackievirus. NO S-nitrosylates the cysteine residue in the active site of protease 3C, inhibiting protease activity and interrupting the viral life cycle. Substituting a serine residue for the active site cysteine renders protease 3C resistant to NO inhibition. Since cysteine proteases are critical for virulence or replication of many viruses, bacteria, and parasites, S-nitrosylation of pathogen cysteine proteases may be a general mechanism of antimicrobial host defenses. (+info)

Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member. (2/10540)

Peroxiredoxin (PRx) exhibits thioredoxin-dependent peroxidase activity and constitutes a family of proteins. Four members of genes from rat tissues were isolated by PCR using degenerated primers based on the sequences which encode a pair of highly conserved Cys-containing domains, and were then cloned to full-length cDNAs. These included two genes which have previously been isolated in rats, PRx I and PRx II, and two rat homologues of PRx III and PRx IV. We showed, for the first time, the simultaneous expression of all four genes in various rat tissues by Northern blotting. Since a discrepancy exists regarding cellular distribution, we further characterized PRx IV by expressing it in COS-1 cells. This clearly demonstrates that PRx IV is a secretory form and functions within the extracellular space. (+info)

Kinetics of oxidation of aliphatic and aromatic thiols by myeloperoxidase compounds I and II. (3/10540)

Myeloperoxidase (MPO) is the most abundant protein in neutrophils and plays a central role in microbial killing and inflammatory tissue damage. Because most of the non-steroidal anti-inflammatory drugs and other drugs contain a thiol group, it is necessary to understand how these substrates are oxidized by MPO. We have performed transient kinetic measurements to study the oxidation of 14 aliphatic and aromatic mono- and dithiols by the MPO intermediates, Compound I (k3) and Compound II (k4), using sequential mixing stopped-flow techniques. The one-electron reduction of Compound I by aromatic thiols (e.g. methimidazole, 2-mercaptopurine and 6-mercaptopurine) varied by less than a factor of seven (between 1.39 +/- 0.12 x 10(5) M(-1) s(-1) and 9.16 +/- 1.63 x 10(5) M(-1) s(-1)), whereas reduction by aliphatic thiols was demonstrated to depend on their overall net charge and hydrophobic character and not on the percentage of thiol deprotonation or redox potential. Cysteamine, cysteine methyl ester, cysteine ethyl ester and alpha-lipoic acid showed k3 values comparable to aromatic thiols, whereas a free carboxy group (e.g. cysteine, N-acetylcysteine, glutathione) diminished k3 dramatically. The one-electron reduction of Compound II was far more constrained by the nature of the substrate. Reduction by methimidazole, 2-mercaptopurine and 6-mercaptopurine showed second-order rate constants (k4) of 1.33 +/- 0.08 x 10(5) M(-1) s(-1), 5.25 +/- 0.07 x 10(5) M(-1) s(-1) and 3.03 +/- 0.07 x 10(3) M(-1) s(-1). Even at high concentrations cysteine, penicillamine and glutathione could not reduce Compound II, whereas cysteamine (4.27 +/- 0.05 x 10(3) M(-1) s(-1)), cysteine methyl ester (8.14 +/- 0.08 x 10(3) M(-1) s(-1)), cysteine ethyl ester (3.76 +/- 0.17 x 10(3) M(-1) s(-1)) and alpha-lipoic acid (4.78 +/- 0.07 x 10(4) M(-1) s(-1)) were demonstrated to reduce Compound II and thus could be expected to be oxidized by MPO without co-substrates. (+info)

Internal electron transfer between hemes and Cu(II) bound at cysteine beta93 promotes methemoglobin reduction by carbon monoxide. (4/10540)

Previous studies showed that CO/H2O oxidation provides electrons to drive the reduction of oxidized hemoglobin (metHb). We report here that Cu(II) addition accelerates the rate of metHb beta chain reduction by CO by a factor of about 1000. A mechanism whereby electron transfer occurs via an internal pathway coupling CO/H2O oxidation to Fe(III) and Cu(II) reduction is suggested by the observation that the copper-induced rate enhancement is inhibited by blocking Cys-beta93 with N-ethylmaleimide. Furthermore, this internal electron-transfer pathway is more readily established at low Cu(II) concentrations in Hb Deer Lodge (beta2His --> Arg) and other species lacking His-beta2 than in Hb A0. This difference is consistent with preferential binding of Cu(II) in Hb A0 to a high affinity site involving His-beta2, which is ineffective in promoting electron exchange between Cu(II) and the beta heme iron. Effective electron transfer is thus affected by Hb type but is not governed by the R left arrow over right arrow T conformational equilibrium. The beta hemes in Cu(II)-metHb are reduced under CO at rates close to those observed for cytochrome c oxidase, where heme and copper are present together in the oxygen-binding site and where internal electron transfer also occurs. (+info)

Plasma total homocysteine and cysteine in relation to glomerular filtration rate in diabetes mellitus. (5/10540)

BACKGROUND: The plasma concentrations of total homocysteine (tHcy) and total cysteine (tCys) are determined by intracellular metabolism and by renal plasma clearance, and we hypothesized that glomerular filtration is a major determinant of plasma tHcy and tCys. We studied the relationships between the glomerular filtration rate (GFR) and plasma tHcy and tCys in populations of diabetic patients with particularly wide ranges of GFR. METHODS: We measured GFR, urine albumin excretion rate (UAER), plasma tHcy, tCys, methionine, vitamin B12, folate, C-peptide, and routine parameters in 50 insulin-dependent diabetes mellitus (IDDM) and 30 non-insulin-dependent diabetes mellitus (NIDDM) patients. All patients underwent intensive insulin treatment and had a serum creatinine concentration below 115 micromol/liter. RESULTS: Mean plasma tHcy in diabetic patients (0.1 micromol/liter) was lower than in normal persons (11.1 micromol/liter, P = 0.0014). Mean plasma tCys in diabetic patients (266.1 micromol/liter) was also lower than in normal persons (281.9 micromol/liter, P = 0.0005). Seventy-three percent of the diabetic patients had relative hyperfiltration. Plasma tHcy and tCys were closely and independently associated with GFR, serum folate, and serum B12. However, plasma tHcy was not independently associated with any of the 22 other variables tested, including age, serum creatinine concentration, UAER, total daily insulin dose, and glycemic control. CONCLUSIONS: Glomerular filtration rate is an independent determinant of plasma tHcy and tCys concentrations, and GFR is rate limiting for renal clearance of both homocysteine and cysteine in diabetic patients without overt nephropathy. Declining GFR explains the age-related increase in plasma tHcy, and hyperfiltration explains the lower than normal mean plasma tHcy and tCys concentrations in populations of diabetic patients. (+info)

