The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding (Q58007398)

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France Keppel

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Costa Georgopoulos

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Manajit K. Hayer-Hartl

Nature structural biology

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publication date

November 1998

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published in

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volume

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issue

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page(s)

977-985

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cites work

Molecular chaperones in cellular protein folding

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GroEL-mediated protein folding

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The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

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

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In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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Residues in chaperonin GroEL required for polypeptide binding and release

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Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

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

21 January 2018

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

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

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ATP induces large quaternary rearrangements in a cage-like chaperonin structure

21 January 2018

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Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

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The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

21 January 2018

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

21 January 2018

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Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.

21 January 2018

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

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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Structural and mechanistic consequences of polypeptide binding by GroEL.

21 January 2018

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Structural aspects of GroEL function

21 January 2018

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Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR

21 January 2018

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

21 January 2018

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beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange

21 January 2018

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Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.

21 January 2018

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A thermodynamic coupling mechanism for GroEL-mediated unfolding

21 January 2018

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Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

21 January 2018

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A structural model for GroEL-polypeptide recognition

21 January 2018

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

21 January 2018

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Molecular chaperones. Opening and closing the Anfinsen cage.

21 January 2018

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Host participation in bacteriophage lambda head assembly

21 January 2018

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The Hsp70 and Hsp60 Chaperone Machines

21 January 2018

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Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms

21 January 2018

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Structure of the Substrate Binding Domain of the Thermosome, an Archaeal Group II Chaperonin

21 January 2018

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

21 January 2018

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Refolding chromatography with immobilized mini-chaperones

21 January 2018

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The pRSET family of T7 promoter expression vectors for Escherichia coli

21 January 2018

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Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL.

21 January 2018

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How to measure and predict the molar absorption coefficient of a protein

21 January 2018

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Renaturation of citrate synthase: influence of denaturant and folding assistants

21 January 2018

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Sequence analysis and phenotypic characterization of groEL mutations that block lambda and T4 bacteriophage growth

21 January 2018

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A new set of useful cloning and expression vectors derived from pBlueScript.

21 January 2018

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The heat-shock-regulated grpE gene of Escherichia coli is required for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds

21 January 2018

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Analysis of gene control signals by DNA fusion and cloning in Escherichia coli

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

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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

Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity

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7 January 2021

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

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7 January 2021

GroE facilitates refolding of citrate synthase by suppressing aggregation

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7 January 2021

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

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7 January 2021

Role of the Host Cell in Bacteriophage Morphogenesis: Effects of a Bacterial Mutation on T4 Head Assembly

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7 January 2021

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

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7 January 2021