Orientation of myosin binding protein C in the cardiac muscle sarcomere determined by domain-specific immuno-EM.
about
Molecular mechanisms of cardiomyopathy phenotypes associated with myosin light chain mutationsThe A31P missense mutation in cardiac myosin binding protein C alters protein structure but does not cause haploinsufficiency.Phosphorylation and calcium antagonistically tune myosin-binding protein C's structure and function.Hypertrophic cardiomyopathy and the myosin mesa: viewing an old disease in a new light.Effects of myosin variants on interacting-heads motif explain distinct hypertrophic and dilated cardiomyopathy phenotypes.The giant protein titin regulates the length of the striated muscle thick filament.The Conformation of Myosin Heads in Relaxed Skeletal Muscle: Implications for Myosin-Based Regulation.Ordering of myosin II filaments driven by mechanical forces: experiments and theory.
P2860
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P2860
Orientation of myosin binding protein C in the cardiac muscle sarcomere determined by domain-specific immuno-EM.
description
2014 nî lūn-bûn
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2014年の論文
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2014年学术文章
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name
Orientation of myosin binding ...... by domain-specific immuno-EM.
@en
Orientation of myosin binding ...... by domain-specific immuno-EM.
@nl
type
label
Orientation of myosin binding ...... by domain-specific immuno-EM.
@en
Orientation of myosin binding ...... by domain-specific immuno-EM.
@nl
prefLabel
Orientation of myosin binding ...... by domain-specific immuno-EM.
@en
Orientation of myosin binding ...... by domain-specific immuno-EM.
@nl
P2093
P2860
P1476
Orientation of myosin binding ...... d by domain-specific immuno-EM
@en
P2093
Kyounghwan Lee
Roger Craig
Samantha P Harris
P2860
P304
P356
10.1016/J.JMB.2014.10.023
P407
P577
2014-11-06T00:00:00Z