(Q27637162)

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G W Farr

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A M Roseman

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B Gowen

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W A Fenton

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H R Saibil

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

7

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language of work or name

English

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publication date

28 December 2001

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published in

Cell

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volume

107

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issue

7

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page(s)

869-79

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cites work

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7 January 2021

Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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The Hsp70 and Hsp60 chaperone machines

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The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

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Release of both native and non-native proteins from a cis-only GroEL ternary complex

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Folding of malate dehydrogenase inside the GroEL-GroES cavity

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

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Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy.

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Cryo-electron microscopy of vitrified specimens

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An extensively modified version of MolScript that includes greatly enhanced coloring capabilities

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Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

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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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Cooperativity in ATP hydrolysis by GroEL is increased by GroES

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Molecular chaperones in cellular protein folding

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

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

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Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition

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A dynamic model for the allosteric mechanism of GroEL

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Protein folding in the central cavity of the GroEL-GroES chaperonin complex

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Docking structures of domains into maps from cryo-electron microscopy using local correlation

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

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Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy

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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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Structure and function in GroEL-mediated protein folding

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Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10

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Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

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A new generation of the IMAGIC image processing system

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Energy transduction in the F1 motor of ATP synthase

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

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

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Structural basis of allosteric changes in the GroEL mutant Arg197→Ala

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

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7 January 2021

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

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7 January 2021

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

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

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

11779463

1 reference

Consolidated OpenCitations Corpus – April 2017