(Q58660250)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9829996%20AND%20SRC:MED&resulttype=core&format=json

6 December 2019

title

GroEL under heat-shock. Switching from a folding to a storing function (English)

1 reference

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6 December 2019

1

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6 December 2019

Arturo Muga

4

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9829996%20AND%20SRC:MED&resulttype=core&format=json

6 December 2019

José María Valpuesta

5

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6 December 2019

author name string

A Galán

2

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6 December 2019

J L Carrascosa

3

1 reference

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6 December 2019

language of work or name

English

0 references

publication date

1 December 1998

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9829996%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

6 December 2019

published in

1 reference

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6 December 2019

volume

273

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9829996%20AND%20SRC:MED&resulttype=core&format=json

6 December 2019

page(s)

32587-32594

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9829996%20AND%20SRC:MED&resulttype=core&format=json

6 December 2019

issue

49

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9829996%20AND%20SRC:MED&resulttype=core&format=json

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

6 December 2019

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Protein folding in the central cavity of the GroEL-GroES chaperonin complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

The formation of symmetrical GroEL-GroES complexes in the presence of ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Conformational changes in the GroEL oligomer during the functional cycle.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

The Hsp70 and Hsp60 chaperone machines

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Symmetric GroEL-GroES complexes can contain substrate simultaneously in both GroEL rings

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Biochemical Characterization of Symmetric GroEL-GroES Complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Prevention of protein denaturation under heat stress by the chaperonin Hsp60

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

An arabinose-inducible expression vector, pAR3, compatible with ColE1-derived plasmids.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

9 Escherichia coli phage T4 topoisomerase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Three-dimensional reconstruction of single particles embedded in ice

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

A variant to the “random approximation” of the reference-free alignment algorithm

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Pattern recognition and classification of images of biological macromolecules using artificial neural networks

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Xmipp: An Image Processing Package for Electron Microscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

A new resolution criterion based on spectral signal-to-noise ratios

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Confidence limits for resolution estimation in image averaging by random subsampling

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

The ATPase activity of chaperonin GroEL is highly stimulated at elevated temperatures.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Effects of the Inter-ring Communication in GroEL Structural and Functional Asymmetry

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Release of both native and non-native proteins from a cis-only GroEL ternary complex.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Conditions of forming protein complexes with GroEL can influence the mechanism of chaperonin-assisted refolding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Inter-ring communication is disrupted in the GroEL mutant Arg13 --> Gly; Ala126 --> Val with known crystal structure.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

Symmetric complexes of GroE chaperonins as part of the functional cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

GroES binding regulates GroEL chaperonin activity under heat shock

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.49.32587

21 January 2018

Identifiers

DOI

10.1074/JBC.273.49.32587

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9829996%20AND%20SRC:MED&resulttype=core&format=json

6 December 2019

1 reference