Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch. - Wikidata - awgldk - TriplyDB

Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch.

Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch.

http://www.wikidata.org/entity/Q36416390

about

The N-terminal region of twitchin binds thick and thin contractile filaments: redundant mechanisms of catch force maintenance.A force-activated kinase in a catch smooth muscle.Myosin binding protein-C: a regulator of actomyosin interaction in striated muscle Catch muscle myorod modulates ATPase activity of Myosin in a phosphorylation-dependent way.Twitchin kinase interacts with MAPKAP kinase 2 in Caenorhabditis elegans striated muscle.Muscle contraction phenotypic analysis enabled by optogenetics reveals functional relationships of sarcomere components in Caenorhabditis elegans Physiological Mechanisms of Eccentric Contraction and Its Applications: A Role for the Giant Titin Protein.Cytoskeletal protein kinases: titin and its relations in mechanosensing.Small-angle X-ray diffraction studies of a molluscan smooth muscle in the catch state Mechanism of catch force: tethering of thick and thin filaments by twitchin.Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin.Myosin loop 2 is involved in the formation of a trimeric complex of twitchin, actin, and myosin.Myosin Mg-ATPase of molluscan muscles is slightly activated by F-actin under catch state in vitro.Why are muscles strong, and why do they require little energy in eccentric action?

P2860

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P2860

Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch.

http://www.wikidata.org/entity/Q36416390

description

2007 nî lūn-bûn

@nan

2007年の論文

@ja

2007年学术文章

@wuu

2007年学术文章

@zh-cn

2007年学术文章

@zh-hans

2007年学术文章

@zh-my

2007年学术文章

@zh-sg

2007年學術文章

@yue

2007年學術文章

@zh

2007年學術文章

@zh-hant

name

Unphosphorylated twitchin form ...... tension maintenance in catch.

@ast

Unphosphorylated twitchin form ...... tension maintenance in catch.

@en

type

label

Unphosphorylated twitchin form ...... tension maintenance in catch.

@ast

Unphosphorylated twitchin form ...... tension maintenance in catch.

@en

prefLabel

Unphosphorylated twitchin form ...... tension maintenance in catch.

@ast

Unphosphorylated twitchin form ...... tension maintenance in catch.

@en

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P1433

The Journal of Experimental Biology

P1476

Unphosphorylated twitchin form ...... tension maintenance in catch.

@en

P2093

Akinori Inoue

http://www.w3.org/2001/XMLSchema#string

Chieko Hamamoto

http://www.w3.org/2001/XMLSchema#string

Daisuke Funabara

http://www.w3.org/2001/XMLSchema#string

David J Hartshorne

http://www.w3.org/2001/XMLSchema#string

Koji Yamamoto

http://www.w3.org/2001/XMLSchema#string

Miki Ueda

http://www.w3.org/2001/XMLSchema#string

Rika Osawa

http://www.w3.org/2001/XMLSchema#string

Satoshi Kanoh

http://www.w3.org/2001/XMLSchema#string

Shugo Watabe

http://www.w3.org/2001/XMLSchema#string

Suechika Suzuki

http://www.w3.org/2001/XMLSchema#string

P2860

Myosin binding protein C, a phosphorylation-dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2

Isoform-specific interaction of the myosin-binding proteins (MyBPs) with skeletal and cardiac myosin is a property of the C-terminal immunoglobulin domain

The myosin cross-bridge cycle and its control by twitchin phosphorylation in catch muscle

Striated muscle twitchin of bivalves has "catchability", the ability to bind thick filaments tightly to thin filaments, representing the catch state.

Catch force links and the low to high force transition of myosin

Aspects of smooth muscle function in molluscan catch muscle.

Phosphorylation of a twitchin-related protein controls catch and calcium sensitivity of force production in invertebrate smooth muscle.

Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion.

An in vitro assay reveals essential protein components for the "catch" state of invertebrate smooth muscle

Matching molecules in the catch mechanism.

P304

4399-4410

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P31

scholarly article

P356

10.1242/JEB.008722

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P433

Pt 24

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P478

210

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P577

2007-12-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

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5791829

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18055628

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P932

2219545

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