An antibiotic isolated from various Streptomyces species. It interferes with protein and DNA synthesis by inhibiting peptidyl transferase or the 80S ribosome system.
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 mitogen-activated protein kinase subfamily that regulates a variety of cellular processes including CELL GROWTH PROCESSES; CELL DIFFERENTIATION; APOPTOSIS; and cellular responses to INFLAMMATION. The P38 MAP kinases are regulated by CYTOKINE RECEPTORS and can be activated in response to bacterial pathogens.
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.
A superfamily of PROTEIN-SERINE-THREONINE KINASES that are activated by diverse stimuli via protein kinase cascades. They are the final components of the cascades, activated by phosphorylation by MITOGEN-ACTIVATED PROTEIN KINASE KINASES, which in turn are activated by mitogen-activated protein kinase kinase kinases (MAP KINASE KINASE KINASES).
Compounds that inhibit cell production of DNA or RNA.
Compounds or factors that act on a specific enzyme to increase its activity.
A subgroup of mitogen-activated protein kinases that activate TRANSCRIPTION FACTOR AP-1 via the phosphorylation of C-JUN PROTEINS. They are components of intracellular signaling pathways that regulate CELL PROLIFERATION; APOPTOSIS; and CELL DIFFERENTIATION.
Antibiotic substance isolated from streptomycin-producing strains of Streptomyces griseus. It acts by inhibiting elongation during protein synthesis.
Pyrrolidines are saturated, heterocyclic organic compounds containing a five-membered ring with four carbon atoms and one nitrogen atom (NRCH2CH2), commonly found as structural components in various alkaloids and used in the synthesis of pharmaceuticals and other organic materials.
An antitumor antibiotic produced by Streptomyces sparsogenes. It inhibits protein synthesis in 70S and 80S ribosomal systems.
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.
The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
Antifungal metabolite from several fungi, mainly Trichoderma viride; inhibits protein synthesis by binding to ribosomes; proposed as antifungal and antineoplastic; used as tool in cellular biochemistry.
Compounds containing 1,3-diazole, a five membered aromatic ring containing two nitrogen atoms separated by one of the carbons. Chemically reduced ones include IMIDAZOLINES and IMIDAZOLIDINES. Distinguish from 1,2-diazole (PYRAZOLES).
Middle portion of the hypothalamus containing the arcuate, dorsomedial, ventromedial nuclei, the TUBER CINEREUM and the PITUITARY GLAND.
Compounds with a six membered aromatic ring containing NITROGEN. The saturated version is PIPERIDINES.
Antibiotic produced by Streptomyces pactum used as an antineoplastic agent. It is also used as a tool in biochemistry because it inhibits certain steps in protein synthesis.
A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. This enzyme is also sometimes dependent on CALCIUM. A wide range of proteins can act as acceptor, including VIMENTIN; SYNAPSINS; GLYCOGEN SYNTHASE; MYOSIN LIGHT CHAINS; and the MICROTUBULE-ASSOCIATED PROTEINS. (From Enzyme Nomenclature, 1992, p277)
A serine-threonine protein kinase family whose members are components in protein kinase cascades activated by diverse stimuli. These MAPK kinases phosphorylate MITOGEN-ACTIVATED PROTEIN KINASES and are themselves phosphorylated by MAP KINASE KINASE KINASES. JNK kinases (also known as SAPK kinases) are a subfamily.
A mitogen-activated protein kinase kinase with specificity for JNK MITOGEN-ACTIVATED PROTEIN KINASES; P38 MITOGEN-ACTIVATED PROTEIN KINASES and the RETINOID X RECEPTORS. It takes part in a SIGNAL TRANSDUCTION pathway that is activated in response to cellular stress.
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.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
Complex mental function having four distinct phases: (1) memorizing or learning, (2) retention, (3) recall, and (4) recognition. Clinically, it is usually subdivided into immediate, recent, and remote memory.
Pathologic partial or complete loss of the ability to recall past experiences (AMNESIA, RETROGRADE) or to form new memories (AMNESIA, ANTEROGRADE). This condition may be of organic or psychologic origin. Organic forms of amnesia are usually associated with dysfunction of the DIENCEPHALON or HIPPOCAMPUS. (From Adams et al., Principles of Neurology, 6th ed, pp426-7)
Inorganic salts or organic esters of arsenious acid.
The profession of writing. Also the identity of the writer as the creator of a literary production.
A proline-directed serine/threonine protein kinase which mediates signal transduction from the cell surface to the nucleus. Activation of the enzyme by phosphorylation leads to its translocation into the nucleus where it acts upon specific transcription factors. p40 MAPK and p41 MAPK are isoforms.
Mitogen-activated protein kinase kinase kinases (MAPKKKs) are serine-threonine protein kinases that initiate protein kinase signaling cascades. They phosphorylate MITOGEN-ACTIVATED PROTEIN KINASE KINASES; (MAPKKs) which in turn phosphorylate MITOGEN-ACTIVATED PROTEIN KINASES; (MAPKs).
An intracellular signaling system involving the MAP kinase cascades (three-membered protein kinase cascades). Various upstream activators, which act in response to extracellular stimuli, trigger the cascades by activating the first member of a cascade, MAP KINASE KINASE KINASES; (MAPKKKs). Activated MAPKKKs phosphorylate MITOGEN-ACTIVATED PROTEIN KINASE KINASES which in turn phosphorylate the MITOGEN-ACTIVATED PROTEIN KINASES; (MAPKs). The MAPKs then act on various downstream targets to affect gene expression. In mammals, there are several distinct MAP kinase pathways including the ERK (extracellular signal-regulated kinase) pathway, the SAPK/JNK (stress-activated protein kinase/c-jun kinase) pathway, and the p38 kinase pathway. There is some sharing of components among the pathways depending on which stimulus originates activation of the cascade.

SHIP is a negative regulator of growth factor receptor-mediated PKB/Akt activation and myeloid cell survival. (1/511)

SHIP is an inositol 5' phosphatase that hydrolyzes the PI3'K product PI(3,4,5)P3. We show that SHIP-deficient mice exhibit dramatic chronic hyperplasia of myeloid cells resulting in splenomegaly, lymphadenopathy, and myeloid infiltration of vital organs. Neutrophils and bone marrow-derived mast cells from SHIP-/- mice are less susceptible to programmed cell death induced by various apoptotic stimuli or by growth factor withdrawal. Engagement of IL3-R and GM-CSF-R in these cells leads to increased and prolonged PI3'K-dependent PI(3,4,5)P3 accumulation and PKB activation. These data indicate that SHIP is a negative regulator of growth factor-mediated PKB activation and myeloid cell survival.  (+info)

Ischemic preconditioning depends on interaction between mitochondrial KATP channels and actin cytoskeleton. (2/511)

