Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding (Q37564668)

21 August 2017

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title

Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding (English)

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21 August 2017

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1

Arthur L Horwich

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author name string

Wayne A Fenton

series ordinal

2

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21 August 2017

1 May 2009

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Quarterly Reviews of Biophysics

21 August 2017

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21 August 2017

42

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21 August 2017

2

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21 August 2017

83-116

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A thermodynamic coupling mechanism for GroEL-mediated unfolding

21 August 2017

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

The Disordered Mobile Loop of GroES Folds into a Defined β-Hairpin upon Binding GroEL

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Direct NMR observation of a substrate protein bound to the chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroEL.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Probing Protein-Chaperone Interactions with Single-Molecule Fluorescence Spectroscopy

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Chaperonin chamber accelerates protein folding through passive action of preventing aggregation

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Topologies of a substrate protein bound to the chaperonin GroEL

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Chaperonin complex with a newly folded protein encapsulated in the folding chamber

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Hsp70 accelerates the recovery of nucleolar morphology after heat shock.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Basis of Substrate Binding by the Chaperonin GroEL†

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Speculations on the functions of the major heat shock and glucose-regulated proteins

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Role of the -phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

GroEL1: a dedicated chaperone involved in mycolic acid biosynthesis during biofilm formation in mycobacteria.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Expansion and compression of a protein folding intermediate by GroEL

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

The 13 angstroms structure of a chaperonin GroEL-protein substrate complex by cryo-electron microscopy.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Identification of the binding surface on beta-lactamase for GroEL by limited proteolysis and MALDI-mass spectrometry

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

The chaperonin GroEL does not recognize apo-alpha-lactalbumin in the molten globule state.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

The hydrophobic nature of GroEL-substrate binding

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

A structural model for GroEL-polypeptide recognition

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

The tail of a chaperonin: the C-terminal region of Escherichia coli GroEL protein

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

GroEL-GroES-mediated protein folding

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Folding of malate dehydrogenase inside the GroEL-GroES cavity

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

No evidence for a forced-unfolding mechanism during ATP/GroES binding to substrate-bound GroEL: no observable protection of metastable Rubisco intermediate or GroEL-bound Rubisco from tritium exchange

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

A thermodynamic coupling mechanism can explain the GroEL-mediated acceleration of the folding of barstar

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

A polypeptide bound by the chaperonin groEL is localized within a central cavity

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Triggering protein folding within the GroEL-GroES complex

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Specificity in chaperonin-mediated protein folding

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Chaperonin-mediated protein folding: fate of substrate polypeptide

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

GroEL stimulates protein folding through forced unfolding

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Concerted release of substrate domains from GroEL by ATP is demonstrated with FRET.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Chaperonin function: folding by forced unfolding

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

GroE facilitates refolding of citrate synthase by suppressing aggregation

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

GroEL/GroES-mediated folding of a protein too large to be encapsulated

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Stopped-flow fluorescence analysis of the conformational changes in the GroEL apical domain: relationships between movements in the apical domain and the quaternary structure of GroEL.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature beta-lactamase.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Secondary structure forming propensity coupled with amphiphilicity is an optimal motif in a peptide or protein for association with chaperonin 60 (GroEL)

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Principles that govern the folding of protein chains

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Sculpting the proteome with AAA(+) proteases and disassembly machines.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Nature and consequences of GroEL-protein interactions.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Quantitative dynamics and binding studies of the 20S proteasome by NMR

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Functional communications between the apical and equatorial domains of GroEL through the intermediate domain.

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

Monitoring Protein Conformation along the Pathway of Chaperonin-Assisted Folding

1 reference

https://api.crossref.org/works/10.1017%2FS0033583509004764

7 January 2021

10.1017/S0033583509004764

Identifiers

DOI

1 reference

release_m7ze6o2wlfdrdgxaq46vczkt6u

21 August 2017

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/m7ze6o2wlfdrdgxaq46vczkt6u

24 November 2022

mapped directly with Wikidata item

PubMed ID

19638247

1 reference

PubMed ID

19638247