The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Inhibition of kinesin-driven microtubule motility by monoclonal antibodies to kinesin heavy chains.
Open accessAbstract
We have prepared and characterized seven mouse monoclonal antibodies (SUK 1-7) to the 130-kD heavy chain of sea urchin egg kinesin. On immunoblots, SUK 3 and SUK 4 cross-reacted with Drosophila embryo 116-kD heavy chains, and SUK 4, SUK 5, SUK 6, and SUK 7 bound to the 120-kD heavy chains of bovine brain kinesin. Three out of seven monoclonal antikinesins (SUK 4, SUK 6, and SUK 7) caused a dose-dependent inhibition of sea urchin egg kinesin-induced microtubule translocation, whereas the other four monoclonal antibodies had no detectable effect on this motility. The inhibitory monoclonal antibodies (SUK 4, SUK 6, and SUK 7) appear to bind to spatially related sites on an ATP-sensitive microtubule binding 45-kD chymotryptic fragment of the 130-kD heavy chain, whereas SUK 2 binds to a spatially distinct site. None of the monoclonal antikinesins inhibited the microtubule activated MgATPase activity of kinesin, suggesting that SUK 4, SUK 6, and SUK 7 uncouple this MgATPase activity from motility.
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Citations
Cites
Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
VALE, R., REESE, T., & SHEETZ, M. (1985) · Cell · doi:10.1016/s0092-8674(85)80099-4 · Cited by 1,993 · cited 1×
“One such enzyme, kinesin (Vale et al., 1985a), binds microtubules in a nucleotide sensitive fashion, and displays a microtubule-activated ATPase activity that drives movement of kinesin-coated objects towards the plus end of microtubules (MTs) ~ in vitro (Vale et al.”
Background
Cited by
Movement of microtubules by single kinesin molecules
Howard, J., Hudspeth, A. J., & Vale, R. D. (1989) · Nature · doi:10.1038/342154a0 · Cited by 885
Dompierre, J. P., Godin, J. D., Charrin, B. C., Cordelières, F. P., King, S. J., Humbert, S., & Saudou, F. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.0037-07.2007 · Cited by 792
Miro1 Is a Calcium Sensor for Glutamate Receptor-Dependent Localization of Mitochondria at Synapses
MacAskill, A. F., Rinholm, J. E., Twelvetrees, A. E., Arancibia-Carcamo, I. L., Muir, J., Fransson, A., Aspenstrom, P., Attwell, D., & Kittler, J. T. (2009) · Neuron · doi:10.1016/j.neuron.2009.01.030 · Cited by 674
Hirokawa, N., Pfister, K. K., Yorifuji, H., Wagner, M. C., Brady, S. T., & Bloom, G. S. (1989) · Cell · doi:10.1016/0092-8674(89)90691-0 · Cited by 477
Motor coordination via a tug-of-war mechanism drives bidirectional vesicle transport
Hendricks, A. G., Perlson, E., Ross, J. L., Schroeder, H. W., Tokito, M., & Holzbaur, E. L. F. (2010) · Current Biology · doi:10.1016/j.cub.2010.02.058 · Cited by 423
Metadata
- Authors
- Ingold, A. L., Cohn, S. A., & Scholey, J. M.
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1988-12-01
- Volume
- 107
- Issue
- 6
- Pages
- 2657-2667
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2169832500
- Cited by
- 175
- References
- 1
- FWCI
- 4.81
- Type
- journal article
- Language
- en
- Open access
- green
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- Ingold, A. L., Cohn, S. A., & Scholey, J. M. (1988). Inhibition of kinesin-driven microtubule motility by monoclonal antibodies to kinesin heavy chains. The Journal of cell biology. https://doi.org/10.1083/jcb.107.6.2657
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