(Q46631403)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18430731%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

title

Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroEL (English)

1 reference

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6 January 2020

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18430731%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

Fumihiro Motojima

series ordinal

4

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18430731%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

author name string

Shigeto Murayama

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18430731%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

Masasuke Yoshida

series ordinal

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18430731%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

language of work or name

English

0 references

publication date

22 April 2008

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18430731%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

6 January 2020

published in

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18430731%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

volume

283

1 reference

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6 January 2020

issue

26

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18430731%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

page(s)

18385-18392

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18430731%20AND%20SRC:MED&resulttype=core&format=json

The Hsp70 and Hsp60 chaperone machines

6 January 2020

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

Chaperonin-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

The chaperonin folding machine

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

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.M709825200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

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.M709825200

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.M709825200

Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

Structural stability of covalently linked GroES heptamer: advantages in the formation of oligomeric structure.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

Chaperonin-mediated folding of green fluorescent protein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

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.M709825200

Discrimination of ATP, ADP, and AMPPNP by chaperonin GroEL: hexokinase treatment revealed the exclusive role of ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

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.M709825200

Topologies of a substrate protein bound to the chaperonin GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

Single-molecule observation of protein-protein interactions in the chaperonin system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

GroEL mediates protein folding with a two successive timer mechanism.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

Identification of in vivo substrates of the chaperonin GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709825200

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.M709825200

21 January 2018

Identifiers

DOI

10.1074/JBC.M709825200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18430731%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

1 reference