Both mitochondrial ATP-sensitive K+ (KATP) channels and the actin cytoskeleton have been proposed to be end-effectors in ischemic preconditioning (PC). For evaluation of the participation of these proposed end effectors, rabbits underwent 30 min of regional ischemia and 3 h of reperfusion. PC by 5-min ischemia + 10-min reperfusion reduced infarct size by 60%. Diazoxide, a mitochondrial KATP-channel opener, administered before ischemia was protective. Protection was lost when diazoxide was given after onset of ischemia. Anisomycin, a p38/JNK activator, reduced infarct size, but protection from both diazoxide and anisomycin was abolished by 5-hydroxydecanoate (5-HD), an inhibitor of mitochondrial KATP channels. Isolated adult rabbit cardiomyocytes were subjected to simulated ischemia by centrifuging the cells into an oxygen-free pellet for 3 h. PC was induced by prior pelleting for 10 min followed by resuspension for 15 min. Osmotic fragility was assessed by adding cells to hypotonic (85 mosmol) Trypan blue. PC delayed the progressive increase in fragility seen in non-PC cells. Incubation with diazoxide or pinacidil was as protective as PC. Anisomycin reduced osmotic fragility, and this was reversed by 5-HD. Interestingly, protection by PC, diazoxide, and pinacidil could be abolished by disruption of the cytoskeleton by cytochalasin D. These data support a role for both mitochondrial KATP channels and cytoskeletal actin in protection by PC.  (+info)

On the complexities of ceramide changes in cells undergoing apoptosis: lack of evidence for a second messenger function in apoptotic induction. (3/511)

The generation of cellular ceramides as a second messenger has been implicated as a regulatory and required step for the induction of apoptosis. In this study, we have applied a recently developed mass spectrometric technique to the determination of changes in physiological ceramide levels during apoptosis induced by tumor necrosis factor plus cycloheximide in U937 cells and the chemical agents anisomycin or geranylgeraniol in HL-60 cells. The mass spectrometric method has significant advantages over traditional methods for ceramide quantitation in that it determines the relative abundance of all ceramide species present in complex biological lipid mixtures individually and simultaneously. We quantitiated ceramides ranging from C14 to C26, finding that their basal levels and relative distribution varied significantly, both within and between different cell types. However, we were not able to detect any significant changes in either total ceramide content or species distribution until 1 h or more post-stimulation with any of these treatments, by which time the cells were in an advanced stage of apoptosis. Differences were also seen between all three treatments in the ceramide species distribution observed in these late stages of apoptosis. These data indicate that in vivo ceramide generation occurs as a consequence of apoptosis rather than as an essential second messenger involved in its induction. They also pose new questions about the potential roles that certain ceramide species may play in the late stages of apoptosis, and demonstrate a clear need to utilize the resolving power of mass spectrometry-based assays in any future investigations into the biological function of ceramides.  (+info)

Trichothecene mycotoxins trigger a ribotoxic stress response that activates c-Jun N-terminal kinase and p38 mitogen-activated protein kinase and induces apoptosis. (4/511)

The trichothecene family of mycotoxins inhibit protein synthesis by binding to the ribosomal peptidyltransferase site. Inhibitors of the peptidyltransferase reaction (e.g. anisomycin) can trigger a ribotoxic stress response that activates c-Jun N-terminal kinase (JNK)/p38 mitogen-activated protein kinases, components of a signaling cascade that regulates cell survival in response to stress. We have found that selected trichothecenes strongly activate JNK/p38 kinases and induce rapid apoptosis in Jurkat T cells. Although the ability of individual trichothecenes to inhibit protein synthesis and activate JNK/p38 kinases are dissociable, both effects contribute to the induction of apoptosis. Among trichothecenes that strongly activate JNK/p38 kinases, induction of apoptosis increases linearly with inhibition of protein synthesis. Among trichothecenes that strongly inhibit protein synthesis, induction of apoptosis increases linearly with activation of JNK/p38 kinases. Trichothecenes that inhibit protein synthesis without activating JNK/p38 kinases inhibit the function (i.e. activation of JNK/p38 kinases and induction of apoptosis) of apoptotic trichothecenes and anisomycin. Harringtonine, a structurally unrelated protein synthesis inhibitor that competes with trichothecenes (and anisomycin) for ribosome binding, also inhibits the activation of JNK/p38 kinases and induction of apoptosis by trichothecenes and anisomycin. Taken together, these results implicate the peptidyltransferase site as a regulator of both JNK/p38 kinase activation and apoptosis.  (+info)

Translational homeostasis: eukaryotic translation initiation factor 4E control of 4E-binding protein 1 and p70 S6 kinase activities. (5/511)

Eukaryotic translation initiation factor 4E (eIF4E) is the mRNA 5' cap binding protein, which plays an important role in the control of translation. The activity of eIF4E is regulated by a family of repressor proteins, the 4E-binding proteins (4E-BPs), whose binding to eIF4E is determined by their phosphorylation state. When hyperphosphorylated, 4E-BPs do not bind to eIF4E. Phosphorylation of the 4E-BPs is effected by the phosphatidylinositol (PI) 3-kinase signal transduction pathway and is inhibited by rapamycin through its binding to FRAP/mTOR (FK506 binding protein-rapamycin-associated protein or mammalian target of rapamycin). Phosphorylation of 4E-BPs can also be induced by protein synthesis inhibitors. These observations led to the proposal that FRAP/mTOR functions as a "sensor" of the translational apparatus (E. J. Brown and S. L. Schreiber, Cell 86:517-520, 1996). To test this model, we have employed the tetracycline-inducible system to increase eIF4E expression. Removal of tetracycline induced eIF4E expression up to fivefold over endogenous levels. Strikingly, upon induction of eIF4E, 4E-BP1 became dephosphorylated and the extent of dephosphorylation was proportional to the expression level of eIF4E. Dephosphorylation of p70(S6k) also occurred upon eIF4E induction. In contrast, the phosphorylation of Akt, an upstream effector of both p70(S6k) and 4E-BP phosphorylation, was not affected by eIF4E induction. We conclude that eIF4E engenders a negative feedback loop that targets a component of the PI 3-kinase signalling pathway which lies downstream of PI 3-kinase.  (+info)

Tri-iodothyronine increases insulin-like growth factor binding protein-2 expression in cultured hepatocytes from hypothyroid rats. (6/511)

Previous evidence suggests the existence of a thyroid hormone-IGF axis in the liver and changes in hepatic insulin-like growth factor binding protein (IGFBP) expression in rats with altered thyroid status have been previously reported. The aim of this study was to check if the higher IGFBP-2 mRNA levels observed in liver of hypothyroid rats could be due to a direct effect of thyroid hormone on the IGFBP-2 gene. In our experiments, cultured hepatocytes isolated from normal and hypothyroid adult rats were used. Northern blot analysis revealed barely detectable IGFBP-2 mRNA in normal rat hepatocytes, but easily detectable signal in hypothyroid rat cells. Therefore, the effect of tri-iodothyronine (T3) was investigated using cultured hepatocytes from hypothyroid rats as an in vitro model. The IGFBP-2 message was increased in a dose-dependent manner in hepatocytes cultured for 12-24 h in the presence of T3. A similar increase occurred in accumulation of IGFBP-2 in the culture medium, as measured by RIA. The effect of T3 on IGFBP-2 transcript levels appeared to consist of enhanced gene transcription and was independent of ongoing protein synthesis, but it was completely abolished by the incubation of hepatocytes with insulin. The latter result confirmed the dominant role of insulin in regulating IGFBP-2 expression by cultured hepatocytes. In vivo experiments confirmed an increase in hepatic IGFBP-2 mRNA and serum IGFBP-2 levels in hypothyroid rats and demonstrated, in addition, a significant increase in these measures in T3-treated rats. Taken together, our in vitro and in vivo results support a role for a thyroid hormone-IGF axis in the liver and suggest that other factors, such as insulin, interact in vivo with thryoid hormone in regulating hepatic IGFBP-2 expression.  (+info)

