Multiple domains of the co-chaperone Hop are important for Hsp70 binding.
about
Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.The architecture of functional modules in the Hsp90 co-chaperone Sti1/HopThe hexosamine signaling pathway: deciphering the "O-GlcNAc code"Hold me tight: Role of the heat shock protein family of chaperones in cardiac diseaseHsp 70/Hsp 90 organizing protein as a nitrosylation target in cystic fibrosis therapy.Heat shock protein 70 (hsp70) as an emerging drug target.Regulation of vascular endothelial cell polarization and migration by Hsp70/Hsp90-organizing proteinIndependent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1).Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiaePrimate chaperones Hsc70 (constitutive) and Hsp70 (induced) differ functionally in supporting growth and prion propagation in Saccharomyces cerevisiae.A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteinsMolecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies.Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteinsTetratricopeptide repeat cochaperones in steroid receptor complexesIn vitro epsilon RNA-dependent protein priming activity of human hepatitis B virus polymerase.Chaperoning the chaperone: a role for the co-chaperone Cpr7 in modulating Hsp90 function in Saccharomyces cerevisiae.Stress-induced phosphoprotein-1 maintains the stability of JAK2 in cancer cellsPharmacological targeting of the Hsp70 chaperone.Hsp70 protein complexes as drug targets.Targeting Hsp90 and its co-chaperones to treat Alzheimer's diseaseThe assembly and intermolecular properties of the Hsp70-Tomm34-Hsp90 molecular chaperone complexHsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.Hop cleavage and function in granzyme B-induced apoptosis.Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation.Novel Entropically Driven Conformation-specific Interactions with Tomm34 Protein Modulate Hsp70 Protein Folding and ATPase Activities.Sequence analyses reveal that a TPR-DP module, surrounded by recombinable flanking introns, could be at the origin of eukaryotic Hop and Hip TPR-DP domains and prokaryotic GerD proteins.Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation.Quantification of interaction strengths between chaperones and tetratricopeptide repeat domain-containing membrane proteins.Co-variation of STI1 and WDR36/UTP21 alters cell proliferation in a glaucoma model.Interactions of S100A2 and S100A6 with the tetratricopeptide repeat proteins, Hsp90/Hsp70-organizing protein and kinesin light chain.Structural Insight into Anaphase Promoting Complex 3 Structure and Docking with a Natural Inhibitory CompoundStructure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp.Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions.The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex.Domain:domain interactions within Hop, the Hsp70/Hsp90 organizing protein, are required for protein stability and structure.Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop.
P2860
Q24520314-E7D030EF-BFF5-4D01-955C-1FF16E09677AQ24548013-5D3FBB5B-4B35-41CC-93A6-12FEEB1C057DQ27676637-B9E29AA0-67B5-4A07-AD79-0745A6D28FEEQ28284365-CEF56C8E-3180-4021-BCF9-3553AC309C1BQ28296634-12D203FE-ED96-4451-A46F-80ED11D76C28Q30433825-41965A6E-AD07-45A9-9A0E-8BBF3AAEE2AFQ33956906-8EF9A6C7-12D3-4B29-8786-510D7C6AB16FQ34257507-D8046029-6D1F-4A6B-AD0D-2434BB3A8990Q34293593-1A5039E6-1BA3-4B1D-91B4-DDB87596CEE8Q34587324-B6ED96EA-CEB4-4729-85E6-E3A8DBAE0B1CQ34587831-F13AB553-BF9A-43D1-AE0D-4A217080D1B9Q35152082-6695CA4A-4150-4837-BBA6-A1F498850EF4Q35313148-4A7F38E7-E6AD-4F22-9860-F94AE6E83CAAQ35640147-B64D2284-0D3C-4570-82E2-E4DBA57D3752Q35924587-64EAC234-1D33-4E76-8F1C-023D000D3622Q35943827-3FEB3519-9490-4AE1-B7E2-EEDEC632872BQ36076894-2A0AEFF7-90A8-4178-BF72-8E55A5A1DCD5Q37580422-6C07129E-1AA6-4343-830E-1F83D4A32272Q37622461-5CB5B8FE-D282-430E-9FFB-EF5D3AC4432FQ38037745-0952C57E-F14A-4A4F-B084-5DFB281A06CEQ38234720-F8E37131-0E91-4E13-9431-DA7E9EE7482FQ38609122-54A97462-605E-4468-A027-906625F60B1DQ39795700-05638654-25BB-40DA-9463-99524E12E877Q40226952-A9B52441-DA31-463E-8BAB-DC0D80C7A4BCQ40483613-A1C92346-9EBF-45D8-8DF4-AF64762150E4Q41098204-DFAED1E9-6055-4A4D-BA8B-FA096533DDAAQ41854250-B39F3F0D-55ED-4379-834D-67A6C35348F4Q41884789-30BC55A7-F866-40DE-88FD-3117C21984D1Q41890146-928CAD1F-3D7A-4099-95AA-504FEA87BB17Q42129535-D85946F2-E75A-4421-853C-221034BD4144Q42185907-DAC4ADB5-0DE5-4222-AFED-AC5B7EE97475Q42314964-D9E118D5-EFD9-4A5F-9BB6-B9A120B7BEAEQ42700283-DE6C40F4-F96C-48C2-ABE8-2C932608D94CQ42791206-D0524051-C47D-47DA-A89F-937E9FE4B394Q42833100-D318B560-5286-4643-8208-6E20035D7C56Q43054514-80E2148C-D0BB-4A9E-A36D-08582D316133Q43984053-AAFBC2DD-C905-4894-9AD3-B183A247E307
P2860
Multiple domains of the co-chaperone Hop are important for Hsp70 binding.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
Multiple domains of the co-chaperone Hop are important for Hsp70 binding.
@en
Multiple domains of the co-chaperone Hop are important for Hsp70 binding.
@nl
type
label
Multiple domains of the co-chaperone Hop are important for Hsp70 binding.
@en
Multiple domains of the co-chaperone Hop are important for Hsp70 binding.
@nl
prefLabel
Multiple domains of the co-chaperone Hop are important for Hsp70 binding.
@en
Multiple domains of the co-chaperone Hop are important for Hsp70 binding.
@nl
P2093
P356
P1476
Multiple domains of the co-chaperone Hop are important for Hsp70 binding
@en
P2093
Daniel L Riggs
David F Smith
Jha'Nae Stoffer
Patricia E Carrigan
Patricia J Roberts
P304
16185-16193
P356
10.1074/JBC.M314130200
P407
P577
2004-02-11T00:00:00Z