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Affinity of myosin S-1 for F-actin, measured by time-resolved fluorescence anisotropy.

Data up to Jan 2025

Published1976
Citations37
References18

Total Citations Per Year

Abstract

References (18)

The Regulation of Rabbit Skeletal Muscle Contraction

1971 • 4,491 citations

Fluorescence Spectroscopy of Proteins

1968 • 699 citations

Synthesis and characterization of two fluorescent sulfhydryl reagents

1973 • 431 citations

The characterization of myosin–product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphatase reaction

1974 • 364 citations

Segmental flexibility of the S-1 moiety of myosin

1973 • 233 citations

Dynamics of Fluorescence Polarization in Macromolecules

1972 • 225 citations

Substructure of the myosin molecule

1973 • 172 citations

Motion of subfragment-1 in myosin and its supramolecular complexes: saturation transfer electron paramagnetic resonance.

1975 • 122 citations

Dissociation constant of the actin-heavy meromyosin subfragment-1 complex

1975 • 99 citations

Mesure de la décroissance de la fluorescence polarisée de la γ-globuline-1-sulfonyl-5-diméthylaminonaphtalène

1969 • 87 citations

Equilibrium binding of adenosine diphosphate to myosin

1969 • 84 citations

Kinetics of formation and dissociation of the actomyosin complex

1969 • 74 citations

Interaction of globular actin with myosin subfragments

1971 • 63 citations

A new method for producing myosin subfragment-1

1972 • 62 citations

Binding of adenosine triphosphate to myosin

1968 • 58 citations

Number and location of adenosine triphosphatase sites of myosin

1970 • 52 citations

Nanosecond pulsefluorometry in polarized light of G‐actin‐ϵ‐ATP and F‐actin‐ϵ‐ADP

1975 • 45 citations

The Site of Force Generation in Muscle Contraction as Deduced from Fluorescence Polarization Studies

1974 • 38 citations

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Affinity of myosin S-1 for F-actin, measured by time-resolved fluorescence anisotropy. (1976) – Proceedings of the National Academy of Sciences | Metascience Observatory Explorer