(Q77298313)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10196153%20AND%20SRC:MED&resulttype=core&format=json

4 December 2019

title

"Half of the sites" binding of D-glyceraldehyde-3-phosphate dehydrogenase folding intermediate with GroEL (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10196153%20AND%20SRC:MED&resulttype=core&format=json

4 December 2019

author name string

J Li

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10196153%20AND%20SRC:MED&resulttype=core&format=json

4 December 2019

C C Wang

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10196153%20AND%20SRC:MED&resulttype=core&format=json

4 December 2019

language of work or name

English

0 references

publication date

1 April 1999

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10196153%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

4 December 2019

published in

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10196153%20AND%20SRC:MED&resulttype=core&format=json

4 December 2019

volume

274

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10196153%20AND%20SRC:MED&resulttype=core&format=json

4 December 2019

issue

16

1 reference

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4 December 2019

page(s)

10790-10794

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10196153%20AND%20SRC:MED&resulttype=core&format=json

Influence of Coenzyme on the Refolding and Reassociation in vitro of Glyceraldehyde-3-phosphate Dehydrogenase from Yeast

4 December 2019

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

Dissociation and aggregation of D-glyceraldehyde-3-phosphate dehydrogenase during denaturation by guanidine hydrochloride

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

An asynchronous unfolding among molecular different regions of lobster D-glyceraldehyde-3-phosphate dehydrogenase and maltotetraose-forming amylase from an Alcaligenes sp. during guanidine denaturation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

Mechanism of Reactivation and Refolding of Glyceraldehyde-3-Phosphate Dehydrogenase from Yeast after Denaturation and Dissociation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

Reassociation and Reactivation of Yeast Glyceraldehyde-3-Phosphate Dehydrogenase after Dissociation in the Presence of ATP

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

Folding intermediates of hyperthermophilic D-glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima are trapped at low temperature

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

The low-temperature folding intermediate of hyperthermophilic D-glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima shows a native-like cooperative unfolding transition

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

Does DsbA have chaperone-like activity?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

Nature and consequences of GroEL-protein interactions.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

Binding of a burst-phase intermediate formed in the folding of denatured D-glyceraldehyde-3-phosphate dehydrogenase by chaperonin 60 and 8-anilino-1-naphthalenesulphonic acid

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

Structural and mechanistic consequences of polypeptide binding by GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

Symmetric complexes of GroE chaperonins as part of the functional cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

Glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

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.274.16.10790

Factors affecting the folding and association of flounder muscle glyceraldehyde-3-phosphate dehydrogenase, in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

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.274.16.10790

Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

How GroES regulates binding of nonnative protein to GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

The hydrophobic nature of GroEL-substrate binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

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.274.16.10790

Conformational changes at the nucleotide binding of GroEL induced by binding of protein substrates. Luminescence studies

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

Insight into the conformation of protein folding intermediate(s) trapped by GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor refined at 2 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

GroEL-mediated folding of structurally homologous dihydrofolate reductases.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.16.10790

21 January 2018

Identifiers

DOI

10.1074/JBC.274.16.10790

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10196153%20AND%20SRC:MED&resulttype=core&format=json

4 December 2019

1 reference