The Hsp70 and Hsp60 Chaperone Machines

Molecular chaperones in cellular protein folding

1996 • 3,540 citations

From Levinthal to pathways to funnels

1997 • 2,277 citations

The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

1994 • 1,322 citations

The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

1997 • 1,250 citations

Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK

1996 • 1,247 citations

Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone

1997 • 1,235 citations

The Biology of heat shock proteins and molecular chaperones.

1994 • 1,226 citations

The biology of heat shock proteins and molecular chaperones

1994 • 1,203 citations

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

1990 • 1,035 citations

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

1992 • 965 citations

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

1991 • 853 citations

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.

1991 • 835 citations

Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

1997 • 797 citations

A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

1997 • 772 citations

Peptide Binding and Release by Proteins Implicated as Catalysts of Protein Assembly

1989 • 763 citations

Peptide-binding specificity of the molecular chaperone BiP

1991 • 763 citations

Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation

1997 • 750 citations

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP

1989 • 737 citations

HSP100/Clp proteins: a common mechanism explains diverse functions

1996 • 653 citations

Residues in chaperonin GroEL required for polypeptide binding and release

1994 • 645 citations

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

1993 • 593 citations

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE.

1994 • 520 citations

A cytoplasmic chaperonin that catalyzes β-actin folding

1992 • 498 citations

Crystal Structure of the Nucleotide Exchange Factor GrpE Bound to the ATPase Domain of the Molecular Chaperone DnaK

1997 • 489 citations

Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein Folding

1994 • 461 citations

Kinetics of Molecular Chaperone Action

1994 • 440 citations

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

1996 • 436 citations

The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding.

1996 • 424 citations

Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

1995 • 423 citations

Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.

1992 • 412 citations

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL

1997 • 406 citations

Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction

1996 • 403 citations

GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1

1997 • 397 citations

The Role of ATP in the Functional Cycle of the DnaK Chaperone System

1995 • 388 citations

The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL

1996 • 385 citations

Calnexin, calreticulin and the folding of glycoproteins

1997 • 377 citations

Protein folding in the central cavity of the GroEL–GroES chaperonin complex

1996 • 373 citations

Interaction of Hsp70 chaperones with substrates

1997 • 372 citations

ATP-induced protein Hsp70 complex dissociation requires K+ but not ATP hydrolysis

1993 • 366 citations

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

1994 • 359 citations

GroEL‐Mediated protein folding

1997 • 336 citations

Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy

1994 • 334 citations

Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL

1995 • 308 citations

A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.

1996 • 304 citations

Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese

1991 • 298 citations

Chaperones get in touch: the Hip-Hop connection

1997 • 289 citations

The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication.

1994 • 285 citations

A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32.

1996 • 281 citations

The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase.

1995 • 268 citations

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein folding

1993 • 266 citations

Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism.

1996 • 249 citations

The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS

1996 • 244 citations

Nucleotide-induced Conformational Changes in the ATPase and Substrate Binding Domains of the DnaK Chaperone Provide Evidence for Interdomain Communication

1995 • 241 citations

Characterization of a functionally important mobile domain of GroES

1993 • 222 citations

A Bipartite Signaling Mechanism Involved in DnaJ-mediated Activation of the Escherichia coli DnaK Protein

1996 • 222 citations

The Second Step of ATP Binding to DnaK Induces Peptide Release

1996 • 219 citations

Hold 'em and Fold 'em: Chaperones and Signal Transduction

1995 • 201 citations

Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry

1994 • 199 citations

A structural model for GroEL–polypeptide recognition

1997 • 191 citations

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

1991 • 189 citations

NMR Structure of the J-domain and the Gly/Phe-rich Region of theEscherichia coliDnaJ Chaperone

1996 • 186 citations

A polypeptide bound by the chaperonin groEL is localized within a central cavity.

1993 • 177 citations

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

1995 • 176 citations

GrpE Accelerates Nucleotide Exchange of the Molecular Chaperone DnaK with an Associative Displacement Mechanism

1997 • 171 citations

Structure of the Substrate Binding Domain of the Thermosome, an Archaeal Group II Chaperonin

1997 • 162 citations

Positive cooperativity in the functioning of molecular chaperone GroEL.

1992 • 160 citations

Nuclear Magnetic Resonance Solution Structure of the Human Hsp40 (HDJ-1) J-domain

1996 • 155 citations

Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment.

1994 • 152 citations

NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain.

1994 • 147 citations

Substrate Shuttling Between the DnaK and GroEL Systems Indicates a Chaperone Network Promoting Protein Folding

1996 • 145 citations

Asymmetrical Interaction of GroEL and GroES in the ATPase Cycle of Assisted Protein Folding

1995 • 142 citations

Destabilization of the complete protein secondary structure on binding to the chaperone GroEL

1994 • 142 citations

Structure of the Heat Shock Protein Chaperonin-10 of Mycobacterium leprae

1996 • 135 citations

The Hydrophobic Nature of GroEL-Substrate Binding

1995 • 135 citations

Lysine 71 of the Chaperone Protein Hsc70 Is Essential for ATP Hydrolysis

1996 • 134 citations

Catalysis of Amide Proton Exchange by the Molecular Chaperones GroEL and SecB

1996 • 134 citations

Modulation of the ATPase Activity of the Molecular Chaperone DnaK by Peptides and the DnaJ and GrpE Heat Shock Proteins

1995 • 133 citations

Specificity in chaperonin-mediated protein folding

1995 • 132 citations

Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds

1995 • 130 citations

The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system 1 1Edited by J.Karn

1997 • 114 citations

PDZ-like Domains Mediate Binding Specificity in the Clp/Hsp100 Family of Chaperones and Protease Regulatory Subunits

1997 • 108 citations

Ligand exchange during cytochrome c folding

1997 • 103 citations

A thermodynamic coupling mechanism for GroEL-mediated unfolding.

1996 • 99 citations

Structural Adaptations in the Specialized Bacteriophage T4 Co-Chaperonin Gp31 Expand the Size of the Anfinsen Cage

1997 • 98 citations

Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae

1997 • 98 citations

Release of both native and non-native proteins from a cis-only GroEL ternary complex

1996 • 96 citations

To Fold or Not to Fold . . .

1993 • 94 citations

Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction

1997 • 92 citations

The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the sigma 32 heat shock transcriptional regulator.

1995 • 91 citations

Solution small-angle x-ray scattering study of the molecular chaperone Hsc70 and its subfragments

1995 • 90 citations

Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL

1997 • 86 citations

The Dissociation of ATP from hsp70 of Saccharomyces cerevisiae Is Stimulated by Both Ydj1p and Peptide Substrates

1995 • 84 citations

Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins.

1994 • 75 citations

Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulators

1995 • 72 citations

Significant hydrogen exchange protection in GroEL‐bound DHFR is maintained during iterative rounds of substrate cycling

1996 • 64 citations

ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain

1994 • 64 citations

Kinetics of Nucleotide-Induced Changes in the Tryptophan Fluorescence of the Molecular Chaperone Hsc70 and Its Subfragments Suggest the ATP-Induced Conformational Change Follows Initial ATP Binding

1995 • 61 citations

Role of mitochondrial GrpE and phosphate in the ATPase cycle of matrix Hsp70

1997 • 52 citations

Effect of GroEL on the Re-folding Kinetics of α-Lactalbumin

1996 • 51 citations

Interactions between the GroE Chaperonins and Rhodanese

1995 • 50 citations

Characterization of Nucleotide-Free Uncoating ATPase and Its Binding to ATP, ADP, and ATP Analogs

1994 • 46 citations

Nucleotide binding properties of bovine brain uncoating ATPase.

1993 • 44 citations

Characterization of a stable, reactivatable complex between chaperonin 60 and mitochondrial rhodanese.

1992 • 43 citations

Kinetic Analysis of Interactions between GroEL and Reduced α-Lactalbumin

1995 • 42 citations

beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange.

1996 • 39 citations

How GroES Regulates Binding of Nonnative Protein to GroEL

1997 • 35 citations

Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin

1995 • 33 citations

ATP induces non-identity of two rings in chaperonin GroEL.

1994 • 33 citations

The 2.4 A crystal structure of the bacterial chaperonin GroEL complex with ATPγS

1996 • 29 citations

GroEL Binds to and Unfolds Rhodanese Posttranslationally

1996 • 23 citations