A cinnamamido ADENOSINE found in STREPTOMYCES alboniger. It inhibits protein synthesis by binding to RNA. It is an antineoplastic and antitrypanosomal agent and is used in research as an inhibitor of protein synthesis.
PUROMYCIN derivative that lacks the methoxyphenylalanyl group on the amine of the sugar ring. It is an antibiotic with antineoplastic properties and can cause nephrosis.
Pathological processes of the KIDNEY without inflammatory or neoplastic components. Nephrosis may be a primary disorder or secondary complication of other diseases. It is characterized by the NEPHROTIC SYNDROME indicating the presence of PROTEINURIA and HYPOALBUMINEMIA with accompanying EDEMA.
Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.
Antibiotic substance isolated from streptomycin-producing strains of Streptomyces griseus. It acts by inhibiting elongation during protein synthesis.
A compound composed of a two CYCLIC PEPTIDES attached to a phenoxazine that is derived from STREPTOMYCES parvullus. It binds to DNA and inhibits RNA synthesis (transcription), with chain elongation more sensitive than initiation, termination, or release. As a result of impaired mRNA production, protein synthesis also declines after dactinomycin therapy. (From AMA Drug Evaluations Annual, 1993, p2015)
An antitumor antibiotic produced by Streptomyces sparsogenes. It inhibits protein synthesis in 70S and 80S ribosomal systems.
A condition characterized by severe PROTEINURIA, greater than 3.5 g/day in an average adult. The substantial loss of protein in the urine results in complications such as HYPOPROTEINEMIA; generalized EDEMA; HYPERTENSION; and HYPERLIPIDEMIAS. Diseases associated with nephrotic syndrome generally cause chronic kidney dysfunction.
Compounds which inhibit the synthesis of proteins. They are usually ANTI-BACTERIAL AGENTS or toxins. Mechanism of the action of inhibition includes the interruption of peptide-chain elongation, the blocking the A site of ribosomes, the misreading of the genetic code or the prevention of the attachment of oligosaccharide side chains to glycoproteins.
A cluster of convoluted capillaries beginning at each nephric tubule in the kidney and held together by connective tissue.
Highly differentiated epithelial cells of the visceral layer of BOWMAN CAPSULE of the KIDNEY. They are composed of a cell body with major CELL SURFACE EXTENSIONS and secondary fingerlike extensions called pedicels. They enwrap the KIDNEY GLOMERULUS capillaries with their cell surface extensions forming a filtration structure. The pedicels of neighboring podocytes interdigitate with each other leaving between them filtration slits that are bridged by an extracellular structure impermeable to large macromolecules called the slit diaphragm, and provide the last barrier to protein loss in the KIDNEY.
The principal alkaloid of ipecac, from the ground roots of Uragoga (or Cephaelis) ipecacuanha or U. acuminata, of the Rubiaceae. It is used as an amebicide in many different preparations and may cause serious cardiac, hepatic, or renal damage and violent diarrhea and vomiting. Emetine inhibits protein synthesis in EUKARYOTIC CELLS but not PROKARYOTIC CELLS.
The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
An antibiotic first isolated from cultures of Streptomyces venequelae in 1947 but now produced synthetically. It has a relatively simple structure and was the first broad-spectrum antibiotic to be discovered. It acts by interfering with bacterial protein synthesis and is mainly bacteriostatic. (From Martindale, The Extra Pharmacopoeia, 29th ed, p106)
An essential branched-chain amino acid important for hemoglobin formation.
The production of PEPTIDES or PROTEINS by the constituents of a living organism. The biosynthesis of proteins on RIBOSOMES following an RNA template is termed translation (TRANSLATION, GENETIC). There are other, non-ribosomal peptide biosynthesis (PEPTIDE BIOSYNTHESIS, NUCLEIC ACID-INDEPENDENT) mechanisms carried out by PEPTIDE SYNTHASES and PEPTIDYLTRANSFERASES. Further modifications of peptide chains yield functional peptide and protein molecules.
Tritium is an isotope of hydrogen (specifically, hydrogen-3) that contains one proton and two neutrons in its nucleus, making it radioactive with a half-life of about 12.3 years, and is used in various applications including nuclear research, illumination, and dating techniques due to its low energy beta decay.
The presence of proteins in the urine, an indicator of KIDNEY DISEASES.
A process of GENETIC TRANSLATION, when an amino acid is transferred from its cognate TRANSFER RNA to the lengthening chain of PEPTIDES.
A multiribosomal structure representing a linear array of RIBOSOMES held together by messenger RNA; (RNA, MESSENGER); They represent the active complexes in cellular protein synthesis and are able to incorporate amino acids into polypeptides both in vivo and in vitro. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.
Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases.
Intermediates in protein biosynthesis. The compounds are formed from amino acids, ATP and transfer RNA, a reaction catalyzed by aminoacyl tRNA synthetase. They are key compounds in the genetic translation process.
An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.
A strongly basic peptide, antibiotic complex from several strains of Streptomyces. It is allergenic and toxic to kidneys and the labyrinth. Viomycin is used in tuberculosis as several different salts and in combination with other agents.
The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains.

Properties of 5-aminolaevulinate synthetase and its relationship to microsomal mixed-function oxidation in the southern armyworm (Spodoptera eridania). (1/1192)

1. Activity of 5-aminolaevulinate synthetase was measured in the midgut and other tissues of the last larval instar of the southern armyworm (Spodoptera eridania Cramer, formerly Prodenia eridania Cramer). 2. Optimum conditions for measuring the activity were established with respect to all variables involved and considerable differences from those reported for mammalian enzyme preparations were found. 3. Maximum activity (20 nmol/h per mg of protein) occurs 18-24 h after the fifth moult and thereafter decreases to trace amounts as the larvae age and approach pupation. 4. Synthetase activity was rapidly induced by oral administration (in the diet) of pentamethylbenzene, phenobarbital, diethyl 1,4-dihydro-2,4,6-trimethylpyridine-3, 5-dicarboxylate, and 2-allyl-2-isopropylacetamide. 5. Puromycin inhibited the induction of synthetase by pentamethylbenzene. 6. Induction of 5-aminolaevulinate synthetase correlated well with the induction of microsomal N-demethylation of p-chloro-N-methylaniline, except for phenobarbital, which induced the microsomal oxidase relatively more than the synthetase.  (+info)

E2F-1 has properties of a radiosensitizer and its regulation by cyclin A kinase is required for cell survival of fibrosarcoma cells lacking p53. (2/1192)

Negative regulation of E2F-1 DNA binding function by cyclin A kinase represents part of an S-phase checkpoint control system that, when activated, leads to apoptosis. In this study, we examined the cellular sensitivity and resistance of isogenic mouse fibrosarcoma cell lines, differing primarily in their p53 status, to ectopic expression of wild-type (wt) E2F-1 and cyclin A kinase binding-defective mutants of it. We found that E2F-1 (wt) potently affected the survival of p53+/+ tumor cells but not that of p53-/- cells. In contrast, expression of cyclin A kinase binding-defective E2F-1 species interfered with cell survival of fibrosarcoma cells irrespective of their p53 status. Finally, expression of E2F-1 (wt) in p53-/- fibrosarcoma cells enhanced the cytotoxic effect of ionizing radiation in vitro and in vivo in a mouse tumor model. These results suggest that E2F-1-dependent activation of an S-phase checkpoint is p53 independent and that E2F-1 possesses radiosensitizing properties in the absence of p53.  (+info)

Re-activation of the peptidyltransferase centre of rabbit reticulocyte ribosomes after inactivation by exposure to low concentrations of magnesium ion. (3/1192)

