Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution (Q27640777)

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Structure and function in GroEL-mediated protein folding

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

The Hsp70 and Hsp60 chaperone machines

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Symmetric complexes of GroE chaperonins as part of the functional cycle

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Catalysis of protein folding by symmetric chaperone complexes

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Catalysis, commitment and encapsulation during GroE-mediated folding.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

A thermodynamic coupling mechanism for GroEL-mediated unfolding

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

A computational approach to simplifying the protein folding alphabet.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Review: allostery in chaperonins

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Chaperonin function: folding by forced unfolding

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

7 January 2021

2 references

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

7 January 2021

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

inferred from DOI database lookup

7 January 2021

based on heuristic

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Structural basis of allosteric changes in the GroEL mutant Arg197-->Ala

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Inter-ring communication is disrupted in the GroEL mutant Arg13 --> Gly; Ala126 --> Val with known crystal structure.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Revised effective ionic radii and systematic studies of interatomic distances in halides and chalcogenides

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

GroEL/GroES: structure and function of a two-stroke folding machine

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinement

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

A structural model for GroEL-polypeptide recognition

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Stabilization of GroEL minichaperones by core and surface mutations

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

From minichaperone to GroEL 1: information on GroEL-polypeptide interactions from crystal packing of minichaperones.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Residues in chaperonin GroEL required for polypeptide binding and release

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

ATP hydrolysis is critical for induction of conformational changes in GroEL that expose hydrophobic surfaces.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Folding of malate dehydrogenase inside the GroEL-GroES cavity

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase?

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

Improved methods for building protein models in electron density maps and the location of errors in these models

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2803%2900184-0

10.1016/S0022-2836(03)00184-0

7 January 2021

Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

2366099

2366099

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference