The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Potent inhibition of dynein adenosinetriphosphatase and of the motility of cilia and sperm flagella by vanadate.
Open accessAbstract
The motility of demembranated sea urchin sperm flagella and that of embryo cilia reactivated with 0.1 mM ATP are completely inhibited by 4 micron and 0.5 micron vanadium(V) [V(V), in vanadate], respectively. The Mg2+-activated ATPase activity (ATP phosphohydrolase, EC 3.6.1.3)of the latent form of dynein 1 is inhibited 50% by 0.5-1 micron V(V), while the Ca2+-activated ATPase activity is much less sensitive. The inhibition of flagellar beat frequency and of dynein 1 ATPase activity by V(V) appears not to be competitive with ATP. In agreement with other reports, the inhibition of (Na,K)-ATPase by V(V) shows a slow onset in the presence of ATP and is relatively rapid in its absence. With dynein, however, the inhibition occurs at a rapid rate whether or not ATP is present. Catechol at a concentration of 1 mM reverses the V(V) inhibition of reactivated sperm motility, dynein ATPase, and (Na, K)-ATPase. Myosin and actomyosin ATPases show no inhibition by concentrations of V(V) up to 500 micron. The inhibition by V(V) provides a possible technique for distinguishing between the actions of dynein and myosin in different forms of cell motility.
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Citations
Cites
The Regulation of Rabbit Skeletal Muscle Contraction
Spudich, J. A., & Watt, S. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62016-2 · Cited by 4,493
Vanadate is a potent (Na,K)-ATPase inhibitor found in ATP derived from muscle.
Cantley, L. C., Josephson, L., Warner, R., Yanagisawa, M., Lechene, C., & Guidotti, G. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40978-1 · Cited by 831
Gibbons, B. H., & Gibbons, I. R. (1972) · The Journal of Cell Biology · doi:10.1083/jcb.54.1.75 · Cited by 570
Self-citationCalcium ion regulation of flagellar beat symmetry in reactivated sea urchin spermatozoa
Brokaw, C. J., Josslin, R., & Bobrow, L. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(74)80487-0 · Cited by 211
Transition metal ion inhibition of enzyme-catalyzed phosphate ester displacement reactions
VanEtten, R. L., Waymack, P. P., & Rehkop, D. M. (1974) · Journal of the American Chemical Society · doi:10.1021/ja00828a053 · Cited by 199
Studies on the Adenosine Triphosphatase Activity of 14 S and 30 S Dynein from Cilia of Tetrahymena
Gibbons, I. R. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96385-4 · Cited by 195
Self-citationSOME PROPERTIES OF BOUND AND SOLUBLE DYNEIN FROM SEA URCHIN SPERM FLAGELLA
Gibbons, I. R., & Fronk, E. (1972) · The Journal of Cell Biology · doi:10.1083/jcb.54.2.365 · Cited by 166
Self-citationGibbons, B. H., & Gibbons, I. R. (1976) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(76)90488-5 · Cited by 71
Self-citationDynein 2. A new adenosine triphosphatase from sea urchin sperm flagella.
Ogawa, K., & Gibbons, I. R. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33125-3 · Cited by 53
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Cited by
Solomon, M. J., Glotzer, M., Lee, T. H., Philippe, M., & Kirschner, M. W. (1990) · Cell · doi:10.1016/0092-8674(90)90504-8 · Cited by 688
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Cytoplasmic dynein is a minus end-directed motor for membranous organelles
Schroer, T. A., Steuer, E. R., & Sheetz, M. P. (1989) · Cell · doi:10.1016/0092-8674(89)90627-2 · Cited by 320
Leclerc, P., De Lamirande, E., & Gagnon, C. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00379-6 · Cited by 295
A latent adenosine triphosphatase form of dynein 1 from sea urchin sperm flagella.
Gibbons, I. R., & Fronk, E. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30290-9 · Cited by 208
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Metadata
- Authors
- Gibbons, I. R., Cosson, M. P., Evans, J. A., Gibbons, B. H., Houck, B., Martinson, K. H., Sale, W. S., & Tang, W. J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1978-05
- Volume
- 75
- Issue
- 5
- Pages
- 2220-2224
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2040116591
- Cited by
- 306
- References
- 9
- FWCI
- 8.42
- Type
- journal article
- Language
- en
- Open access
- green
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- The paper
- Gibbons, I. R., Cosson, M. P., Evans, J. A., Gibbons, B. H., Houck, B., Martinson, K. H., Sale, W. S., & Tang, W. J. (1978). Potent inhibition of dynein adenosinetriphosphatase and of the motility of cilia and sperm flagella by vanadate. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.75.5.2220
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