MEK kinase 3 directly activates MKK6 and MKK7, specific activators of the p38 and c-Jun NH2-terminal kinases. (7/511)

Mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase kinase kinase 3 (MEKK3) activates the c-Jun NH2-terminal kinase (JNK) pathway, although no substrates for MEKK3 have been identified. We have examined the regulation by MEKK3 of MAPK kinase 7 (MKK7) and MKK6, two novel MAPK kinases specific for JNK and p38, respectively. Coexpression of MKK7 with MEKK3 in COS-7 cells enhanced MKK7 autophosphorylation and its ability to activate recombinant JNK1 in vitro. MKK6 autophosphorylation and in vitro activation of p38alpha were also observed following coexpression of MKK6 with MEKK3. MEKK2, a closely related homologue of MEKK3, also activated MKK7 and MKK6 in COS-7 cells. Importantly, immunoprecipitates of either MEKK3 or MEKK2 directly activated recombinant MKK7 and MKK6 in vitro. These data identify MEKK3 as a MAPK kinase kinase specific for MKK7 and MKK6 in the JNK and p38 pathways. We have also examined whether MEKK3 or MEKK2 activates p38 in intact cells using MAPK-activated protein kinase-2 (MAPKAPK2) as an affinity ligand and substrate. Anisomycin, sorbitol, or the expression of MEKK3 in HEK293 cells enhanced MAPKAPK2 phosphorylation, whereas MEKK2 was less effective. Furthermore, MAPKAPK2 phosphorylation induced by MEKK3 or cellular stress was abolished by the p38 inhibitor SB-203580, suggesting that MEKK3 is coupled to p38 activation in intact cells.  (+info)

Use of a drug-resistant mutant of stress-activated protein kinase 2a/p38 to validate the in vivo specificity of SB 203580. (8/511)

Stress-activated protein kinase 2a, also called p38, is inhibited by SB 203580 and this drug has been used widely to implicate this enzyme in the regulation of many physiological processes. Here, we introduce a novel method of general application, which can be used to establish whether the effects of SB 203580 are mediated via inhibition of stress-activated protein kinase 2a/p38 or whether they result from 'non-specific' effects. Four events thought to occur upon activation of stress-activated protein kinase 2a/p38 have been established unequivocally. These are the activation of mitogen-activated protein kinase-activated protein kinase-2 and mitogen- and stress-activated protein kinase-1 and the phosphorylation of their presumed substrates, heat shock protein 27 and the transcription factor cyclic AMP response element binding protein, respectively. In contrast, the SB 203580-induced activation of c-Raf is independent of stress-activated protein kinase 2a/p38 inhibition.  (+info)

Anisomycin is an antibiotic derived from the bacterium Streptomyces griseolus. It is a potent inhibitor of protein synthesis and has been found to have antitumor, antiviral, and immunosuppressive properties. In medicine, it has been used experimentally in the treatment of some types of cancer, but its use is limited due to its significant side effects, including neurotoxicity.

In a medical or scientific context, 'anisomycin' refers specifically to this antibiotic compound and not to any general concept related to aniso- (meaning "unequal" or "asymmetrical") or -mycin (suffix indicating a bacterial antibiotic).

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.

p38 Mitogen-Activated Protein Kinases (p38 MAPKs) are a family of conserved serine-threonine protein kinases that play crucial roles in various cellular processes, including inflammation, immune response, differentiation, apoptosis, and stress responses. They are activated by diverse stimuli such as cytokines, ultraviolet radiation, heat shock, osmotic stress, and lipopolysaccharides (LPS).

Once activated, p38 MAPKs phosphorylate and regulate several downstream targets, including transcription factors and other protein kinases. This regulation leads to the expression of genes involved in inflammation, cell cycle arrest, and apoptosis. Dysregulation of p38 MAPK signaling has been implicated in various diseases, such as cancer, neurodegenerative disorders, and autoimmune diseases. Therefore, p38 MAPKs are considered promising targets for developing new therapeutic strategies to treat these conditions.

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.

Mitogen-Activated Protein Kinases (MAPKs) are a family of serine/threonine protein kinases that play crucial roles in various cellular processes, including proliferation, differentiation, transformation, and apoptosis, in response to diverse stimuli such as mitogens, growth factors, hormones, cytokines, and environmental stresses. They are highly conserved across eukaryotes and consist of a three-tiered kinase module composed of MAPK kinase kinases (MAP3Ks), MAPK kinases (MKKs or MAP2Ks), and MAPKs.

Activation of MAPKs occurs through a sequential phosphorylation and activation cascade, where MAP3Ks phosphorylate and activate MKKs, which in turn phosphorylate and activate MAPKs at specific residues (Thr-X-Tyr or Ser-Pro motifs). Once activated, MAPKs can further phosphorylate and regulate various downstream targets, including transcription factors and other protein kinases.

There are four major groups of MAPKs in mammals: extracellular signal-regulated kinases (ERK1/2), c-Jun N-terminal kinases (JNK1/2/3), p38 MAPKs (p38α/β/γ/δ), and ERK5/BMK1. Each group of MAPKs has distinct upstream activators, downstream targets, and cellular functions, allowing for a high degree of specificity in signal transduction and cellular responses. Dysregulation of MAPK signaling pathways has been implicated in various human diseases, including cancer, diabetes, neurodegenerative disorders, and inflammatory diseases.

Nucleic acid synthesis inhibitors are a class of antimicrobial, antiviral, or antitumor agents that block the synthesis of nucleic acids (DNA or RNA) by interfering with enzymes involved in their replication. These drugs can target various stages of nucleic acid synthesis, including DNA transcription, replication, and repair, as well as RNA transcription and processing.

Examples of nucleic acid synthesis inhibitors include:

1. Antibiotics like quinolones (e.g., ciprofloxacin), rifamycins (e.g., rifampin), and trimethoprim, which target bacterial DNA gyrase, RNA polymerase, or dihydrofolate reductase, respectively.
2. Antiviral drugs like reverse transcriptase inhibitors (e.g., zidovudine, lamivudine) and integrase strand transfer inhibitors (e.g., raltegravir), which target HIV replication by interfering with viral enzymes required for DNA synthesis.
3. Antitumor drugs like antimetabolites (e.g., methotrexate, 5-fluorouracil) and topoisomerase inhibitors (e.g., etoposide, doxorubicin), which interfere with DNA replication and repair in cancer cells.

These drugs have been widely used for treating various bacterial and viral infections, as well as cancers, due to their ability to selectively inhibit the growth of target cells without affecting normal cellular functions significantly. However, they may also cause side effects related to their mechanism of action or off-target effects on non-target cells.

Enzyme activators, also known as allosteric activators or positive allosteric modulators, are molecules that bind to an enzyme at a site other than the active site, which is the site where the substrate typically binds. This separate binding site is called the allosteric site. When an enzyme activator binds to this site, it changes the shape or conformation of the enzyme, which in turn alters the shape of the active site. As a result, the affinity of the substrate for the active site increases, leading to an increase in the rate of the enzymatic reaction.

Enzyme activators play important roles in regulating various biological processes within the body. They can be used to enhance the activity of enzymes that are involved in the production of certain hormones or neurotransmitters, for example. Additionally, enzyme activators may be useful as therapeutic agents for treating diseases caused by deficiencies in enzyme activity.

It's worth noting that there are also molecules called enzyme inhibitors, which bind to an enzyme and decrease its activity. These can be either competitive or non-competitive, depending on whether they bind to the active site or an allosteric site, respectively. Understanding the mechanisms of both enzyme activators and inhibitors is crucial for developing drugs and therapies that target specific enzymes involved in various diseases and conditions.

JNK (c-Jun N-terminal kinase) Mitogen-Activated Protein Kinases are a subgroup of the Ser/Thr protein kinases that are activated by stress stimuli and play important roles in various cellular processes, including inflammation, apoptosis, and differentiation. They are involved in the regulation of gene expression through phosphorylation of transcription factors such as c-Jun. JNKs are activated by a variety of upstream kinases, including MAP2Ks (MKK4/SEK1 and MKK7), which are in turn activated by MAP3Ks (such as ASK1, MEKK1, MLKs, and TAK1). JNK signaling pathways have been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory diseases.

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.

Pyrrolidines are not a medical term per se, but they are a chemical compound that can be encountered in the field of medicine and pharmacology. Pyrrolidine is an organic compound with the molecular formula (CH2)4NH. It is a cyclic secondary amine, which means it contains a nitrogen atom surrounded by four carbon atoms in a ring structure.

Pyrrolidines can be found in certain natural substances and are also synthesized for use in pharmaceuticals and research. They have been used as building blocks in the synthesis of various drugs, including some muscle relaxants, antipsychotics, and antihistamines. Additionally, pyrrolidine derivatives can be found in certain plants and fungi, where they may contribute to biological activity or toxicity.

It is important to note that while pyrrolidines themselves are not a medical condition or diagnosis, understanding their chemical properties and uses can be relevant to the study and development of medications.

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."

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.

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.

I'm sorry for any confusion, but "Trichodermin" is not a widely recognized term in medical terminology. It is, however, a secondary metabolite produced by some species of fungi, specifically certain types of Trichoderma. It has been studied for its antimicrobial properties, particularly against other fungi. But it's not a term commonly used in medical contexts. If you have any more questions or need information on a different medical topic, I'd be happy to help!

Imidazoles are a class of heterocyclic organic compounds that contain a double-bonded nitrogen atom and two additional nitrogen atoms in the ring. They have the chemical formula C3H4N2. In a medical context, imidazoles are commonly used as antifungal agents. Some examples of imidazole-derived antifungals include clotrimazole, miconazole, and ketoconazole. These medications work by inhibiting the synthesis of ergosterol, a key component of fungal cell membranes, leading to increased permeability and death of the fungal cells. Imidazoles may also have anti-inflammatory, antibacterial, and anticancer properties.

I believe you may be referring to the "ventral" part of the hypothalamus, as there isn't a widely recognized anatomical division called the "middle" hypothalamus. The ventral hypothalamus is a region that contains several critical structures, including:

1. The infundibular stem: This is a funnel-shaped structure that extends downward from the hypothalamus and forms the beginning of the pituitary stalk. It contains tuber cinereum and the median eminence.
2. Tuber cinereum: A region with several nuclei, including the arcuate nucleus, which plays a role in regulating feeding behavior, growth hormone release, and sexual function.
3. Median eminence: A crucial area where the hypothalamus interacts with the pituitary gland. It contains nerve terminals that release neurohormones into the portal capillaries, which then carry these substances to the anterior pituitary to regulate hormone secretion.

The ventral hypothalamus is essential for various functions, such as releasing and inhibiting hormones, regulating body temperature, hunger, thirst, sleep, emotional behavior, and parental behaviors.

I'm sorry for any confusion, but "Pyridines" is not a medical term. It is a chemical term that refers to a class of organic compounds with the chemical structure of a six-membered ring containing one nitrogen atom and five carbon atoms (heterocyclic aromatic compound).

In a biological or medical context, pyridine derivatives can be found in various natural and synthetic substances. For example, some medications contain pyridine rings as part of their chemical structure. However, "Pyridines" itself is not a medical term or condition.

Pactamycin is an antitumor antibiotic that is produced by the bacterium Streptomyces pactum. It works by inhibiting protein synthesis in cells, which can ultimately lead to cell death. Pactamycin has been studied for its potential use in treating various types of cancer, although it is not currently approved for clinical use in humans.

In addition to its antitumor activity, pactamycin has also been found to have antibacterial and antiviral properties. However, its use as a therapeutic agent is limited by its toxicity, which can cause side effects such as hearing loss, kidney damage, and bone marrow suppression.

It's important to note that pactamycin is primarily used in research settings to study its mechanisms of action and potential therapeutic uses. It should only be handled by trained professionals in a controlled laboratory environment.

Calcium-calmodulin-dependent protein kinases (CAMKs) are a family of enzymes that play a crucial role in intracellular signaling pathways. They are activated by the binding of calcium ions and calmodulin, a ubiquitous calcium-binding protein, to their regulatory domain.

Once activated, CAMKs phosphorylate specific serine or threonine residues on target proteins, thereby modulating their activity, localization, or stability. This post-translational modification is essential for various cellular processes, including synaptic plasticity, gene expression, metabolism, and cell cycle regulation.

There are several subfamilies of CAMKs, including CaMKI, CaMKII, CaMKIII (also known as CaMKIV), and CaMK kinase (CaMKK). Each subfamily has distinct structural features, substrate specificity, and regulatory mechanisms. Dysregulation of CAMK signaling has been implicated in various pathological conditions, such as neurodegenerative diseases, cancer, and cardiovascular disorders.

Mitogen-Activated Protein Kinase Kinases (MAP2K or MEK) are a group of protein kinases that play a crucial role in intracellular signal transduction pathways. They are so named because they are activated by mitogens, which are substances that stimulate cell division, and other extracellular signals.

MAP2Ks are positioned upstream of the Mitogen-Activated Protein Kinases (MAPK) in a three-tiered kinase cascade. Once activated, MAP2Ks phosphorylate and activate MAPKs, which then go on to regulate various cellular processes such as proliferation, differentiation, survival, and apoptosis.

