Synchronized domain-opening motion of GroEL is essential for communication between the two rings. (Q53898975)

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English	Synchronized domain-opening motion of GroEL is essential for communication between the two rings.	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

11139586

retrieved

22 May 2018

reference URL

http://europepmc.org/abstract/MED/11139586

title

Synchronized domain-opening motion of GroEL is essential for communication between the two rings. (English)

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Europe PubMed Central

PubMed publication ID

11139586

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22 May 2018

reference URL

http://europepmc.org/abstract/MED/11139586

author

Fumihiro Motojima

series ordinal

3

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Europe PubMed Central

PubMed publication ID

11139586

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22 May 2018

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http://europepmc.org/abstract/MED/11139586

Toru Hisabori

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4

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Europe PubMed Central

PubMed publication ID

11139586

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22 May 2018

reference URL

http://europepmc.org/abstract/MED/11139586

author name string

Shiseki K

series ordinal

1

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Europe PubMed Central

PubMed publication ID

11139586

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22 May 2018

reference URL

http://europepmc.org/abstract/MED/11139586

Murai N

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2

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PubMed publication ID

11139586

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22 May 2018

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http://europepmc.org/abstract/MED/11139586

Yoshida M

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5

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PubMed publication ID

11139586

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22 May 2018

reference URL

http://europepmc.org/abstract/MED/11139586

Taguchi H

series ordinal

6

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PubMed publication ID

11139586

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22 May 2018

reference URL

http://europepmc.org/abstract/MED/11139586

language of work or name

English

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publication date

3 January 2001

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Europe PubMed Central

PubMed publication ID

11139586

retrieved

22 May 2018

reference URL

http://europepmc.org/abstract/MED/11139586

published in

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

11139586

retrieved

22 May 2018

reference URL

http://europepmc.org/abstract/MED/11139586

volume

276

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Europe PubMed Central

PubMed publication ID

11139586

retrieved

22 May 2018

reference URL

http://europepmc.org/abstract/MED/11139586

issue

14

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Europe PubMed Central

PubMed publication ID

11139586

retrieved

22 May 2018

reference URL

http://europepmc.org/abstract/MED/11139586

page(s)

11335-11338

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PubMed publication ID

11139586

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22 May 2018

reference URL

http://europepmc.org/abstract/MED/11139586

cites work

The Hsp70 and Hsp60 chaperone machines

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21 January 2018

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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21 January 2018

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

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21 January 2018

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

1 reference

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reference URL

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retrieved

21 January 2018

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

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M010348200

retrieved

21 January 2018

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

1 reference

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reference URL

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retrieved

21 January 2018

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

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reference URL

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retrieved

21 January 2018

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

1 reference

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21 January 2018

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

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21 January 2018

A malachite green colorimetric assay for protein phosphatase activity

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21 January 2018

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

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21 January 2018

Molecular cloning and nucleotide sequence of 3-isopropylmalate dehydrogenase gene (leuB) from an extreme thermophile, Thermus aquaticus YT-1.

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21 January 2018

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

1 reference

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reference URL

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21 January 2018

Structure and function in GroEL-mediated protein folding

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21 January 2018

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

1 reference

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.M010348200

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21 January 2018

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

1 reference

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Crossref

reference URL

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21 January 2018

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

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21 January 2018

Structural basis of allosteric changes in the GroEL mutant Arg197→Ala

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21 January 2018

GroEL locked in a closed conformation by an interdomain cross-link can bind ATP and polypeptide but cannot process further reaction steps

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M010348200

retrieved

21 January 2018

Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M010348200

retrieved

21 January 2018

Refolding and Reassembly of Active Chaperonin GroEL After Denaturation

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M010348200

retrieved

21 January 2018

Identifiers

DOI

10.1074/JBC.M010348200

1 reference

stated in

Europe PubMed Central

PubMed publication ID

11139586

retrieved

22 May 2018

reference URL

http://europepmc.org/abstract/MED/11139586

PubMed publication ID

11139586

1 reference

stated in

Europe PubMed Central

PubMed publication ID

11139586

retrieved

22 May 2018

reference URL

http://europepmc.org/abstract/MED/11139586

 

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