Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis (Q44430539)

2 December 2017

title

Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis (English)

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2 December 2017

3

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2 December 2017

5

Sebastian Doniach

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2 December 2017

Anne S Meyer

1

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Joel Gillespie

object named as

Joel R Gillespie

series ordinal

2

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Judith Frydman

series ordinal

6

object named as

Judith Frydman

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2 December 2017

Ian S Millet

4

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2 December 2017

language of work or name

English

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publication date

1 May 2003

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2 December 2017

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2 December 2017

volume

113

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2 December 2017

issue

3

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2 December 2017

page(s)

369-381

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Solution structural studies and low-resolution model of the Schizosaccharomyces pombe sap1 protein.

2 December 2017

cites work

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X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-

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Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms

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Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones

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7 January 2021

Group II chaperonins: new TRiC(k)s and turns of a protein folding machine

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7 January 2021

ATP-induced structural change of the thermosome is temperature-dependent

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

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Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.

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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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7 January 2021

The thermosome: chaperonin with a built-in lid

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Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1

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Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin

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Protein folding: versatility of the cytosolic chaperonin TRiC/CCT.

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7 January 2021

ATP Binding Induces Large Conformational Changes in the Apical and Equatorial Domains of the Eukaryotic Chaperonin Containing TCP-1 Complex

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7 January 2021

3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin

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7 January 2021

The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin

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7 January 2021

Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates

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7 January 2021

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Group II chaperonin in an open conformation examined by electron tomography

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Purification of muscle actin

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7 January 2021

The active site of myosin.

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7 January 2021

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

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7 January 2021

Structure and function in GroEL-mediated protein folding

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7 January 2021

G protein mechanisms: insights from structural analysis

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7 January 2021

MgATP binding to the nucleotide-binding domains of the eukaryotic cytoplasmic chaperonin induces conformational changes in the putative substrate-binding domains

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7 January 2021

Reconstruction of low-resolution three-dimensional density maps from one-dimensional small-angle X-ray solution scattering data for biomolecules

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7 January 2021

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction

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7 January 2021

Preparation of tubulin from brain

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7 January 2021

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

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7 January 2021

Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like co-chaperonin

1 reference

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7 January 2021

10.1016/S0092-8674(03)00307-6

Identifiers

DOI

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2 December 2017

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