There are several subfamilies of MAP2Ks, including MEK1/2, MEK3/6 (also known as MKK3/6), MEK4/7 (also known as MKK4/7), and MEK5. Each MAP2K is specific to activating a particular MAPK, and they are activated by different MAP3Ks (MAP kinase kinase kinases) in response to various extracellular signals.

Dysregulation of the MAPK/MAP2K signaling pathways has been implicated in numerous diseases, including cancer, cardiovascular disease, and neurological disorders. Therefore, targeting these pathways with therapeutic agents has emerged as a promising strategy for treating various diseases.

MAP Kinase Kinase 4 (MAP2K4 or MKK4) is a serine/threonine protein kinase that plays a crucial role in intracellular signal transduction pathways, particularly the mitogen-activated protein kinase (MAPK) cascades. These cascades are involved in various cellular processes such as proliferation, differentiation, survival, and apoptosis in response to extracellular stimuli like cytokines, growth factors, and stress signals.

MAP2K4 specifically activates the c-Jun N-terminal kinase (JNK) pathway by phosphorylating and activating JNK proteins. The activation of JNK leads to the phosphorylation and regulation of various transcription factors, ultimately influencing gene expression and cellular responses. Dysregulation of MAP2K4 has been implicated in several diseases, including cancer and inflammatory disorders.

Enzyme activation refers to the process by which an enzyme becomes biologically active and capable of carrying out its specific chemical or biological reaction. This is often achieved through various post-translational modifications, such as proteolytic cleavage, phosphorylation, or addition of cofactors or prosthetic groups to the enzyme molecule. These modifications can change the conformation or structure of the enzyme, exposing or creating a binding site for the substrate and allowing the enzymatic reaction to occur.

For example, in the case of proteolytic cleavage, an inactive precursor enzyme, known as a zymogen, is cleaved into its active form by a specific protease. This is seen in enzymes such as trypsin and chymotrypsin, which are initially produced in the pancreas as inactive precursors called trypsinogen and chymotrypsinogen, respectively. Once they reach the small intestine, they are activated by enteropeptidase, a protease that cleaves a specific peptide bond, releasing the active enzyme.

Phosphorylation is another common mechanism of enzyme activation, where a phosphate group is added to a specific serine, threonine, or tyrosine residue on the enzyme by a protein kinase. This modification can alter the conformation of the enzyme and create a binding site for the substrate, allowing the enzymatic reaction to occur.

Enzyme activation is a crucial process in many biological pathways, as it allows for precise control over when and where specific reactions take place. It also provides a mechanism for regulating enzyme activity in response to various signals and stimuli, such as hormones, neurotransmitters, or changes in the intracellular environment.

Enzyme inhibitors are substances that bind to an enzyme and decrease its activity, preventing it from catalyzing a chemical reaction in the body. They can work by several mechanisms, including blocking the active site where the substrate binds, or binding to another site on the enzyme to change its shape and prevent substrate binding. Enzyme inhibitors are often used as drugs to treat various medical conditions, such as high blood pressure, abnormal heart rhythms, and bacterial infections. They can also be found naturally in some foods and plants, and can be used in research to understand enzyme function and regulation.

In the context of medical and clinical neuroscience, memory is defined as the brain's ability to encode, store, retain, and recall information or experiences. Memory is a complex cognitive process that involves several interconnected regions of the brain and can be categorized into different types based on various factors such as duration and the nature of the information being remembered.

The major types of memory include:

1. Sensory memory: The shortest form of memory, responsible for holding incoming sensory information for a brief period (less than a second to several seconds) before it is either transferred to short-term memory or discarded.
2. Short-term memory (also called working memory): A temporary storage system that allows the brain to hold and manipulate information for approximately 20-30 seconds, although this duration can be extended through rehearsal strategies. Short-term memory has a limited capacity, typically thought to be around 7±2 items.
3. Long-term memory: The memory system responsible for storing large amounts of information over extended periods, ranging from minutes to a lifetime. Long-term memory has a much larger capacity compared to short-term memory and is divided into two main categories: explicit (declarative) memory and implicit (non-declarative) memory.

Explicit (declarative) memory can be further divided into episodic memory, which involves the recollection of specific events or episodes, including their temporal and spatial contexts, and semantic memory, which refers to the storage and retrieval of general knowledge, facts, concepts, and vocabulary, independent of personal experience or context.

Implicit (non-declarative) memory encompasses various forms of learning that do not require conscious awareness or intention, such as procedural memory (skills and habits), priming (facilitated processing of related stimuli), classical conditioning (associative learning), and habituation (reduced responsiveness to repeated stimuli).

Memory is a crucial aspect of human cognition and plays a significant role in various aspects of daily life, including learning, problem-solving, decision-making, social interactions, and personal identity. Memory dysfunction can result from various neurological and psychiatric conditions, such as dementia, Alzheimer's disease, stroke, traumatic brain injury, and depression.

Amnesia is a condition characterized by memory loss, which can be temporary or permanent. It may result from brain damage or disease, and it can affect various aspects of memory, such as the ability to recall past events (retrograde amnesia), the ability to form new memories (anterograde amnesia), or both. Amnesia can also affect a person's sense of identity and their ability to learn new skills.

There are several types of amnesia, including:

1. Anterograde amnesia: This type of amnesia affects the ability to form new memories after an injury or trauma. People with anterograde amnesia may have difficulty learning new information and remembering recent events.
2. Retrograde amnesia: Retrograde amnesia affects the ability to recall memories that were formed before an injury or trauma. People with retrograde amnesia may have trouble remembering events, people, or facts from their past.
3. Transient global amnesia: This is a temporary form of amnesia that usually lasts for less than 24 hours. It is often caused by a lack of blood flow to the brain, and it can be triggered by emotional stress, physical exertion, or other factors.
4. Korsakoff's syndrome: This is a type of amnesia that is caused by alcohol abuse and malnutrition. It is characterized by severe memory loss, confusion, and disorientation.
5. Dissociative amnesia: This type of amnesia is caused by psychological factors, such as trauma or stress. People with dissociative amnesia may have trouble remembering important personal information or events that are emotionally charged.

The treatment for amnesia depends on the underlying cause. In some cases, memory may improve over time, while in other cases, it may be permanent. Treatment may involve medication, therapy, or rehabilitation to help people with amnesia cope with their memory loss and develop new skills to compensate for their memory impairments.

Arsenites are inorganic compounds that contain arsenic in the trivalent state (arsenic-III). They are formed by the reaction of arsenic trioxide (As2O3) or other trivalent arsenic compounds with bases such as sodium hydroxide, potassium hydroxide, or ammonia.

The most common and well-known arsenite is sodium arsenite (NaAsO2), which has been used in the past as a wood preservative and pesticide. However, due to its high toxicity and carcinogenicity, its use has been largely discontinued. Other examples of arsenites include potassium arsenite (KAsO2) and calcium arsenite (Ca3(AsO3)2).

