Cardiac troponin I phosphorylation and the force-length relationship.

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Cardiac troponin I phosphorylation and the force-length relationship.

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2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年学术文章

@wuu

2013年学术文章

@zh

2013年学术文章

@zh-cn

2013年学术文章

@zh-hans

2013年学术文章

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2013年学术文章

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2013年學術文章

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2013年學術文章

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Cardiac troponin I phosphorylation and the force-length relationship.

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Cardiac troponin I phosphorylation and the force-length relationship.

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Item

label

Cardiac troponin I phosphorylation and the force-length relationship.

@en

Cardiac troponin I phosphorylation and the force-length relationship.

@nl

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Cardiac troponin I phosphorylation and the force-length relationship.

@en

Cardiac troponin I phosphorylation and the force-length relationship.

@nl

P1476

Cardiac troponin I phosphorylation and the force-length relationship.

@en

P2860

Posttranslational modifications of cardiac troponin T: an overview

Generation and functional characterization of knock-in mice harboring the cardiac troponin I-R21C mutation associated with hypertrophic cardiomyopathy.

Myosin binding protein-C phosphorylation is the principal mediator of protein kinase A effects on thick filament structure in myocardium.

Impact of site-specific phosphorylation of protein kinase A sites Ser23 and Ser24 of cardiac troponin I in human cardiomyocytes

Mechanisms that match ATP supply to demand in cardiac pacemaker cells during high ATP demand.

cAMP and mitochondria.

Length dependence of striated muscle force generation is controlled by phosphorylation of cTnI at serines 23/24.

Length dependence of force generation exhibit similarities between rat cardiac myocytes and skeletal muscle fibres.

P304

6135-6136

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P31

scholarly article

P356

10.1113/JPHYSIOL.2013.265090

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P407

English

P433

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P478

591

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P50

Yael Yaniv

P577

2013-12-01T00:00:00Z

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P698

24339151

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P921

phosphorylation

P932

3892466

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