Search results for "ubiquitination process"

showing 1 items of 1 documents

Heat Shock Proteins: Cell Protection through Protein Triage

2010

Heat shock proteins (HSPs) are chaperones that catalyze the proper folding of nascent proteins and the refolding of denatured proteins. The ubiquitin-proteasome system is an error-checking system that directs improperly folded proteins for destruction. A coordinated interaction between the HSPs (renaturation) and the proteasome (degradation) must exist to assure protein quality control mechanisms. Although it still remains unknown how the decision of folding vs. degradation is taken, many pieces of evidence demonstrate that HSPs interact directly or indirectly with the proteasome, assuring quite selectively the proteasomal degradation of certain proteins under stress conditions. In this rev…

Proteasome Endopeptidase ComplexHSP27 Heat-Shock Proteinslcsh:MedicinePlasma protein bindingModels Biologicallcsh:TechnologyGeneral Biochemistry Genetics and Molecular Biologycell stressHsp27Heat shock proteinAnimalsHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock Proteinslcsh:ScienceMini-Review ArticleGeneral Environmental Sciencebiologylcsh:Tubiquitination processlcsh:RGeneral MedicineCrystallinsHsp90Hsp70Cell biologyproteasomeBiochemistryProteasomeheat shock proteinsbiology.proteinlcsh:QSignal transductionProtein qualityProtein BindingSignal TransductionThe Scientific World Journal
researchProduct