Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo.
about
Heterozygous yeast deletion collection screens reveal essential targets of Hsp90Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organismsIn vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysisHsp90: a specialized but essential protein-folding toolGlucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cyclesThe early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitroS100A1 is a novel molecular chaperone and a member of the Hsp70/Hsp90 multichaperone complexSpecific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substratesHsp90-Tau complex reveals molecular basis for specificity in chaperone actionRoles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG In vivoUnfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a molecular chaperone, assists its reactivationExceptional sensitivity of Rubisco activase to thermal denaturation in vitro and in vivoThe 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 refoldingUbiquilin-1 is a molecular chaperone for the amyloid precursor proteinComplexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cellsSubstrate recognition and function of the R2TP complex in response to cellular stressFunctions of the Hsp90 chaperone system: lifting client proteins to new heightsStructural features and chaperone activity of the NudC protein family.Structural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis MechanismIn vivo analysis of the Hsp90 cochaperone Sti1 (p60)Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependenceCpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties.Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydrationHow high G+C Gram-positive bacteria and in particular bifidobacteria cope with heat stress: protein players and regulatorsNatural iminosugar (+)-lentiginosine inhibits ATPase and chaperone activity of hsp90Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregationB-subunit of phosphate-specific transporter from Mycobacterium tuberculosis is a thermostable ATPaseIdentification of the plant compound geraniin as a novel Hsp90 inhibitorClient Proteins and Small Molecule Inhibitors Display Distinct Binding Preferences for Constitutive and Stress-Induced HSP90 Isoforms and Their Conformationally Restricted MutantsA transmembrane guanylyl cyclase (DAF-11) and Hsp90 (DAF-21) regulate a common set of chemosensory behaviors in caenorhabditis elegansCharacterization of the 105-kDa molecular chaperoneThe 90-kDa heat shock protein Hsp90 protects tubulin against thermal denaturationChemical cross-linking of the chloroplast localized small heat-shock protein, Hsp21, and the model substrate citrate synthaseThe Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-grpE system.Cyclophilins and their possible role in the stress response.Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids.Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.
P2860
Q21134948-5001C037-CB7F-4D4E-BB56-C3227C461AC9Q21266601-A7F29898-0014-42BD-8D2C-0B98E30F89F2Q22008008-0424B935-F043-46B8-92B7-BD4768BCE5CFQ24291482-ABDAB09A-DAE8-43CC-BD31-4323F83B07D4Q24299657-9E940267-541C-4DEA-A385-77C1B6F85CB7Q24300223-F72CEE00-25E7-4CE6-AE91-1F334D79FDBDQ24300601-F3D0E454-BF8C-49E2-9D30-7F3A56A63767Q24313523-409A31A8-7BEA-40DA-9B73-9AB5BEE18DC3Q24338386-C4E2C466-B7AC-479F-9761-A1BCE1462C78Q24338439-5C2B63D4-DA60-477C-BA61-5CD56DB5E8EEQ24521559-2BC63988-9C2F-47F3-AFED-79D8CF42F697Q24533503-EF62E7AF-3EC9-4EDE-918C-03AB610F31D2Q24535389-0D3C4313-D9FA-46C1-991A-C4CE1BB572D4Q24535594-8A069821-8C0B-4365-AEE9-FE58441327ECQ24548039-6408CDB5-E43F-4B28-B03F-B310538BC9E4Q24562938-200CF557-573F-463A-8957-E68310BF2437Q24634983-E6BD0AE2-E499-401B-B18E-434259484426Q24653464-750E18F5-5FE8-4218-BB0C-2428C1A96C00Q26824496-8FF0E6C8-520C-452C-8F1C-790038649CF2Q27024085-BDE64852-A253-4F4E-A952-C50A3DEF063DQ27667619-23CFA37C-0FEE-4AEC-920E-2F373514FEC9Q27681454-715CFA08-112D-4332-B18B-C54C3FCF82C9Q27937090-8153005D-87EB-442F-A6E6-3061335F4A74Q27937497-D3E88F0B-E1B1-400D-9EB3-8A9B27F92BB0Q27938998-1B3C8F3D-F620-443B-B702-13D307DB2E21Q28215605-9750B75B-B51C-4422-80CB-B5C9E29829A2Q28257892-5CF59C51-37F2-4733-8F8A-503E26B40D73Q28482390-1A51D0F9-C4CD-400A-A8EC-D21227111A90Q28486726-0ADB1982-BD76-4D5D-AA89-EFF4974AB6B3Q28487441-55CFACD7-DEA0-4140-A8A3-D515413AD1C7Q28533486-0FD8915C-96C7-4EE3-A293-DBE0FD0EBB6FQ28550576-FC867DF2-AF7B-418E-8F1E-B6C8D19A3950Q28769077-5A3A494D-93AE-40D0-BBF1-9BDF459A4EDCQ29012569-933531E2-E211-4D49-8A25-91CF87B2686CQ30493832-7F9105CA-4536-4A5F-9731-5591325055B1Q33287601-633F387F-EACB-47C4-A019-187CB2051C12Q33744171-90FD0DAA-E5AB-4CC4-AA41-EDAAEC8A579AQ33815808-E4C7FE39-D693-4AB8-8250-46CD346F4819Q33885913-BA187AEC-B388-4483-B1AB-C3A815511656Q33885969-2BB1D4F0-E51E-485B-BE31-2235DA389678
P2860
Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo.
description
1995 nî lūn-bûn
@nan
1995 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մարտին 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
Transient interaction of Hsp90 ...... ations for heat shock in vivo.
@ast
Transient interaction of Hsp90 ...... ations for heat shock in vivo.
@en
Transient interaction of Hsp90 ...... ations for heat shock in vivo.
@nl
type
label
Transient interaction of Hsp90 ...... ations for heat shock in vivo.
@ast
Transient interaction of Hsp90 ...... ations for heat shock in vivo.
@en
Transient interaction of Hsp90 ...... ations for heat shock in vivo.
@nl
prefLabel
Transient interaction of Hsp90 ...... ations for heat shock in vivo.
@ast
Transient interaction of Hsp90 ...... ations for heat shock in vivo.
@en
Transient interaction of Hsp90 ...... ations for heat shock in vivo.
@nl
P2093
P2860
P356
P1476
Transient interaction of Hsp90 ...... ations for heat shock in vivo.
@en
P2093
P2860
P304
P356
10.1074/JBC.270.13.7288
P407
P577
1995-03-01T00:00:00Z