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The isolated heavy chain of an Acanthamoeba myosin contains full enzymatic activity.

Data up to Jan 2025

Published1978
Citations45
References19

Total Citations Per Year

Abstract

References (19)

PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin

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1978 • 489 citations

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1977 • 300 citations

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1975 • 163 citations

Macromolecular Composition of an Amoeba Plasma Membrane

1973 • 145 citations

Acanthamoeba cofactor protein is a heavy chain kinase required for actin activation of the Mg2+-ATPase activity of Acanthamoeba myosin I

1977 • 126 citations

Light Chains from Slow‐Twitch Muscle Myosin.

1976 • 123 citations

Characterization of a second myosin from Acanthamoeba castellanii

1978 • 111 citations

Acanthamoeba myosin II.

1977 • 102 citations

Role of myosin light chains in calcium regulation

1974 • 88 citations

Cyclic AMP‐induced phosphorylation in Dictyostelium of a polypeptide comigrating with myosin heavy chains

1978 • 82 citations

Evidence for the involvement of light chains in the biological functioning of myosin

1969 • 78 citations

Distribution of alkali light chains in myosin: isolation of isoenzymes

1977 • 69 citations

Myosin phosphorylation, cell motility and smooth muscle contraction

1978 • 42 citations

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The isolated heavy chain of an Acanthamoeba myosin contains full enzymatic activity. (1978) – Journal of Biological Chemistry | Metascience Observatory Explorer