Reconciling theories of chaperonin accelerated folding with experimental evidence (Q37620229)

21 August 2017

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title

Reconciling theories of chaperonin accelerated folding with experimental evidence (English)

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21 August 2017

2

Joan-Emma Shea

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21 August 2017

Andrew I Jewett

1

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21 August 2017

publication date

23 October 2009

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Cellular and Molecular Life Sciences

21 August 2017

published in

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21 August 2017

volume

67

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21 August 2017

issue

2

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21 August 2017

page(s)

255-276

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Chaperonin GroEL meets the substrate protein as a "load" of the rings.

21 August 2017

cites work

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Crossref

https://api.crossref.org/works/10.1007%2FS00018-009-0164-6

Chaperonin-mediated protein folding

21 January 2018

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Crossref

https://api.crossref.org/works/10.1007%2FS00018-009-0164-6

Rattling the cage: computational models of chaperonin-mediated protein folding

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1007%2FS00018-009-0164-6

Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitro

21 January 2018

1 reference

12 December 2020

GroEL-GroES-mediated protein folding requires an intact central cavity

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12 December 2020

The effect of macromolecular crowding on chaperonin-mediated protein folding

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12 December 2020

Thinking outside the box: new insights into the mechanism of GroEL-mediated protein folding.

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12 December 2020

Protein Folding: Importance of the Anfinsen Cage

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12 December 2020

Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli beta-galactosidase

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12 December 2020

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

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12 December 2020

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

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12 December 2020

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

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12 December 2020

The ATPase activity of GroEL is supported at high temperatures by divalent cations that stabilize its structure

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12 December 2020

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

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12 December 2020

Protein folding and misfolding

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12 December 2020

Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms

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12 December 2020

Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin

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12 December 2020

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

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12 December 2020

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

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12 December 2020

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

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12 December 2020

GroEL stimulates protein folding through forced unfolding

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12 December 2020

Folding of newly translated proteins in vivo: the role of molecular chaperones

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12 December 2020

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

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12 December 2020

Potential for modulation of the hydrophobic effect inside chaperonins

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12 December 2020

Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition

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12 December 2020

Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

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12 December 2020

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

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12 December 2020

Global minimization of an off-lattice potential energy function using a chaperone-based refolding method

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12 December 2020

The importance of sequence diversity in the aggregation and evolution of proteins

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12 December 2020

Effects of crowding and confinement on the structures of the transition state ensemble in proteins.

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12 December 2020

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

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12 December 2020

Landscape approaches for determining the ensemble of folding transition states: success and failure hinge on the degree of frustration

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12 December 2020

Catalysis of protein folding by symmetric chaperone complexes

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12 December 2020

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

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12 December 2020

Atomic-level observation of macromolecular crowding effects: escape of a protein from the GroEL cage

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12 December 2020

Identification of in vivo substrates of the chaperonin GroEL

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12 December 2020

Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB

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12 December 2020

Chaperonin function: folding by forced unfolding

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12 December 2020

Monitoring Protein Conformation along the Pathway of Chaperonin-Assisted Folding

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12 December 2020

In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System

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12 December 2020

Reversible folding of rhodanese. Presence of intermediate(s) at equilibrium

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12 December 2020

Spin glasses and the statistical mechanics of protein folding

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12 December 2020

Review: allostery in chaperonins

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12 December 2020

Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.

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12 December 2020

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

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12 December 2020

Malleability of protein folding pathways: a simple reason for complex behaviour

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12 December 2020

The Hsp70 and Hsp60 chaperone machines

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12 December 2020

Single-molecule observation of protein-protein interactions in the chaperonin system

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12 December 2020

The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding

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12 December 2020

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

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12 December 2020

Recombination of protein domains facilitated by co-translational folding in eukaryotes

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12 December 2020

Molecular crowding enhances native state stability and refolding rates of globular proteins

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12 December 2020

Nanopore-protein interactions dramatically alter stability and yield of the native state in restricted spaces.