1. The larger subrivosomal particles of rabbit reticulocytes retained full activity in the puromycin reaction and in poly(U)-directed polyphenylalanine synthesis after 4h at 0 degrees C when buffered 0.5M-NH4Cl/10-30mM-MgCl2 was the solvent. 2. Activity in the puromycin reaction was diminished to approx 10% after 15-30 min at 0 degrees C when the concentration of MgCl2 was lowered to 2mM. 3. Activity was not restored when the concentration of MgCl2 was raised from 2mM to 10-30 mM at 0 degrees C. However, activity was recovered as measured by both assay systems when the ribosome fraction was heated to 37 degrees C at the higher concentrations of MgCl2. 4. Recovery of activity was noted during the course of the polyphenylalanine synthesis in 50 mM-KCl/5mM-MgCl2/25mM-Tris/HCl, pH 7.6, at 37 degrees C. Re-activation was slow at 20 degrees C and below. 5. No more than about 5% of the protein moiety of the subparticle was lost in 0.5M-NH4Cl on decreasing MgCl2 concentration from 10mM to 2mM. No proteins were detected in the supernatant fractions by gel electrophoresis after ribosomes were separated by differential centrifugation. The supernatant fraction was not essential for the recovery of activity. However, at higher (e.g. 1M) concentrations of NH4Cl, proteins were split from the subparticle. 6. The loss and regain of activity found on lowering and restoring the concentration of MgCl2 at 0.5M-NH4Cl appears to arise from a conformational change that does not seem to be associated with a loss and regain of particular proteins. 7. A 2% decrease in E260 was noticed when the concentration of Mg2+ was restored, and the change in the spectrum indicated a net increase of approx. 100A-U base-pairs per subribosomal particle. 8. When the concentration of Mg2+ was restored, S20,W of the subparticle remained at 52+/- 1S until the sample was incubated at 37 degrees C when S20,W increased to 56 +/- 1S compared with the value of 58 +/- 1S for the subparticle as originally isolated.  (+info)

Reassembly of the peptidyltransferase centre of larger subparticles of rabbit reticulocyte ribosomes from a core-particle and split-protein fraction. (4/1192)

We report the reconstruction, from a core-particle and split-protein fraction, of the larger subribosomal particle of rabbit reticulocytes. The reassembled particle was active in polyphenylalanine synthesis and in the puromycin reaction. The core-particles and split-protein fractions were obtained by treatment of the larger subparticle with salt solutions containing NH4+ and Mg2+ in the molar ratio 40:1 over the range 2.25-2.75 M-NH4Cl/56-69mM-MgCl2 at 0 degrees C. This treatment led to the loss of about eight proteins (approx. 17% of the protein moiety), which were found wholly or largely in the split-protein fraction as shown by two-dimensional gel electrophoresis. The core particle retained 5S rRNA and had much decreased (no more than 10% of control) ability to function in the puromycin reaction or in poly (U)-directed polyphenylalanine synthesis. Activity was recovered when the recombined core-particle and split-protein fractions were dialysed overnight at 4 degrees C against 0.3M-NH4Cl/15mM-MgCl2/1mM-dithiothreitol/15% (v/v) glycerol/20mM-Tris/HCl, pH 7.6, and then heated for 1 h at 37 degreesEES C. The recovery was 40-80% of the original activity. Raising the concentration of MgCL2 to 300 mM in 2.5 M-NH4CL led to the removal of seven rather than eight proteins, and the core particle remained active in the puromycin reaction. We infer that the protein retained by raising the concentration of Mg2+ is an essential component of the peptidyltransferase centre of the ribosome.  (+info)

Selection of RNA replicons capable of persistent noncytopathic replication in mammalian cells. (5/1192)

The natural life cycle of alphaviruses, a group of plus-strand RNA viruses, involves transmission to vertebrate hosts via mosquitoes. Chronic infections are established in mosquitoes (and usually in mosquito cell cultures), but infection of susceptible vertebrate cells typically results in rapid shutoff of host mRNA translation and cell death. Using engineered Sindbis virus RNA replicons expressing puromycin acetyltransferase as a dominant selectable marker, we identified mutations allowing persistent, noncytopathic replication in BHK-21 cells. Two of these adaptive mutations involved single-amino-acid substitutions in the C-terminal portion of nsP2, the viral helicase-protease. At one of these loci, nsP2 position 726, numerous substitution mutations were created and characterized in the context of RNA replicons and infectious virus. Our results suggest a direct correlation between the level of viral RNA replication and cytopathogenicity. This work also provides a series of alphavirus replicons for noncytopathic gene expression studies (E. V. Agapov, I. Frolov, B. D. Lindenbach, B. M. Pragai, S. Schlesinger, and C. M. Rice, Proc. Natl. Acad. Sci. USA 95:12989-12994, 1998) and a general strategy for selecting RNA viral mutants adapted to different cellular environments.  (+info)

Novel roles for classical factors at the interface between translation termination and initiation. (6/1192)

The pathway of bacterial ribosome recycling following translation termination has remained obscure. Here, we elucidate two essential steps and describe the roles played by the three translation factors EF-G, RRF, and IF3. Release factor RF3 is known to catalyze the dissociation of RF1 or RF2 from ribosomes after polypeptide release. We show that the next step is dissociation of 50S subunits from the 70S posttermination complex and that it is catalyzed by RRF and EF-G and requires GTP hydrolysis. Removal of deacylated tRNA from the resulting 30S:mRNA:tRNA posttermination complex is then necessary to permit rapid 30S subunit recycling. We show that this step requires initiation factor IF3, whose role was previously thought to be restricted to promoting specific 30S initiation complex formation from free 30S subunits.  (+info)

Kinetochore fibers are not involved in the formation of the first meiotic spindle in mouse oocytes, but control the exit from the first meiotic M phase. (7/1192)

During meiosis, two successive divisions occur without any intermediate S phase to produce haploid gametes. The first meiotic division is unique in that homologous chromosomes are segregated while the cohesion between sister chromatids is maintained, resulting in a reductional division. Moreover, the duration of the first meiotic M phase is usually prolonged when compared with mitotic M phases lasting 8 h in mouse oocytes.We investigated the spindle assembly pathway and its role in the progression of the first meiotic M phase in mouse oocytes. During the first 4 h, a bipolar spindle forms and the chromosomes congress near the equatorial plane of the spindle without stable kinetochore- microtubule end interactions. This late prometaphase spindle is then maintained for 4 h with chromosomes oscillating in the central region of the spindle. The kinetochore-microtubule end interactions are set up at the end of the first meiotic M phase (8 h after entry into M phase). This event allows the final alignment of the chromosomes and exit from metaphase. The continuous presence of the prometaphase spindle is not required for progression of the first meiotic M phase. Finally, the ability of kinetochores to interact with microtubules is acquired at the end of the first meiotic M phase and determines the timing of polar body extrusion.  (+info)

Sordarin inhibits fungal protein synthesis by blocking translocation differently to fusidic acid. (8/1192)

Sordarin derivatives are selective inhibitors of fungal protein synthesis, which specifically impair elongation factor 2 (EF-2) function. We have studied the effect of sordarin on the ribosome-dependent GTPase activity of EF-2 from Candida albicans in the absence of any other component of the translation system. The effect of sordarin turned out to be dependent both on the ratio of ribosomes to EF-2 and on the nature of the ribosomes. When the amount of EF-2 exceeded that of ribosomes sordarin inhibited the GTPase activity following an inverted bell-shaped dose-response curve, whereas when EF-2 and ribosomes were in equimolar concentrations sordarin yielded a typical sigmoidal dose-dependent inhibition. However, when ricin-treated ribosomes were used, sordarin stimulated the hydrolysis of GTP. These results were compared with those obtained with fusidic acid, showing that both drugs act in a different manner. All these data are consistent with sordarin blocking the elongation cycle at the initial steps of translocation, prior to GTP hydrolysis. In agreement with this conclusion, sordarin prevented the formation of peptidyl-[(3)H]puromycin on polysomes from Candida albicans.  (+info)

Puromycin is an antibiotic and antiviral protein synthesis inhibitor. It works by being incorporated into the growing peptide chain during translation, causing premature termination and release of the incomplete polypeptide. This results in the inhibition of protein synthesis and ultimately leads to cell death. In research, puromycin is often used as a selective agent in cell culture to kill cells that have not been transfected with a plasmid containing a resistance gene for puromycin.

