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。Is Protein Folding a Thermodynamically Unfavorable, Active, Energy-Dependent Process?
Irina Sorokina et al.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2022)
Somatic mutation rates scale with lifespan across mammals
Alex Cagan et al.
NATURE (2022)
Codon-specific Ramachandran plots show amino acid backbone conformation depends on identity of the translated codon
Aviv A. Rosenberg et al.
NATURE COMMUNICATIONS (2022)
Assembly mechanism of early Hsp90-Cdc37-kinase complexes
Dimitra Keramisanou et al.
SCIENCE ADVANCES (2022)
Advances towards Understanding the Mechanism of Action of the Hsp90 Complex
Chrisostomos Prodromou et al.
BIOMOLECULES (2022)
Nonrefoldability is Pervasive Across the E. coli Proteome
Philip To et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2021)
Synonymous codon substitutions perturb cotranslational protein folding in vivo and impair cell fitness
Ian M. Walsh et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2020)
Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein
Rahmi Imamoglu et al.
NATURE COMMUNICATIONS (2020)
Post-translational modifications of Hsp70 family proteins: Expanding the chaperone code
Nitika et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2020)
Post-translational modifications of Hsp90 and translating the chaperone code
Sarah J. Backe et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2020)
ATP-Driven Nonequilibrium Activation of Kinase Clients by the Molecular Chaperone Hsp90
Huafeng Xu
BIOPHYSICAL JOURNAL (2020)
The ATP-powered gymnastics of TRiC/CCT: an asymmetric protein folding machine with a symmetric origin story
Daniel Gestaut et al.
CURRENT OPINION IN STRUCTURAL BIOLOGY (2019)
Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones
Matthias P. Mayer et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2019)
Dancing with the Diva: Hsp90-Client Interactions
Martina Radli et al.
JOURNAL OF MOLECULAR BIOLOGY (2018)
Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins
Pierre Goloubinoff et al.
NATURE CHEMICAL BIOLOGY (2018)
Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions
Ashok Sekhar et al.
ELIFE (2018)
Cochaperones enable Hsp70 to use ATP energy to stabilize native proteins out of the folding equilibrium
Huafeng Xu
SCIENTIFIC REPORTS (2018)
The HSP90 chaperone machinery
Florian H. Schopf et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2017)
Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibrium
Shaon Chakrabarti et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2017)
How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches
Kliment A. Verba et al.
TRENDS IN BIOCHEMICAL SCIENCES (2017)
Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondria! Hsp90 TRAP1
Daniel Elnatan et al.
ELIFE (2017)
HSP90 Shapes the Consequences of Human Genetic Variation
Georgios I. Karras et al.
CELL (2017)
Computational and theoretical advances in studies of intrinsically disordered proteins
Robert B. Best
CURRENT OPINION IN STRUCTURAL BIOLOGY (2017)
The HSP90 Molecular Chaperone-An Enigmatic ATPase
Laurence H. Pearl
BIOPOLYMERS (2016)
The Molecular Chaperone DnaK Is a Source of Mutational Robustness
Jose Aguilar-Rodriguez et al.
GENOME BIOLOGY AND EVOLUTION (2016)
Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37
Dimitra Keramisanou et al.
MOLECULAR CELL (2016)
Importance of cycle timing for the function of the molecular chaperone Hsp90
Bettina K. Zierer et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2016)
Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling
Paolo De Los Rios et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2016)
Hsp70 biases the folding pathways of client proteins
Ashok Sekhar et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2016)
In vivo aspects of protein folding and quality control
David Balchin et al.
SCIENCE (2016)
STRUCTURAL BIOLOGY Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase
Kliment A. Verba et al.
SCIENCE (2016)
Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes
Thomas Reid Alderson et al.
STRUCTURE (2016)
The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding
Manajit Hayer-Hartl et al.
TRENDS IN BIOCHEMICAL SCIENCES (2016)
Importance of cycle timing for the function of the molecular chaperone Hsp90
Bettina K. Zierer et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2016)
Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling
Paolo De Los Rios et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2016)
The yin-yang of kinase activation and unfolding explains the peculiarity of VaI600 in the activation segment of BRAF
Christina Kiel et al.
ELIFE (2016)
Hsp90•Cdc37 Complexes with Protein Kinases Form Cooperatively with Multiple Distinct Interaction Sites
Julia M. Eckl et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2015)
The Mechanism and Function of Group II Chaperonins
Tom Lopez et al.
JOURNAL OF MOLECULAR BIOLOGY (2015)
Translational tuning optimizes nascent protein folding in cells
Soo Jung Kim et al.
SCIENCE (2015)
Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP
Jiao Yang et al.
STRUCTURE (2015)
Pathways of allosteric regulation in Hsp70 chaperones
Roman Kityk et al.
NATURE COMMUNICATIONS (2015)
Structural Basis for the Inhibition of HSP70 and DnaK Chaperones by Small-Molecule Targeting of a C-Terminal Allosteric Pocket
Julia I-Ju Leu et al.