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12 December 2020

GroEL/GroES-dependent reconstitution of alpha2 beta2 tetramers of humanmitochondrial branched chain alpha-ketoacid decarboxylase. Obligatory interaction of chaperonins with an alpha beta dimeric intermediate

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12 December 2020

Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding

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12 December 2020

Protein misfolding, evolution and disease

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12 December 2020

Cell-free translation reconstituted with purified components

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12 December 2020

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

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12 December 2020

To fold or not to fold....

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12 December 2020

Statistical mechanics of kinetic proofreading in protein folding in vivo

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12 December 2020

Directed evolution of substrate-optimized GroEL/S chaperonins

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12 December 2020

Annealing function of GroEL: structural and bioinformatic analysis.

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12 December 2020

Transient aggregates in protein folding are easily mistaken for folding intermediates

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12 December 2020

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

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12 December 2020

Protein misassembly in vitro.

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12 December 2020

Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding

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12 December 2020

Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis

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12 December 2020

Simulations of beta-hairpin folding confined to spherical pores using distributed computing

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12 December 2020

Folding behavior of chaperonin-mediated substrate protein

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12 December 2020

Crowding and hydration effects on protein conformation: a study with sol-gel encapsulated proteins.

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12 December 2020

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

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12 December 2020

Triggering protein folding within the GroEL-GroES complex

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12 December 2020

Expansion and compression of a protein folding intermediate by GroEL

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12 December 2020

On the role of groES in the chaperonin-assisted folding reaction. Three case studies

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12 December 2020

Topologies of a substrate protein bound to the chaperonin GroEL

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12 December 2020

Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures

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12 December 2020

Stabilization of Proteins in Confined Spaces†

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12 December 2020

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

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12 December 2020

For protein misassembly, it's the "I" decade

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12 December 2020

Emerging ideas on the molecular basis of protein and peptide aggregation

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12 December 2020

The Agrobacterium tumefaciens DnaK: ATPase cycle, oligomeric state and chaperone properties

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12 December 2020

Intermolecular aggregations are responsible for the slow kinetics observed in the folding of cytochrome c at neutral pH

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12 December 2020

Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins

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12 December 2020

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

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12 December 2020

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

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12 December 2020

The role of heat-shock and chaperone proteins in protein folding: possible molecular mechanisms

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12 December 2020

A role for confined water in chaperonin function

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12 December 2020

Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains

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12 December 2020

The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor

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12 December 2020

Protein folding and misfolding: mechanism and principles.

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12 December 2020

GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL-GroES complex.

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12 December 2020

Revisiting the GroEL-GroES reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant.

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12 December 2020

Compact Intermediate States in Protein Folding

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12 December 2020

Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP.

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12 December 2020

Thermodynamics and kinetics of protein folding under confinement

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12 December 2020

The allosteric mechanism of the chaperonin GroEL: a dynamic analysis

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12 December 2020

Protein folding Folding with a two-stroke motor

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12 December 2020

Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins

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12 December 2020

How protein thermodynamics and folding mechanisms are altered by the chaperonin cage: molecular simulations

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12 December 2020

Do chaperonins boost protein yields by accelerating folding or preventing aggregation?

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12 December 2020

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

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12 December 2020

A chaperone-mimetic effect of serum albumin on rhodanese

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12 December 2020

Manipulating biopolymer dynamics by anisotropic nanoconfinement

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12 December 2020

Implications of macromolecular crowding for protein assembly.

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12 December 2020

An expanded conformation of single-ring GroEL-GroES complex encapsulates an 86 kDa substrate.

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12 December 2020

Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Chaperonin chamber accelerates protein folding through passive action of preventing aggregation

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12 December 2020

Protein synthesis by pure translation systems.

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12 December 2020

Protein tertiary structure recognition using optimized Hamiltonians with local interactions

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12 December 2020

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

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12 December 2020

Protein folding in the cell: competing models of chaperonin function.

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12 December 2020

Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL.

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12 December 2020

Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli.

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12 December 2020

Probing the "annealing" mechanism of GroEL minichaperone using molecular dynamics simulations

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12 December 2020

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

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12 December 2020

Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli

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12 December 2020

Rhodanese folding is controlled by the partitioning of its folding intermediates

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12 December 2020

Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin

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12 December 2020

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

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12 December 2020

Protein folding under confinement: a role for solvent

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12 December 2020

Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes

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12 December 2020

Theory of protein folding

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12 December 2020

Effects of confinement in chaperonin assisted protein folding: rate enhancement by decreasing the roughness of the folding energy landscape

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12 December 2020

Intermediates: ubiquitous species on folding energy landscapes?

