Chaperoning myosin assembly in muscle formation and aging.

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Insights into muscle degeneration from heritable inclusion body myopathies Titin and Nebulin in Thick and Thin Filament Length Regulation.The central domain of UNC-45 chaperone inhibits the myosin power stroke.

P2860

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P2860

Chaperoning myosin assembly in muscle formation and aging.

Item

http://www.wikidata.org/entity/Q42770507

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2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

2013年论文

@zh

2013年论文

@zh-cn

name

Chaperoning myosin assembly in muscle formation and aging.

@en

Chaperoning myosin assembly in muscle formation and aging.

@nl

type

Item

label

Chaperoning myosin assembly in muscle formation and aging.

@en

Chaperoning myosin assembly in muscle formation and aging.

@nl

prefLabel

Chaperoning myosin assembly in muscle formation and aging.

@en

Chaperoning myosin assembly in muscle formation and aging.

@nl

P1476

Chaperoning myosin assembly in muscle formation and aging.

@en

P2860

GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.

Myosin II co-chaperone general cell UNC-45 overexpression is associated with ovarian cancer, rapid proliferation, and motility

The UNC-45 chaperone is critical for establishing myosin-based myofibrillar organization and cardiac contractility in the Drosophila heart model

The Myosin Chaperone UNC-45 Is Organized in Tandem Modules to Support Myofilament Formation in C. elegans

The UCS domain protein She4p binds to myosin motor domains and is essential for class I and class V myosin function.

Striated muscle cytoarchitecture: an intricate web of form and function

The p97/VCP ATPase is critical in muscle atrophy and the accelerated degradation of muscle proteins

Unc45b forms a cytosolic complex with Hsp90 and targets the unfolded myosin motor domain

The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis

Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein

P304

e25644

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P31

scholarly article

P356

10.4161/WORM.25644

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P478

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Thorsten Hoppe

Wojciech Pokrzywa

P577

2013-07-17T00:00:00Z

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261956871

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24778937

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P921

molecular chaperones

P932

3875649

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Chaperoning myosin assembly in muscle formation and aging.

about

P2860

P2860

Chaperoning myosin assembly in muscle formation and aging.

description

name

type

label

prefLabel

P1433

P1476

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P921

P932