Variants of ribonuclease inhibitor that resist oxidation. (6/10540)

Human ribonuclease inhibitor (hRI) is a cytosolic protein that protects cells from the adventitious invasion of pancreatic-type ribonucleases. hRI has 32 cysteine residues. The oxidation of these cysteine residues to form disulfide bonds is a rapid, cooperative process that inactivates hRI. The most proximal cysteine residues in native hRI are two pairs that are adjacent in sequence: Cys94 and Cys95, and Cys328 and Cys329. A cystine formed from such adjacent cysteine residues would likely contain a perturbing cis peptide bond within its eight-membered ring, which would disrupt the structure of hRI and could facilitate further oxidation. We find that replacing Cys328 and Cys329 with alanine residues has little effect on the affinity of hRI for bovine pancreatic ribonuclease A (RNase A), but increases its resistance to oxidation by 10- to 15-fold. Similar effects are observed for the single variants, C328A hRI and C329A hRI, suggesting that oxidation resistance arises from the inability to form a Cys328-Cys329 disulfide bond. Replacing Cys94 and Cys95 with alanine residues increases oxidation resistance to a lesser extent, and decreases the affinity of hRI for RNase A. The C328A, C329A, and C328A/C329A variants are likely to be more useful than wild-type hRI for inhibiting pancreatic-type ribonucleases in vitro and in vivo. We conclude that replacing adjacent cysteine residues can confer oxidation resistance in a protein. (+info)

Metal-catalyzed oxidation of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: inactivation and destabilization by oxidation of active-site cysteines. (7/10540)

The in vitro instability of the phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase [DAHPS(Phe)] from Escherichia coli has been found to be due to a metal-catalyzed oxidation mechanism. DAHPS(Phe) is one of three differentially feedback-regulated isoforms of the enzyme which catalyzes the first step of aromatic biosynthesis, the formation of DAHP from phosphoenolpyruvate and D-erythrose-4-phosphate. The activity of the apoenzyme decayed exponentially, with a half-life of about 1 day at room temperature, and the heterotetramer slowly dissociated to the monomeric state. The enzyme was stabilized by the presence of phosphoenolpyruvate or EDTA, indicating that in the absence of substrate, a trace metal(s) was the inactivating agent. Cu2+ and Fe2+, but none of the other divalent metals that activate the enzyme, greatly accelerated the rate of inactivation and subunit dissociation. Both anaerobiosis and the addition of catalase significantly reduced Cu2+-catalyzed inactivation. In the spontaneously inactivated enzyme, there was a net loss of two of the seven thiols per subunit; this value increased with increasing concentrations of added Cu2+. Dithiothreitol completely restored the enzymatic activity and the two lost thiols in the spontaneously inactivated enzyme but was only partially effective in reactivation of the Cu2+-inactivated enzyme. Mutant enzymes with conservative replacements at either of the two active-site cysteines, Cys61 or Cys328, were insensitive to the metal attack. Peptide mapping of the Cu2+-inactivated enzyme revealed a disulfide linkage between these two cysteine residues. All results indicate that DAHPS(Phe) is a metal-catalyzed oxidation system wherein bound substrate protects active-site residues from oxidative attack catalyzed by bound redox metal cofactor. A mechanism of inactivation of DAHPS is proposed that features a metal redox cycle that requires the sequential oxidation of its two active-site cysteines. (+info)

Functional importance and local environments of the cysteines in the tetracycline resistance protein encoded by plasmid pBR322. (8/10540)

The properties of the cysteines in the pBR322-encoded tetracycline resistance protein have been examined. Cysteines are important but not essential for tetracycline transport activity. None of the cysteines reacted with biotin maleimide, suggesting that they are shielded from the aqueous phase or reside in a negatively charged local environment. (+info)

The enzyme cysteine synthase, using sulfide sources, converts this ester into cysteine, releasing acetate. The cysteine ... l-Cysteine is also used as a processing aid for baking. In the field of personal care, cysteine is used for permanent-wave ... N-Acetyl-l-cysteine is a derivative of cysteine wherein an acetyl group is attached to the nitrogen atom. This compound is sold ... Again, the cysteine is used for breaking up the disulfide bonds in the hair's keratin. Cysteine is a very popular target for ...

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

L-Cysteine is the product of several processes as well. In addition to the reactions below, L-cysteine is also a product of ... Cysteine metabolism refers to the biological pathways that consume or create cysteine. The pathways of different amino acids ... L-cysteine is consumed in several ways as shown below. L-Cysteine is also consumed in methionine and glutathione metabolism as ... D-cysteine desulfhydrase Sulfur metabolism (Articles lacking sources from December 2009, All articles lacking sources, Sulfur ...

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

In enzymology, a cysteine synthase (EC 2.5.1.47) is an enzyme that catalyzes the chemical reaction O3-acetyl-L-serine + ... Ikegami F, Kaneko M, Lambein F, Kuo Y-H, Murakoshi I (1987). "Difference between uracilylalanine synthases and cysteine ... This enzyme participates in 3 metabolic pathways: cysteine metabolism, selenoamino acid metabolism, and sulfur metabolism. It ... cysteine synthetase, S-sulfocysteine synthase, 3-O-acetyl-L-serine:hydrogen-sulfide, and 2-amino-2-carboxyethyltransferase. ...

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

In enzymology, a cysteine transaminase (EC 2.6.1.3) is an enzyme that catalyzes the chemical reaction L-cysteine + 2- ... Other names in common use include cysteine aminotransferase, L-cysteine aminotransferase, and CGT. This enzyme participates in ... The systematic name of this enzyme class is L-cysteine:2-oxoglutarate aminotransferase. ... the two substrates of this enzyme are L-cysteine and 2-oxoglutarate, whereas its two products are mercaptopyruvate and L- ...

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

The enzyme cysteine lyase (EC 4.4.1.10) catalyzes the chemical reaction L-cysteine + sulfite ⇌ {\displaystyle \ ... and L-cysteine hydrogen-sulfide-lyase (adding sulfite). This enzyme participates in cysteine and taurine metabolism. It employs ... Genes encoding cysteine lyase (CL) originated around 300 million years ago by a tandem gene duplication and ... The systematic name of this enzyme class is L-cysteine hydrogen-sulfide-lyase (adding sulfite; L-cysteate-forming). Other names ...

