Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein
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Mechanisms of Hsp90 regulationGRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumA truncated form of p23 down-regulates telomerase activity via disruption of Hsp90 functionProtein kinase A-dependent translocation of Hsp90 alpha impairs endothelial nitric-oxide synthase activity in high glucose and diabetesAssociation of NASP with HSP90 in mouse spermatogenic cells: stimulation of ATPase activity and transport of linker histones into nucleiRegulation and function of the human HSP90AA1 geneLPS induces pp60c-src-mediated tyrosine phosphorylation of Hsp90 in lung vascular endothelial cells and mouse lung.Heat shock proteins: cellular and molecular mechanisms in the central nervous system.Hsp-90 and the biology of nematodes.Systems analysis of chaperone networks in the malarial parasite Plasmodium falciparum.Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function.Heat shock cognate protein 70 is involved in rotavirus cell entry.Pnck induces ligand-independent EGFR degradation by probable perturbation of the Hsp90 chaperone complex.Post-translational modifications of Hsp90 and their contributions to chaperone regulationInvolvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunitsAn acetylation site in the middle domain of Hsp90 regulates chaperone function.Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment.Heat-shock treatment-mediated increase in transduction by recombinant adeno-associated virus 2 vectors is independent of the cellular heat-shock protein 90Heat-shock protein 90 inhibitors as novel cancer chemotherapeutics - an update.Src-mediated phosphorylation of Hsp90 in response to vascular endothelial growth factor (VEGF) is required for VEGF receptor-2 signaling to endothelial NO synthase.Targeting chaperones in transformed systems--a focus on Hsp90 and cancer.Human, vector and parasite Hsp90 proteins: A comparative bioinformatics analysis.A proteomic screen identified stress-induced chaperone proteins as targets of Akt phosphorylation in mesangial cellsThe myosin-binding UCS domain but not the Hsp90-binding TPR domain of the UNC-45 chaperone is essential for function in Caenorhabditis elegansTwo-dimensional electrophoresis-based characterization of post-translational modifications of mammalian 20S proteasome complexes.Broad action of Hsp90 as a host chaperone required for viral replication.Regulation of molecular chaperones through post-translational modifications: decrypting the chaperone code.Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes.p90 ribosomal S6 kinase and p70 ribosomal S6 kinase link phosphorylation of the eukaryotic chaperonin containing TCP-1 to growth factor, insulin, and nutrient signaling.Inhibition of apoptosome formation by suppression of Hsp90beta phosphorylation in tyrosine kinase-induced leukemias.Global effects of BCR/ABL and TEL/PDGFRbeta expression on the proteome and phosphoproteome: identification of the Rho pathway as a target of BCR/ABL.Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole.Regulatory Mechanisms of Hsp90.Protein kinase D2 and heat shock protein 90 beta are required for BCL6-associated zinc finger protein mRNA stabilization induced by vascular endothelial growth factor-A.Proteome analysis reveals phosphorylation of ATP synthase beta -subunit in human skeletal muscle and proteins with potential roles in type 2 diabetes.Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies.Detecting Posttranslational Modifications of Hsp90.Hsp90 inhibition renders iNOS aggregation and the clearance of iNOS aggregates by proteasomes requires SPSB2.The HSP90 chaperone machinery.Thr90 phosphorylation of Hsp90α by protein kinase A regulates its chaperone machinery.
P2860
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P2860
Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein
description
2001 nî lūn-bûn
@nan
2001 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Hsp90 phosphorylation is linke ...... ovirus cell attachment protein
@ast
Hsp90 phosphorylation is linke ...... ovirus cell attachment protein
@en
Hsp90 phosphorylation is linke ...... ovirus cell attachment protein
@nl
type
label
Hsp90 phosphorylation is linke ...... ovirus cell attachment protein
@ast
Hsp90 phosphorylation is linke ...... ovirus cell attachment protein
@en
Hsp90 phosphorylation is linke ...... ovirus cell attachment protein
@nl
prefLabel
Hsp90 phosphorylation is linke ...... ovirus cell attachment protein
@ast
Hsp90 phosphorylation is linke ...... ovirus cell attachment protein
@en
Hsp90 phosphorylation is linke ...... ovirus cell attachment protein
@nl
P2093
P2860
P3181
P356
P1476
Hsp90 phosphorylation is linke ...... ovirus cell attachment protein
@en
P2093
P2860
P304
P3181
P356
10.1074/JBC.M105562200
P407
P577
2001-08-31T00:00:00Z