Protein rescue from aggregates by powerful molecular chaperone machines

Key Points When cells are exposed to stresses, proteins may misfold and aggregate. Molecular chaperones function in a myriad of cellular activities, including protein folding, remodelling and, in the case of yeast heat shock protein 104 (Hsp104) and bacterial ClpB, in the disaggregation of aggregate...

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Veröffentlicht in:	Nature reviews. Molecular cell biology 2013-10, Vol.14 (10), p.617-629
Hauptverfasser:	Doyle, Shannon M., Genest, Olivier, Wickner, Sue
Format:	Artikel
Sprache:	eng
Schlagworte:	631/535 631/80 631/80/470 Aggregates Alzheimer Disease - genetics Alzheimer Disease - pathology Alzheimer's disease Amyloidosis - genetics Amyloidosis - pathology ATP Bacteria Biochemistry Cancer Research Cell aggregation Cell Biology Cell division Control systems Crystal structure Developmental Biology Genetic aspects Heat shock proteins Humans Life Sciences Molecular chaperones Molecular Chaperones - chemistry Molecular Chaperones - genetics Molecular Chaperones - metabolism Parkinson Disease - genetics Parkinson Disease - pathology Parkinson's disease Peptide Hydrolases - metabolism Polypeptides Prion Diseases - genetics Prion Diseases - pathology Prions Properties Protein Conformation Protein Folding Protein Unfolding Protein-protein interactions Proteins Proteins - chemistry Proteins - genetics Proteins - metabolism Quality Control review-article Ribonucleic acid RNA Stem Cells Substrates (Biochemistry) Yeast Yeast fungi
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