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

... (CDO) is a non-heme iron enzyme that catalyzes the conversion of L-cysteine to cysteine sulfinic acid ( ... cysteine sulfinate). CDO plays an important role in cysteine catabolism, regulating intracellular levels of cysteine and ... CDO is responsible for the first major step in metabolism of cysteine. CDO oxidizes to cysteine sulfinic acid (which exists ... Stipanuk MH, Dominy JE, Lee JI, Coloso RM (June 2006). "Mammalian cysteine metabolism: new insights into regulation of cysteine ...

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

In fact, the latex of dozens of different plant families are known to contain cysteine proteases. Cysteine proteases are used ... The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases Cysteine+endopeptidases at the US National ... Plant cysteine proteases isolated from these plants have been found to have high proteolytic activities that are known to ... Cysteine proteases are used as feed additives for livestock to improve the digestibility of proteins and amino acids. Protease ...

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

In enzymology, a cysteine desulfurase (EC 2.8.1.7) is an enzyme that catalyzes the chemical reaction L-cysteine + [enzyme]- ... The systematic name of this enzyme class is L-cysteine:[enzyme cysteine] sulfurtransferase. Other names in common use include ... the two substrates of this enzyme are L-cysteine and [enzyme]-cysteine], whereas its two products are L-alanine and [enzyme]-S- ... Zheng L, White RH, Cash VL, Jack RF, Dean DR (1993). "Cysteine desulfurase activity indicates a role for NIFS in metallocluster ...

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

This box: view edit Except where noted otherwise, data relate to Standard temperature and pressure. Reliability of data general note. ^a 52-90-4 (Chemical data pages, Chemical data pages cleanup ...

https://en.wikipedia.org/wiki/Cysteine_(data_page)

... s (also cysteine-rich peptide, CRP, disulphide-rich peptide) are small proteins that contain a large ... CRPs that form these typically have an even number of cysteines. Cysteines can coordinate one or more metal ions by forming a ... These cysteines either cross-link to form disulphide bonds, or bind metal ions by chelation, stabilising the protein's tertiary ... CRPs include a highly conserved secretion peptide signal at the N-terminus and a cysteine-rich region at the C-terminus. In an ...

https://en.wikipedia.org/wiki/Cysteine-rich_protein

L-cysteine ⇌ {\displaystyle \rightleftharpoons } NMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine The nucleoside ... Phosphopantothenate-cysteine ligase from the bacterium Escherichia coli uses cytidine triphosphate (CTP) as an energy donor, ... PDBe-KB provides an overview of all the structure information available in the PDB for Human Phosphopantothenate-cysteine ... In enzymology, a phosphopantothenate-cysteine ligase also known as phosphopantothenoylcysteine synthetase (PPCS) is an enzyme ( ...

https://en.wikipedia.org/wiki/Phosphopantothenate—cysteine_ligase

... is derived from cysteine. Cysteine is formed from cystathionine via the cystathionine gamma-lyase enzyme ... It is distinct from cysteine sulfinic acid, H(O)SCH2CH(NH2)CO2H. Peptides containing the cysteine sulfinic acid residue are ... by cysteine lyase or cystathionine gamma-lyase or enters the cysteine sulfinic acid pathway where it is oxidized by cysteine ... Cysteine sulfinic acid is the organic compound with the nominal formula HO2SCH2CH(NH2)CO2H . It is a rare example of an amino ...

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

L-cysteine + ATP ⇌ {\displaystyle \rightleftharpoons } γ-glutamyl cysteine + ADP + Pi GSH, and by extension GCL, is critical to ... Glutamate-cysteine ligase (GCL) EC 6.3.2.2), previously known as γ-glutamylcysteine synthetase (GCS), is the first enzyme of ... The plant glutamate cysteine ligase is a redox-sensitive homodimeric enzyme, conserved in the plant kingdom. In an oxidizing ... Animal glutamate cysteine ligase (GCL) is a heterodimeric enzyme composed of two protein subunits that are coded by independent ...

https://en.wikipedia.org/wiki/Glutamate–cysteine_ligase

In enzymology, a cysteine-tRNA ligase (EC 6.1.1.16) is an enzyme that catalyzes the chemical reaction ATP + L-cysteine + ... and cysteine translase. This enzyme participates in cysteine metabolism and aminoacyl-trna biosynthesis. As of late 2007, 3 ... The systematic name of this enzyme class is L-cysteine:tRNACys ligase (AMP-forming). Other names in common use include ... L-cysteine, and tRNA(Cys), whereas its 3 products are AMP, diphosphate, and L-cysteinyl-tRNA(Cys). This enzyme belongs to the ...

https://en.wikipedia.org/wiki/Cysteine—tRNA_ligase

A white solid, it is the methyl ester of the amino acid cysteine. Under the brand name Mecysteine, cysteine methyl ester is a ... Cysteine methyl ester is also used as a building block for synthesis of N,S-heterocycles. Page CP (2018). "Respiratory System: ... Cysteine methyl ester is the organic compound with the formula HSCH2CH(NH2)CO2CH3. ...

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

Other names in common use include cysteine conjugate aminotransferase, and cysteine-conjugate alpha-ketoglutarate transaminase ... In enzymology, a cysteine-conjugate transaminase (EC 2.6.1.75) is an enzyme that catalyzes the chemical reaction S-(4- ... The systematic name of this enzyme class is S-(4-bromophenyl)-L-cysteine:2-oxoglutarate aminotransferase. ... L-cysteine and 2-oxoglutarate, whereas its two products are S-(4-bromophenyl)mercaptopyruvate and L-glutamate. This enzyme ...

https://en.wikipedia.org/wiki/Cysteine-conjugate_transaminase

The enzyme D-cysteine desulfhydrase (EC 4.4.1.15) catalyzes the chemical reaction D-cysteine + H2O ⇌ {\displaystyle \ ... Schmidt A; Erdle I (1983). "A cysteine desulfhydrase specific for D-cysteine from the green-alga Chlorella fusca". Z. ... Schmidt A (1982). "A cysteine desulfhydrase from spinach leaves specific for D-cysteine". Z. Pflanzenphysiol. 107: 301-312. ... and D-cysteine sulfide-lyase (deaminating). This enzyme participates in cysteine metabolism. Nagasawa T, Ishii T, Kumagai H, ...

https://en.wikipedia.org/wiki/D-cysteine_desulfhydrase

"Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K+ channel ... Cysteine-rich secretory proteins, often abbreviated as CRISPs, are a group of glycoproteins. They are a subgroup of the CRISP, ... The primary structure is also rich in cysteine that form disulfide bonds, particularly in the hinge region and CRD. CRISPs are ... The larger domain is a CAP-like 'Pathogenesis-related 1' domain (PR-1), followed by the smaller ShK-like 'Cysteine-Rich Domain ...

