(Q73703980)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10777521%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

title

Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form (English)

1 reference

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6 November 2019

2

1 reference

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6 November 2019

author name string

Y H Watanabe

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10777521%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

H Taguchi

series ordinal

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10777521%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

M Yoshida

series ordinal

4

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10777521%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

language of work or name

English

0 references

publication date

1 April 2000

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10777521%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

6 November 2019

published in

1 reference

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6 November 2019

volume

275

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10777521%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

issue

17

1 reference

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6 November 2019

page(s)

12388-12392

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10777521%20AND%20SRC:MED&resulttype=core&format=json

Genetic evidence for a functional relationship between Hsp104 and Hsp70.

6 November 2019

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

Protein disaggregation mediated by heat-shock protein Hsp104.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

The Hsp70 and Hsp60 chaperone machines

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

The role of ATP in the functional cycle of the DnaK chaperone system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

A novel factor required for the assembly of the DnaK and DnaJ chaperones of Thermus thermophilus

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

K+ is an indispensable cofactor for GrpE stimulation of ATPase activity of DnaK x DnaJ complex from Thermus thermophilus.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

Functional properties of the molecular chaperone DnaK from Thermus thermophilus

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

Hsp104 is a highly conserved protein with two essential nucleotide-binding sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

Nucleotide-dependent oligomerization of ClpB from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

Molecular chaperones in cellular protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

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.275.17.12388

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.275.17.12388

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.275.17.12388

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.275.17.12388

GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

Molecular cloning, expression, and characterization of chaperonin-60 and chaperonin-10 from a thermophilic bacterium, Thermus thermophilus HB8.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

Chaperonin from thermophile Thermus thermophilus

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

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.275.17.12388

GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12388

21 January 2018

Identifiers

DOI

10.1074/JBC.275.17.12388

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10777521%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

1 reference