Interaction with GroEL destabilises non-amphiphilic secondary structure in a peptide (Q73196301)

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2 November 2019

title

Interaction with GroEL destabilises non-amphiphilic secondary structure in a peptide (English)

1 reference

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2 November 2019

author name string

M Preuss

series ordinal

1

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2 November 2019

A D Miller

series ordinal

2

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2 November 2019

publication date

1 November 1999

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2 November 2019

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2 November 2019

volume

461

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2 November 2019

issue

3

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2 November 2019

page(s)

131-135

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The general concept of molecular chaperones

2 November 2019

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

21 January 2018

2 references

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21 January 2018

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inferred from DOI database lookup

7 January 2021

based on heuristic

A structural model for GroEL-polypeptide recognition

1 reference

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Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

Interaction of GroEL with conformational states of horse cytochrome c

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

Dominant forces in the recognition of a transient folding intermediate of alpha-lactalbumin by GroEL

21 January 2018

1 reference

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Nature and consequences of GroEL-protein interactions.

21 January 2018

1 reference

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Individual subunits of bacterial luciferase are molten globules and interact with molecular chaperones

21 January 2018

1 reference

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

21 January 2018

1 reference

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Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

The chaperonin GroEL binds to late-folding non-native conformations present in native Escherichia coli and murine dihydrofolate reductases

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

Two conformational states of β-lactamase bound to GroEL: a biophysical characterization 1 1Edited by A. R. Fersht

21 January 2018

1 reference

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Insight into the conformation of protein folding intermediate(s) trapped by GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

The region of alpha-lactalbumin recognized by GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

Hydrogen-exchange kinetics of reduced alpha-lactalbumin bound to the chaperonin GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

The chaperonin GroEL binds a polypeptide in an .alpha.-helical conformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901442-8

10.1016/S0014-5793(99)01442-8

21 January 2018

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10567683%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

1 reference