https://en.wikipedia.org/wiki/Cysteine-rich_secretory_protein

... is a protein that in humans is encoded by the CRIP3 gene. GRCh38: Ensembl release 89: ENSG00000146215 ... "Entrez Gene: Cysteine rich protein 3". Retrieved 2018-01-02. v t e (Genes on human chromosome 6, All stub articles, Human ...

https://en.wikipedia.org/wiki/Cysteine_rich_protein_3

Dominy JE, Hwang J, Stipanuk MH (2007). "Overexpression of cysteine dioxygenase reduces intracellular cysteine and glutathione ... Cysteine dioxygenase type 1 is a protein that in humans is encoded by the CDO1 gene. GRCh38: Ensembl release 89: ... PDBe-KB provides an overview of all the structure information available in the PDB for Human Cysteine dioxygenase type 1 PDBe- ... KB provides an overview of all the structure information available in the PDB for Mouse Cysteine dioxygenase type 1 v t e ( ...

https://en.wikipedia.org/wiki/Cysteine_dioxygenase_type_1

... , also known as thialysine, is a toxic analog of the amino acid lysine in which the second carbon of the ...

https://en.wikipedia.org/wiki/S-Aminoethyl-L-cysteine

... may refer to: Protein geranylgeranyltransferase type I Protein ...

https://en.wikipedia.org/wiki/Geranylgeranyl-diphosphate:protein-cysteine_geranyltransferase

The enzyme cysteine-S-conjugate β-lyase (EC 4.4.1.13) catalyzes the chemical reaction an L-cysteine-S-conjugate + H2O = a thiol ... glutamine transaminase K/cysteine conjugate β-lyase, and L-cysteine-S-conjugate thiol-lyase (deaminating). It employs one ... Tateishi M, Suzuki S, Shimizu H (1978). "Cysteine conjugate β-lyase in rat liver. A novel enzyme catalyzing formation of thiol- ... The systematic name of this enzyme class is L-cysteine-S-conjugate thiol-lyase (deaminating; pyruvate-forming). Other names in ...

https://en.wikipedia.org/wiki/Cysteine-S-conjugate_beta-lyase

... an S-substituted N-acetyl-L-cysteine Thus, the two substrates of this enzyme are acetyl-CoA and S-substituted L-cysteine, ... In enzymology, a cysteine-S-conjugate N-acetyltransferase (EC 2.3.1.80) is an enzyme that catalyzes the chemical reaction ... The systematic name of this enzyme class is acetyl-CoA:S-substituted L-cysteine N-acetyltransferase. This enzyme participates ... Duffel MW, Jakoby WB (1982). "Cysteine S-conjugate N-acetyltransferase from rat kidney microsomes". Mol. Pharmacol. 21 (2): 444 ...

https://en.wikipedia.org/wiki/Cysteine-S-conjugate_N-acetyltransferase

The CAP superfamily (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins (CAP)) is a large ... Many of these proteins contain a C-terminal Cysteine-rich secretory protein (Crisp) domain. This domain is found in the ... It contains 10 conserved cysteines which are all involved in disulphide bonds and is structurally related to the ion channel ... Gibbs GM, Scanlon MJ, Swarbrick J, Curtis S, Gallant E, Dulhunty AF, O'Bryan MK (February 2006). "The cysteine-rich secretory ...

https://en.wikipedia.org/wiki/Cysteine-rich_secretory_protein_superfamily

It has a relatively unusual γ-bond between the constituent amino acids, L-glutamic acid and L-cysteine and is a key ... Mice that have had the glutamate-cysteine ligase (GCL) gene knocked out do not develop beyond the embryo stage and die before ... GGC is synthesized from L-glutamic acid and L-cysteine in the cytoplasm of virtually all cells in an adenosine triphosphate ( ... γ -L-Glutamyl-L-cysteine, also known as γ-glutamylcysteine (GGC), is a dipeptide found in animals, plants, fungi, some bacteria ...

https://en.wikipedia.org/wiki/Gamma-L-Glutamyl-L-cysteine

In molecular biology, the protein domain SRCR is short for Scavenger receptor cysteine-rich domain. They are found solely in ... Hohenester E; Sasaki T; Timpl R (1999). "Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ... 2011). "A novel scavenger receptor-cysteine-rich (SRCR) domain containing scavenger receptor identified from mollusk mediated ...

https://en.wikipedia.org/wiki/Scavenger_receptor_cysteine-rich_protein_domain

... may refer to: S-alkylcysteine lyase, an enzyme Alliinase, an enzyme This disambiguation page ... lists articles associated with the title S-alkyl-L-cysteine sulfoxide lyase. If an internal link led you here, you may wish to ...

https://en.wikipedia.org/wiki/S-alkyl-L-cysteine_sulfoxide_lyase

... protein S-methyl-L-cysteine Thus, the two substrates of this enzyme are DNA containing 6-O-methylguanine and protein L-cysteine ... whereas its two products are DNA and protein S-methyl-L-cysteine. The S-methyl-L-cysteine residue irreversibly inactivates the ... The systematic name of this enzyme class is DNA-6-O-methylguanine:[protein]-L-cysteine S-methyltransferase. As of late 2007, 11 ... In enzymology, a methylated-DNA-[protein]-cysteine S-methyltransferase (EC 2.1.1.63) is an enzyme that catalyzes the chemical ...

https://en.wikipedia.org/wiki/Methylated-DNA—(protein)-cysteine_S-methyltransferase

... is a protein that in humans is encoded by the CRISPLD1 gene. GRCh38: ... "Entrez Gene: Cysteine rich secretory protein LCCL domain containing 1". Retrieved 2017-01-26. v t e (Articles with short ...

https://en.wikipedia.org/wiki/Cysteine_rich_secretory_protein_lccl_domain_containing_1

L-cysteine (2CYEMA) and N-acetyl-S-(1-cyano-2-hydroxyethyl)-L-cysteine (1CYHEMA) in participants from the 2011-2016 National ... Characterization of acrylonitrile exposure in the United States based on urinary n-acetyl-S-(2-cyanoethyl)-L-cysteine (2CYEMA ... Characterization of acrylonitrile exposure in the United States based on urinary n-acetyl-S-(2-cyanoethyl)-L-cysteine (2CYEMA ...

https://pubmed.ncbi.nlm.nih.gov/33424026/

... is a specially modified form of the dietary amino acid cysteine. When taken orally, NAC is thought to ... What Is the Scientific Evidence for N-Acetyl Cysteine (NAC)?. Safety Issues. Interactions You Should Know About. References. ... This N-Acetyl Cysteine (NAC) page on EmpowHER Womens Health works best with javascript enabled in your browser.. Toggle ... N-Acetyl Cysteine (NAC). Principal Proposed Uses. • Angina Pectoris. (in Combination With Conventional Treatment) , Chronic ...

