Molecular chaperones and protein quality control.

By Bernd Bukau, Jonathan S. Weissman, A. Horwich. Cell, 2006

1,584 citations recorded by the source corpus.

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.

Subfields: Biotechnology, Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/2a5058e7119b48dd6488b71a43d6563c353682fa

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. Jeffrey L. Brodsky
2. J. Tyedmers
3. S. Vembar
4. Axel Mogk
5. M. Jäättelä
6. Bernd Bukau

In Molecular Biology

1. K. Scharf
2. Ingo Ebersberger
3. Thomas Berberich
4. L. Nover
5. J. Tyedmers
6. Axel Mogk
7. M. Jäättelä
8. Bernd Bukau

Citations in the corpus

• The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions (2007, background): “chaperone-mediated autophagy, prevention of protein aggregation under stress conditions, and disassembly of clathrincoated vesicles (reviewed in [14,17]).”
• The plant heat stress transcription factor (Hsf) family: structure, function and evolution. (2012, background): “They are essential for maintenance and/or restoration of protein homeostasis [12–17].”
• Heat shock protein 70 regulates the abscisic acid-induced antioxidant response of maize to combined drought and heat stress (2010, background): “HSP70 is one of the major classes of chaperone molecules and is involved in a variety of tasks in eukaryotic cells (Frydman 2001; Hartl and Hayer-Hartl 2002; Neupert and Brunner 2002; Mayer 2005; Bukau et al. 2006; Voellmy and Boellmann 2007).”
• The Hsp70 chaperone machinery: J-proteins as drivers of functional specificity (2010, neutral): “Later events in polypeptide folding include binding of soluble J proteins (3) and recruitment of soluble HSP70 before the completion of translation (4) and after nascent chain release (5).”
• Cellular strategies for controlling protein aggregation (2010, background): “The main chaperone classes that prevent the accumulation of misfolded conformers include the heat shock proteins (HSPs) HSP60 and HSP70, which exhibit ATP-dependent refolding activitie”
• Effects of multiple conformers per compound upon 3-D similarity search and bioassay data analysis (2012, neutral): “coli [46,47].”
• One step at a time: endoplasmic reticulum-associated degradation (2008, background): “To prevent misfolding-induced toxicity, aberrant proteins are often destroye”