Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase.
about
Heterozygous yeast deletion collection screens reveal essential targets of Hsp90In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysisExperimental illumination of a fitness landscapeAha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperoneCooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signalingThe Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKRGenetic analysis of viable Hsp90 alleles reveals a critical role in Drosophila spermatogenesisThe human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refoldingThe ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domainsThe p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficaciesCDC37 is required for p60v-src activity in yeastReview: The HSP90 molecular chaperone-an enigmatic ATPaseThe 'active life' of Hsp90 complexesModeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimerA molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperoneActivity of IPI-504, a novel heat-shock protein 90 inhibitor, in patients with molecularly defined non-small-cell lung cancer.Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response.SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteinsContribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae.The proper folding of a long C-terminal segment of the yeast Lys14p regulator is required for activation of LYS genes in response to the metabolic effector.The hsp90 molecular chaperone modulates multiple telomerase activities.Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cellsA two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).Hsp90 is regulated by a switch point in the C-terminal domainFunctional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae.Hsp90 enables Ctf13p/Skp1p to nucleate the budding yeast kinetochore.Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.HSP90 controls SIR2 mediated gene silencingFolding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins.The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90.In vivo analysis of the Hsp90 cochaperone Sti1 (p60)Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependenceDegradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery.The yeast CDC37 gene interacts with MPS1 and is required for proper execution of spindle pole body duplication.In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone.Tpo1-mediated spermine and spermidine export controls cell cycle delay and times antioxidant protein expression during the oxidative stress response.Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones.The molecular chaperone Hsp90 is required for high osmotic stress response in Saccharomyces cerevisiae.Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.
P2860
Q21134948-AC082CE9-2064-4CA7-B742-3C3692622EDCQ22008008-98445F9F-9FCB-497D-87EC-5D0165B3F590Q22066261-954897B7-5EAC-4DC7-9D5F-B59ED7DD1697Q24295270-94765B83-42A9-46C7-9C08-542304F14759Q24520322-36EC1818-F98E-473D-B193-0090AD4B1298Q24535594-A8258D2C-FDEA-4BE9-A949-A3960BDE6DB1Q24548039-4F080BA4-B7B0-469F-B2BB-AF86F395E4A0Q24562938-E7049632-8F77-44A9-96E3-07C73EA86B46Q24599484-60A82122-A8F4-4DB1-A846-778E78D9CE71Q24609487-7D267414-C3EE-4C28-86D8-119E6062672DQ24655034-8C4BAFD1-A6B4-41EC-BF9E-BBAA7492BC3AQ26753822-70D7B57D-7B3C-46BA-B664-47DD789DFB90Q26829003-0353278E-0390-4D0A-BFC7-510582E0B7F9Q27335863-291D39A3-BB69-4992-9450-099672EB04BFQ27739168-DBD3FEBA-3AD6-4393-927B-84CCB0AC22D4Q27851585-B1AB8453-0F70-4788-AE33-D965CEB8C62DQ27929962-067E86B9-9056-42D0-9AB4-310F0AC85CF0Q27930015-F5E612F0-C83F-4444-96A6-78BFB5CBFB68Q27930200-E179DE54-711E-4800-8058-62E54A4292E7Q27930630-C3E66159-FC07-4DB1-9FBD-564AED2F011BQ27930828-1EDBC1A2-0E66-45E4-A662-C26C062E1ECDQ27931200-4AABA0A7-7E90-47C2-88A0-702DBED68B6EQ27932386-DE3A0EBE-3380-4D3D-AAAD-8E7E1799CE5EQ27933174-DBE7EA62-4944-48B2-A4D3-D270C86309A8Q27933447-A92C5843-5EA7-4B63-B2EA-8542B2E235C7Q27934627-E05A379B-6928-4BC3-B818-9D245C36E370Q27934755-EE21D663-8536-4B19-BAA9-314906BF4A8AQ27935459-50E55AA0-0F25-4F9D-B0FA-43C06E295DB5Q27935523-0FCC16BD-15A4-4A75-B05D-24C6772A08B6Q27936139-01F4BBE6-2A6B-4E1B-9D41-40888F4D8EB3Q27936475-4DF145BC-E3BD-4A36-9A9D-7FD1EB5B60E8Q27937090-3165317F-3B15-408B-AD57-2DE21A08C309Q27937497-F19F18C3-3153-40C1-858A-571C7C633915Q27937556-2BDFFE71-2EF4-483F-BB51-C972A1E1BD54Q27937845-B2845E59-8D8F-4745-9314-D0B2E4492F66Q27937958-6BD1E0E7-ADD3-4A95-8A6C-EE8A965CC384Q27938313-A48A622F-F15D-45E8-9EE5-579729AF3F1DQ27938505-DDD89157-5FBC-439A-BBBA-65F50B633FAAQ27939955-CE6456DE-0A97-4456-A185-E685F32F254CQ27940000-0E7845AC-1E3E-4DA7-B16A-4198105B1D83
P2860
Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase.
description
1995 nî lūn-bûn
@nan
1995 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Mutational analysis of Hsp90 f ...... receptor and a protein kinase.
@ast
Mutational analysis of Hsp90 f ...... receptor and a protein kinase.
@en
Mutational analysis of Hsp90 f ...... receptor and a protein kinase.
@nl
type
label
Mutational analysis of Hsp90 f ...... receptor and a protein kinase.
@ast
Mutational analysis of Hsp90 f ...... receptor and a protein kinase.
@en
Mutational analysis of Hsp90 f ...... receptor and a protein kinase.
@nl
prefLabel
Mutational analysis of Hsp90 f ...... receptor and a protein kinase.
@ast
Mutational analysis of Hsp90 f ...... receptor and a protein kinase.
@en
Mutational analysis of Hsp90 f ...... receptor and a protein kinase.
@nl
P2860
P3181
P356
P1476
Mutational analysis of Hsp90 f ...... receptor and a protein kinase.
@en
P2093
D F Nathan
S Lindquist
P2860
P304
P3181
P356
10.1128/MCB.15.7.3917
P407
P577
1995-07-01T00:00:00Z