Allosteric inhibition of kinesin-5 modulates its processive directional motility.

@article{Kwok2006AllostericIO,
  title={Allosteric inhibition of kinesin-5 modulates its processive directional motility.},
  author={Benjamin H. Kwok and Lukas C Kapitein and Jeffrey H. