Science · 1998 · 99 citations · 8 references
Members of the kinesin superfamily of motor proteins are essential for mitotic and meiotic spindle organization, chromosome segregation, organelle and vesicle transport, and many other processes that require microtubule-based transport. A compound, adociasulfate-2, was isolated from a marine sponge, Haliclona (also known as Adocia) species, that inhibited kinesin activity by targeting its motor domain and mimicking the activity of the microtubule. Thus, the kinesin-microtubule interaction site could be a useful target for small molecule modulators, and adociasulfate-2 should serve as an archetype for specific inhibitors of kinesin functions.
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Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
F. Jon Kull, Elena P. Sablin, Rebecca Lau et al. · Nature · 1996 · 644 citations · Full text
Microtubule Interaction Site of the Kinesin Motor
Günther Woehlke, Aaron Ruby, Cynthia L. Hart et al. · Cell · 1997 · 389 citations · Full text
D. John Faulkner · Natural Product Reports · 1997 · 185 citations