https://www.empowher.com/media/reference/n-acetyl-cysteine-nac

... comes from the amino acid L-cysteine. It has many uses, and is available as both a prescription drug and a dietary supplement. ... Cysteine, Cystéine, Cysteine Hydrochloride, Cystine, Hydrochlorure de Cystéine, L-Cysteine, L-Cystéine, L-Cysteine HCl, L- ... Allergy: Dont use N-acetyl cysteine if you are allergic to acetyl cysteine.. Asthma: N-acetyl cysteine might cause ... Taking N-acetyl cysteine by mouth seems to reduce flu symptoms.. *Kidney failure. Taking N-acetyl cysteine by mouth seems to ...

https://medlineplus.gov/druginfo/natural/1018.html

Cysteine and methionine are sulfur-containing amino acids. Cysteine is synthesized from serine through different pathways in ... is converted to cysteine [MD:M00338]. Cysteine is metabolized to pyruvate in multiple routes. Methionine is an essential amino ... Cysteine and methionine metabolism [ Pathway menu , Organism menu , Pathway entry , Show description , Download , Help ] ... In bacteria and plants, cysteine is converted from serine (via acetylserine) by transfer of hydrogen sulfide [MD:M00021]. In ...

https://www.genome.jp/pathway/rn00270+RC02863

CSRNP_N; Cysteine/serine-rich nuclear protein N-terminus. * XM_024449214.2 → XP_024304982.1 cysteine/serine-rich nuclear ... CSRNP_N; Cysteine/serine-rich nuclear protein N-terminus. * XM_047429621.1 → XP_047285577.1 cysteine/serine-rich nuclear ... CSRNP_N; Cysteine/serine-rich nuclear protein N-terminus. * XM_024449213.2 → XP_024304981.1 cysteine/serine-rich nuclear ... CSRNP_N; Cysteine/serine-rich nuclear protein N-terminus. * XM_047429619.1 → XP_047285575.1 cysteine/serine-rich nuclear ...

https://www.ncbi.nlm.nih.gov/gene/81566

SspA complex proteinCYSTEINEPYRIDOXAL-5-PHOSPHATE

https://www.ncbi.nlm.nih.gov/structure/?term=txid47951[Organism:noexp]

... mBio. 2022 Jun 28;13( ... This work identifies the cysteine desulfurase IscS as the critical target of 2AA in Pseudomonas aeruginosa. A single ... encoding cysteine desulfurase). Damage to IscS was identified as a significant cause of growth defects of P. aeruginosa during ...

https://pubmed.ncbi.nlm.nih.gov/35652590/

FOLITE- folic acid, magnesium citrate, calcium citrate, vitamin d3, n-acetyl-l-cysteine tablet. Number of versions: 3. ... FOLITE- folic acid, magnesium citrate, calcium citrate, vitamin d3, n-acetyl-l-cysteine tablet. If this SPL contains ... Label: FOLITE- folic acid, magnesium citrate, calcium citrate, vitamin d3, n-acetyl-l-cysteine tablet. ... FOLITE- folic acid, magnesium citrate, calcium citrate, vitamin d3, n-acetyl-l-cysteine tablet. ...

https://dailymed.nlm.nih.gov/dailymed/drugInfo.cfm?setid=c6589bc2-9237-414d-89dd-619725f41eab

L-cysteine , C5H11NO3S2 , CID 170018 - structure, chemical names, physical and chemical properties, classification, patents, ...

https://pubchem.ncbi.nlm.nih.gov/compound/170018

ALPHA.-KETOGLUTARIC ACID OR COPPER OR CYSTEINE OR DIETHYL OXALAC... (7426) .ALPHA.-KETOGLUTARIC ACID OR COPPER OR CYSTEINE OR ... Did you mean: .alpha. ketoglutaric acid OR copper OR cysteine OR diethyl oxaloacetate OR fumaric acid OR germanium sesquioxide ... Did you mean: .alpha. ketoglutaric acid OR copper OR cysteine OR diethyl oxaloacetate OR fumaric acid OR germanium sesquioxide ... "cysteine"[MeSH Terms] OR "cysteine"[All Fields]) OR (DIETHYL[All Fields] AND OXALACETATE[All Fields]) OR ("fumaric acid"[All ...

https://ncbi.nlm.nih.gov/books/NBK501922/?term=.ALPHA.-KETOGLUTARIC+ACID+OR+COPPER+OR+CYSTEINE+OR+DIETHYL+OXALACETATE+OR+FUMARIC+ACID+OR+GERMANIUM+SESQUIOXIDE+OR+90045-36-6+OR+MANGANESE+CATION+(2+)+OR+SUS+SCROFA+PANCREAS+OR+SUS+SCROFA+SPLEEN+OR+SUS+SCROFA+STOMACH+OR+ZINC

This material is based upon work supported by the National Science Foundation under grant DEB#1545288, 10/1/2015-9/30/19 and DEB#1929393, 09/01/2019-08/31/2024. Any opinions, findings, conclusions, or recommendations expressed in the material are those of the author(s) and do not necessarily reflect the views of the National Science Foundation.. ...

https://lternet.edu/biblio/proteolytic-enzymes-serine-and-cysteine-peptidases/

... ... Project Title: Glycine and N-Acetyl Cysteine Supplemented Diet Improves Inflammatory-Based Fibrosis in the Aging Heart. ... N-Acetyl-Cysteine) with or without DCSL1 (Dendritic Cell-Specific Intercellular Adhesion Molecule 3-Grabbing Non-integrin ... glycine and N-acetyl cysteine = glutathione precursors) or by reducing macrophage polarization (via DCSL1). However, we only ...

https://ods.od.nih.gov/Funding/abstract.aspx?g=3R01AG059599-03S1&print=1

Fabrication of a cysteine monolayer is also practical; the sulfur headgroup on cysteine allows for a one-step synthesis onto a ... Cysteine is also inherently biocompatible because it is an amino acid that exists in, and is produced by, our body. ... Cysteine is selected as the coating material because it is a small biomolecule, highly zwitterionic at physiological pH, ... By optimizing the fabrication process, a monolayer cysteine coating of 8.64Å in thickness is achieved. X-ray photoelectron ...

https://uwspace.uwaterloo.ca/handle/10012/11762

Results 1 - 10 of 216 for ALANINE OR ARGININE OR ASPARTIC ACID OR CYSTEINE OR GLUTAMIC ACID OR GLYCINE OR HISTIDINE OR ... Did you mean ALANINE OR ARGININE OR ASPARTIC ACID OR CYSTEINE OR glutamine ACID OR GLYCINE OR HISTIDINE OR ISOLEUCINE OR ...