Puromycin aminonucleoside is not a medical condition, but rather a laboratory reagent used in research. It is a synthetic antibiotic and analogue of the amino acid tyrosine, which specifically inhibits protein synthesis in eukaryotic cells by interacting with the peptidyl transferase center of the 60S ribosomal subunit. This compound has been widely used as a tool to study various cellular processes, including programmed cell death (apoptosis), autophagy, and lysosome biogenesis. Prolonged exposure to puromycin aminonucleoside can induce cytopathic effects, such as vacuolization and detachment of cells, which are often used as markers for its effectiveness in inhibiting protein synthesis.

Nephrosis is an older term that was used to describe a group of kidney diseases, primarily characterized by the damage and loss of function in the glomeruli - the tiny filtering units within the kidneys. This results in the leakage of large amounts of protein (primarily albumin) into the urine, a condition known as proteinuria.

The term "nephrosis" was often used interchangeably with "minimal change nephropathy," which is a specific type of kidney disorder that demonstrates little to no changes in the glomeruli under a microscope, despite significant protein leakage. However, current medical terminology and classifications prefer the use of more precise terms to describe various kidney diseases, such as minimal change disease, focal segmental glomerulosclerosis, or membranous nephropathy, among others.

It is important to consult with a healthcare professional or refer to updated medical resources for accurate and current information regarding kidney diseases and their specific diagnoses.

Ribosomes are complex macromolecular structures composed of ribonucleic acid (RNA) and proteins that play a crucial role in protein synthesis within cells. They serve as the site for translation, where messenger RNA (mRNA) is translated into a specific sequence of amino acids to create a polypeptide chain, which eventually folds into a functional protein.

Ribosomes consist of two subunits: a smaller subunit and a larger subunit. These subunits are composed of ribosomal RNA (rRNA) molecules and proteins. In eukaryotic cells, the smaller subunit is denoted as the 40S subunit, while the larger subunit is referred to as the 60S subunit. In prokaryotic cells, these subunits are named the 30S and 50S subunits, respectively. The ribosome's overall structure resembles a "doughnut" or a "cotton reel," with grooves and binding sites for various factors involved in protein synthesis.

Ribosomes can be found floating freely within the cytoplasm of cells or attached to the endoplasmic reticulum (ER) membrane, forming part of the rough ER. Membrane-bound ribosomes are responsible for synthesizing proteins that will be transported across the ER and ultimately secreted from the cell or inserted into the membrane. In contrast, cytoplasmic ribosomes synthesize proteins destined for use within the cytoplasm or organelles.

In summary, ribosomes are essential components of cells that facilitate protein synthesis by translating mRNA into functional polypeptide chains. They can be found in various cellular locations and exist as either free-floating entities or membrane-bound structures.

Cycloheximide is an antibiotic that is primarily used in laboratory settings to inhibit protein synthesis in eukaryotic cells. It is derived from the actinobacteria species Streptomyces griseus. In medical terms, it is not used as a therapeutic drug in humans due to its significant side effects, including liver toxicity and potential neurotoxicity. However, it remains a valuable tool in research for studying protein function and cellular processes.

The antibiotic works by binding to the 60S subunit of the ribosome, thereby preventing the transfer RNA (tRNA) from delivering amino acids to the growing polypeptide chain during translation. This inhibition of protein synthesis can be lethal to cells, making cycloheximide a useful tool in studying cellular responses to protein depletion or misregulation.

In summary, while cycloheximide has significant research applications due to its ability to inhibit protein synthesis in eukaryotic cells, it is not used as a therapeutic drug in humans because of its toxic side effects.

Dactinomycin is an antineoplastic antibiotic, which means it is used to treat cancer. It is specifically used to treat certain types of testicular cancer, Wilms' tumor (a type of kidney cancer that occurs in children), and some gestational trophoblastic tumors (a type of tumor that can develop in the uterus after pregnancy). Dactinomycin works by interfering with the DNA in cancer cells, which prevents them from dividing and growing. It is often used in combination with other chemotherapy drugs as part of a treatment regimen.

Dactinomycin is administered intravenously (through an IV) and its use is usually limited to hospitals or specialized cancer treatment centers due to the need for careful monitoring during administration. Common side effects include nausea, vomiting, and hair loss. More serious side effects can include bone marrow suppression, which can lead to an increased risk of infection, and tissue damage at the site where the drug is injected. Dactinomycin can also cause severe allergic reactions in some people.

It's important to note that dactinomycin should only be used under the supervision of a qualified healthcare professional, as its use requires careful monitoring and management of potential side effects.

Sparsomycin is an antitumor antibiotic that is isolated from Streptomyces sp. It is used in research and biochemical studies as an inhibitor of the protein synthesis elongation factor-1 (EF-1) and has been investigated for its potential therapeutic use in cancer treatment. However, it has not been approved for clinical use in humans due to its narrow therapeutic index and significant toxicity.

In medical terms, sparsomycin is defined as:

"A cytotoxic antibiotic produced by Streptomyces sp., with the molecular formula C46H72N10O15P. It inhibits protein synthesis in eukaryotic cells by binding to elongation factor-1 (EF-1) and preventing the formation of the ternary complex required for peptide bond formation during translation. Sparsomycin has been studied for its potential therapeutic use in cancer treatment, but its clinical development has been limited due to its significant toxicity."

Nephrotic syndrome is a group of symptoms that indicate kidney damage, specifically damage to the glomeruli—the tiny blood vessel clusters in the kidneys that filter waste and excess fluids from the blood. The main features of nephrotic syndrome are:

1. Proteinuria (excess protein in urine): Large amounts of a protein called albumin leak into the urine due to damaged glomeruli, which can't properly filter proteins. This leads to low levels of albumin in the blood, causing fluid buildup and swelling.
2. Hypoalbuminemia (low blood albumin levels): As albumin leaks into the urine, the concentration of albumin in the blood decreases, leading to hypoalbuminemia. This can cause edema (swelling), particularly in the legs, ankles, and feet.
3. Edema (fluid retention and swelling): With low levels of albumin in the blood, fluids move into the surrounding tissues, causing swelling or puffiness. The swelling is most noticeable around the eyes, face, hands, feet, and abdomen.
4. Hyperlipidemia (high lipid/cholesterol levels): The kidneys play a role in regulating lipid metabolism. Damage to the glomeruli can lead to increased lipid production and high cholesterol levels in the blood.

Nephrotic syndrome can result from various underlying kidney diseases, such as minimal change disease, membranous nephropathy, or focal segmental glomerulosclerosis. Treatment depends on the underlying cause and may include medications to control inflammation, manage high blood pressure, and reduce proteinuria. In some cases, dietary modifications and lifestyle changes are also recommended.

Protein synthesis inhibitors are a class of medications or chemical substances that interfere with the process of protein synthesis in cells. Protein synthesis is the biological process by which cells create proteins, essential components for the structure, function, and regulation of tissues and organs. This process involves two main stages: transcription and translation.

Translation is the stage where the genetic information encoded in messenger RNA (mRNA) is translated into a specific sequence of amino acids, resulting in a protein molecule. Protein synthesis inhibitors work by targeting various components of the translation machinery, such as ribosomes, transfer RNAs (tRNAs), or translation factors, thereby preventing or disrupting the formation of new proteins.