Arsenites are highly toxic and can cause a range of health effects, including skin irritation, nausea, vomiting, diarrhea, abdominal pain, and death in severe cases. Long-term exposure to arsenites has been linked to an increased risk of cancer, particularly lung, bladder, and skin cancer.

In the context of medical research, authorship refers to the recognition of individuals who have made significant contributions to the development and completion of a scientific paper or research project. The International Committee of Medical Journal Editors (ICMJE) has established guidelines for determining authorship, which include the following four criteria:

1. Substantial contribution to the conception or design of the work; or the acquisition, analysis, or interpretation of data for the work.
2. Drafting the work or revising it critically for important intellectual content.
3. Final approval of the version to be published.
4. Agreement to be accountable for all aspects of the work in ensuring that questions related to the accuracy or integrity of any part of the work are appropriately investigated and resolved.

All authors should meet these criteria, and their contributions should be clearly described in the manuscript. It is important to note that authorship should not be granted based on position or status alone, but rather on the basis of substantial intellectual contribution and commitment to the work.

Mitogen-Activated Protein Kinase 1 (MAPK1), also known as Extracellular Signal-Regulated Kinase 2 (ERK2), is a protein kinase that plays a crucial role in intracellular signal transduction pathways. It is a member of the MAPK family, which regulates various cellular processes such as proliferation, differentiation, apoptosis, and stress response.

MAPK1 is activated by a cascade of phosphorylation events initiated by upstream activators like MAPKK (Mitogen-Activated Protein Kinase Kinase) in response to various extracellular signals such as growth factors, hormones, and mitogens. Once activated, MAPK1 phosphorylates downstream targets, including transcription factors and other protein kinases, thereby modulating their activities and ultimately influencing gene expression and cellular responses.

MAPK1 is widely expressed in various tissues and cells, and its dysregulation has been implicated in several pathological conditions, including cancer, inflammation, and neurodegenerative diseases. Therefore, understanding the regulation and function of MAPK1 signaling pathways has important implications for developing therapeutic strategies to treat these disorders.

MAP (Mitogen-Activated Protein) Kinase Kinase Kinases (MAP3K or MAPKKK) are a group of protein kinases that play a crucial role in intracellular signal transduction pathways, which regulate various cellular processes such as proliferation, differentiation, survival, and apoptosis. They are called "kinases" because they catalyze the transfer of a phosphate group from ATP to specific serine or threonine residues on their target proteins.

MAP3Ks function upstream of MAP Kinase Kinases (MKKs or MAP2K) and MAP Kinases (MPKs or MAPK) in the MAP kinase cascade. Upon activation by various extracellular signals, such as growth factors, cytokines, stress, and hormones, MAP3Ks phosphorylate and activate MKKs, which subsequently phosphorylate and activate MPKs. Activated MPKs then regulate the activity of downstream transcription factors and other target proteins to elicit appropriate cellular responses.

There are several subfamilies of MAP3Ks, including ASK, DLK, TAK, MEKK, MLK, and ZAK, among others. Each subfamily has distinct structural features and functions in different signaling pathways. Dysregulation of MAP kinase cascades, including MAP3Ks, has been implicated in various human diseases, such as cancer, inflammation, and neurodegenerative disorders.

Mitogen-activated protein kinase (MAPK) signaling system is a crucial pathway for the transmission and regulation of various cellular responses in eukaryotic cells. It plays a significant role in several biological processes, including proliferation, differentiation, apoptosis, inflammation, and stress response. The MAPK cascade consists of three main components: MAP kinase kinase kinase (MAP3K or MEKK), MAP kinase kinase (MAP2K or MEK), and MAP kinase (MAPK).

The signaling system is activated by various extracellular stimuli, such as growth factors, cytokines, hormones, and stress signals. These stimuli initiate a phosphorylation cascade that ultimately leads to the activation of MAPKs. The activated MAPKs then translocate into the nucleus and regulate gene expression by phosphorylating various transcription factors and other regulatory proteins.

There are four major MAPK families: extracellular signal-regulated kinases (ERK1/2), c-Jun N-terminal kinases (JNK1/2/3), p38 MAPKs (p38α/β/γ/δ), and ERK5. Each family has distinct functions, substrates, and upstream activators. Dysregulation of the MAPK signaling system can lead to various diseases, including cancer, diabetes, cardiovascular diseases, and neurological disorders. Therefore, understanding the molecular mechanisms underlying this pathway is crucial for developing novel therapeutic strategies.

