(Q43600500)

25 November 2017

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

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25 November 2017

4

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25 November 2017

T Inobe

1

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25 November 2017

T Makio

series ordinal

2

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25 November 2017

E Takasu-Ishikawa

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3

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25 November 2017

K Kuwajima

series ordinal

5

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25 November 2017

1 February 2001

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25 November 2017

14

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Biochimica et Biophysica Acta

inferred from page(s)

published in

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25 November 2017

1545

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25 November 2017

160-173

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25 November 2017

1-2

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GroEL-mediated protein folding

25 November 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Structure and function in GroEL-mediated protein folding

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

The Hsp70 and Hsp60 chaperone machines

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Structural aspects of GroEL function

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

The hydrophobic nature of GroEL-substrate binding

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

The chaperonin GroEL does not recognize apo-alpha-lactalbumin in the molten globule state.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Effect of GroEL on the re-folding kinetics of alpha-lactalbumin

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Dominant forces in the recognition of a transient folding intermediate of alpha-lactalbumin by GroEL

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

GroEL recognises sequential and non-sequential linear structural motifs compatible with extended beta-strands and alpha-helices

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Minimal and optimal mechanisms for GroE-mediated protein folding

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

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

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Chaperonin function: folding by forced unfolding

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

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

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Allosteric control by ATP of non-folded protein binding to GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Transient kinetic analysis of adenosine 5'-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Nucleotide binding-promoted conformational changes release a nonnative polypeptide from the Escherichia coli chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Cooperative effects of potassium, magnesium, and magnesium-ADP on the release of Escherichia coli dihydrofolate reductase from the chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: evidence for noncooperative nucleotide binding

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

In vivoanalysis of integration of membrane proteins inEscherichia coli

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

GroE facilitates refolding of citrate synthase by suppressing aggregation

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

The mitochondrial protein import motor: dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Mutation Ala2-->Ser destabilizes intersubunit interactions in the molecular chaperone GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

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

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

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

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https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

How GroES regulates binding of nonnative protein to GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

ATP hydrolysis induces an intermediate conformational state in GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2800%2900274-0

7 January 2021

10.1016/S0167-4838(00)00274-0

Identifiers

DOI

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25 November 2017

1 reference