http://vsearch.nlm.nih.gov/vivisimo/cgi-bin/query-meta?v:project=medlineplus&query=ALANINE+OR+ARGININE+OR+ASPARTIC+ACID+OR+CYSTEINE+OR+GLUTAMIC+ACID+OR+GLYCINE+OR+HISTIDINE+OR+ISOLEUCINE+OR+LEUCINE+OR+LYSINE+OR+METHIONINE+OR+PHENYLALANINE+OR+PROLINE+OR+SERINE+OR+TAURINE+OR+THREONINE+OR+TRYPTOPHAN+OR+TYROSINE+OR+VALINE

N-Acetyl Cysteine has several properties that make it a must have in your arsenal for battling the flu. ... A form of the amino acid cysteine and a component of protein, NAC is a precursor to glutathione, the bodys principal ... However, an increasing number of people are learning that supplementing with N-Acetyl Cysteine (NAC) is a simple and effective ... In addition to the research clearly demonstrating this supplements ability to battle the flu, N-Acetyl Cysteine has several ...

https://www.liversupport.com/n-acetyl-cysteine-reduces-flu-symptoms/

Cortexi is a company that specializes in developing high-quality supplements that are designed to support overall health and well-being. One of their most popular ...

https://24x7nutra.com/tag/n-acetyl-cysteine/

Hi! Can I get a quote for a GreenScreen Assessment of N-Acetyl-S-(3-amino-3-oxopropyl)cysteine [81690-92-8]?. ... Is anyone else interested in sharing the cost of a GreenScreen assessment of N-Acetyl-S-(3-amino-3-oxopropyl)cysteine [81690-92 ... Profile for "N-Acetyl-S-(3-amino-3-oxopropyl)cysteine" on Pharos: https://pharosproject.net/chemicals/2205041 ...

https://pharosproject.net/chemicals/2205041

You can also browse global suppliers,vendor,prices,Price,manufacturers of L-Cysteine monohydrochloride(52-89-1). At last,L- ... Cysteine monohydrochloride(52-89-1) safety, risk, hazard and MSDS, CAS,cas number,Use,cas no may also be you need. ... Visit ChemicalBook To find more L-Cysteine monohydrochloride(52-89-1) information like chemical properties,Structure,melting ... L-Cysteine monohydrochloride. Synonyms. L-CYSTEINE HCL;L-CYSTEINE HYDROCHLORIDE;CYSTEINE HYDROCHLORIDE;CYSTEINE HCL;L-cysteine ...

https://www.chemicalbook.com/ChemicalProductProperty_EN_CB6694980.htm

ATP + H2O + cysteine-[cysteine-binding protein][side 1] = ADP + phosphate + cysteine[side 2] + [cysteine-binding protein][side ... Ligand cysteine-[cysteine-binding protein][side 1]. Please wait a moment until all data is loaded. This message will disappear ... Links to other databases for cysteine-[cysteine-binding protein][side 1]. top print hide ... view of cysteine-[cysteine-binding protein][side 1] (241360 - ) ...

https://www.brenda-enzymes.org/ligand.php?brenda_ligand_id=241360

Steverding, Dietmar, Caffrey, Conor R. and Lima, Ana-Paule (2011) Cysteine peptidases of kinetoplastid parasites. Advances in ...

https://ueaeprints.uea.ac.uk/id/eprint/35692/

In this investigation, we evaluated the biological effects of C. sinensis extract and cysteine on production of ... Subcultured callus of T. brevifoliatreated with cysteine (100 mg/L) showed lower activity of PPO, while those treated with ... Use of C. sinensis extract and cysteine failed to suppress the browning phenomenon, however tissues treated with ... Subcultured callus of T. brevifoliatreated with cysteine (100 mg/L) showed lower activity of PPO, while those treated with ...

https://academicjournals.org/journal/JMPR/article-stat/37259DD21747

Keratinocyte Basal Medium MCDB 153 w/o Methionine, Cysteine, Calcium Culture Media 10 L - 1 kit is backordered and will ship as ... Keratinocyte Basal Medium MCDB 153 w/o Methionine, Cysteine, Calcium Culture Media 10 L ... Keratinocyte Basal Medium MCDB 153 w/o Methionine, Cysteine, Calcium Culture Media 10 L. ... Keratinocyte Basal Medium MCDB 153 w/o Methionine, Cysteine, Calcium Culture Media 10 L. ...

https://dnamethsoc.com/products/keratinocyte-basal

... of total radioactivity is associated with S-carboxymethyl-L-cysteine, indicating that Br-AAF reacts primarily with a cysteine ... Affinity alkylation of hamster hepatic arylamine N-acetyltransferases: isolation of a modified cysteine residue.. H G Cheon, L ... Affinity alkylation of hamster hepatic arylamine N-acetyltransferases: isolation of a modified cysteine residue.. H G Cheon, L ... Affinity alkylation of hamster hepatic arylamine N-acetyltransferases: isolation of a modified cysteine residue.. H G Cheon, L ...

https://molpharm.aspetjournals.org/content/42/1/82

The cystatin D sequence contains all regions of relevance for cysteine proteinase inhibitory activity and also the 4 cysteine ... The cystatin D sequence contains all regions of relevance for cysteine proteinase inhibitory activity and also the 4 cysteine ... Structure and expression of the gene encoding cystatin D, a novel human cysteine proteinase inhibitor. *Mark ... a novel human cysteine proteinase inhibitor}}, url = {{http://www.jbc.org/cgi/reprint/266/30/20538}}, volume = {{266}}, year ...

https://lup.lub.lu.se/search/publication/1106111

Similar to other characterized CsPDV cysteine motifs, the VHv1.4 motifs are also characterized by six cysteines at conserved ... The VHv1.4 cDNA is 1338 bp long and has an ORF that encodes 322 amino acids with two complete and one partial cysteine motifs. ... a member of the cysteine-rich gene family. The VHv1.4 and the VHv1.1 proteins are 62% identical overall; at the N termini ... have been previously isolated and grouped into a cysteine-rich gene family. In this report, a CsPDV gene encoding an abundant ...

https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-77-4-797

ALLMAX NAC helps to increase the levels of Glutathione which is considered the most powerful antioxidant

https://allmaxnutrition.com/collections/vitamins-and-minerals/products/nac

Biochemical characterization of a thermostable cysteine synthase from Geobacillus stearothermophilus V. C. P. Saavedra, M. V. ... Dive into the research topics of Biochemical characterization of a thermostable cysteine synthase from Geobacillus ...

