Molecular mechanisms of spatial protein quality control

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Molecular mechanisms of spatial protein quality control

Evidence is now accumulating that damaged proteins are not randomly distributed but often concentrated in microscopically visible and functionally distinct inclusion bodies. How misfolded proteins are organized into these compartments, however, is still unknown. We have recently begun to investigate stress-inducible protein quality control (PQC) bodies in yeast cells. Surprisingly, we found tha...

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Molecular chaperones and protein quality control.

In living cells, both newly made and preexisting polypeptide chains are at constant risk for misfolding and aggregation. In accordance with the wide diversity of misfolded forms, elaborate quality-control strategies have evolved to counter these inevitable mishaps. Recent reports describe the removal of aggregates from the cytosol; reveal mechanisms for protein quality control in the endoplasmi...

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Molecular Chaperones and Protein Quality Control

Bernd Bukau,1 Jonathan Weissman,2 and Arthur Horwich3,4,* 1Zentrum fur Molekulare Biologie, Universität Heidelberg, 69120 Heidelberg, Germany 2Department of Cellular and Molecular Pharmacology and Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94143, USA 3Department of Genetics and Howard Hughes Medical Institute, Yale University School of Medicine, ...

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Molecular chaperones in protein quality control.

Proteins must fold into their correct three-dimensional conformation in order to attain their biological function. Conversely, protein aggregation and misfolding are primary contributors to many devastating human diseases, such as prion-mediated infections, Alzheimer's disease, type II diabetes and cystic fibrosis. While the native conformation of a polypeptide is encoded within its primary ami...

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Glycoprotein folding and quality-control mechanisms in protein-folding diseases

Biosynthesis of proteins--from translation to folding to export--encompasses a complex set of events that are exquisitely regulated and scrutinized to ensure the functional quality of the end products. Cells have evolved to capitalize on multiple post-translational modifications in addition to primary structure to indicate the folding status of nascent polypeptides to the chaperones and other p...

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ژورنال

عنوان ژورنال: Prion

سال: 2012

ISSN: 1933-6896,1933-690X

DOI: 10.4161/pri.22470