Molecular Chaperones and Protein Quality Control
Copyright policy )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 endoplasmic reticulum; and provide new insight into two classes of molecular chaperones, the Hsp70 system and the AAA+ (Hsp100) unfoldases.
- University of California, San Francisco United States
- Heidelberg University Germany
- Yale University United States
- Scripps Research Institute United States
Protein Folding, Biochemistry, Genetics and Molecular Biology(all), Protozoan Proteins, Proteins, Endopeptidase Clp, Endoplasmic Reticulum, Adenosine Triphosphate, Cytosol, Allosteric Regulation, Protein Biosynthesis, Animals, Humans, HSP70 Heat-Shock Proteins, Heat-Shock Proteins, Molecular Chaperones
Protein Folding, Biochemistry, Genetics and Molecular Biology(all), Protozoan Proteins, Proteins, Endopeptidase Clp, Endoplasmic Reticulum, Adenosine Triphosphate, Cytosol, Allosteric Regulation, Protein Biosynthesis, Animals, Humans, HSP70 Heat-Shock Proteins, Heat-Shock Proteins, Molecular Chaperones
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