Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone.
about
Hsp90-Tau complex reveals molecular basis for specificity in chaperone actionParalog Specific Hsp90 Inhibitors - A Brief History and a Bright FutureQuality control and fate determination of Hsp90 client proteinsComparing protein folding in vitro and in vivo: foldability meets the fitness challengeFunctions of the Hsp90 chaperone system: lifting client proteins to new heightsCorresponding functional dynamics across the Hsp90 Chaperone family: insights from a multiscale analysis of MD simulationsStructural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis MechanismMechanistic Asymmetry in Hsp90 DimersExploring the Functional Complementation between Grp94 and Hsp90Differential modulation of functional dynamics and allosteric interactions in the Hsp90-cochaperone complexes with p23 and Aha1: a computational study.A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.Uniqueness of models from small-angle scattering data: the impact of a hydration shell and complementary NMR restraints.An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humansIdentification and characterization of novel ER-based hsp90 gene in the red flour beetle, Tribolium castaneum.Misfolded proteins induce aggregation of the lectin Yos9.Probing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics.Conformational selection underlies recognition of a molybdoenzyme by its dedicated chaperoneThe charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function.Genome-scale co-evolutionary inference identifies functions and clients of bacterial Hsp90A phase I study of the HSP90 inhibitor retaspimycin hydrochloride (IPI-504) in patients with gastrointestinal stromal tumors or soft-tissue sarcomas.The ribosomal biogenesis protein Utp21 interacts with Hsp90 and has differing requirements for Hsp90-associated proteins.Post-translational modifications of Hsp90 and their contributions to chaperone regulationCasein kinase 2 phosphorylation of Hsp90 threonine 22 modulates chaperone function and drug sensitivity.Identifying sequential substrate binding at the single-molecule level by enzyme mechanical stabilizationCross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activityChaperoning the chaperone: a role for the co-chaperone Cpr7 in modulating Hsp90 function in Saccharomyces cerevisiae.Molecular and thermodynamic insights into the conformational transitions of Hsp90.Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling.Heat shock protein 90 in plants: molecular mechanisms and roles in stress responses.Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.Chemical Tools to Investigate Mechanisms Associated with HSP90 and HSP70 in Disease.Crowding Activates Heat Shock Protein 90.Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesisDesigned Hsp90 heterodimers reveal an asymmetric ATPase-driven mechanism in vivo.Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone.ATP-driven molecular chaperone machines.Weak protein-ligand interactions studied by small-angle X-ray scattering.Emerging applications of small angle solution scattering in structural biology.Activation of Hsp90 Enzymatic Activity and Conformational Dynamics through Rationally Designed Allosteric Ligands.Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90.
P2860
Q24338439-B2D3B0D2-2C1E-4154-A344-9349D9D28A01Q26748800-D5DA2AB5-AEEC-4673-983E-50016BF335E9Q26853052-583317EC-5423-4725-A045-905CA2F1DBADQ26991933-DD6FA4E0-3625-4566-8C32-6615A47A6298Q27024085-8A227B09-ACD1-4577-8EA5-64F4F9260F04Q27331720-3666CA8C-10E6-4212-A8E3-F055239EC609Q27681454-478082DC-CFF7-4485-941B-02C3B704E422Q28080783-2A4E7F92-6210-4EE5-AA57-772DD5070E57Q28553251-088B0FBB-DC8D-494C-92C1-C80391B0D657Q30353164-B4CFB57D-7D76-4DFA-8439-E29685126EC7Q30402024-ED02F13E-B7F0-43EE-BD26-0B4DDC5F3621Q30885745-3C5DB72F-E78C-4FB5-BE47-4C12089E05B5Q33761192-783DD0FF-00E1-45C9-9A6A-12C06C3F8B34Q34099871-5A04A4A2-A342-45DD-B8C8-8FC2CFA024C4Q34170723-6AE32BC3-CD3F-4A21-9037-F34A1C537BD3Q34280087-F5B5F271-9E37-463C-B9DC-860CC0DC7BB9Q34490108-C8DE9C4E-EB53-4DB2-B901-EC270F90393AQ34752562-F239D07E-0AB5-48AC-BB30-67D68F33A997Q34845890-356EBA81-90E5-4338-A881-0B98D7537701Q35089528-3CC7C01A-69C8-46F8-BB7E-37902ADC7E8FQ35125386-EA3957D5-6C6C-4AFD-A6E0-EA8A64D2B7D2Q35581165-1DAAFD3D-A6A8-4B70-A79E-C2D7C9DD460CQ35640239-6D57BCEE-E36E-4638-9314-F2E6FC4A052DQ35743849-2B062C69-DC8E-4D80-9320-1BDE5B10784CQ35764464-6E1D9F99-E95F-484E-B7F5-008DC3BB2D54Q36076894-4CAC10AE-F1E5-4AE2-9867-B5C5B543D38DQ36105301-523B6C8E-5735-4982-9F8A-07356CAFD8B7Q36328268-524D7697-2338-4654-9AC1-86DDC229C5D3Q36538289-45DD986A-C125-4B09-9B39-5A5A2FF2E730Q36604957-DC721728-D198-4034-9BCB-F660D9145560Q36655158-6066B2C5-9E1D-4C21-B712-CAE8BD3BABECQ36744829-AD539324-1149-455F-965C-50E05557F1A6Q37189539-63BB2EF1-37CD-43A3-8C39-C21432BC4E04Q37582269-F9A53353-DED1-41CE-9051-42E81DCDFC27Q37661766-5D7551EA-B18E-4D2F-8440-03374C1E4A19Q38123448-654D5633-D5DF-4D80-9DE9-483B13E1DA40Q38192762-08EC5998-BFCF-441F-9877-C8881A93E2D1Q38291388-F4C0E3BF-823F-4E85-AE88-E5ABE945A7B3Q38842676-4A6719A7-0554-490B-A055-22886D2539C1Q38951781-2BCA2969-AE18-4592-80FB-654ACD3DA309
P2860
Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone.
description
2011 nî lūn-bûn
@nan
2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Substrate binding drives large ...... the Hsp90 molecular chaperone.
@ast
Substrate binding drives large ...... the Hsp90 molecular chaperone.
@en
type
label
Substrate binding drives large ...... the Hsp90 molecular chaperone.
@ast
Substrate binding drives large ...... the Hsp90 molecular chaperone.
@en
prefLabel
Substrate binding drives large ...... the Hsp90 molecular chaperone.
@ast
Substrate binding drives large ...... the Hsp90 molecular chaperone.
@en
P2093
P2860
P1433
P1476
Substrate binding drives large ...... the Hsp90 molecular chaperone.
@en
P2093
David A Agard
Laura A Lavery
Timothy O Street
P2860
P304
P356
10.1016/J.MOLCEL.2011.01.029
P577
2011-04-01T00:00:00Z