These inhibitors have clinical applications in treating various conditions, including bacterial and viral infections, cancer, and autoimmune disorders. Some examples of protein synthesis inhibitors include:

1. Antibiotics: Certain antibiotics, like tetracyclines, macrolides, aminoglycosides, and chloramphenicol, target bacterial ribosomes and inhibit their ability to synthesize proteins, thereby killing or inhibiting the growth of bacteria.
2. Antiviral drugs: Protein synthesis inhibitors are used to treat viral infections by targeting various stages of the viral replication cycle, including protein synthesis. For example, ribavirin is an antiviral drug that can inhibit viral RNA-dependent RNA polymerase and mRNA capping, which are essential for viral protein synthesis.
3. Cancer therapeutics: Some chemotherapeutic agents target rapidly dividing cancer cells by interfering with their protein synthesis machinery. For instance, puromycin is an aminonucleoside antibiotic that can be incorporated into elongating polypeptide chains during translation, causing premature termination and inhibiting overall protein synthesis in cancer cells.
4. Immunosuppressive drugs: Protein synthesis inhibitors are also used as immunosuppressants to treat autoimmune disorders and prevent organ rejection after transplantation. For example, tacrolimus and cyclosporine bind to and inhibit the activity of calcineurin, a protein phosphatase that plays a crucial role in T-cell activation and cytokine production.

In summary, protein synthesis inhibitors are valuable tools for treating various diseases, including bacterial and viral infections, cancer, and autoimmune disorders. By targeting the protein synthesis machinery of pathogens or abnormal cells, these drugs can selectively inhibit their growth and proliferation while minimizing harm to normal cells.

A kidney glomerulus is a functional unit in the nephron of the kidney. It is a tuft of capillaries enclosed within a structure called Bowman's capsule, which filters waste and excess fluids from the blood. The glomerulus receives blood from an afferent arteriole and drains into an efferent arteriole.

The process of filtration in the glomerulus is called ultrafiltration, where the pressure within the glomerular capillaries drives plasma fluid and small molecules (such as ions, glucose, amino acids, and waste products) through the filtration membrane into the Bowman's space. Larger molecules, like proteins and blood cells, are retained in the blood due to their larger size. The filtrate then continues down the nephron for further processing, eventually forming urine.

Podocytes are specialized cells that make up the visceral epithelial layer of the glomerular basement membrane in the kidney. They have long, interdigitating foot processes that wrap around the capillaries of the glomerulus and play a crucial role in maintaining the filtration barrier of the kidney. The slit diaphragms between the foot processes allow for the passage of small molecules while retaining larger proteins in the bloodstream. Podocytes also contribute to the maintenance and regulation of the glomerular filtration rate, making them essential for normal renal function. Damage or loss of podocytes can lead to proteinuria and kidney disease.

Emetine is a medication that is derived from the plant ipecacuanha. It is an alkaloid that has been used in the treatment of certain parasitic infections, particularly those caused by intestinal amoebae. Emetine works by inhibiting protein synthesis in the parasites, which helps to eliminate them from the body.

Emetine is administered orally or by injection and is typically used as a last resort when other treatments have failed. It can cause significant side effects, including nausea, vomiting, and diarrhea, as well as more serious complications such as heart rhythm abnormalities and muscle weakness. As a result, its use is generally restricted to cases where the benefits of treatment outweigh the risks.

It's important to note that emetine should only be used under the close supervision of a healthcare provider, and its use carries a number of precautions and contraindications. It is not recommended for use in pregnant women or people with certain medical conditions, such as heart disease or kidney disease.

Protein biosynthesis is the process by which cells generate new proteins. It involves two major steps: transcription and translation. Transcription is the process of creating a complementary RNA copy of a sequence of DNA. This RNA copy, or messenger RNA (mRNA), carries the genetic information to the site of protein synthesis, the ribosome. During translation, the mRNA is read by transfer RNA (tRNA) molecules, which bring specific amino acids to the ribosome based on the sequence of nucleotides in the mRNA. The ribosome then links these amino acids together in the correct order to form a polypeptide chain, which may then fold into a functional protein. Protein biosynthesis is essential for the growth and maintenance of all living organisms.

Chloramphenicol is an antibiotic medication that is used to treat a variety of bacterial infections. It works by inhibiting the ability of bacteria to synthesize proteins, which essential for their growth and survival. This helps to stop the spread of the infection and allows the body's immune system to clear the bacteria from the body.

Chloramphenicol is a broad-spectrum antibiotic, which means that it is effective against many different types of bacteria. It is often used to treat serious infections that have not responded to other antibiotics. However, because of its potential for serious side effects, including bone marrow suppression and gray baby syndrome, chloramphenicol is usually reserved for use in cases where other antibiotics are not effective or are contraindicated.

Chloramphenicol can be given by mouth, injection, or applied directly to the skin in the form of an ointment or cream. It is important to take or use chloramphenicol exactly as directed by a healthcare provider, and to complete the full course of treatment even if symptoms improve before all of the medication has been taken. This helps to ensure that the infection is fully treated and reduces the risk of antibiotic resistance.

Leucine is an essential amino acid, meaning it cannot be produced by the human body and must be obtained through the diet. It is one of the three branched-chain amino acids (BCAAs), along with isoleucine and valine. Leucine is critical for protein synthesis and muscle growth, and it helps to regulate blood sugar levels, promote wound healing, and produce growth hormones.

Leucine is found in various food sources such as meat, dairy products, eggs, and certain plant-based proteins like soy and beans. It is also available as a dietary supplement for those looking to increase their intake for athletic performance or muscle recovery purposes. However, it's important to consult with a healthcare professional before starting any new supplement regimen.

Peptide biosynthesis is the process by which cells synthesize peptides, short chains of amino acids. This process is mediated by enzymes called peptide synthetases, which catalyze the formation of peptide bonds between individual amino acids to create a longer chain. Peptide biosynthesis typically occurs through one of two pathways: ribosomal or non-ribosomal.

Ribosomal peptide biosynthesis involves the use of the cell's translational machinery, including the ribosome and transfer RNAs (tRNAs), to synthesize peptides from a messenger RNA (mRNA) template. This process is highly regulated and typically results in the production of small, linear peptides that are further modified by enzymes to create bioactive molecules such as hormones or neurotransmitters.

Non-ribosomal peptide biosynthesis (NRPS), on the other hand, is a more complex process that involves large multifunctional enzyme complexes called non-ribosomal peptide synthetases (NRPSs). These enzymes are capable of synthesizing a wide variety of structurally diverse peptides, including cyclic and branched peptides, as well as those containing non-proteinogenic amino acids. NRPSs typically consist of multiple modules, each responsible for adding a single amino acid to the growing peptide chain. The modular nature of NRPS systems allows for great diversity in the types of peptides that can be synthesized, making them important sources of bioactive molecules with potential therapeutic applications.

Tritium is not a medical term, but it is a term used in the field of nuclear physics and chemistry. Tritium (symbol: T or 3H) is a radioactive isotope of hydrogen with two neutrons and one proton in its nucleus. It is also known as heavy hydrogen or superheavy hydrogen.

Tritium has a half-life of about 12.3 years, which means that it decays by emitting a low-energy beta particle (an electron) to become helium-3. Due to its radioactive nature and relatively short half-life, tritium is used in various applications, including nuclear weapons, fusion reactors, luminous paints, and medical research.

In the context of medicine, tritium may be used as a radioactive tracer in some scientific studies or medical research, but it is not a term commonly used to describe a medical condition or treatment.

Proteinuria is a medical term that refers to the presence of excess proteins, particularly albumin, in the urine. Under normal circumstances, only small amounts of proteins should be found in the urine because the majority of proteins are too large to pass through the glomeruli, which are the filtering units of the kidneys.

However, when the glomeruli become damaged or diseased, they may allow larger molecules such as proteins to leak into the urine. Persistent proteinuria is often a sign of kidney disease and can indicate damage to the glomeruli. It is usually detected through a routine urinalysis and may be confirmed with further testing.

