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Myosin chaperonesUnc45 activates Hsp90-dependent folding of the myosin motor domainUnc45b forms a cytosolic complex with Hsp90 and targets the unfolded myosin motor domainHeat-shock protein 90alpha1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos.A Toxoplasma gondii class XIV myosin, expressed in Sf9 cells with a parasite co-chaperone, requires two light chains for fast motility.Functional diversity among a family of human skeletal muscle myosin motors.Hsp90 protein in fission yeast Swo1p and UCS protein Rng3p facilitate myosin II assembly and function.UNC-45B chaperone: the role of its domains in the interaction with the myosin motor domain.Getting folded: chaperone proteins in muscle development, maintenance and disease.Drosophila UNC-45 accumulates in embryonic blastoderm and in muscles, and is essential for muscle myosin stability.Scaffolds and chaperones in myofibril assembly: putting the striations in striated muscle.Fibrosis, not cell size, delineates beta-myosin heavy chain reexpression during cardiac hypertrophy and normal aging in vivo.Tracking UNC-45 chaperone-myosin interaction with a titin mechanical reporter.Visualizing myosin-actin interaction with a genetically-encoded fluorescent strain sensor.The myosin-binding UCS domain but not the Hsp90-binding TPR domain of the UNC-45 chaperone is essential for function in Caenorhabditis elegansStructural basis for drug-induced allosteric changes to human β-cardiac myosin motor activityAt the Start of the Sarcomere: A Previously Unrecognized Role for Myosin Chaperones and Associated Proteins during Early Myofibrillogenesis.Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methodsTransgenic expression and purification of myosin isoforms using the Drosophila melanogaster indirect flight muscle system.Myosin assembly, maintenance and degradation in muscle: Role of the chaperone UNC-45 in myosin thick filament dynamics.UNC-45a promotes myosin folding and stress fiber assembly.Green fluorescent protein impairs actin-myosin interactions by binding to the actin-binding site of myosin.Chaperone-mediated reversible inhibition of the sarcomeric myosin power stroke.
P2860
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P2860
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Folding of the striated muscle myosin motor domain.
@en
type
label
Folding of the striated muscle myosin motor domain.
@en
prefLabel
Folding of the striated muscle myosin motor domain.
@en
P2093
P2860
P356
P1476
Folding of the striated muscle myosin motor domain.
@en
P2093
Diana Chow
Donald A Winkelmann
Rajani Srikakulam
P2860
P304
36799-36807
P356
10.1074/JBC.M204101200
P407
P577
2002-07-10T00:00:00Z