Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes.
about
Direct and Propagated Effects of Small Molecules on Protein-Protein Interaction NetworksThe emerging role of native mass spectrometry in characterizing the structure and dynamics of macromolecular complexes.Functions of the Hsp90 chaperone system: lifting client proteins to new heightsPlasmodium falciparum Hop (PfHop) Interacts with the Hsp70 Chaperone in a Nucleotide-Dependent Fashion and Exhibits Ligand SelectivityMechanistic Asymmetry in Hsp90 DimersSelective targeting of the stress chaperome as a therapeutic strategyMass spectrometry quantifies protein interactions--from molecular chaperones to membrane porins.Dynamic protein ligand interactions--insights from MS.Proteomic analysis reveals heat shock protein 70 has a key role in polycythemia Vera.Structure of a designed protein cage that self-assembles into a highly porous cube.Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain.Hsp70 forms antiparallel dimers stabilized by post-translational modifications to position clients for transfer to Hsp90.Modification of the zonal elution method for detection of transient protein-protein interactions involving ligand exchange.Dissecting heterogeneous molecular chaperone complexes using a mass spectrum deconvolution approach.Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs.Finding the right balance: a personal journey from individual proteins to membrane-embedded motors: based on a lecture delivered at the 36th FEBS Congress in Torino, Italy, June 2011.Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.The interchange of immunophilins leads to parallel pathways and different intermediates in the assembly of Hsp90 glucocorticoid receptor complexes.The Mechanism of Hsp90 ATPase Stimulation by Aha1Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1.A DNA nanoscope via auto-cycling proximity recordingIntegration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.The joining of the Hsp90 and Hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry.Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop.Quantitation of the Noncovalent Cellular Retinol-Binding Protein, Type 1 Complex Through Native Mass Spectrometry.Ion Mobility-Mass Spectrometry Reveals Evidence of Specific Complex Formation between Human Histone Deacetylase 8 and Poly-r(C)-binding Protein 1.STIP1(HOP) binds HSP90 and HSP70:HSP40:nascent proteinAdapting to stress - chaperome networks in cancer.
P2860
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P2860
Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes.
description
2011 nî lūn-bûn
@nan
2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Heterogeneity and dynamics in ...... rotein 90 chaperone complexes.
@ast
Heterogeneity and dynamics in ...... rotein 90 chaperone complexes.
@en
type
label
Heterogeneity and dynamics in ...... rotein 90 chaperone complexes.
@ast
Heterogeneity and dynamics in ...... rotein 90 chaperone complexes.
@en
prefLabel
Heterogeneity and dynamics in ...... rotein 90 chaperone complexes.
@ast
Heterogeneity and dynamics in ...... rotein 90 chaperone complexes.
@en
P2093
P2860
P356
P1476
Heterogeneity and dynamics in ...... rotein 90 chaperone complexes.
@en
P2093
Ima-obong Ebong
Marco A Saraiva
Sophie E Jackson
Soumya Daturpalli
P2860
P304
17939-17944
P356
10.1073/PNAS.1106261108
P407
P577
2011-10-19T00:00:00Z