Literature DB >> 16678092

Molecular chaperones and protein quality control.

Bernd Bukau1, Jonathan Weissman, Arthur Horwich.   

Abstract

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.

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Year:  2006        PMID： 16678092     DOI： 10.1016/j.cell.2006.04.014

Source DB:  PubMed          Journal:  Cell        ISSN： 0092-8674            Impact factor:   41.582


  591 in total

1.  High-throughput screen for Escherichia coli heat shock protein 70 (Hsp70/DnaK): ATPase assay in low volume by exploiting energy transfer.

Authors:  Yoshinari Miyata; Lyra Chang; Anthony Bainor; Thomas J McQuade; Christopher P Walczak; Yaru Zhang; Martha J Larsen; Paul Kirchhoff; Jason E Gestwicki
Journal:  J Biomol Screen       Date:  2010-10-06

2.  Unfolded protein response-regulated Drosophila Fic (dFic) protein reversibly AMPylates BiP chaperone during endoplasmic reticulum homeostasis.

Authors:  Hyeilin Ham; Andrew R Woolery; Charles Tracy; Drew Stenesen; Helmut Krämer; Kim Orth
Journal:  J Biol Chem       Date:  2014-11-13       Impact factor: 5.157

3.  A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation.

Authors:  Qiuyan Wang; Yanfen Liu; Nia Soetandyo; Kheewoong Baek; Ramanujan Hegde; Yihong Ye
Journal:  Mol Cell       Date:  2011-06-24       Impact factor: 17.970

4.  Induction of heat shock proteins by hyperthermia and noise overstimulation in hsf1 -/- mice.

Authors:  Tzy-Wen Gong; Damon A Fairfield; Lynne Fullarton; David F Dolan; Richard A Altschuler; David C Kohrman; Margaret I Lomax
Journal:  J Assoc Res Otolaryngol       Date:  2011-09-20

5.  The large Hsp70 Grp170 binds to unfolded protein substrates in vivo with a regulation distinct from conventional Hsp70s.

Authors:  Julia Behnke; Linda M Hendershot
Journal:  J Biol Chem       Date:  2013-12-10       Impact factor: 5.157

Review 6.  An emerging concept of prion infections as a form of transmissible cerebral amyloidosis.

Authors:  Omar Lupi; Marcius Achiame Peryassu
Journal:  Prion       Date:  2007 Oct-Dec       Impact factor: 3.931

7.  Hsp90-Tau complex reveals molecular basis for specificity in chaperone action.

Authors:  G Elif Karagöz; Afonso M S Duarte; Elias Akoury; Hans Ippel; Jacek Biernat; Tania Morán Luengo; Martina Radli; Tatiana Didenko; Bryce A Nordhues; Dmitry B Veprintsev; Chad A Dickey; Eckhard Mandelkow; Markus Zweckstetter; Rolf Boelens; Tobias Madl; Stefan G D Rüdiger
Journal:  Cell       Date:  2014-02-27       Impact factor: 41.582

8.  Structural and functional insights into TRiC chaperonin from a psychrophilic yeast, Glaciozyma antarctica.

Authors:  Nur Athirah Yusof; Shazilah Kamaruddin; Farah Diba Abu Bakar; Nor Muhammad Mahadi; Abdul Munir Abdul Murad
Journal:  Cell Stress Chaperones       Date:  2019-01-16       Impact factor: 3.667

9.  Sequential duplications of an ancient member of the DnaJ-family expanded the functional chaperone network in the eukaryotic cytosol.

Authors:  Chandan Sahi; Jacek Kominek; Thomas Ziegelhoffer; Hyun Young Yu; Maciej Baranowski; Jaroslaw Marszalek; Elizabeth A Craig
Journal:  Mol Biol Evol       Date:  2013-01-16       Impact factor: 16.240

10.  SAHA enhances Proteostasis of epilepsy-associated α1(A322D)β2γ2 GABA(A) receptors.

Authors:  Xiao-Jing Di; Dong-Yun Han; Ya-Juan Wang; Mark R Chance; Ting-Wei Mu
Journal:  Chem Biol       Date:  2013-11-07
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