GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform specificity.
about
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
Q24300926-F139C277-758E-43BF-8251-EB8DB21B8424Q28247643-941BF6FB-FAD4-455A-8C8F-309471B7E44AQ31106786-7B5461BA-85D1-452C-8689-9A4D7857FE54Q33838809-D7820B8D-18B8-45AD-977A-92498EEC9AFBQ34477894-F0677632-3AAE-43BD-9EA8-80674D63B531Q36811722-02BC88D2-EDAF-4CB9-B7E8-DC0618D71246Q37293018-9ED16075-6B49-481C-9420-D76B4DD2D13DQ39354283-873D4BF5-A3E2-4AE1-AD85-404E57D80E00Q40362044-1B15A03D-F81E-4DC4-B690-088F6F643BFCQ41176499-7775F9E8-A48B-40F1-81FA-C5AC4113DF26Q41791230-7B95345E-85A2-4039-A923-DA3786A75F75Q43187716-DC94CA3D-0C8F-4551-925E-93AA3B02053FQ44646010-66DF3646-E8AC-46AD-835F-40184A1AD35DQ45930645-9EDFF70F-3103-488E-90F2-45AD4E68C7C1Q47243892-3B411340-2626-484D-AC2C-7EF4849EB7FAQ47621531-511BA42D-9924-4E73-AD59-937AF54581B6Q48022737-BD739F14-CDB1-4059-AFF1-47D523B15EE0
P2860
GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform specificity.
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
P2093
P2860
P356
P1476
GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform specificity.
@en
P2093
Ahmed Chadli
David O Toft
Sara J Felts
P2860
P304
P356
10.1074/JBC.C800017200
P407
P577
2008-02-19T00:00:00Z