The severity of proteinuria can vary, and it can be a symptom of various underlying conditions such as diabetes, hypertension, glomerulonephritis, and other kidney diseases. Treatment for proteinuria depends on the underlying cause and may include medications to control blood pressure, manage diabetes, or reduce protein loss in the urine.

Translational peptide chain elongation is the process during protein synthesis where activated amino acids are added to the growing peptide chain in a sequence determined by the genetic code present in messenger RNA (mRNA). This process involves several steps:

1. Recognition of the start codon on the mRNA by the small ribosomal subunit, which binds to the mRNA and brings an initiator tRNA with a methionine or formylmethionine amino acid attached into the P site (peptidyl site) of the ribosome.
2. The large ribosomal subunit then joins the small subunit, forming a complete ribosome complex.
3. An incoming charged tRNA with an appropriate amino acid, complementary to the next codon on the mRNA, binds to the A site (aminoacyl site) of the ribosome.
4. Peptidyl transferase, a catalytic domain within the large ribosomal subunit, facilitates the formation of a peptide bond between the amino acids attached to the tRNAs in the P and A sites. The methionine or formylmethionine initiator amino acid is now covalently linked to the second amino acid via this peptide bond.
5. Translocation occurs, moving the tRNA with the growing peptide chain from the P site to the E site (exit site) and shifting the mRNA by one codon relative to the ribosome. The uncharged tRNA is then released from the E site.
6. The next charged tRNA carrying an appropriate amino acid binds to the A site, and the process repeats until a stop codon is reached on the mRNA.
7. Upon encountering a stop codon, release factors recognize it and facilitate the release of the completed polypeptide chain from the final tRNA in the P site. The ribosome then dissociates from the mRNA, allowing for further translational events to occur.

Translational peptide chain elongation is a crucial step in protein synthesis and requires precise coordination between various components of the translation machinery, including ribosomes, tRNAs, amino acids, and numerous accessory proteins.

Polyribosomes, also known as polysomes, are clusters of ribosomes that are translating the same mRNA molecule simultaneously. They can be found in the cytoplasm of eukaryotic cells and are responsible for the synthesis of proteins. The mRNA molecule serves as a template for the translation process, with multiple ribosomes moving along it and producing multiple copies of the same protein. This allows for efficient and rapid production of large quantities of a single protein. Polyribosomes can be found in high numbers in cells that are actively synthesizing proteins, such as secretory cells or cells undergoing growth and division.

Carbon isotopes are variants of the chemical element carbon that have different numbers of neutrons in their atomic nuclei. The most common and stable isotope of carbon is carbon-12 (^{12}C), which contains six protons and six neutrons. However, carbon can also come in other forms, known as isotopes, which contain different numbers of neutrons.

Carbon-13 (^{13}C) is a stable isotope of carbon that contains seven neutrons in its nucleus. It makes up about 1.1% of all carbon found on Earth and is used in various scientific applications, such as in tracing the metabolic pathways of organisms or in studying the age of fossilized materials.

Carbon-14 (^{14}C), also known as radiocarbon, is a radioactive isotope of carbon that contains eight neutrons in its nucleus. It is produced naturally in the atmosphere through the interaction of cosmic rays with nitrogen gas. Carbon-14 has a half-life of about 5,730 years, which makes it useful for dating organic materials, such as archaeological artifacts or fossils, up to around 60,000 years old.

Carbon isotopes are important in many scientific fields, including geology, biology, and medicine, and are used in a variety of applications, from studying the Earth's climate history to diagnosing medical conditions.

Peptidyl transferase is not a medical term per se, but rather a biochemical term used to describe an enzymatic function or activity. It is often mentioned in the context of molecular biology, protein synthesis, and ribosome structure.

Peptidyl transferase refers to the catalytic activity of ribosomes that facilitates the formation of peptide bonds between amino acids during protein synthesis. More specifically, peptidyl transferase is responsible for transferring the peptidyl group (the growing polypeptide chain) from the acceptor site (A-site) to the donor site (P-site) of the ribosome, creating a new peptide bond and elongating the polypeptide chain. This activity occurs within the large subunit of the ribosome, near the peptidyl transferase center (PTC).

While it is often attributed to the ribosomal RNA (rRNA) component of the ribosome, recent research suggests that both rRNA and specific ribosomal proteins contribute to this enzymatic activity.

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis. It serves as the adaptor molecule that translates the genetic code present in messenger RNA (mRNA) into the corresponding amino acids, which are then linked together to form a polypeptide chain during protein synthesis.

Aminoacyl tRNA is a specific type of tRNA molecule that has been charged or activated with an amino acid. This process is called aminoacylation and is carried out by enzymes called aminoacyl-tRNA synthetases. Each synthetase specifically recognizes and attaches a particular amino acid to its corresponding tRNA, ensuring the fidelity of protein synthesis. Once an amino acid is attached to a tRNA, it forms an aminoacyl-tRNA complex, which can then participate in translation and contribute to the formation of a new protein.

Phenylalanine is an essential amino acid, meaning it cannot be produced by the human body and must be obtained through diet or supplementation. It's one of the building blocks of proteins and is necessary for the production of various molecules in the body, such as neurotransmitters (chemical messengers in the brain).

Phenylalanine has two forms: L-phenylalanine and D-phenylalanine. L-phenylalanine is the form found in proteins and is used by the body for protein synthesis, while D-phenylalanine has limited use in humans and is not involved in protein synthesis.

Individuals with a rare genetic disorder called phenylketonuria (PKU) must follow a low-phenylalanine diet or take special medical foods because they are unable to metabolize phenylalanine properly, leading to its buildup in the body and potential neurological damage.

Viomycin is an antibiotic that belongs to the class of drugs known as aminoglycosides. It works by binding to bacterial ribosomes and interfering with protein synthesis, leading to bacterial cell death. Viomycin is primarily used to treat tuberculosis and other mycobacterial infections that are resistant to other antibiotics. However, its use is limited due to its potential toxicity to the kidneys and hearing.

Here's a medical definition of Viomycin from Stedman's Medical Dictionary:

"A crystalline, basic polypeptide antibiotic produced by certain strains of Streptomyces floridae var. violaceusniger; used in the treatment of tuberculosis and other mycobacterial infections."

Transfer RNA (tRNA) is a type of RNA molecule that plays a crucial role in protein synthesis, the process by which cells create proteins. In protein synthesis, tRNAs serve as adaptors, translating the genetic code present in messenger RNA (mRNA) into the corresponding amino acids required to build a protein.

Each tRNA molecule has a distinct structure, consisting of approximately 70-90 nucleotides arranged in a cloverleaf shape with several loops and stems. The most important feature of a tRNA is its anticodon, a sequence of three nucleotides located in one of the loops. This anticodon base-pairs with a complementary codon on the mRNA during translation, ensuring that the correct amino acid is added to the growing polypeptide chain.

Before tRNAs can participate in protein synthesis, they must be charged with their specific amino acids through an enzymatic process involving aminoacyl-tRNA synthetases. These enzymes recognize and bind to both the tRNA and its corresponding amino acid, forming a covalent bond between them. Once charged, the aminoacyl-tRNA complex is ready to engage in translation and contribute to protein formation.

In summary, transfer RNA (tRNA) is a small RNA molecule that facilitates protein synthesis by translating genetic information from messenger RNA into specific amino acids, ultimately leading to the creation of functional proteins within cells.

