Multiple states of a nucleotide-bound group 2 chaperonin. - Wikidata - awgldk - TriplyDB

Multiple states of a nucleotide-bound group 2 chaperonin.

Multiple states of a nucleotide-bound group 2 chaperonin.

http://www.wikidata.org/entity/Q37286298

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Mechanism of folding chamber closure in a group II chaperonin Chaperone machines for protein folding, unfolding and disaggregation Crystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding Cycle Crystal Structure of Group II Chaperonin in the Open State Dual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin Chamber Chaperonins from an Antarctic archaeon are predominantly monomeric: crystal structure of an open state monomer Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle.Mechanism of nucleotide sensing in group II chaperonins ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin Flexible interwoven termini determine the thermal stability of thermosomes Multiscale natural moves refine macromolecules using single-particle electron microscopy projection images Asymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiC Single-molecule fluorescence polarization study of conformational change in archaeal group II chaperonin.MESMER: minimal ensemble solutions to multiple experimental restraints.Weak intra-ring allosteric communications of the archaeal chaperonin thermosome revealed by normal mode analysis The structural dynamics of macromolecular processes.Insights into chaperonin function from studies on archaeal thermosomes.ATP-driven molecular chaperone machines.Internal (His)₆-tagging delivers a fully functional hetero-oligomeric class II chaperonin in high yield.Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM.The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.Intraring allostery controls the function and assembly of a hetero-oligomeric class II chaperonin.Time-Resolved Measurement of the ATP-Dependent Motion of the Group II Chaperonin by Diffracted Electron Tracking.Accurate flexible refinement of atomic models against medium-resolution cryo-EM maps using damped dynamics

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Multiple states of a nucleotide-bound group 2 chaperonin.

http://www.wikidata.org/entity/Q37286298

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on April 2008

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Multiple states of a nucleotide-bound group 2 chaperonin.

@en

Multiple states of a nucleotide-bound group 2 chaperonin.

@nl

type

label

Multiple states of a nucleotide-bound group 2 chaperonin.

@en

Multiple states of a nucleotide-bound group 2 chaperonin.

@nl

prefLabel

Multiple states of a nucleotide-bound group 2 chaperonin.

@en

Multiple states of a nucleotide-bound group 2 chaperonin.

@nl

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J.STR.2008.01.016

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Multiple states of a nucleotide-bound group 2 chaperonin.

@en

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Daniel K Clare

http://www.w3.org/2001/XMLSchema#string

George W Farr

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Helen R Saibil

http://www.w3.org/2001/XMLSchema#string

Joel Quispe

http://www.w3.org/2001/XMLSchema#string

Scott Stagg

http://www.w3.org/2001/XMLSchema#string

P2860

Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis

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

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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

Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin

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

SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields

Accurate determination of local defocus and specimen tilt in electron microscopy

Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets.

A new generation of the IMAGIC image processing system

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528-534

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scholarly article

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10.1016/J.STR.2008.01.016

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4

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16

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Arthur L. Horwich

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2008-04-01T00:00:00Z

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5452884

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18400175

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2719814

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