Injection of anisomycin into the hippocampus has been proposed for selective removal of memories. Because of anisomycin's wide ... Anisomycin interferes with protein and DNA synthesis by inhibiting peptidyl transferase or the 80S ribosome system. Anisomycin ... Butler, K. (1966). "Anisomycin. II.1 Biosynthesis of Anisomycin". The Journal of Organic Chemistry. 31 (1): 317-20. doi:10.1021 ... Anisomycin is used as a component of Martin Lewis agar, an in vitro diagnostic product which is used extensively in the United ...
Anisomycin inhibits the production of proteins. In tests where it is delivered to the lateral and basal nuclei in the amygdala ... "Anisomycin - an overview , ScienceDirect Topics". www.sciencedirect.com. Retrieved 2022-05-05. Doyère, Valérie; Dębiec, Jacek; ...
Schaefer, John P; Wheatley, Peter J (1967). "The Structure of Anisomycin". Chemical Communications. London: 578-79. "cremation ... Schaefer on the structure of anisomycin. Wheatley's last position was in the Department of Physical Chemistry at Cambridge. ...
These include anisomycin, cycloheximide, chloramphenicol, tetracycline, streptomycin, erythromycin, and puromycin. Prokaryotic ...
Sensitivity to novobiocin, bacitracin, anisomycin, aphidicolin, and rifampicin have been observed. However, no sensitivity has ...
When anisomycin is applied to the hippocampus, active memories are unable to fully consolidate and are lost. When anisomycin is ... In research, commonly used PSI's include anisomycin, cycloheximide, and puromycin - although the use of puromycin has stopped ... anisomycin has been shown to cause a substantial catecholamine release that co-occurs with neural suppression, which has not ... Anisomycin administered at a dose that inhibits 95% of protein synthesis and associated electrical activity is not the highest ...
Ducret C, Maira SM, Dierich A, Wasylyk B (2000). "The net repressor is regulated by nuclear export in response to anisomycin, ...
Anisomycin achieved this anti-metastatic activity in part by decreasing the abundance of the death receptor inhibiting protein ... showed that anisomycin can sensitize metastatic epithelial cells to anoikis and reduce circulating tumor cell implantation in ... September 2007). "A chemical screen identifies anisomycin as an anoikis sensitizer that functions by decreasing FLIP protein ...
It is resistant to many antibiotics, including Vancomycin and Tetracycline, but can be killed by Anisomycin. This organism does ...
Frey U, Krug M, Reymann KG, Matthies H (June 1988). "Anisomycin, an inhibitor of protein synthesis, blocks late phases of LTP ...
The rats that were injected with anisomycin after consolidation had taken place, retained the fear reaction to the tone. ... Groups of rats were then injected with anisomycin, an antibiotic that restricts protein synthesis, at different points in time ... by means of immediate amygdala infusions of the protein synthesis inhibitor anisomycin, but not by infusions made six hours ... the protein synthesis inhibitor anisomycin) and both require the transcription factor CREB. However, recent amygdala research ...
Frey, Uwe; Krug, Manfred; Reymann, Klaus G.; Matthies, Hansjuergen (1988). "Anisomycin, an inhibitor of protein synthesis, ... as proven by injecting anisomycin into a dendritic spine and observing the resulting absence of late LTP. To achieve ...
"Inhibition of protein synthesis and JNK activation are not required for cell death induced by anisomycin and anisomycin ...
... but not medium-term retention of olfactory memories in honeybees is impaired by actinomycin D and anisomycin". The European ...
... and the antibiotics anisomycin and sinefungin. Tohyama, Shigehiro; Kakinuma, Katsumi; Eguchi, Tadashi (January 2006). "The ...
After receiving post-retrieval an intra-amygdalar infusion of a known amnesic agent, anisomycin, rats failed to recall a ...
... the infusion of proteasome inhibitors into the CA1 of the hippocampus immediately after retrieval prevented anisomycin-induced ...
2005). "Complete inhibition of anisomycin and UV radiation but not cytokine induced JNK and p38 activation by an aryl- ...
The molecular formula C14H19NO4 (molar mass: 265.31 g/mol, exact mass: 265.1314 u) may refer to: Anisomycin, also known as ...
... anisomycin MeSH D03.383.773.107 - bepridil MeSH D03.383.773.165 - clemastine MeSH D03.383.773.170 - 3,4-dichloro-n-methyl-n-(2 ...
Anisomycin Anvisa (2023-07-24). "RDC Nº 804 - Listas de Substâncias Entorpecentes, Psicotrópicas, Precursoras e Outras sob ...
... the death effector TRAIL or chemical drugs such as anisomycin. PUMA protein is degraded in a proteasome dependent manner and ...
Anisomycin, Thiolutin, Wortmannin, K252a, Staurosporine, K252C, Bafilomycin, Alamethicin, Leptomycin, A23187, Chelerythrine, ... Anisomycin, Thapsigargin, cyclopamine, Thiostrepton, Staurosporine, Mithramycin, Midostaurin, Wortmannin, K252a, Geldanamycin ...
... "fungicidal substances of the anisomycin group".[citation needed] This bacterium can also be used to determine the nutrient ...
Androgen Anethole Angiotensinogen Anisomycin Antidiuretic hormone (ADH) Anti-Müllerian hormone (AMH) Arabinose Arginine ...
... and anisomycin treatment or JDP2 is also regulated by other kinases such as p38 MAPK and doublecortin like protein kinase. ...
Injection of anisomycin into the hippocampus has been proposed for selective removal of memories. Because of anisomycins wide ... Anisomycin interferes with protein and DNA synthesis by inhibiting peptidyl transferase or the 80S ribosome system. Anisomycin ... Butler, K. (1966). "Anisomycin. II.1 Biosynthesis of Anisomycin". The Journal of Organic Chemistry. 31 (1): 317-20. doi:10.1021 ... Anisomycin is used as a component of Martin Lewis agar, an in vitro diagnostic product which is used extensively in the United ...
Mode of action of anisomycin. J. Biol. Chem. 242:3226-3233. View this article via: PubMed Google Scholar ... Anisomycin acts a positive control, since recovery of protein synthesis from inhibition with this compound occurs within an ... HeLa cells were incubated for 1 hour with 10 μM anisomycin, 5 μM FA, 0.4 μM silvestrol, or MeOH. Cells were then washed with ...
Anisomycin is a phenylpyrolidine derivative that strongly activates JNK (33); thus, it was used as a positive control in the ... In this study, 20 µM DHA, 100 µM PDTC, 10 µM JNK inhibitor SP600125 and 10 µM anisomycin, were used to treat the cells. ... Anisomycin markedly increased the level of phospho-JNK in HUVECs (Fig. 1A and B). ... Cano E, Hazzalin CA and Mahadevan LC: Anisomycin-activated protein kinases p45 and p55 but not mitogen-activated protein ...
Confocal immunofluorescent analysis of HeLa cells, anisomycin-treated (left) or untreated (right), using Phospho-HSP27 (Ser82) ... Confocal immunofluorescent analysis of HeLa cells, anisomycin-treated (left) or untreated (right), using Phospho-HSP27 (Ser82) ...
I. A. Mawji, C. D. Simpson, M. Gronda et al., "A chemical screen identifies anisomycin as an anoikis sensitizer that functions ... Anisomycin can sensitize cells to anoikis by decreasing FLIP protein levels and inhibits distal tumor formation in a mouse ...
... anisomycin) at concentrations that do not inhibit N gonorrhoeae. ...
Anisomycin anoikis sensitizer CAS Number 22862_76_6. 10mg. 115.78 €. -. Stressmarq. SIH-266-50MG. Anisomycin anoikis sensitizer ...
Chiral syntheses of the antibiotics anisomycin and pentenomycin from carbohydrates. J. P. H. Verheyden, A. C. Richardson, R. S ...
Anisomycin was purchased from Sigma Aldrich Inc. Endoribonuclease-prepared siRNAs (esiRNAs) directed against STK38L were ... we treated DAN-G and KP-1N cells with the apoptosis-inducing agent anisomycin, and showed comparable effects in both cell lines ...
Synonyms: anisomycin, Flagecidin, (-) Anisomycin, Upjohn 204t3, Anisomycin hydrochloride, Spectrum_001534, Prestwick3_000412, ... Anisomycin (17 suppliers). IUPAC Name: [(2R,3S,4S)-4-hydroxy-2-[(4-methoxyphenyl)methyl]pyrrolidin-3-yl] acetate , CAS Registry ...
Complete inhibition of anisomycin and UV radiation but not cytokine induced JNK and p38 activation by an aryl-substituted ... these data demonstrate that MLK7 is the MAPKKK required for modulation of the stress-activated MAPKs downstream of anisomycin ...
