Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.
about
Interaction between protein phosphatase 5 and the A subunit of protein phosphatase 2A: evidence for a heterotrimeric form of protein phosphatase 5Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions.Negative feedback regulation of ASK1 by protein phosphatase 5 (PP5) in response to oxidative stressSerine/threonine protein phosphatase 5 (PP5) participates in the regulation of glucocorticoid receptor nucleocytoplasmic shuttlingSteroid Receptor-Associated Immunophilins: A Gateway to Steroid SignallingFunctions of the Hsp90 chaperone system: lifting client proteins to new heightsHuman Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domainCns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cellsThe phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones.Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties.The emerging role of peptidyl-prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's diseaseThe activity of protein phosphatase 5 towards native clients is modulated by the middle- and C-terminal domains of Hsp90Identification of the nuclear receptor CAR:HSP90 complex in mouse liver and recruitment of protein phosphatase 2A in response to phenobarbitalHSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptorThe serine/threonine phosphatase PP5 interacts with CDC16 and CDC27, two tetratricopeptide repeat-containing subunits of the anaphase-promoting complexp50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding siteCharacterization of the Ah receptor-associated protein, ARA9A Proteomics Approach to Investigate miR-153-3p and miR-205-5p Targets in Neuroblastoma CellsDefects of protein phosphatase 2A causes corticosteroid insensitivity in severe asthmaSelective activators of protein phosphatase 5 target the auto-inhibitory mechanism.Heat shock proteins: cellular and molecular mechanisms in the central nervous system.Protein Ser/Thr phosphatases--the ugly ducklings of cell signalling.High yield expression of serine/threonine protein phosphatase type 5, and a fluorescent assay suitable for use in the detection of catalytic inhibitors.To fold or not to fold: modulation and consequences of Hsp90 inhibition.The helix 1-3 loop in the glucocorticoid receptor LBD is a regulatory element for FKBP cochaperones.Crosstalk in inflammation: the interplay of glucocorticoid receptor-based mechanisms and kinases and phosphatasesIdentification of conserved residues required for the binding of a tetratricopeptide repeat domain to heat shock protein 90.Identification of a functional link for the p53 tumor suppressor protein in dexamethasone-induced growth suppression.Regulation of apoptosis signal-regulating kinase 1 (ASK1) by polyamine levels via protein phosphatase 5.Steroid resistance in the squirrel monkey: an old subject revisited.Hsp90: chaperoning signal transduction.PAPP5 is involved in the tetrapyrrole mediated plastid signalling during chloroplast developmentPnck induces ligand-independent EGFR degradation by probable perturbation of the Hsp90 chaperone complex.Versatile TPR domains accommodate different modes of target protein recognition and functionThe role of serine/threonine protein phosphatases in exocytosisManagement of cytoskeleton architecture by molecular chaperones and immunophilins.
P2860
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P2860
Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.
description
1997 nî lūn-bûn
@nan
1997 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Protein phosphatase 5 is a maj ...... an FK506-binding immunophilin.
@ast
Protein phosphatase 5 is a maj ...... an FK506-binding immunophilin.
@en
Protein phosphatase 5 is a maj ...... an FK506-binding immunophilin.
@nl
type
label
Protein phosphatase 5 is a maj ...... an FK506-binding immunophilin.
@ast
Protein phosphatase 5 is a maj ...... an FK506-binding immunophilin.
@en
Protein phosphatase 5 is a maj ...... an FK506-binding immunophilin.
@nl
prefLabel
Protein phosphatase 5 is a maj ...... an FK506-binding immunophilin.
@ast
Protein phosphatase 5 is a maj ...... an FK506-binding immunophilin.
@en
Protein phosphatase 5 is a maj ...... an FK506-binding immunophilin.
@nl
P2093
P2860
P356
P1476
Protein phosphatase 5 is a maj ...... an FK506-binding immunophilin.
@en
P2093
Chinkers M
Galigniana MD
Owens-Grillo JK
Silverstein AM
P2860
P304
16224-16230
P356
10.1074/JBC.272.26.16224
P407
P577
1997-06-01T00:00:00Z