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Heavy Meromyosin

Known as: H Meromyosin, H-Meromyosin, Meromyosin, Heavy 
National Institutes of Health

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Related topics

1 relation

Broader (1)

Myosin Subfragments

Papers overview

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Highly Cited
2004
Highly Cited
2004
The elongation and contraction of actin bundles are induced by double-headed myosins in a motor concentration-dependent manner.
Highly Cited
2003
Highly Cited
2003
Actomyosin motility on nanostructured surfaces.
2000
2000
Kinetics of Smooth Muscle Heavy Meromyosin with One Thiophosphorylated Head*
Actin-activated MgATPase of smooth muscle heavy meromyosin is activated by thiophosphorylation of two regulatory light chains… 
Highly Cited
1990
Highly Cited
1990
Characterization of caldesmon binding to myosin.
Highly Cited
1981
Highly Cited
1981
Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. III. The multi-domain structure of actin-heavy meromyosin complex.
Heavy meromyosin (HMM) prepared by chymotryptic digestion retains DTNB light chain and subfragment-2 (S2) in addition to the two… 
Highly Cited
1980
Highly Cited
1980
The binding of heavy meromyosin to F-actin.
The binding of heavy meromyosin (HMM), a soluble two-headed fragment of myosin, to F-actin was examined at mu = 0.22 M, 22… 
1978
1978
Actin-like filaments in the endothelial cells of adult rat brain capillaries
Highly Cited
1975
Highly Cited
1975
Actin in erythrocyte ghosts and its association with spectrin. Evidence for a nonfilamentous form of these two molecules in situ
Actin was isolated from erythrocyte ghosts. It is identical to muscle actin in its molecular weight, net charge, ability to… 
1972
1972
An actin-like protein from amoebae of dictyostelium discoideum.
Highly Cited
1971
Highly Cited
1971
Electron microscopical observations on actinoid and myosinoid filaments in blood platelets.
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