The Hsp70 and Hsp60 chaperone machines (Q29547601)

PubMed

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9476895

23 April 2017

0 references

Bukau B

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9476895

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9476895

23 April 2017

Horwich AL

1 reference

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23 April 2017

language of work or name

1 reference

23 April 2017

publication date

6 February 1998

1 reference

PubMed

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9476895

23 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9476895

23 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9476895

23 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9476895

23 April 2017

page(s)

351-66

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PubMed

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9476895

To fold or not to fold....

23 April 2017

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The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

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

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication

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7 January 2021

Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

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7 January 2021

A structural model for GroEL-polypeptide recognition

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The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

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

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

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

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From Levinthal to pathways to funnels

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

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7 January 2021

GroEL-mediated protein folding

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7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

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7 January 2021

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

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7 January 2021

Peptide binding and release by proteins implicated as catalysts of protein assembly

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7 January 2021

Peptide-binding specificity of the molecular chaperone BiP

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7 January 2021

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

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7 January 2021

Chaperones get in touch: the Hip-Hop connection

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7 January 2021

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

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7 January 2021

A cytoplasmic chaperonin that catalyzes beta-actin folding

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7 January 2021

Characterization of nucleotide-free uncoating ATPase and its binding to ATP, ADP, and ATP analogues

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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

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7 January 2021

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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

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7 January 2021

Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK

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7 January 2021

Molecular chaperones in cellular protein folding

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7 January 2021

Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.

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7 January 2021

Calnexin, calreticulin and the folding of glycoproteins

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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

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Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins.

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A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein

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7 January 2021

Effect of GroEL on the re-folding kinetics of alpha-lactalbumin

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7 January 2021

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

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7 January 2021

Characterization of a functionally important mobile domain of GroES.

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

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7 January 2021

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

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7 January 2021

PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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

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7 January 2021

The hydrophobic nature of GroEL-substrate binding

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7 January 2021

Protein folding Folding with a two-stroke motor

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7 January 2021

Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae

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7 January 2021

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

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7 January 2021

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

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7 January 2021

The role of ATP in the functional cycle of the DnaK chaperone system

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7 January 2021

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

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7 January 2021

Kinetic analysis of interactions between GroEL and reduced alpha-lactalbumin. Effect of GroES and nucleotides

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7 January 2021

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

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7 January 2021

GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism.

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7 January 2021

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

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7 January 2021

NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone

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7 January 2021

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

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7 January 2021

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

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7 January 2021

Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain

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7 January 2021

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

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7 January 2021

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

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7 January 2021

GroEL binds to and unfolds rhodanese posttranslationally

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7 January 2021

Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

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7 January 2021

The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

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7 January 2021

Interaction of Hsp70 chaperones with substrates

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7 January 2021

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

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7 January 2021

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

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7 January 2021

HSP100/Clp proteins: a common mechanism explains diverse functions

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7 January 2021

Kinetics of molecular chaperone action

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7 January 2021

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

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7 January 2021

Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding

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7 January 2021

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

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7 January 2021

How GroES regulates binding of nonnative protein to GroEL.

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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.

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7 January 2021

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

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7 January 2021

The second step of ATP binding to DnaK induces peptide release.

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7 January 2021

Specificity in chaperonin-mediated protein folding

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7 January 2021

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

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7 January 2021

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

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7 January 2021

A thermodynamic coupling mechanism for GroEL-mediated unfolding

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7 January 2021

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

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7 January 2021

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

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7 January 2021

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction

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7 January 2021

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

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7 January 2021

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

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7 January 2021

Ligand exchange during cytochrome c folding

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7 January 2021

Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

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7 January 2021

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

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7 January 2021

Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB

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7 January 2021

Structural analysis of substrate binding by the molecular chaperone DnaK

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7 January 2021

The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates

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7 January 2021