... the effects of which were impaired by the JNK activator anisomycin. In summary, our study suggests that melatonin protects ...
Anisomycin. 8.00mg. Vancomycin. 0.10mg. Bromo thymol blue. 1.00mg. Bromo cresol purple. 1.00mg. ...
Furthermore, we combined treatment F-nec with anisomycin, a JNK activator. As we expected, anisomycin partially restored the ... Anisomycin, a JNK activator (20 mg/kg, MCE), was administered combined with F-nec by i. p. injection to further investigate the ... 6A-D). In contrast, combined F-nec treatment with anisomycin, a JNK activator, the reduced hepatic JNK activation induced by F- ... In addition, a specific inhibitor of c-Jun NH (2)-terminal kinases (JNK) SP600125 and its activator anisomycin are used to ...
The p38 MAPK activator anisomycin was used to identify the underlying mechanisms of the effects of ADSC-Exos on TGF-ß1-induced ... However, anisomycin treatment alleviated these ADSC-Exos-induced changes. In conclusion, findings from the present study ...
Mutations outside the anisomycin-binding site can make ribosomes drug-resistant. pubmed doi rcsb ...
The protein synthesis inhibitor anisomycin clogged the effect of field activation on launch probability. These results indicate ... synthesis inhibitor anisomycin clogged the effect of field activation on launch probability. These results indicate that ...
Anisomycin and dimethyl sulphoxide (DMSO) had been bought from Sigma (St. Louis, MO). For anisomycin treatment, cells had been ... cultured in serum free of charge IMEM for 24 h and treated with DMSO or 50ng/ml anisomycin for 15 min. Traditional western blot ...
In this episode of the Epigenetics Podcast, we caught up with Ines Drinnenberg from Institute Curie to talk about her work on the formation of CenH3-deficient kinetochores. The laboratory of Ines Drinneberg focuses on centromeres and how different strategies of centromere organization have evolved in different organisms.
MK-801, but not anisomycin, inhibits the induction of tolerance to ischemia in the gerbil hippocampus. //Neurosci. Lett. 1992; ...
However, when the anisomycin was administered one day after training, the engram cell was not affected. This tells us that ... as evidenced by a study involving animals administered with the protein synthesis inhibitor anisomycin. The results showed that ...
had been unaffected, a higher inhibition of viral proteins expression was showed after treatment with anisomycin. DENV RNA ... synthesis was low in anisomycin treated civilizations highly, but the substance didnt exert a primary inhibitory influence on ...
western blot: 4-20 μg/mL using extract of human Jurkat cells activated with anisomycin. ...
We first proved that both anisomycin and ionizing radiation conducted to apoptosis through activation of p38 MAPK in human ... In the present study, by using two different activators of p38 MAPK, namely anisomycin and ionizing radiation, we depicted how ... In the present study, by using two different activators of p38 MAPK, namely anisomycin and ionizing radiation, we depicted how ... We first proved that both anisomycin and ionizing radiation conducted to apoptosis through activation of p38 MAPK in human ...
Extinction with social support is blocked by the protein synthesis inhibitors anisomycin and rapamycin and by the inhibitor of ...
In rats, the protein translation inhibitor anisomycin impaired memory persistence when injected into the dorsal hippocampus 12 ...
... anisomycin, cycloheximide, chloramphenicol, antibiotic medication, streptomycin, erythromycin, puromycin and so on. Game ...
... then treated with 100 ng/mL Anisomycin for 30 minutes at 37°C. Cells were lysed in 8 mL of SureFire Ultra Lysis Buffer. ...
  • findings revealed that melatonin effectively counteracted high-glucose/high fat-hypoxia-induced cardiomyocyte apoptosis and contractile dysfunction through a JNK-mediated mechanism, the effects of which were impaired by the JNK activator anisomycin. (physiciansweekly.com)
  • In addition, a specific inhibitor of c-Jun NH (2)-terminal kinases (JNK) SP600125 and its activator anisomycin are used to elucidate its mechanisms in acute liver failure therapy. (pdgfr740y-pactivator.com)
  • In rats, the protein translation inhibitor anisomycin impaired memory persistence when injected into the dorsal hippocampus 12 h after inhibitory avoidance (IA) training without affecting memory formation. (hormonessignaling.com)
  • Because of anisomycin's wide use as a protein synthesis inhibitor, there have been many studies centered on the biosynthesis of anisomycin. (wikipedia.org)
  • The protein synthesis inhibitor anisomycin clogged the effect of field activation on launch probability. (islamophobiacon.com)
  • Measurement of Fos protein expression (a marker for neuronal activation) and evaluation with anisomycin (an inhibitor of de novo protein synthesis) will be used in rats to investigate the neurobiological substrates of extinction learning following cocaine self-administration training. (grantome.com)
  • Partial inhibition of DNA synthesis occurs at anisomycin concentrations that effect 95% inhibition of protein synthesis. (wikipedia.org)
  • The exact formulation has changed over the years but includes agents active against gram-positive bacteria (vancomycin), gram-negative bacteria (colistin, trimethoprim), and fungi (nystatin, anisomycin) at concentrations that do not inhibit N gonorrhoeae . (medscape.com)
  • Anisomycin, also known as flagecidin, is an antibiotic produced by Streptomyces griseolus which inhibits eukaryotic protein synthesis. (wikipedia.org)
  • Anisomycin can activate stress-activated protein kinases, MAP kinase and other signal transduction pathways. (wikipedia.org)
  • Anisomycin interferes with protein and DNA synthesis by inhibiting peptidyl transferase or the 80S ribosome system. (wikipedia.org)
  • For anisomycin treatment, cells had been cultured in serum free of charge IMEM for 24 h and treated with DMSO or 50ng/ml anisomycin for 15 min. (aurora-kinase.com)
  • In the present study, by using two different activators of p38 MAPK, namely anisomycin and ionizing radiation, we depicted how ceramide generated by acid sphingomyelinase was involved in p38 MAPK-dependent apoptosis of endothelial cells. (hal.science)
  • We first proved that both anisomycin and ionizing radiation conducted to apoptosis through activation of p38 MAPK in human microvascular endothelial cells HMEC-1. (hal.science)
  • To prepare the lysate, A549 cells were grown to confluence in T175 flasks in 10% FBS containing medium, then treated with 100 ng/mL Anisomycin for 30 minutes at 37°C. Cells were lysed in 8 mL of SureFire Ultra Lysis Buffer. (revvity.com)
  • had been unaffected, a higher inhibition of viral proteins expression was showed after treatment with anisomycin. (dc-thera.org)
  • Of this suspension, 100-µL samples were cultured without dilution and after 10- and 100-fold dilutions on buffered charcoal yeast extract agar with alpha-ketoglutarate (BCYE-alpha) and a selective supplement with dyes and the antibiotics polymyxin, anisomycin, and vancomycin (Legionella MWY Selective Supplement SR118, Oxoid Ltd., Hampshire, England). (medscape.com)
  • The exact formulation has changed over the years but includes agents active against gram-positive bacteria (vancomycin), gram-negative bacteria (colistin, trimethoprim), and fungi (nystatin, anisomycin) at concentrations that do not inhibit N gonorrhoeae. (medscape.com)
  • Using the MILLIPLEX ® Bcl-2 Family Apoptosis Panel 1 and Panel 2 , changes in the expression and interactions of Bcl-2 family members were analyzed in response to known apoptotic drugs, including camptothecin (topoisomerase inhibitor), anisomycin (protein translation inhibitor), and AT101 (BH3 mimetic drug). (sigmaaldrich.com)
  • Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (PubMed:24512202). (nih.gov)
  • While at UM, Respondent falsified twenty-four (24) Western blots for phosphorylated JNK or MMK4 expression in mN/SF exposed to UV light, H2O2, cadmium, or anisomycin in the seven (7) presentations and twenty-six (26) data files in the research record, when the images were duplicated and falsely relabeled Western blots of unrelated experiments. (nih.gov)