ACS CHEMICAL BIOLOGY (2014)
Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions
Christopher J. Oldfield et al.
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 83 (2014)
Glucocorticoid Receptor Function Regulated by Coordinated Action of the Hsp90 and Hsp70 Chaperone Cycles
Elaine Kirschke et al.
CELL (2014)
VER-155008, a small molecule inhibitor of HSP70 with potent anti-cancer activity on lung cancer cell lines
Wei Wen et al.
EXPERIMENTAL BIOLOGY AND MEDICINE (2014)
Active Cage Mechanism of Chaperonin-Assisted Protein Folding Demonstrated at Single-Molecule Level
Amit J. Gupta et al.
JOURNAL OF MOLECULAR BIOLOGY (2014)
Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption
Paolo De Los Rios et al.
ELIFE (2014)
ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system
Sigrun Polier et al.
NATURE CHEMICAL BIOLOGY (2013)
Protein rescue from aggregates by powerful molecular chaperone machines
Shannon M. Doyle et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2013)
A global view of Hsp90 functions
Gabriela Chiosis et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2013)
Hsp70 chaperone dynamics and molecular mechanism
Matthias P. Mayer
TRENDS IN BIOCHEMICAL SCIENCES (2013)
ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin
Daniel K. Clare et al.
CELL (2012)
Microscopic reversibility as the organizing principle of molecular machines
R. Dean Astumian
NATURE NANOTECHNOLOGY (2012)
Constructing ensembles for intrinsically disordered proteins
Charles K. Fisher et al.
CURRENT OPINION IN STRUCTURAL BIOLOGY (2011)
Unstructural biology coming of age
Peter Tompa
CURRENT OPINION IN STRUCTURAL BIOLOGY (2011)
Molecular chaperones in protein folding and proteostasis
F. Ulrich Hartl et al.
NATURE (2011)
The client protein p53 adopts a molten globule-like state in the presence of Hsp90
Sung Jean Park et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2011)
Conformational dynamics of the molecular chaperone Hsp90
Kristin A. Krukenberg et al.
QUARTERLY REVIEWS OF BIOPHYSICS (2011)
Binding of a Small Molecule at a Protein-Protein Interface Regulates the Chaperone Activity of Hsp70-Hsp40
Susanne Wisen et al.
ACS CHEMICAL BIOLOGY (2010)
Cellular Proteomes Have Broad Distributions of Protein Stability
Kingshuk Ghosh et al.
BIOPHYSICAL JOURNAL (2010)
Chaperonin-Catalyzed Rescue of Kinetically Trapped States in Protein Folding
Kausik Chakraborty et al.
CELL (2010)
Role of DnaJ G/F-rich Domain in Conformational Recognition and Binding of Protein Substrates
Judit Perales-Calvo et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2010)
The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
Sandeep K. Sharma et al.
NATURE CHEMICAL BIOLOGY (2010)
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Mikko Taipale et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2010)
Single-molecule spectroscopy of protein folding in a chaperonin cage
Hagen Hofmann et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2010)
The Human Cdc37•Hsp90 Complex Studied by Heteronuclear NMR Spectroscopy
Sridhar Sreeramulu et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2009)
Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding
Arthur L. Horwich et al.
QUARTERLY REVIEWS OF BIOPHYSICS (2009)
Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution
D. Allan Drummond et al.
CELL (2008)
A role for confined water in chaperonin function
Jeremy L. England et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2008)
Molecular chaperones and protein kinase quality control
Avrom J. Caplan et al.
TRENDS IN CELL BIOLOGY (2007)
A silent polymorphism in the MDR1 gene changes substrate specificity
Chava Kimchi-Sarfaty et al.
SCIENCE (2007)
GroEL-Mediated protein folding: Making the impossible, possible
Zong Lin et al.
CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY (2006)
Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein
Yun-Chi Tang et al.
CELL (2006)
Molecular chaperones and protein quality control
Bernd Bukau et al.
CELL (2006)
Protein stability promotes evolvability
JD Bloom et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2006)
Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding
CW Park et al.
NATURE METHODS (2005)
Protein tolerance to random amino acid change
HH Guo et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2004)
Effects of confinement in chaperonin assisted protein folding: Rate enhancement by decreasing the roughness of the folding energy landscape
A Baumketner et al.
JOURNAL OF MOLECULAR BIOLOGY (2003)
The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70
P Wittung-Stafshede et al.
BIOCHEMISTRY (2003)
Activation of the ATPase activity of Hsp90 by the stress-regulated cochaperone Aha1
B Panaretou et al.
MOLECULAR CELL (2002)
CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90
S Rüdiger et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2002)
Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc97
G Siligardi et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Hsp90 as a capacitor of phenotypic variation
C Queitsch et al.
NATURE (2002)
Why are proteins marginally stable?
DM Taverna et al.
PROTEINS-STRUCTURE FUNCTION AND GENETICS (2002)
ATP-bound states of GroEL captured by cryo-electron microscopy
NA Ranson et al.
CELL (2001)
Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone
S Rüdiger et al.
EMBO JOURNAL (2001)