(Q33830195)

29 July 2017

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title

GroEL-substrate interactions: molding the fold, or folding the mold? (English)

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29 July 2017

Feltham JL

1

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29 July 2017

Gierasch LM

series ordinal

2

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29 July 2017

language of work or name

English

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publication date

1 January 2000

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29 July 2017

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29 July 2017

volume

100

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29 July 2017

issue

2

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29 July 2017

page(s)

193-196

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Model peptide studies demonstrate that amphipathic secondary structures can be recognized by the chaperonin GroEL (cpn60)

29 July 2017

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

A structural model for GroEL-polypeptide recognition

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

Kinetic studies of beta-sheet protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

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%2FS0092-8674%2800%2981557-3

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%2FS0092-8674%2800%2981557-3

7 January 2021

GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism.

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

In vivo observation of polypeptide flux through the bacterial chaperonin system.

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

Identification of in vivo substrates of the chaperonin GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

Characterization of a functionally important mobile domain of GroES.

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo.

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

Secondary structure forming propensity coupled with amphiphilicity is an optimal motif in a peptide or protein for association with chaperonin 60 (GroEL)

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

Chaperonin function: folding by forced unfolding

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

Structure and function in GroEL-mediated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

Identification of substrate binding site of GroEL minichaperone in solution

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

Basis of Substrate Binding by the Chaperonin GroEL†

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2981557-3

7 January 2021

10.1016/S0092-8674(00)81557-3

Identifiers

DOI

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29 July 2017

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