about
ARSACS, a spastic ataxia common in northeastern Québec, is caused by mutations in a new gene encoding an 11.5-kb ORFHeat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetasesPhosphorylation of HSF1 by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 bindingAha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperoneCofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone systemXAP2 inhibits glucocorticoid receptor activity in mammalian cellsHsp70 regulates the interaction between the peroxisome targeting signal type 1 (PTS1)-receptor Pex5p and PTS1The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKRA subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.A unique molecular chaperone Cosmc required for activity of the mammalian core 1 beta 3-galactosyltransferaseThe hsp90 chaperone complex regulates intracellular localization of the dioxin receptorHsp70-RAP46 interaction in downregulation of DNA binding by glucocorticoid receptorThe cochaperone Bag-1L enhances androgen receptor action via interaction with the NH2-terminal region of the receptorImpact of protein kinase PKR in cell biology: from antiviral to antiproliferative actionHeat shock protein 90 targeting therapy: state of the art and future perspectiveChaperoning steroidal physiology: lessons from mouse genetic models of Hsp90 and its cochaperonesStructure and Functional Studies of the CS Domain of the Essential H/ACA Ribonucleoparticle Assembly Protein SHQ1Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae.Sti1 is a novel activator of the Ssa proteins.Hsp90 enables Ctf13p/Skp1p to nucleate the budding yeast kinetochore.Cns1 is an activator of the Ssa1 ATPase activity.Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties.Understanding the role of heat shock protein isoforms in male fertility, aging and apoptosisHsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment proteinErbB2 degradation mediated by the co-chaperone protein CHIPInhibition of MDM2 by hsp90 contributes to mutant p53 stabilizationPhosphorylation and hsp90 binding mediate heat shock stabilization of p53Binding of ATP to heat shock protein 90: evidence for an ATP-binding site in the C-terminal domainDrugging the cancer kinome: progress and challenges in developing personalized molecular cancer therapeuticsC-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balancesHeat shock proteins and heat shock factor 1 in carcinogenesis and tumor development: an updateThe Hsp90 family of proteins in Arabidopsis thalianaExtracellular heat shock protein (Hsp)70 and Hsp90α assist in matrix metalloproteinase-2 activation and breast cancer cell migration and invasionDifferentially expressed genes in Hirudo medicinalis ganglia after acetyl-L-carnitine treatmentRab-alphaGDI activity is regulated by a Hsp90 chaperone complexUnc45 activates Hsp90-dependent folding of the myosin motor domainUnc45b forms a cytosolic complex with Hsp90 and targets the unfolded myosin motor domainC-terminal domain of SMYD3 serves as a unique HSP90-regulated motif in oncogenesisA transmembrane guanylyl cyclase (DAF-11) and Hsp90 (DAF-21) regulate a common set of chemosensory behaviors in caenorhabditis elegansHsp90 as a capacitor of phenotypic variation
P2860
Q22011182-DC8625B3-DB0F-44FA-AAAE-6528C252E94CQ22254677-13FA1128-38C9-4B9F-AF33-966FBA664FD4Q24294328-B8B40E9D-0051-4576-AAAC-365E0DBD9696Q24295270-D50285CD-631C-4E99-9787-7F26462A2ADBQ24307587-2410D6E7-294D-42D1-9CE9-54C0D051CFF6Q24317168-B0C33B3B-3B33-4502-9B46-276C342CB4D9Q24533332-BD64CE45-C2B4-4D7A-9209-62294BACF568Q24535594-0BA36FF5-4C2F-4C82-9E83-B101AB28CB3FQ24541564-BFC94D79-D1B6-4A44-BC55-6EEDDF25DE33Q24543917-1023336F-DAEE-448C-9FA2-5B153C6A6F5CQ24550978-D42C63BA-F87F-4708-8AEE-3F16BC02ECEDQ24596488-DC8DF076-D719-4501-AF86-B1F044471963Q24652993-1719A477-541E-4960-9303-E5440FA8B81DQ24672548-C8D44CDD-DE5E-4658-AD2F-DC9363924A37Q26776302-7A8063AA-D41E-4B1E-876B-FB574755BA98Q27011776-4883C57A-D53C-4B21-BE8C-C8AB71388F38Q27652939-E112EA71-977A-4087-BEC4-B7E0694D1881Q27930200-239DE04F-311E-4419-BD3A-9024E122BC14Q27931140-0DA8019F-FBA5-4FF4-9222-22B5113E50FAQ27934627-8CD98B33-D024-4004-9E15-828E9583F220Q27938204-444323D5-3628-4084-AC64-5DE4BA0AC94AQ27938998-23E0AA68-7AC7-4606-876C-13EFC1EA66BBQ28080885-7D6317D4-399B-463A-80C2-C9041BAF47D5Q28204780-1BAD30E7-B684-4025-8AF8-4D916179758DQ28208008-390F4558-F461-4EDB-969C-6ADF3EC63E58Q28212970-09809714-F9C8-4982-B34F-0C7CF9821485Q28214608-9C67FC92-6868-4746-8097-E49D9AE4B58AQ28216259-DFD3C05D-47A0-40E4-A5B3-8AACC7AF6823Q28254233-9683F8DC-CC00-4DDB-962B-59163E5C8600Q28271643-3856B1FD-A9B5-4D1D-A443-53FE9BF8B41CQ28272905-2BA6C289-9373-40F6-BE26-C7BCAE3167DFQ28361507-E4014D88-2514-472C-9937-E3D03DCC32A8Q28477776-9A37324D-C97B-4D13-84B9-2767C4BABA0AQ28484844-5DFC80EE-0249-4EED-B19E-A9AE8BC50E42Q28578339-17C9CA67-354F-4620-9461-D3129DDEA411Q28586476-69331E42-EEDC-4AC3-8F6E-BBD33B99540AQ28588643-15648D7D-1ECE-4DCF-A759-1DD350286B09Q28596567-9F2D047D-2EC7-463E-A7D9-BBE1FD219579Q28769077-DC475774-F58A-4CD9-9D3E-05F4C28B7E68Q29618584-A64BB9E5-4217-4498-8E3E-C4A752C2E190
P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Hsp90 & Co. - a holding for folding.
@ast
Hsp90 & Co. - a holding for folding.
@en
type
label
Hsp90 & Co. - a holding for folding.
@ast
Hsp90 & Co. - a holding for folding.
@en
prefLabel
Hsp90 & Co. - a holding for folding.
@ast
Hsp90 & Co. - a holding for folding.
@en
P1476
Hsp90 & Co. - a holding for folding.
@en
P2093
P304
P356
10.1016/S0968-0004(99)01373-0
P577
1999-04-01T00:00:00Z