https://cris.unica.edu.pe/en/publications/biochemical-characterization-of-a-thermostable-cysteine-synthase--2/fingerprints/

Its catalytic cysteine (Cys72-SH) has a low pKa that facilitates oxidation of the thiol to form cysteine sulfenic acid. When ... Sulfenamide Formation Protects Methionine Sulfoxide Reductase A from Hyperoxidation of its Catalytic Cysteine. Wednesday, ... However, sulfenic acid is vulnerable to "irreversible" oxidation to cysteine sulfinic acid (hyperoxidation). We observed that ... As a consequence, the sulfenic acid remains available for facile, irreversible oxidation to cysteine sulfinic acid. ...

https://researchfestival.nih.gov/2015/posters/sulfenamide-formation-protects-methionine-sulfoxide-reductase

Characterization of a family of novel cysteine- serine-rich nuclear proteins (CSRNP). (nih.gov)
A novel cysteine protease, designated as microsciadin, was purified from the latex of Euphorbia microsciadia by a combination of sequential usage of SP-Sepharose Fast Flow column in two different pHs and a final gel filtration chromatography. (bmmj.org)

Cysteine and methionine are sulfur-containing amino acids. (genome.jp)
Keratinocyte Basal Medium MCDB 153 w/o Methionine, Cysteine, Calcium Culture Media 10 L - 1 kit is backordered and will ship as soon as it is back in stock. (dnamethsoc.com)

The VHv1.4 cDNA is 1338 bp long and has an ORF that encodes 322 amino acids with two complete and one partial cysteine motifs. (microbiologyresearch.org)
Similar to other characterized CsPDV cysteine motifs, the VHv1.4 motifs are also characterized by six cysteines at conserved positions and variable inter-cysteine amino acids. (microbiologyresearch.org)

Cysteine is synthesized from serine through different pathways in different organism groups. (genome.jp)
The protein encoded by this gene belongs to the CSRNP family of nuclear proteins that share conserved regions, including cysteine- and serine- rich regions, a basic domain, a transcriptional activation domain, and bind the sequence 'AGAGTG', thus have the hallmark of transcription factors. (nih.gov)

L-cysteine is a sulfur-containing amino acid. (chemicalbook.com)

The enzyme was strongly inhibited by Iodoacetamide, E-64 and Hg 2+ ions indicated that it belongs to the cysteine protease family. (bmmj.org)
The cysteine protease cathepsin B is a potential drug target for reducing brain amyloid-β (Aβ) and improving memory in Alzheimer's disease (AD), as reduction of cathepsin B in transgenic mice expressing human wild-type amyloid-β protein precursor (AβPP) results in significantly decreased brain Aβ. (nih.gov)
To evaluate that issue, was orally administered a cysteine protease inhibitor, E64d, to normal guinea pigs or transgenic mice expressing human AβPP, both of which express the human wild-type β-secretase site sequence. (nih.gov)

The cystatin D sequence contains all regions of relevance for cysteine proteinase inhibitory activity and also the 4 cysteine residues that form disulfide bridges in the other members of cystatin Family 2. (lu.se)
N-acetyl-cysteine is a by-product of glutathione and is popular due to its cysteine residues and the role it has on glutathione maintenance and metabolism. (biomedcentral.com)

In addition, pretreatment of NAT II with N-ethylmaleimide completely prevented the labeling of NAT II with [14C]Br-AAF, which suggests that a cysteine thiol is the target nucleophile of Br-AAF. (aspetjournals.org)
Its catalytic cysteine (Cys72-SH) has a low pKa that facilitates oxidation of the thiol to form cysteine sulfenic acid. (nih.gov)

However, an increasing number of people are learning that supplementing with N-Acetyl Cysteine (NAC) is a simple and effective strategy for defending against influenza. (liversupport.com)

We found a significant improvement in cardiac function accompanied by reduced fibrosis in aged mice via restoring reduced glutathione (GSH) levels (by treating mice with GlyNAC, glycine and N-acetyl cysteine = glutathione precursors) or by reducing macrophage polarization (via DCSL1). (nih.gov)
A form of the amino acid cysteine and a component of protein, NAC is a precursor to glutathione, the body's principal antioxidant that neutralizes free radicals and detoxifies harmful substances. (liversupport.com)
Glutathione and N-acetyl-cysteine (NAC) are antioxidants which are quite popular for their ability to minimize oxidative stress and the downstream negative effects thought to be associated with oxidative stress. (biomedcentral.com)

Dive into the research topics of 'Biochemical characterization of a thermostable cysteine synthase from Geobacillus stearothermophilus V'. Together they form a unique fingerprint. (edu.pe)

The focus of our work is on the mechanism(s) of improving diastolic dysfunction, reducing cardiac fibrosis and inflammation in mice treated with GlyNAC (glycine + N-Acetyl-Cysteine) with or without DCSL1 (Dendritic Cell-Specific Intercellular Adhesion Molecule 3-Grabbing Non-integrin ligand 1). (nih.gov)

The degree of surface fouling from various plasma proteins and human blood was quantified by a liquid interface quartz crystal microbalance in real time, and a zwitterionic cysteine surface can reduce fouling from BSA by 95%, fibrinogen by 93%, and human blood by 93% compared with an untreated gold surface. (uwaterloo.ca)

DNA sequence analyses show that the VHv1.4 gene shares regions of significant identity (73-97%) with the VHv1.1 gene, a member of the cysteine-rich gene family. (microbiologyresearch.org)

Although many dietary supplement products contain N-acetyl cysteine, the US FDA states that it's illegal for dietary supplements to contain N-acetyl cysteine since it's technically an approved drug. (medlineplus.gov)

Inhaling a prescription form of N-acetyl cysteine helps treat collapsed lungs caused by mucus blockage. (medlineplus.gov)
Inhaling a prescription form of N-acetyl cysteine is helpful to prepare people for diagnostic lung tests. (medlineplus.gov)
Inhaling a prescription form of N-acetyl cysteine helps prevent crusting in people with a tube in the windpipe. (medlineplus.gov)
N-acetyl cysteine (NAC) is a specially modified form of the dietary amino acid cysteine. (empowher.com)
N-acetyl cysteine (NAC) is a stable form of the non-essential amino acid cysteine. (hannasherbshop.com)

Affinity alkylation of hamster hepatic arylamine N-acetyltransferases: isolation of a modified cysteine residue. (aspetjournals.org)

Taking prescription N-acetyl cysteine by mouth or by IV reduces the death rate and prevents permanent harm caused by acetaminophen poisoning. (medlineplus.gov)

