A dynamic model for the allosteric mechanism of GroEL (Q28145239)

scientific article (publication date: 15 September 2000)

Language	Label	Description	Also known as
English	A dynamic model for the allosteric mechanism of GroEL	scientific article (publication date: 15 September 2000)

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instance of

scholarly article

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title

A dynamic model for the allosteric mechanism of GroEL (English)

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4

M Karplus

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author name string

J Ma

series ordinal

1

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P B Sigler

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2

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Z Xu

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3

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language of work or name

English

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publication date

15 September 2000

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published in

Journal of Molecular Biology

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volume

302

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issue

2

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page(s)

303-13

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cites work

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

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[24] Probing conformations of GroEL-bound substrate proteins by mass spectrometry

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GroES in the asymmetric GroEL14-GroES7 complex exchanges via an associative mechanism

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Conformational changes in the chaperonin GroEL: new insights into the allosteric mechanism

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GroEL-mediated protein folding

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

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Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

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

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Residues in chaperonin GroEL required for polypeptide binding and release

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The allosteric mechanism of the chaperonin GroEL: a dynamic analysis

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

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Tension in haemoglobin revealed by Fe-His(F8) bond rupture in the fully liganded T-state

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The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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

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GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism.

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

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Cooperativity in ATP hydrolysis by GroEL is increased by GroES

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A structural model for GroEL-polypeptide recognition

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Protein folding in the cell

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https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.2000.4014

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

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1006/JMBI.2000.4014

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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11 October 2022

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10.1006/JMBI.2000.4014

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Consolidated OpenCitations Corpus – April 2017

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2021221

OpenCitations bibliographic resource ID

2021221

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stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2021221

A dynamic model for the allosteric mechanism of GroEL (Q28145239)

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A dynamic model for the allosteric mechanism of GroEL (Q28145239)

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