... -resistant transformants are selected in LB agar medium supplemented with 125 µg/ml of puromycin. But use of puromycin ... Puromycin is soluble in water (50 mg/ml) as colorless solution at 10 mg/ml. Puromycin is stable for one year as solution when ... Also of note, puromycin is critical in mRNA display. In this reaction, a puromycin molecule is chemically attached to the end ... Resistance to puromycin is conferred by the pac gene encoding a puromycin N-acetyl-transferase (PAC) that was found in a ...
Puromycin-sensitive amino peptidase also known as cytosol alanyl aminopeptidase or alanine aminopeptidase (AAP) (EC 3.4.11.14) ... Thompson MW, Tobler A, Fontana A, Hersh LB (May 1999). "Cloning and analysis of the gene for the human puromycin-sensitive ... Tobler AR, Constam DB, Schmitt-Gräff A, Malipiero U, Schlapbach R, Fontana A (March 1997). "Cloning of the human puromycin- ... Yanagi K, Tanaka T, Kato K, Sadik G, Morihara T, Kudo T, Takeda M (December 2009). "Involvement of puromycin-sensitive ...
This enzyme participates in puromycin biosynthesis. Rao MM, Rebello PF, Pogell BM (1969). "Biosynthesis of puromycin in ... puromycin Thus, the two substrates of this enzyme are S-adenosyl methionine and O-demethylpuromycin, whereas its two products ... are S-adenosylhomocysteine and puromycin. This enzyme belongs to the family of transferases, specifically those transferring ...
Ideally, the linker between the 3' end of an mRNA and the puromycin has to be flexible and long enough to allow the puromycin ... Compared to the cleavable ester bond in a tyrosyl-tRNA, puromycin has a non-hydrolysable amide bond. As a result, puromycin ... Puromycin is an analogue of the 3' end of a tyrosyl-tRNA with a part of its structure mimics a molecule of adenosine, and the ... In contrast, the puromycin DNA spacer linker used in mRNA display technology is much smaller comparing to a ribosome. This ...
Puromycin is an inhibitor of ribosomal translation. Pactamycin interrupts the binding in the Shine-Dalgarno binding region in ...
It contains resistance genes against ampicillin and puromycin. Release 1 of the TRC lentiviral shRNA libraries consist of about ...
... produces puromycin, a type of antibiotic. List of Streptomyces species A New Species of Streptomyces. C ... Feb., 1954), pages 16-23 (abstract) L. Sankaran and Burton M. Pogell (1975-12-01). "Biosynthesis of Puromycin in Streptomyces ...
Conney, AH; Gilman, AG (1963). "Puromycin inhibition of enzyme induction by 3-methylcholanthrene and phenobarbital". The ...
These include anisomycin, cycloheximide, chloramphenicol, tetracycline, streptomycin, erythromycin, and puromycin. Prokaryotic ...
This puromycin-sensitive enzyme is a Co2+-activated zinc-sialoglycoprotein. Starnes WL, Behal FJ (July 1974). "A human liver ... puromycin-sensitive aminopeptidase, soluble alanyl aminopeptidase, cytosol aminopeptidase III, alanine aminopeptidase) is an ...
It is competitive with puromycin suggesting a highly similar binding site. The first step in blasticidin S biosynthesis is the ...
U2555 modification can also intervene with transferring peptidyl-tRNA to puromycin. Furthermore, the chemical modification of ...
Vectorial discharge of peptides released by puromycin from attached ribosomes. Proc. Natl. Acad. Sci. USA 56:608-15 Redman CM, ... Vectorial discharge of peptides released by puromycin from attached ribosomes. Proc. Natl. Acad. Sci. USA 56:608-15 Adesnik M. ...
2004). "Altered expression of NDST-1 messenger RNA in puromycin aminonucleoside nephrosis". J. Lab. Clin. Med. 143 (2): 106-14 ...
Puromycin has a structure similar to that of the tyrosinyl aminoacyl-tRNA. Thus, it binds to the ribosomal A site and ... participates in peptide bond formation, producing peptidyl-puromycin. However, it does not engage in translocation and quickly ...
... implication in puromycin aminonucleoside nephrotoxicity". American Journal of Physiology. Renal Physiology. 296 (6): F1307- ...
While studying the effect of proteoglycan composition on nephritic permselectivity, it was noted that puromycin treatment of ... and puromycin affects their posttranslational modification". Am. J. Physiol. Renal Physiol. 288 (4): F748-56. doi:10.1152/ ...
2011). Puromycin-sensitive aminopeptidase (PSA/NPEPPS) impedes development of neuropathology in HPSA/TAU P301L double- ... 2010). Overexpression of puromycin sensitive aminopeptidase (PSA/NPEPPS) reduces soluble tau and delays development of ... 2009). Effect of puromycin sensitive aminopeptidase overexpression on TAU protein metabolism in vivo. Alzheimers & Dementia. 5 ...
Sankaran L, Pogell BM (December 1975). "Biosynthesis of puromycin in Streptomyces alboniger: regulation and properties of O- ... Puromycin (from S. alboniger) Streptomycin (from S. griseus) Tetracycline (from S. rimosus and S. aureofaciens) Oleandomycin ( ...
... she also published results for her research with Puromycin in multiple journals and archives. She also worked with fellow ...
L. Sankaran & Burton M. Pogell (1975-12-01). "Biosynthesis of Puromycin in Streptomyces alboniger: Regulation and Properties of ... Puromycin (Streptomyces alboniger) Spenolimycin (Streptomyces gilvospiralis) Streptomycin (Streptomyces griseus) Tetracycline ( ...
In research, commonly used PSI's include anisomycin, cycloheximide, and puromycin - although the use of puromycin has stopped ... Burka, E. R., Ballas, S. K., & Sabesin, S. M. (1975). Toxic effect of puromycin on erythrocyte membranes which is unrelated to ... Flexner LB, Flexner JB (1966). Effect of acetoxycycloheximide and of an acetoxycycloheximide-puromycin mixture on cerebral ... considering Puromycin has cytotoxic qualities, so its possible that other PSI might have similar effects that manifest in the ...
"The distribution of messenger RNA in the cytoplasm of normal and puromycin treated HeLa cells , WorldCat.org". www.worldcat.org ...
... protein breakdown-protein structure-mistranslation-amino acid analogs-puromycin). Proc Natl Acad Sci U S A. 1972 Feb;69(2):422- ... Protein breakdown-protein structure-mistranslation-amino acid analogs-puromycin)". Proceedings of the National Academy of ...
Puromycin, and Chloramphenicol". The Journal of General Physiology. 50 (3): 647-659. doi:10.1085/jgp.50.3.647. PMC 2225675. ...
One method uses compounds such as harringtonine, puromycin or lactimidomycin to stop ribosomes at translation initiation sites ...
... is a 65 kDa protein that catalyzes the formation of puromycin-sensitive 80S preinitiation complexes (Zoll et al., 2002).[ ...
... such as mRNA display where the mRNA gene is linked to the protein at the end of translation by puromycin. Alternatively the ...
An example of how antibiotics produce selective toxicity are chloramphenicol and puromycin, which inhibit the bacterial ...
... puromycin, 1,10-phenanthroline, D-phenylalanine, ACE inhibitors, DPP-4 inhibitors, and exogenous MMP inhibitors like batimastat ...
Puromycin-resistant transformants are selected in LB agar medium supplemented with 125 µg/ml of puromycin. But use of puromycin ... Puromycin is soluble in water (50 mg/ml) as colorless solution at 10 mg/ml. Puromycin is stable for one year as solution when ... Also of note, puromycin is critical in mRNA display. In this reaction, a puromycin molecule is chemically attached to the end ... Resistance to puromycin is conferred by the pac gene encoding a puromycin N-acetyl-transferase (PAC) that was found in a ...
