| D002772 |
Cholera Toxin |
An ENTEROTOXIN from VIBRIO CHOLERAE. It consists of two major protomers, the heavy (H) or A subunit and the B protomer which consists of 5 light (L) or B subunits. The catalytic A subunit is proteolytically cleaved into fragments A1 and A2. The A1 fragment is a MONO(ADP-RIBOSE) TRANSFERASE. The B protomer binds cholera toxin to intestinal epithelial cells and facilitates the uptake of the A1 fragment. The A1 catalyzed transfer of ADP-RIBOSE to the alpha subunits of heterotrimeric G PROTEINS activates the production of CYCLIC AMP. Increased levels of cyclic AMP are thought to modulate release of fluid and electrolytes from intestinal crypt cells. |
Cholera Toxin A,Cholera Toxin B,Cholera Toxin Protomer A,Cholera Toxin Protomer B,Cholera Toxin Subunit A,Cholera Toxin Subunit B,Choleragen,Choleragenoid,Cholera Enterotoxin CT,Cholera Exotoxin,Cholera Toxin A Subunit,Cholera Toxin B Subunit,Procholeragenoid,Enterotoxin CT, Cholera,Exotoxin, Cholera,Toxin A, Cholera,Toxin B, Cholera,Toxin, Cholera |
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| D004768 |
Enterotoxins |
Substances that are toxic to the intestinal tract causing vomiting, diarrhea, etc.; most common enterotoxins are produced by bacteria. |
Staphylococcal Enterotoxin,Enterotoxin,Staphylococcal Enterotoxins,Enterotoxin, Staphylococcal,Enterotoxins, Staphylococcal |
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| D004926 |
Escherichia coli |
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. |
Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli |
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| D006027 |
Glycosides |
Any compound that contains a constituent sugar, in which the hydroxyl group attached to the first carbon is substituted by an alcoholic, phenolic, or other group. They are named specifically for the sugar contained, such as glucoside (glucose), pentoside (pentose), fructoside (fructose), etc. Upon hydrolysis, a sugar and nonsugar component (aglycone) are formed. (From Dorland, 28th ed; From Miall's Dictionary of Chemistry, 5th ed) |
Glycoside |
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| D006358 |
Hot Temperature |
Presence of warmth or heat or a temperature notably higher than an accustomed norm. |
Heat,Hot Temperatures,Temperature, Hot,Temperatures, Hot |
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| D014315 |
Triterpenes |
A class of terpenes (the general formula C30H48) formed by the condensation of six isoprene units, equivalent to three terpene units. |
Triterpene,Triterpenoid,Triterpenoids |
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| D055550 |
Protein Stability |
The ability of a protein to retain its structural conformation or its activity when subjected to physical or chemical manipulations. |
Protein Stabilities,Stabilities, Protein,Stability, Protein |
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| D062105 |
Molecular Docking Simulation |
A computer simulation technique that is used to model the interaction between two molecules. Typically the docking simulation measures the interactions of a small molecule or ligand with a part of a larger molecule such as a protein. |
Molecular Docking,Molecular Docking Simulations,Molecular Docking Analysis,Analysis, Molecular Docking,Docking Analysis, Molecular,Docking Simulation, Molecular,Docking, Molecular,Molecular Docking Analyses,Molecular Dockings,Simulation, Molecular Docking |
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| D019704 |
Protein Disulfide-Isomerases |
Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE. |
Protein Disulfide Isomerase,Protein Disulfide-Isomerase,Disulfide Interchange Enzyme,Disulfide Isomerase,Glycosylation Site-Binding Protein,Sulfhydryl-Disulfide Interchange Enzyme,Thiol-Disulfide Transhydrogenase,Trypanothione-Glutathione Thioltransferase,Disulfide Isomerase, Protein,Disulfide-Isomerase, Protein,Disulfide-Isomerases, Protein,Enzyme, Disulfide Interchange,Enzyme, Sulfhydryl-Disulfide Interchange,Glycosylation Site Binding Protein,Interchange Enzyme, Disulfide,Interchange Enzyme, Sulfhydryl-Disulfide,Isomerase, Disulfide,Isomerase, Protein Disulfide,Protein Disulfide Isomerases,Protein, Glycosylation Site-Binding,Site-Binding Protein, Glycosylation,Sulfhydryl Disulfide Interchange Enzyme,Thiol Disulfide Transhydrogenase,Thioltransferase, Trypanothione-Glutathione,Transhydrogenase, Thiol-Disulfide,Trypanothione Glutathione Thioltransferase |
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| D020134 |
Catalytic Domain |
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction. |
Active Site,Catalytic Core,Catalytic Region,Catalytic Site,Catalytic Subunit,Reactive Site,Active Sites,Catalytic Cores,Catalytic Domains,Catalytic Regions,Catalytic Sites,Catalytic Subunits,Core, Catalytic,Cores, Catalytic,Domain, Catalytic,Domains, Catalytic,Reactive Sites,Region, Catalytic,Regions, Catalytic,Site, Active,Site, Catalytic,Site, Reactive,Sites, Active,Sites, Catalytic,Sites, Reactive,Subunit, Catalytic,Subunits, Catalytic |
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