Using a large population database, and taking genotype as a starting point, we aimed to determine whether individuals harboring a NOTCH3 cysteine altering variant have a higher load of small vessel disease markers on brain magnetic resonance imaging than controls, as well as a higher risk of stroke and cognitive impairment. (elsevier.com)
The case group consisted of individuals harboring a NOTCH3 cysteine altering variant (n=118). (elsevier.com)

Three related C. sonorensis polydnavirus (CsPDV) genes, which are expressed in parasitized H. virescens , have been previously isolated and grouped into a cysteine-rich gene family. (microbiologyresearch.org)
Structure and evolutionary implications of a 'cysteine-rich' Campoletis sonorensis polydnavirus gene family. (microbiologyresearch.org)

X-ray photoelectron spectroscopy confirms the protonation of the amine group and the deprotonation of the carboxyl group, and that 87.84% of the surface cysteine is zwitterionic when fabricated at room temperature. (uwaterloo.ca)

Taking N-acetyl cysteine by mouth, with or without other drugs, might help to prevent kidney problems caused by dyes used during some X-ray exams. (medlineplus.gov)

Prescription N-acetyl cysteine products are available under the guidance of a healthcare provider. (medlineplus.gov)

In addition to the research clearly demonstrating this supplement's ability to battle the flu, N-Acetyl Cysteine has several properties that make it a must have in your arsenal for staying healthy this winter. (liversupport.com)

But a drug called mesna seems to work better than N-acetyl cysteine. (medlineplus.gov)
This work identifies the cysteine desulfurase IscS as the critical target of 2AA in Pseudomonas aeruginosa. (nih.gov)

The adsorption kinetics of zwitterionic cysteine onto a gold surface is studied through monitoring a liquid interface quartz-crystal microbalance in real time and the rate constants are calculated. (uwaterloo.ca)

N-acetyl cysteine is an antioxidant that might play a role in preventing cancer. (medlineplus.gov)

There is also no good evidence to support using N-acetyl cysteine for COVID-19. (medlineplus.gov)

L-Cysteine hydrochloride, anhydrous is widely used as additive in food production. (chemicalbook.com)

People commonly use N-acetyl cysteine for cough and other lung conditions. (medlineplus.gov)
Taking N-acetyl cysteine by mouth for at least 6 months seems to decrease flare-ups by about 40% in people with moderate to severe COPD. (medlineplus.gov)
In people with COPD who need to be hospitalized, taking N-acetyl cysteine in addition to regular treatment helps with recovery. (medlineplus.gov)
Taking N-acetyl cysteine by mouth seems to reduce levels of a blood fat called lipoprotein(a) in people with high levels of this blood fat. (medlineplus.gov)

Background and Purpose: Cysteine altering NOTCH3 variants, which have previously been exclusively associated with the rare hereditary small vessel disease cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy, have a population frequency of 1:300 worldwide. (elsevier.com)

Taking N-acetyl cysteine by mouth or by IV seems to improve chest pain when used with the drug nitroglycerin. (medlineplus.gov)
Taking N-acetyl cysteine by mouth might improve irritability in children and adolescents with autism. (medlineplus.gov)
Taking N-acetyl cysteine by mouth seems to reduce shortness of breath and coughing from this condition. (medlineplus.gov)
Also, taking N-acetyl cysteine by mouth for 3-36 months seems to prevent flare-ups. (medlineplus.gov)
Taking N-acetyl cysteine by mouth seems to reduce homocysteine levels, a possible risk factor for heart disease. (medlineplus.gov)
Taking N-acetyl cysteine by mouth seems to reduce flu symptoms. (medlineplus.gov)

Anatomy5

Organisms3

Chemicals and Drugs91

Analytical, Diagnostic and Therapeutic Techniques and Equipment16

Phenomena and Processes35

Information Science3

An antiviral mechanism of nitric oxide: inhibition of a viral protease. (1/10540)

Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member. (2/10540)

Kinetics of oxidation of aliphatic and aromatic thiols by myeloperoxidase compounds I and II. (3/10540)

Internal electron transfer between hemes and Cu(II) bound at cysteine beta93 promotes methemoglobin reduction by carbon monoxide. (4/10540)

Plasma total homocysteine and cysteine in relation to glomerular filtration rate in diabetes mellitus. (5/10540)

Variants of ribonuclease inhibitor that resist oxidation. (6/10540)

Metal-catalyzed oxidation of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: inactivation and destabilization by oxidation of active-site cysteines. (7/10540)

Functional importance and local environments of the cysteines in the tetracycline resistance protein encoded by plasmid pBR322. (8/10540)

Cysteine

Cysteine Endopeptidases

Cysteine Proteases

Cysteine Dioxygenase

Cysteine Proteinase Inhibitors

Cysteine Synthase

Amino Acid Sequence

Disulfides

Molecular Sequence Data

Sulfhydryl Compounds

Cystine

Mutagenesis, Site-Directed

Cathepsins

Cystatins

Oxidation-Reduction

Cathepsin L

Papain

Binding Sites

Glutathione

Sulfhydryl Reagents

Cathepsin B

Sequence Homology, Amino Acid

Models, Molecular

Base Sequence

Recombinant Proteins

Kinetics

Carbon-Sulfur Lyases

Protein Conformation

Mutation

Ethylmaleimide

Escherichia coli

Serine O-Acetyltransferase

Protein Structure, Tertiary

Sulfur

Dithiothreitol

Mesylates

Dithionitrobenzoic Acid

Amino Acid Substitution

Cloning, Molecular

Protein Binding

Iodoacetamide

Structure-Activity Relationship

Reducing Agents

Sequence Alignment

Sulfinic Acids

Substrate Specificity

Methionine

Iodoacetic Acid

Amino Acids

Cystathionine gamma-Lyase

Lyases

Protein Structure, Secondary

Electrophoresis, Polyacrylamide Gel

Endopeptidases

Alkylation

Thioredoxins

Sulfenic Acids

Catalysis

Amino Acids, Sulfur

Bacterial Proteins

Hydrogen-Ion Concentration

Protein Processing, Post-Translational

Catalytic Domain

Cell Line

4-Chloromercuribenzenesulfonate

Acetylcysteine

Osteonectin

Chromatography, High Pressure Liquid

Lipoylation

Conserved Sequence

Glutamate-Cysteine Ligase

Oxidoreductases Acting on Sulfur Group Donors

Protease Inhibitors

Ethyl Methanesulfonate

Iodoacetates

Taurine

Cystatin B

Peptide Fragments

Dipeptides

Histidine