Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins - Wikidata - wikimedia - TriplyDB

Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins

Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins

http://www.wikidata.org/entity/Q35640147

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FKBP51 and FKBP52 in signaling and disease Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes.Differential targeting of androgen and glucocorticoid receptors induces ER stress and apoptosis in prostate cancer cells: a novel therapeutic modality.Serine/threonine protein phosphatase 5 (PP5) interacts with substrate under heat stress conditions and forms protein complex in Arabidopsis.pRb controls estrogen receptor alpha protein stability and activity.FKBP14 overexpression contributes to osteosarcoma carcinogenesis and indicates poor survival outcome Proteomics of human prostate cancer biospecimens: the global, systems-wide perspective for protein markers with potential clinical utility.HSP90AB1: Helping the good and the bad.Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.Chaperones and the maturation of steroid hormone receptor complexes The interchange of immunophilins leads to parallel pathways and different intermediates in the assembly of Hsp90 glucocorticoid receptor complexes.Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.Enzymatic characterization of a lysin encoded by bacteriophage EL.Dimerization of a heat shock protein 90 inhibitor enhances inhibitory activity.Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies.

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P2860

Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins

http://www.wikidata.org/entity/Q35640147

description

2011 nî lūn-bûn

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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2011年论文

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2011年论文

@zh-cn

name

Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins

@ast

Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins

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type

label

Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins

@ast

Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins

@en

prefLabel

Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins

@ast

Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins

@en

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Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins

@en

P2093

Chuan Xiao

http://www.w3.org/2001/XMLSchema#string

Citlally Ramirez

http://www.w3.org/2001/XMLSchema#string

Ricardo A Bernal

http://www.w3.org/2001/XMLSchema#string

Zacariah L Hildenbrand

http://www.w3.org/2001/XMLSchema#string

P2860

Hsp90: a specialized but essential protein-folding tool

Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor

Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes

The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo

The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding

The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

EMAN: semiautomated software for high-resolution single-particle reconstructions

Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones.

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43-58

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scholarly article

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10.18632/ONCOTARGET.225

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1-2

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2

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Sudheer K Molugu

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2011-01-01T00:00:00Z

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50289603

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21378414

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3248148

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