Search results for "Glyceraldehyde-3-Phosphate Dehydrogenases"

showing 3 items of 23 documents

Glyceraldehyde-3-phosphate dehydrogenase regulates endothelin-1 expression by a novel, redox-sensitive mechanism involving mRNA stability

2008

17 pages.-- PMID: 18809573 [PubMed].-- Printed version published on Dec 2008.

Untranslated regionUmbilical VeinsRNA StabilityRNA StabilityGlyceraldehyde-3'-phosphate dehydrogenase (GAPDH)Plasma protein bindingstomatognathic systemHumansmRNA stabilityS-Glutathionylation3' Untranslated RegionsMolecular BiologyGlyceraldehyde 3-phosphate dehydrogenaseRegulation of gene expressionMessenger RNAEndothelin-1biologyThree prime untranslated regionGlyceraldehyde-3-Phosphate DehydrogenasesArticlesCell BiologyGlutathioneOxidative StressGene Expression RegulationBiochemistryEndothelin-1 (ET-1)biology.proteinOxidation-ReductionProtein Binding
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The catalytic mechanism of glyceraldehyde 3-phosphate dehydrogenase from Trypanosoma cruzi elucidated via the QM/MM approach

2013

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been identified as a key enzyme involved in glycolysis processes for energy production in the Trypanosoma cruzi parasite. This enzyme catalyses the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) in the presence of inorganic phosphate (Pi) and nicotinamide adenosine dinucleotide (NAD+). The catalytic mechanism used by GAPDH has been intensively investigated. However, the individual roles of Pi and the C3 phosphate of G3P (Ps) sites, as well as some residues such as His194 in the catalytic mechanism, remain unclear. In this study, we have employed Molecular Dynamics (MD) simulations within hybrid quantum mechanical/molecular …

biocatalysisEnzims proteolíticsParàsitsStereochemistryTrypanosoma cruziGeneral Physics and AstronomyDehydrogenaseMolecular Dynamics SimulationNicotinamide adenine dinucleotideOxidative PhosphorylationSubstrate Specificityglyceraldehyde 3 phosphate dehydrogenaseQM/MMchemistry.chemical_compoundstomatognathic systemGlyceraldehydePhysical and Theoretical Chemistrynicotinamide adenine dinucleotideGlyceraldehyde 3-phosphate dehydrogenasechemistry.chemical_classificationbiologyGlyceraldehyde-3-Phosphate DehydrogenasesActive siteNADmolecular dynamicsEnzymechemistryBiochemistryBiocatalysisbiology.proteinQuantum TheoryNAD+ kinaseOxidation-ReductionPhysical Chemistry Chemical Physics
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The Candida albicans cell wall-associated glyceraldehyde-3-phosphate dehydrogenase activity increases in response to starvation and temperature upshi…

2002

We have determined the effect of environmental factors (mild thermal upshift and starvation) on the Candida albicans cell wall-associated glyceraldehyde-3-phosphate dehydrogenase (cwGAPDH) activity. Temperature upshift (from 28 to 37 degrees C) and/ or starvation (at 28 or 37 degrees C in water) of exponentially growing yeast cells caused an increase in cwGAPDH activity (3 to 5-, and 7 to 8-fold, respectively). This increase in activity did not correlate with an increase in the amount of cwGAPDH protein present, as determined by flow cytometry, immunoelectron microscopy and Western-blotting. These results indicate that thermal upshift and starvation cause an activation of the cwGAPDH in C. …

biologymedicine.diagnostic_testImmunoelectron microscopyTemperatureGlyceraldehyde-3-Phosphate DehydrogenasesDehydrogenaseGeneral Medicinebiology.organism_classificationYeastCorpus albicansFlow cytometryCell wallFungal ProteinsInfectious DiseasesBiochemistryCell WallCandida albicansbiology.proteinmedicineCandida albicansGlyceraldehyde 3-phosphate dehydrogenaseMedical mycology
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