(Q31120057)

29 June 2017

A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation (English)

1 reference

29 June 2017

6

Arthur L Horwich

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Robert B. Best

object named as

Robert B Best

2

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Helen Saibil

7

object named as

Helen R Saibil

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29 June 2017

B Trevor Sewell

1

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29 June 2017

Shaoxia Chen

3

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29 June 2017

Alan M Roseman

4

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29 June 2017

George W Farr

5

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29 June 2017

10 October 2004

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Nature Structural & Molecular Biology

29 June 2017

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29 June 2017

11

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29 June 2017

11

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29 June 2017

1128-1133

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The chaperonin folding machine

29 June 2017

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

21 January 2018

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

21 January 2018

1 reference

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

21 January 2018

1 reference

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

21 January 2018

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

21 January 2018

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ATP-bound states of GroEL captured by cryo-electron microscopy

21 January 2018

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Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT

21 January 2018

1 reference

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

21 January 2018

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Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

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Salt bridges at the inter-ring interface regulate the thermostat of GroEL.

21 January 2018

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

21 January 2018

1 reference

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

21 January 2018

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A dynamic model for the allosteric mechanism of GroEL

21 January 2018

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Transient kinetic analysis of ATP-induced allosteric transitions in the eukaryotic chaperonin containing TCP-1.

21 January 2018

1 reference

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

MRC image processing programs

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

CHARMM: A program for macromolecular energy, minimization, and dynamics calculations

21 January 2018

1 reference

All-atom empirical potential for molecular modeling and dynamics studies of proteins

21 January 2018

1 reference

Polar hydrogen positions in proteins: Empirical energy placement and neutron diffraction comparison

21 January 2018

1 reference

Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding

21 January 2018

1 reference

Structure and function in GroEL-mediated protein folding

21 January 2018

1 reference

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

31 March 2020

1 reference

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

31 March 2020

1 reference

31 March 2020

Identifiers

DOI

10.1038/NSMB844

1 reference

Dimensions Publication ID

29 June 2017

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