Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins
出版年份 2014 全文链接
标题
Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins
作者
关键词
Hsp70, Hsp110, Hsp40, GroEL, Disaggregase, Polypeptide unfoldase, Holdase, Translocase
出版物
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 71, Issue 17, Pages 3311-3325
出版商
Springer Nature
发表日期
2014-04-24
DOI
10.1007/s00018-014-1627-y
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- The metazoan protein disaggregase and amyloid depolymerase system
- (2014) Mariana P Torrente et al. Prion
- Unique Structural Modulation of a Non-Native Substrate by Cochaperone DnaJ
- (2013) Satyam Tiwari et al. BIOCHEMISTRY
- 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
- Conserved Distal Loop Residues in the Hsp104 and ClpB Middle Domain Contact Nucleotide-binding Domain 2 and Enable Hsp70-dependent Protein Disaggregation
- (2013) Morgan E. DeSantis et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- 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
- Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor
- (2013) J. Lee et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Molecular chaperones and protein folding as therapeutic targets in Parkinson’s disease and other synucleinopathies
- (2013) Darius Ebrahimi-Fakhari et al. Acta Neuropathologica Communications
- An Interdomain Energetic Tug-of-War Creates the Allosterically Active State in Hsp70 Molecular Chaperones
- (2012) Anastasia Zhuravleva et al. CELL
- Metazoan Hsp70 machines use Hsp110 to power protein disaggregation
- (2012) Heike Rampelt et al. EMBO JOURNAL
- Arsenite interferes with protein folding and triggers formation of protein aggregates in yeast
- (2012) T. Jacobson et al. JOURNAL OF CELL SCIENCE
- You Got to Know When to Hold (or Unfold) ‘Em…
- (2012) Daniel N. Hebert et al. MOLECULAR CELL
- Concerted Action of the Ribosome and the Associated Chaperone Trigger Factor Confines Nascent Polypeptide Folding
- (2012) Anja Hoffmann et al. MOLECULAR CELL
- Chaperoning protein evolution
- (2012) Paolo De Los Rios et al. Nature Chemical Biology
- Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces
- (2012) Fabian Seyffer et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- A tightly regulated molecular toggle controls AAA+ disaggregase
- (2012) Yuki Oguchi et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Ribosome-associated chaperones as key players in proteostasis
- (2012) Steffen Preissler et al. TRENDS IN BIOCHEMICAL SCIENCES
- Small Heat Shock Proteins Potentiate Amyloid Dissolution by Protein Disaggregases from Yeast and Humans
- (2012) Martin L. Duennwald et al. PLOS BIOLOGY
- The ribosomal tunnel as a functional environment for nascent polypeptide folding and translational stalling
- (2011) Daniel N Wilson et al. CURRENT OPINION IN STRUCTURAL BIOLOGY
- Molecular chaperones in protein folding and proteostasis
- (2011) F. Ulrich Hartl et al. NATURE
- Mechanics of Hsp70 chaperones enables differential interaction with client proteins
- (2011) Rainer Schlecht et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- 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
- Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling
- (2011) O. Genest et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- 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
- Inhibition of α-synuclein aggregation by small heat shock proteins
- (2011) Ilona B. Bruinsma et al. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
- The Stress of Protein Misfolding: From Single Cells to Multicellular Organisms
- (2011) T. Gidalevitz et al. Cold Spring Harbor Perspectives in Biology
- Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells
- (2010) Andrija Finka et al. CELL STRESS & CHAPERONES
- ATP Binding to Hsp90 Is Sufficient for Effective Chaperoning of p53 Protein
- (2010) Dawid Walerych et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- 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
- The Heat Shock Response: Life on the Verge of Death
- (2010) Klaus Richter et al. MOLECULAR CELL
- Tackling unintelligent design
- (2010) R. John Ellis NATURE
- CSPα promotes SNARE-complex assembly by chaperoning SNAP-25 during synaptic activity
- (2010) Manu Sharma et al. NATURE CELL 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
- Cellular strategies for controlling protein aggregation
- (2010) Jens Tyedmers et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- Common ground for protein translocation: access control for mitochondria and chloroplasts
- (2010) Enrico Schleiff et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- Protein Folding in the Cytoplasm and the Heat Shock Response
- (2010) R. M. Vabulas et al. Cold Spring Harbor Perspectives in Biology
- Importing Mitochondrial Proteins: Machineries and Mechanisms
- (2009) Agnieszka Chacinska et al. CELL
- Disaggregating Chaperones: An Unfolding Story
- (2009) Sandeep Sharma et al. CURRENT PROTEIN & PEPTIDE SCIENCE
- Heavy metal ions are potent inhibitors of protein folding
- (2008) Sandeep K. Sharma et al. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Monitoring Protein Conformation along the Pathway of Chaperonin-Assisted Folding
- (2008) Shruti Sharma et al. CELL
- Structural Basis for the Cooperation of Hsp70 and Hsp110 Chaperones in Protein Folding
- (2008) Sigrun Polier et al. CELL
- Guidelines for the nomenclature of the human heat shock proteins
- (2008) Harm H. Kampinga et al. CELL STRESS & CHAPERONES
- Structure of the Hsp110:Hsc70 Nucleotide Exchange Machine
- (2008) Jonathan P. Schuermann et al. MOLECULAR CELL
- Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments
- (2008) Tobias Haslberger et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- GroEL stimulates protein folding through forced unfolding
- (2008) Zong Lin et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Chaperonin chamber accelerates protein folding through passive action of preventing aggregation
- (2008) A. C. Apetri et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Interaction of the J-Protein Heterodimer Pam18/Pam16 of the Mitochondrial Import Motor with the Translocon of the Inner Membrane
- (2007) Patrick R. D'Silva et al. MOLECULAR BIOLOGY OF THE CELL
Find the ideal target journal for your manuscript
Explore over 38,000 international journals covering a vast array of academic fields.
SearchBecome a Peeref-certified reviewer
The Peeref Institute provides free reviewer training that teaches the core competencies of the academic peer review process.
Get Started