Plasmid FASTHDR-Cterm-mClover3-Puromycin from Dr. Oscar Perezs lab is published in CRISPR J. 2021 Nov 30. doi: 10.1089/crispr. ... FASTHDR-Cterm-mClover3-Puromycin was a gift from Oscar Perez (Addgene plasmid # 167205 ; http://n2t.net/addgene:167205 ; RRID: ... arms to create homologous recombination donor vector for C-terminal gene tagging with mClover3 and selection with Puromycin ...
Start Over You searched for: Subject Puromycin âś– Remove constraint Subject: Puromycin Subject Protein Biosynthesis âś– Remove ... 1. Puromycin Inhibition of Protein Synthesis: Incorporation of Puromycin into Peptide Chains Date: [15 April 1964] ...
Tag: puromycin antibiotic. Smartphone colorimetric assay of acid phosphatase based on a controlled iodine-mediated etching of ...
PUROMYCIN INHIBITION OF PROTEIN SYNTHESIS: INCORPORATION OF PUROMYCIN INTO PEPTIDE CHAINS (English) ... PUROMYCIN INHIBITION OF PROTEIN SYNTHESIS: INCORPORATION OF PUROMYCIN INTO PEPTIDE CHAINS. scientific article ... A dissociative effect of puromycin on the pathway of protein synthesis by Ehrlich ascites tumor cells ...
Empowering cell culture and process liquid workflows
Tag: puromycin storage. Targeting ErbB3 Receptor in Cancer with Inhibitory Antibodies from LlamaTargeting ErbB3 Receptor in ...
Puromycin. Health and Medicine Reference Covering Thousands of Diseases and Prescription Drugs. ... Puromycin. Home. Diseases. Medicines. A. B. C. D. E. F. G. H. I. J. K. L. M. N. O. P. Morning-after pill. Pacerone. Paclitaxel ... Puromycin. Pyrazinamide. Pyridostigmine bromide. Pyridoxine. Pyrimethamine. Pyrithione zinc. Pyritinol. ViroPharma Incorporated ...
Tag: puromycin storage. Exosomal‑miR‑1184 derived from mesenchymal stem cells alleviates cisplatin‑associated acute kidney ...
is backordered. We will ship it separately in 10 to 15 days.. ...
... To Order Contact us: [email protected]. [Linking ... template="default" type="products" search="CHO-GFP stable cells Puromycin" header="4″ limit="82″ start="4″ showCatalogNumber=" ...
The virus contains a Puromycin antibiotic selection marker which allow to select the positive transduced cells. ...
This lentivirus also contain the Puromycin selection marker under the constitutive RSV promoter for antibiotic selection. See ...
University of Maine , Orono, ME 04469 , 207.581.1865 ...
CRISPR TGS, pINT-ALL-EFS-Puromycin, Glycerol stock, species Mouse. Save 0 ...
Puromycin Dihydrochloride is an aminonucleoside antibiotic produced by Streptomyces alboniger. It inhibits peptidyl transfer on ... Puromycin works by inhibiting peptidyl transfer on both prokaryotic and eukaryotic ribosomes; resistance is conferred by the ...
Puromycin (Stylomycin) * is an antibiotic obtained from a species of actinomycete, Streptomyces albo-niger.† In addition to its ... Clinical Evaluation of Puromycin in Human neoplastic Disease. JANE C. WRIGHT, M.D.; VERA B. DOLGOPOL, M.D.; MYRA LOGAN, M.D.; ... Clinical Evaluation of Puromycin in Human neoplastic Disease. AMA Arch Intern Med. 1955;96(1):61-77. doi:10.1001/archinte. ... Puromycin (Stylomycin) * is an antibiotic obtained from a species of actinomycete, Streptomyces albo-niger.† In addition to its ...
Puromycin titer. * P24 titer by ELISA. * USP sterility / mycoplasma / endotoxin. Add-On Services. * Vector concentration (ultra ...
We studied a model of experimental tubulointerstitial nephritis associated with puromycin aminonucleoside (PAN) nephrosis. ...
... puromycin acetyltransferase, ITRs, inverted terminal repeats. We designed GLoPro to have inducible expression to prevent ...
Specific inhibitors of puromycin-sensitive aminopeptidase with a 3-(halogenated phenyl)-2,4(1H,3H)-quinazolinedione skeleton. ... Specific inhibitors of puromycin-sensitive aminopeptidase with a 3-(halogenated phenyl)-2,4(1H,3H)-quinazolinedione skeleton. ... Specific inhibitors of puromycin-sensitive aminopeptidase with a 3-(halogenated phenyl)-2,4(1H,3H)-quinazolinedione skeleton. ... N2 - Specific puromycin-sensitive aminopeptidase (PSA) inhibitors with a 3-(halogenated phenyl)-2,4(1H,3H)-quinazolinedione ...
Nephrotic syndrome induced by puromycin aminonucleoside (PAN) in rats reproduces the biological and clinical signs of the human ... Over-expression of adenosine deaminase in mouse podocytes does not reverse puromycin aminonucleoside resistance. Access & ...
puromycin-insensitive leucyl-specific aminopeptidase. *type 1 tumor necrosis factor receptor shedding aminopeptidase regulator ...
involved_in cellular response to puromycin IEA Inferred from Electronic Annotation. more info ...
Puromycin selection was applied for approximately 6-8 days. Resistant clones were picked and cultured for downstream ...
Antibiotic Selection Markers (Puromycin, Neomycin, Hygromycin, etc.). * The mir-E vector panel is linked here so you may see ...
In rat models, puromycin aminonucleoside (PAN) or cisplatin (CDDP) induce glomerular and proximal tubular injuries, ... Puromycin, Doxorubicin (glomerular toxicants); Lithium, Furosemide (tubular and collecting duct toxicants); α-Naphthyl ...
Expresses human NEUROGENIN2 (hNGN2), eGFP and puromycin resistance gene under control of TetON promoter. This 3rd generation ...
  • Puromycin is an aminonucleoside antibiotic, derived from the Streptomyces alboniger bacterium, that causes premature chain termination during translation taking place in the ribosome. (wikipedia.org)
  • The biosynthetic pathway of the aminonucleoside antibiotic puromycin, as deduced from the molecular analysis of the pur cluster of Streptomyces alboniger. (kegg.jp)
  • This lentivirus also contain the Puromycin selection marker under the constitutive RSV promoter for antibiotic selection. (gentarget.com)
  • The mechanism of inhibition is not well understood, however puromycin can be used to distinguish between aminopeptidase M (active) and cytosol alanyl aminopeptidase (inhibited by puromycin). (wikipedia.org)
  • Puromycin shows appreciable inhibition against the mammary adenocarcinoma of the C3H mouse, the mammary adenocarcinoma 755 of the C57BL mouse, and a glioblastoma cultivated in the chick embryo. (jamanetwork.com)
  • Puromycin is a reversible inhibitor of dipeptidyl-peptidase II (serine peptidase) and cytosol alanyl aminopeptidase (metallopeptidase). (wikipedia.org)
  • Specific puromycin-sensitive aminopeptidase (PSA) inhibitors with a 3-(halogenated phenyl)-2,4(1H,3H)-quinazolinedione skeleton were prepared and their structure-activity relationships were investigated. (elsevierpure.com)
  • Resistance to puromycin is conferred by the pac gene encoding a puromycin N-acetyl-transferase (PAC) that was found in a Streptomyces producer strain. (wikipedia.org)
  • Plates containing puromycin are stable for 1 month when stored at 4 °C.[citation needed] Puromycin resistance in yeast can also be conferred through expression of the puromycin N-acetyl-transferase (pac) gene. (wikipedia.org)
  • Expresses human NEUROGENIN2 (hNGN2), eGFP and puromycin resistance gene under control of TetON promoter. (addgene.org)
  • Puromycin (Stylomycin) * is an antibiotic obtained from a species of actinomycete, Streptomyces albo-niger. (jamanetwork.com)
  • Deletion of the gene encoding the multidrug efflux pump Pdr5 sensitizes cells to puromycin. (wikipedia.org)
  • Puromycin is stable for one year as solution when stored at -20 °C. The recommended dose as a selection agent in cell cultures is within a range of 1-10 ÎĽg/ml, although it can be toxic to eukaryotic cells at concentrations as low as 1 ÎĽg/ml. (wikipedia.org)
  • But use of puromycin for E. coli selection requires precise pH adjustment and also depends on which strain is selected. (wikipedia.org)
