GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.
about
Myosin chaperonesUnc45 activates Hsp90-dependent folding of the myosin motor domainLack of developmental redundancy between Unc45 proteins in zebrafish muscle developmentHsp90 and co-chaperones twist the functions of diverse client proteins.Celastrol inhibits Hsp90 chaperoning of steroid receptors by inducing fibrillization of the Co-chaperone p23Progesterone receptor isoform functions in normal breast development and breast cancerThe cochaperone SGTA (small glutamine-rich tetratricopeptide repeat-containing protein alpha) demonstrates regulatory specificity for the androgen, glucocorticoid, and progesterone receptors.The UNC-45 myosin chaperone: from worms to flies to vertebrates.Control of steroid receptor dynamics and function by genomic actions of the cochaperones p23 and Bag-1LDeep sequencing of the murine olfactory receptor neuron transcriptome.Versatile TPR domains accommodate different modes of target protein recognition and functionDual function of the UNC-45b chaperone with myosin and GATA4 in cardiac developmentLoss of function of myosin chaperones triggers Hsf1-mediated transcriptional response in skeletal muscle cells.Loss of unc45a precipitates arteriovenous shunting in the aortic arches.The myosin-binding UCS domain but not the Hsp90-binding TPR domain of the UNC-45 chaperone is essential for function in Caenorhabditis elegansPlasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms.Conformational dynamics of the molecular chaperone Hsp90GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform specificity.Identification of Glioblastoma Phosphotyrosine-Containing Proteins with Two-Dimensional Western Blotting and Tandem Mass SpectrometryDrosophila UNC-45 prevents heat-induced aggregation of skeletal muscle myosin and facilitates refolding of citrate synthase.Rng3, a member of the UCS family of myosin co-chaperones, associates with myosin heavy chains cotranslationally.A heat shock protein 90 inhibitor that modulates the immunophilins and regulates hormone receptors without inducing the heat shock responseUNC45A localizes to centrosomes and regulates cancer cell proliferation through ChK1 activation.Chaperoning myosin assembly in muscle formation and aging.Myosin assembly, maintenance and degradation in muscle: Role of the chaperone UNC-45 in myosin thick filament dynamics.Proteomic and functional analysis of human sperm detergent resistant membranes.Conserved conformational changes in the ATPase cycle of human Hsp90.UNC-45a promotes myosin folding and stress fiber assembly.Traffic lights for retinoids in oncology: molecular markers of retinoid resistance and sensitivity and their use in the management of cancer differentiation therapy
P2860
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P2860
GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.
description
2006 nî lūn-bûn
@nan
2006 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մարտին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway
@nl
GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.
@ast
GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.
@en
type
label
GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway
@nl
GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.
@ast
GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.
@en
prefLabel
GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway
@nl
GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.
@ast
GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.
@en
P2093
P2860
P1476
GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.
@en
P2093
Ahmed Chadli
David F Gordon
David Toft
J Dinny Graham
Kathryn B Horwitz
M Greg Abel
Sara J Felts
Twila A Jackson
William M Wood
P2860
P304
P356
10.1128/MCB.26.5.1722-1730.2006
P407
P577
2006-03-01T00:00:00Z