Structural studies on the co-chaperone Hop and its complexes with Hsp90.
about
A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting proteinThe crystal structure of the N-terminal region of BUB1 provides insight into the mechanism of BUB1 recruitment to kinetochoresMechanisms of Hsp90 regulationThe 'active life' of Hsp90 complexesModeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimerThe architecture of functional modules in the Hsp90 co-chaperone Sti1/HopCrystal structure of c5321: a protective antigen present in uropathogenic Escherichia coli strains displaying an SLR foldExploring the Functional Complementation between Grp94 and Hsp90C-terminal sequences of hsp70 and hsp90 as non-specific anchors for tetratricopeptide repeat (TPR) proteinsATPase activity and ATP-dependent conformational change in the co-chaperone HSP70/HSP90-organizing protein (HOP)A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.Hsp 70/Hsp 90 organizing protein as a nitrosylation target in cystic fibrosis therapy.HOP is a monomer: investigation of the oligomeric state of the co-chaperone HOP.Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis.Heat shock protein 70 (hsp70) as an emerging drug target.Regulation of vascular endothelial cell polarization and migration by Hsp70/Hsp90-organizing proteinProteomic analysis of nasal epithelial cells from cystic fibrosis patientsProbing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics.Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells.Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone.Versatile TPR domains accommodate different modes of target protein recognition and functionBalance between folding and degradation for Hsp90-dependent client proteins: a key role for CHIP.Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex.ATP analog enhances the actions of a heat shock protein 90 inhibitor in multiple myeloma cells.Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes.Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteinsA novel class of small molecule inhibitors of Hsp90.Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activityAdvances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment.Molecularly targeted agents as radiosensitizers in cancer therapy--focus on prostate cancer.New developments in Hsp90 inhibitors as anti-cancer therapeutics: mechanisms, clinical perspective and more potential.Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket.Characterization of celastrol to inhibit hsp90 and cdc37 interaction.Alternate strategies of Hsp90 modulation for the treatment of cancer and other diseases.BUB1 and BUBR1: multifaceted kinases of the cell cycle.Conformational dynamics of the molecular chaperone Hsp90Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity.Structure and function of SET and MYND domain-containing proteins.Novel Entropically Driven Conformation-specific Interactions with Tomm34 Protein Modulate Hsp70 Protein Folding and ATPase Activities.Hop/Sti1 phosphorylation inhibits its co-chaperone function.
P2860
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P2860
Structural studies on the co-chaperone Hop and its complexes with Hsp90.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Structural studies on the co-chaperone Hop and its complexes with Hsp90.
@en
Structural studies on the co-chaperone Hop and its complexes with Hsp90.
@nl
type
label
Structural studies on the co-chaperone Hop and its complexes with Hsp90.
@en
Structural studies on the co-chaperone Hop and its complexes with Hsp90.
@nl
prefLabel
Structural studies on the co-chaperone Hop and its complexes with Hsp90.
@en
Structural studies on the co-chaperone Hop and its complexes with Hsp90.
@nl
P2093
P1476
Structural studies on the co-chaperone Hop and its complexes with Hsp90.
@en
P2093
E T Coulstock
J G Grossmann
S C Onuoha
S E Jackson
P304
P356
10.1016/J.JMB.2008.02.013
P407
P577
2008-02-14T00:00:00Z