  • For hassle-free selection and optimum results the use of specially modified puromycin is possible. (wikipedia.org)
  • citation needed] Puromycin is poorly active on E. coli. (wikipedia.org)
  • Also of note, puromycin is critical in mRNA display. (wikipedia.org)
  • In this reaction, a puromycin molecule is chemically attached to the end of an mRNA template, which is then translated into protein. (wikipedia.org)
  • The puromycin can then form a covalent link to the growing peptide chain allowing the mRNA to be physically linked to its translational product. (wikipedia.org)
  • As puromycin inhibits protein synthesis in eukaryotic cells, researchers were able to show that injections of this drug will result in both short-term as well as long-term memory loss in mice. (wikipedia.org)
  • Toxicity studies in mice indicate the LD 50 values of puromycin to be 360 mg/kg. (jamanetwork.com)
  • Puromycin acts quickly and can kill up to 99% of nonresistant cells within 2 days. (wikipedia.org)
  • WRIGHT JC , DOLGOPOL VB , LOGAN M , PRIGOT A , WRIGHT LT. Clinical Evaluation of Puromycin in Human neoplastic Disease. (jamanetwork.com)
  • Puromycin is soluble in water (50 mg/ml) as colorless solution at 10 mg/ml. (wikipedia.org)
  • Puromycin is an antibiotic protein synthesis inhibitor which causes premature chain termination during translation. (wikipedia.org)
  • Puromycin is an aminonucleoside antibiotic, derived from the Streptomyces alboniger bacterium, that causes premature chain termination during translation taking place in the ribosome. (wikipedia.org)
  • Puromycin dihydrochloride is a aminonuclease antibiotic that inhibits protein synthesis. (openwetware.org)
  • Prior to using the puromycin antibiotic, titrate the selection agent to determine the optimal concentration for target cell line. (openwetware.org)
  • The minimum antibiotic concentration to use is the lowest concentration that kills 100% of the cells in 3-5 days from the start of puromycin selection. (openwetware.org)
  • Puromycin is an aminonucleoside antibiotic that causes early chain termination within the ribosome during translation. (goldbio.com)
  • Puromycin Hydrochloride Solution is the hydrochloride salt form of puromycin, an aminonuclease antibiotic agent isolated from the bacterium Streptomyces alboniger. (canvaxbiotech.com)
  • The RPM is based on ribosome-catalyzed puromycylation of nascent chains immobilized on ribosomes by antibiotic chain elongation inhibitors followed by detection of puromycylated ribosome-bound nascent chains with a puromycin (PMY)-specific monoclonal antibody in fixed and permeabilized cells. (nih.gov)
  • Ampicillin and puromycin antibiotic resistance genes provide selection in bacterial or mammalian cells respectively. (sigmaaldrich.com)
  • As puromycin inhibits protein synthesis in eukaryotic cells, researchers were able to show that injections of this drug will result in both short-term as well as long-term memory loss in mice. (wikipedia.org)
  • Here, we demonstrated the C-terminus-specific fluorescence labeling of histidine-tagged thrombopoietin (TPO), a ligand for Mpl, with desthiobiotin-tagged fluorescent puromycin. (elsevierpure.com)
  • Its gene product is puromycin-N-acetyl-transferase which inactivates puromycin through acetylation. (goldbio.com)
  • Puromycin is soluble in water (50 mg/ml) as colorless solution at 10 mg/ml. (wikipedia.org)
  • Puromycin is soluble in water and is often used as a selective agent in molecular biology research. (goldbio.com)
  • Lentiviral vector-human synapsin 1 promoter, Puro contains Multiple Cloning Sites (MCS) downstream of the human synapsin 1 promoter, and a puromycin selection marker driven by the PGK promoter. (cellomicstech.com)
  • GenTargetDescription:Pre-made lentiviral particles expressing nuclear permeable CRE recombinase under EF1a promoter with puromycin marker. (reportergene.com)
  • GenTargetDescription:Pre-made lentiviral particles expressing nuclear permeable CRE recombinase under EF1a promoter with Puromycin marker, provided in DMEM medium with 10% FBS.Storage conditions: (-80°C) Shipping. (reportergene.com)
  • 48 hours post- shRNA transfection , aspirate the medium and replace with fresh medium containing puromycin at the appropriate concentration. (openwetware.org)
  • Tumor necrosis factor receptor-associated factor 6 (TRAF6) plays a role in diffuse large B cell lymphoma (DLBCL) biological processes.TRAF6 Stable Knockdown HT Cell Line was generated via lentivirus transduction with TRAF6 shRNA plasmids, and the transfectant was selected with puromycin. (topsan.org)
  • The growth of bacteria, protozoa, algae and mammalian cells is quickly halted by puromycin. (goldbio.com)
  • T6411HEK293T cells were tranfected with pGIPZ lentiviral shRNAs targeting PC4, and were selected with 3 µg/ml puromycin to establish the PC4 Knockdown. (topsan.org)
  • In this reaction, a puromycin molecule is chemically attached to the end of an mRNA template, which is then translated into protein. (wikipedia.org)
  • Acting as an analog of the 3′ terminal end of aminoacyl-tRNA, puromycin incorporates itself into a growing polypeptide chain and causes its premature termination, thereby inhibiting protein synthesis. (canvaxbiotech.com)
  • Puromycin labeling does not allow protein synthesis to be measured in energy-starved cells. (nih.gov)
  • 6. Effect of a low-protein diet on expression of non-muscle type myosin heavy-chain isoforms in glomeruli of rats with puromycin aminonucleoside nephrosis. (nih.gov)
  • Lot-to-lot variations in potency exist for all selection antibiotics, each new lot of puromycin should be titrated. (openwetware.org)
  • Puromycin is stable for one year as solution when stored at -20 °C. The recommended dose as a selection agent in cell cultures is within a range of 1-10 ÎĽg/ml, although it can be toxic to eukaryotic cells at concentrations as low as 1 ÎĽg/ml. (wikipedia.org)
  • Lethal concentrations of puromycin are much higher for strains of Saccharomyces cerevisiae than mammalian cell lines. (wikipedia.org)
  • Puromycin is used in cell biology as a selective agent in cell culture systems. (wikipedia.org)
  • 8. Key molecular events in puromycin aminonucleoside nephrosis rats. (nih.gov)
  • 7. Altered expression of NDST-1 messenger RNA in puromycin aminonucleoside nephrosis. (nih.gov)
  • 13. Impact of cyclosporin on podocyte ZO-1 expression in puromycin aminonucleoside nephrosis rats. (nih.gov)
  • The puromycin can then form a covalent link to the growing peptide chain allowing the mRNA to be physically linked to its translational product. (wikipedia.org)
  • For hassle-free selection and optimum results the use of specially modified puromycin is possible. (wikipedia.org)
  • The cell populations were selected with puromycin and then differentiated for 7 days to form myotubes. (nih.gov)
  • Following puromycin removal, low-level latent infection was maintained. (nih.gov)
  • Also of note, puromycin is critical in mRNA display. (wikipedia.org)
  • The working puromycin concentration for mammalian cell lines ranges from 1-10 µg/ml. (openwetware.org)
  • Research has shown puromycin to be effective against certain tumors. (goldbio.com)
  • Iodoquinol, puromycin, and nitazoxanide are also effective against balantidiasis. (medscape.com)
  • Link to all annotated objects annotated to puromycin metabolic process. (planteome.org)
  • Link to all direct and indirect annotations to puromycin metabolic process. (planteome.org)
  • Puromycin-resistant transformants are selected in LB agar medium supplemented with 125 µg/ml of puromycin. (wikipedia.org)