Hsp110 Is aBona FideChaperone Using ATP to Unfold Stable Misfolded Polypeptides and Reciprocally Collaborate with Hsp70 to Solubilize Protein Aggregates
Published 2013 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Hsp110 Is aBona FideChaperone Using ATP to Unfold Stable Misfolded Polypeptides and Reciprocally Collaborate with Hsp70 to Solubilize Protein Aggregates
Authors
Keywords
-
Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 288, Issue 29, Pages 21399-21411
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2013-06-05
DOI
10.1074/jbc.m113.479253
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis
- (2013) Andrija Finka et al. CELL STRESS & CHAPERONES
- Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides
- (2013) Smriti Priya et al. FEBS LETTERS
- Biophysical Characterization of Two Different Stable Misfolded Monomeric Polypeptides That Are Chaperone-Amenable Substrates
- (2013) Antonino Natalello et al. JOURNAL OF MOLECULAR BIOLOGY
- GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP
- (2013) S. Priya et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Metazoan Hsp70 machines use Hsp110 to power protein disaggregation
- (2012) Heike Rampelt et al. EMBO JOURNAL
- Comparative Proteomic Analysis of Eleven Common Cell Lines Reveals Ubiquitous but Varying Expression of Most Proteins
- (2012) Tamar Geiger et al. MOLECULAR & CELLULAR PROTEOMICS
- Structure and Dynamics of the ATP-Bound Open Conformation of Hsp70 Chaperones
- (2012) Roman Kityk et al. MOLECULAR CELL
- Chaperoning protein evolution
- (2012) Paolo De Los Rios et al. Nature Chemical Biology
- Rational Design of Oncocin Derivatives with Superior Protease Stabilities and Antibacterial Activities Based on the High-Resolution Structure of the Oncocin-DnaK Complex
- (2011) Daniel Knappe et al. CHEMBIOCHEM
- Unique Peptide Substrate Binding Properties of 110-kDa Heat-shock Protein (Hsp110) Determine Its Distinct Chaperone Activity
- (2011) Xinping Xu et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Molecular Chaperones and Associated Cellular Clearance Mechanisms against Toxic Protein Conformers in Parkinson’s Disease
- (2011) Marie-Pierre Hinault et al. Neurodegenerative Diseases
- The Mammalian Disaggregase Machinery: Hsp110 Synergizes with Hsp70 and Hsp40 to Catalyze Protein Disaggregation and Reactivation in a Cell-Free System
- (2011) James Shorter PLoS One
- Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones
- (2011) A. Zhuravleva et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate
- (2011) Sandeep K. Sharma et al. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
- Binding of a Small Molecule at a Protein–Protein Interface Regulates the Chaperone Activity of Hsp70–Hsp40
- (2010) Susanne Wisén et al. ACS Chemical Biology
- Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells
- (2010) Andrija Finka et al. CELL STRESS & CHAPERONES
- Protein folding on the ribosome
- (2010) Lisa D Cabrita et al. CURRENT OPINION IN STRUCTURAL BIOLOGY
- Stable α-Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-domain Co-chaperones
- (2010) Marie-Pierre Hinault et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Interaction of the Hsp110 Molecular Chaperones from S. cerevisiae with Substrate Protein
- (2010) Sigrun Polier et al. JOURNAL OF MOLECULAR BIOLOGY
- A story of thrift unfolds
- (2010) François Baneyx et al. Nature Chemical Biology
- The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
- (2010) Sandeep K Sharma et al. Nature Chemical Biology
- Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
- (2009) E. B. Bertelsen et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Hsp110 Is a Nucleotide-activated Exchange Factor for Hsp70
- (2008) Claes Andréasson et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Molecular Mechanism of Thioflavin-T Binding to the Surface of β-Rich Peptide Self-Assemblies
- (2008) Matthew Biancalana et al. JOURNAL OF MOLECULAR BIOLOGY
- Molecular Basis for Regulation of the Heat Shock Transcription Factor σ32 by the DnaK and DnaJ Chaperones
- (2008) Fernanda Rodriguez et al. MOLECULAR CELL
- Structure of the Hsp110:Hsc70 Nucleotide Exchange Machine
- (2008) Jonathan P. Schuermann et al. MOLECULAR CELL
Discover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversationAdd your recorded webinar
Do you already have a recorded webinar? Grow your audience and get more views by easily listing your recording on Peeref.
Upload Now