(Q74128859)

English

Divalent cations can induce the exposure of GroEL hydrophobic surfaces and strengthen GroEL hydrophobic binding interactions. Novel effects of Zn2+ GroEL interactions

scientific article published on 01 February 1998

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scholarly article

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9452440%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

Divalent cations can induce the exposure of GroEL hydrophobic surfaces and strengthen GroEL hydrophobic binding interactions. Novel effects of Zn2+ GroEL interactions (English)

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9452440%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

author name string

B T Brazil

1

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9 November 2019

J Ybarra

2

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9 November 2019

P M Horowitz

3

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9 November 2019

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publication date

1 February 1998

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9 November 2019

Journal of Biological Chemistry

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9 November 2019

273

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9 November 2019

6

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9 November 2019

3257-3263

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9 November 2019

Principles that govern the folding of protein chains

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

Molecular Chaperones

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

GroE facilitates refolding of citrate synthase by suppressing aggregation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

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/10.1074%2FJBC.273.6.3257

21 January 2018

Purification and properties of groE, a host protein involved in bacteriophage assembly

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

The hydrophobic nature of GroEL-substrate binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

Nature and consequences of GroEL-protein interactions.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

Effect of divalent cations on the molecular structure of the GroEL oligomer.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

The chaperonin GroEL is destabilized by binding of ADP

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

ATP induces large quaternary rearrangements in a cage-like chaperonin structure.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.6.3257

21 January 2018

Identifiers

10.1074/JBC.273.6.3257

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9452440%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9452440%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

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