(Q72465574)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7836352%20AND%20SRC:MED&resulttype=core&format=json

26 October 2019

title

The hydrophobic nature of GroEL-substrate binding (English)

1 reference

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26 October 2019

Z Lin

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7836352%20AND%20SRC:MED&resulttype=core&format=json

26 October 2019

F P Schwartz

series ordinal

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7836352%20AND%20SRC:MED&resulttype=core&format=json

26 October 2019

E Eisenstein

series ordinal

1 reference

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26 October 2019

language of work or name

English

0 references

publication date

1 January 1995

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7836352%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

26 October 2019

published in

1 reference

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26 October 2019

volume

270

1 reference

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26 October 2019

issue

1 reference

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26 October 2019

page(s)

1011-1014

1 reference

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26 October 2019

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Demonstration by genetic suppression of interaction of GroE products with many proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

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/10.1074%2FJBC.270.3.1011

Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Molecular chaperone functions of heat-shock proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequences of beta-lactamase precursor.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature beta-lactamase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Catalysis of a protein folding reaction: thermodynamic and kinetic analysis of subtilisin BPN' interactions with its propeptide fragment.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Energetics of folding subtilisin BPN'

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Rapid measurement of binding constants and heats of binding using a new titration calorimeter

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

21 January 2018

Protein stability curves

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Folding of subtilisin BPN': characterization of a folding intermediate.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Sequential mechanism of refolding of carbonic anhydrase B.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Cooperativity in protein-folding kinetics

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Some factors in the interpretation of protein denaturation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Dominant forces in protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Physiochemical aspects of drug-protein interactions: a general perspective

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Hydrophobic effect in protein folding and other noncovalent processes involving proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Heat capacity and entropy changes in processes involving proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Secondary structure of bovine αS1- and β-casein in solution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

Association of alpha-S-casein C in the alkaline pH range.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.3.1011

21 January 2018

Identifiers

DOI

10.1074/JBC.270.3.1011

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7836352%20AND%20SRC:MED&resulttype=core&format=json

26 October 2019

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7836352%20AND%20SRC:MED&resulttype=core&format=json