Multivalent binding of nonnative substrate proteins by the chaperonin GroEL. (Q53915559)

22 May 2018

title

Multivalent binding of nonnative substrate proteins by the chaperonin GroEL. (English)

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22 May 2018

author

Neil Ranson

4

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22 May 2018

author name string

G W Farr

1

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22 May 2018

K Furtak

2

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22 May 2018

M B Rowland

3

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22 May 2018

H R Saibil

5

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22 May 2018

T Kirchhausen

6

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22 May 2018

A L Horwich

7

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22 May 2018

language of work or name

English

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publication date

1 March 2000

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22 May 2018

published in

Cell

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22 May 2018

volume

100

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22 May 2018

issue

5

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22 May 2018

page(s)

561-573

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22 May 2018

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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

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Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping

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GroEL-mediated protein folding

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Residues in chaperonin GroEL required for polypeptide binding and release

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SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields

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Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

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Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding

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7 January 2021

Structural aspects of GroEL function

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Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Eukaryotic type II chaperonin CCT interacts with actin through specific subunits

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Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds

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Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction

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

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

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

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Chaperonin function: folding by forced unfolding

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7 January 2021

Structure and function in GroEL-mediated protein folding

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7 January 2021

How GroES regulates binding of nonnative protein to GroEL.

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Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism

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A thermodynamic coupling mechanism for GroEL-mediated unfolding

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7 January 2021

Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

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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

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

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7 January 2021

Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB

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7 January 2021

10.1016/S0092-8674(00)80692-3

Identifiers

DOI

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22 May 2018

1 reference

22 May 2018