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Photosensitized cleavage of dynein heavy chains. Cleavage at the “V1 site” by irradiation at 365 nm in the presence of ATP and vanadate.

Data up to Jan 2025

Published1987
Citations131
References19

Total Citations Per Year

Abstract

References (19)

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Potent inhibition of dynein adenosinetriphosphatase and of the motility of cilia and sperm flagella by vanadate.

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Relationship between the latent adenosine triphosphatase state of dynein 1 and its ability to recombine functionally with KCl-extracted sea urchin sperm flagella.

1979 • 99 citations

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1984 • 91 citations

Chapter 23 Preparation and Purification of Dynein

1982 • 82 citations

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1984 • 49 citations

Steady-state kinetic study of vanadate-induced inhibition of ciliary dynein adenosinetriphosphatase activity from Tetrahymena

1981 • 42 citations

Organic anions stabilize the reactivated motility of sperm flagella and the latency of dynein 1 ATPase activity.

1985 • 39 citations

Interactions between vanadate and 1,2-aromatic diols. Complex formation and oxidation-reduction

1979 • 26 citations

Activation of dynein 1 adenosine triphosphatase by monovalent salts and inhibition by vanadate.

1986 • 19 citations

Phosphorothioate analogs of adenosine 5'-triphosphate as substrates of dynein from Tetrahymena cilia

1986 • 16 citations

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Photosensitized cleavage of dynein heavy chains. Cleavage at the “V1 site” by irradiation… (1987) – Journal of Biological Chemistry | Metascience Observatory Explorer