(Q33879856)

29 July 2017

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title

Protein folding and unfolding by Escherichia coli chaperones and chaperonins (English)

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29 July 2017

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Gottesman ME

1

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29 July 2017

Hendrickson WA

series ordinal

2

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29 July 2017

publication date

1 April 2000

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Current Opinion in Microbiology

29 July 2017

published in

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29 July 2017

volume

3

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29 July 2017

issue

2

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29 July 2017

page(s)

197-202

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Structural analysis of substrate binding by the molecular chaperone DnaK

29 July 2017

cites work

1 reference

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7 January 2021

NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction

1 reference

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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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain

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7 January 2021

Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

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7 January 2021

A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone

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7 January 2021

GHKL, an emergent ATPase/kinase superfamily

1 reference

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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

1 reference

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7 January 2021

The influence of C-terminal extension on the structure of the “J-domain” in E. coli DnaJ

1 reference

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7 January 2021

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

1 reference

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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.

1 reference

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7 January 2021

Interaction of DnaK with native proteins and membrane proteins correlates with their accessible hydrophobicity

1 reference

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7 January 2021

On the mechanism of FtsH-dependent degradation of the sigma 32 transcriptional regulator of Escherichia coli and the role of the Dnak chaperone machine

1 reference

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7 January 2021

Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli.

1 reference

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7 January 2021

Successive action of Escherichia coli chaperones in vivo.

1 reference

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7 January 2021

Peptide-induced conformational changes in the molecular chaperone DnaK

1 reference

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7 January 2021

Kinetics of the reactions of the Escherichia coli molecular chaperone DnaK with ATP: evidence that a three-step reaction precedes ATP hydrolysis

1 reference

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7 January 2021

Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling

1 reference

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7 January 2021

Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.

1 reference

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7 January 2021

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

1 reference

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7 January 2021

GrpE alters the affinity of DnaK for ATP and Mg2+. Implications for the mechanism of nucleotide exchange.

1 reference

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7 January 2021

ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli

1 reference

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7 January 2021

Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.

1 reference

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7 January 2021

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

1 reference

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7 January 2021

Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

Trigger factor and DnaK cooperate in folding of newly synthesized proteins.

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

Chaperone properties of bacterial elongation factor EF-G and initiation factor IF2

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

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

1 reference

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7 January 2021

A structural model for GroEL-polypeptide recognition

1 reference

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7 January 2021

The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

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

1 reference

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7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

Identification of in vivo substrates of the chaperonin GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

Basis of Substrate Binding by the Chaperonin GroEL†

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

GroEL recognises sequential and non-sequential linear structural motifs compatible with extended beta-strands and alpha-helices

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

Chaperone rings in protein folding and degradation.

1 reference

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7 January 2021

GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

GroEL/GroES promote dissociation/reassociation cycles of a heterodimeric intermediate during alpha(2)beta(2) protein assembly. Iterative annealing at the quaternary structure level

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

Rapid degradation of an abnormal protein in Escherichia coli proceeds through repeated cycles of association with GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

Concurrent chaperone and protease activities of ClpAP and the requirement for the N-terminal ClpA ATP binding site for chaperone activity

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis

1 reference

https://api.crossref.org/works/10.1016%2FS1369-5274%2800%2900075-8

7 January 2021

10.1016/S1369-5274(00)00075-8

Identifiers

DOI

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29 July 2017

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