(Q46815859)

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Hydrophilic residues 526 KNDAAD 531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity.

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31 December 2019

Hydrophilic residues 526 KNDAAD 531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity (English)

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18184659%20AND%20SRC:MED&resulttype=core&format=json

31 December 2019

protein folding

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Tomohiro Mizobata

4

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31 December 2019

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Kodai Machida

1

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31 December 2019

Akane Kono-Okada

2

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31 December 2019

Kunihiro Hongo

3

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31 December 2019

Yasushi Kawata

5

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9 January 2008

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31 December 2019

Journal of Biological Chemistry

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31 December 2019

283

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31 December 2019

6886-6896

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31 December 2019

11

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31 December 2019

Protein folding in the cell

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

Molecular chaperones in cellular protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

Molecular chaperones in the cytosol: from nascent chain to folded protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

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.M708002200

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.M708002200

21 January 2018

Functional communications between the apical and equatorial domains of GroEL through the intermediate domain.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

The strongly conserved carboxyl-terminus glycine-methionine motif of the Escherichia coli GroEL chaperonin is dispensable.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

A comparison between the sulfhydryl reductants tris(2-carboxyethyl)phosphine and dithiothreitol for use in protein biochemistry

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

Multiple structural transitions of the GroEL subunit are sensitive to intermolecular interactions with cochaperonin and refolding polypeptide.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

17 The use of singlet-singlet energy transfer to study macromolecular assemblies

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

An improved assay for nanomole amounts of inorganic phosphate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

BeF(x) stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

Escherichia coli chaperonins cpn60 (groEL) and cpn10 (groES) do not catalyse the refolding of mitochondrial malate dehydrogenase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of .alpha.-glucosidase from yeast

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

GroEL/GroES-mediated folding of a protein too large to be encapsulated

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

A simple method for displaying the hydropathic character of a protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

Molecular chaperones. Opening and closing the Anfinsen cage.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

GroEL-GroES-mediated protein folding requires an intact central cavity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

GroEL-GroES-mediated protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

The 13 angstroms structure of a chaperonin GroEL-protein substrate complex by cryo-electron microscopy.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

MOLMOL: a program for display and analysis of macromolecular structures

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M708002200

21 January 2018

Identifiers

10.1074/JBC.M708002200

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18184659%20AND%20SRC:MED&resulttype=core&format=json

31 December 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18184659%20AND%20SRC:MED&resulttype=core&format=json

31 December 2019

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