The molecular architecture of the eukaryotic chaperonin TRiC/CCT
about
Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitroProgrammed cell death protein 5 interacts with the cytosolic chaperonin containing tailless complex polypeptide 1 (CCT) to regulate β-tubulin foldingChaperones in hepatitis C virus infectionContribution of the Type II Chaperonin, TRiC/CCT, to OncogenesisChaperone machines for protein folding, unfolding and disaggregationThe dynamic conformational cycle of the group I chaperonin C-termini revealed via molecular dynamics simulationThe molecular architecture of the Dam1 kinetochore complex is defined by cross-linking based structural modelling.The Crystal Structures of the Eukaryotic Chaperonin CCT Reveal Its Functional PartitioningStructure and mechanism of the Rubisco-assembly chaperone Raf1ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure.Dynamics, flexibility, and allostery in molecular chaperoninsCross-link guided molecular modeling with ROSETTAExploration of the dynamic properties of protein complexes predicted from spatially constrained protein-protein interaction networksAnalysis of nidogen-1/laminin γ1 interaction by cross-linking, mass spectrometry, and computational modeling reveals multiple binding modesThe structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCTAssisted protein folding at low temperature: evolutionary adaptation of the Antarctic fish chaperonin CCT and its client proteinsCharacterization of native protein complexes and protein isoform variation using size-fractionation-based quantitative proteomicsIn vivo protein interaction network analysis reveals porin-localized antibiotic inactivation in Acinetobacter baumannii strain AB5075xTract: software for characterizing conformational changes of protein complexes by quantitative cross-linking mass spectrometryXLmap: an R package to visualize and score protein structure models based on sites of protein cross-linkingDissociation behavior of a bifunctional tempo-active ester reagent for peptide structure analysis by free radical initiated peptide sequencing (FRIPS) mass spectrometry.Structure of full-length p53 tumor suppressor probed by chemical cross-linking and mass spectrometry.Automated assignment of MS/MS cleavable cross-links in protein 3D-structure analysis.The advancement of chemical cross-linking and mass spectrometry for structural proteomics: from single proteins to protein interaction networks.Reliable identification of cross-linked products in protein interaction studies by 13C-labeled p-benzoylphenylalanine.Trifunctional cross-linker for mapping protein-protein interaction networks and comparing protein conformational statesProbing large conformational rearrangements in wild-type and mutant spectrin using structural mass spectrometryAsymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiCStructure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexesA new in vivo cross-linking mass spectrometry platform to define protein-protein interactions in living cells.Conformational States of macromolecular assemblies explored by integrative structure calculation.Structures of the Gβ-CCT and PhLP1-Gβ-CCT complexes reveal a mechanism for G-protein β-subunit folding and Gβγ dimer assembly.Conformational flexibility and subunit arrangement of the modular yeast Spt-Ada-Gcn5 acetyltransferase complexA direct regulatory interaction between chaperonin TRiC and stress-responsive transcription factor HSF1.Structural insight into the cooperation of chloroplast chaperonin subunits.Probing structures of large protein complexes using zero-length cross-linking.Gln40 deamidation blocks structural reconfiguration and activation of SCF ubiquitin ligase complex by Nedd8.Folding of large multidomain proteins by partial encapsulation in the chaperonin TRiC/CCT.A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle.
P2860
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P2860
The molecular architecture of the eukaryotic chaperonin TRiC/CCT
description
2012 nî lūn-bûn
@nan
2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT
@nl
The molecular architecture of the eukaryotic chaperonin TRiC/CCT
@ast
The molecular architecture of the eukaryotic chaperonin TRiC/CCT
@en
type
label
The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT
@nl
The molecular architecture of the eukaryotic chaperonin TRiC/CCT
@ast
The molecular architecture of the eukaryotic chaperonin TRiC/CCT
@en
prefLabel
The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT
@nl
The molecular architecture of the eukaryotic chaperonin TRiC/CCT
@ast
The molecular architecture of the eukaryotic chaperonin TRiC/CCT
@en
P2093
P2860
P50
P3181
P1433
P1476
The molecular architecture of the eukaryotic chaperonin TRiC/CCT
@en
P2093
Andreas Bracher
Bryan Chen
Leonie Mönkemeyer
Lukasz A Joachimiak
Sebastian Pechmann
Steve Ludtke
Thomas Walzthoeni
P2860
P304
P3181
P356
10.1016/J.STR.2012.03.007
P577
2012-04-12T00:00:00Z