(Q41026044)

25 September 2017

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title

Molecular chaperones in protein folding and translocation (English)

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25 September 2017

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Clarke AR

1

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25 September 2017

publication date

1 February 1996

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Current Opinion in Structural Biology

25 September 2017

published in

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25 September 2017

volume

6

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25 September 2017

issue

1

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25 September 2017

page(s)

43-50

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https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

25 September 2017

1 reference

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Effect of nucleotide on the binding of peptides to 70-kDa heat shock protein

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

A mutant at position 87 of the GroEL chaperonin is affected in protein binding and ATP hydrolysis.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Different conformations for the same polypeptide bound to chaperones DnaK and GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

DnaK ATPase activity revisited

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Can Hsp70 proteins act as force-generating motors?

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Binding of a chaperonin to the folding intermediates of lactate dehydrogenase

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

The chaperonin GroEL does not recognize apo-alpha-lactalbumin in the molten globule state.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Partner proteins determine multiple functions of Hsp70

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Cooperation of the molecular chaperone Ydj1 with specific Hsp70 homologs to suppress protein aggregation

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Uncoating ATPase is a member of the 70 kilodalton family of stress proteins.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Mechanisms of intracellular protein transport

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Kinetics of molecular chaperone action

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Molecular chaperones. Opening and closing the Anfinsen cage.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

The influence of chaperonins on protein folding. A mechanism for increasing the yield of the native form

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Refolding of barnase in the presence of GroE

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

The molecular chaperonin cpn60 displays local flexibility that is reduced after binding with an unfolded protein

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Symmetric complexes of GroE chaperonins as part of the functional cycle

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

The formation of symmetrical GroEL-GroES complexes in the presence of ATP.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin-assisted folding.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2896%2980093-5

7 January 2021

10.1016/S0959-440X(96)80093-5

Identifiers

DOI

1 reference

25 September 2017

1 reference