GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform specificity.

GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform specificity.

Item
http://www.wikidata.org/entity/Q39646236
A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathwaysApproaches for defining the Hsp90-dependent proteome.Lack of developmental redundancy between Unc45 proteins in zebrafish muscle developmentNovel Hsp90 partners discovered using complementary proteomic approaches.The UNC-45 myosin chaperone: from worms to flies to vertebrates.A Remodeled Hsp90 Molecular Chaperone Ensemble with the Novel Cochaperone Aarsd1 Is Required for Muscle Differentiation.The levels of retinoic acid-inducible gene I are regulated by heat shock protein 90-alpha.The hERG channel is dependent upon the Hsp90α isoform for maturation and trafficking.The first report of direct inhibitors that target the C-terminal MEEVD region on heat shock protein 90.Mutation of the Ser18 phosphorylation site on the sole Saccharomyces cerevisiae UCS protein, She4, can compromise high-temperature survival.Hsp90 regulates NADPH oxidase activity and is necessary for superoxide but not hydrogen peroxide production.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.Bag-1M inhibits the transactivation of the glucocorticoid receptor via recruitment of corepressors.UCS protein function is partially restored in the Saccharomyces cerevisiae she4 mutant with expression of the human UNC45-GC, but not UNC45-SM.UNC-45a promotes myosin folding and stress fiber assembly.Substrate specificity in the context of molecular chaperones.
P2860

GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform specificity.

Item
http://www.wikidata.org/entity/Q39646236
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform specificity.
@en
GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform specificity.
@nl
type
label
GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform specificity.
@en
GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform specificity.
@nl
prefLabel
GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform specificity.
@en
GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform specificity.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P921
P932
P356
P1433
P1476
GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform specificity.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P921
P932