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12 December 2020

A simple model of chaperonin-mediated protein folding

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12 December 2020

Simulations of chaperone-assisted folding.

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12 December 2020

Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding

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12 December 2020

Molecular chaperones in the cytosol: from nascent chain to folded protein

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12 December 2020

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Refolding of barnase in the presence of GroE

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12 December 2020

Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones

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12 December 2020

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

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12 December 2020

SCOP: a structural classification of proteins database for the investigation of sequences and structures

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12 December 2020

Accelerated folding in the weak hydrophobic environment of a chaperonin cavity: creation of an alternate fast folding pathway

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12 December 2020

Interactions between amino acid side chains in cylindrical hydrophobic nanopores with applications to peptide stability

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12 December 2020

GroEL-GroES-mediated protein folding

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12 December 2020

Binding of a chaperonin to the folding intermediates of lactate dehydrogenase

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12 December 2020

Allosteric control by ATP of non-folded protein binding to GroEL

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12 December 2020

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

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12 December 2020

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

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12 December 2020

In vivo newly translated polypeptides are sequestered in a protected folding environment

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12 December 2020

Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity

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12 December 2020

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

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12 December 2020

A Simple Semiempirical Model for the Effect of Molecular Confinement upon the Rate of Protein Folding

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12 December 2020

Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle.

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12 December 2020

Folding funnels and frustration in off-lattice minimalist protein landscapes

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12 December 2020

Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60.

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12 December 2020

Confinement effects on the thermodynamics of protein folding: Monte Carlo simulations

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12 December 2020

A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo.

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12 December 2020

Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Folding of malate dehydrogenase inside the GroEL-GroES cavity

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12 December 2020

Allosteric regulation of chaperonins.

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12 December 2020

Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation

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12 December 2020

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

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12 December 2020

Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage

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12 December 2020

Polar confinement modulates solvation behavior of methane molecules.

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12 December 2020

The energy landscape theory of protein folding: insights into folding mechanisms and scenarios

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12 December 2020

Protein folding in confined and crowded environments

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12 December 2020

Setting the chaperonin timer: a two-stroke, two-speed, protein machine

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12 December 2020

A folding machine for many but a master of none

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12 December 2020

Exploring the origins of topological frustration: design of a minimally frustrated model of fragment B of protein A.

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12 December 2020

Universality and diversity of the protein folding scenarios: a comprehensive analysis with the aid of a lattice model

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12 December 2020

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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12 December 2020

Topological and energetic factors: what determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteins

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Folding on the chaperone: yield enhancement through loose binding

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12 December 2020

Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.

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12 December 2020

The GroEL/GroES cis cavity as a passive anti-aggregation device

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12 December 2020

Converging concepts of protein folding in vitro and in vivo

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12 December 2020

GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side

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12 December 2020

Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.

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12 December 2020

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

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12 December 2020

Essential role of the chaperonin folding compartment in vivo

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12 December 2020

Kinetic model for the coupling between allosteric transitions in GroEL and substrate protein folding and aggregation

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12 December 2020

GroEL mediates protein folding with a two successive timer mechanism.

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12 December 2020

Dimeric trigger factor stably binds folding-competent intermediates and cooperates with the DnaK-DnaJ-GrpE chaperone system to allow refolding

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12 December 2020

Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding

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12 December 2020

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

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12 December 2020

Modeling Hsp70-mediated protein folding

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12 December 2020

Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli

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12 December 2020

Aggregation events occur prior to stable intermediate formation during refolding of interleukin 1beta

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12 December 2020

Chaperonin-mediated protein folding: fate of substrate polypeptide

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12 December 2020

How GroES regulates binding of nonnative protein to GroEL.

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12 December 2020

Kinetic partitioning of protein folding and aggregation.

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12 December 2020

Probing Protein-Chaperone Interactions with Single-Molecule Fluorescence Spectroscopy

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12 December 2020

10.1007/S00018-009-0164-6

Identifiers

DOI

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21 August 2017

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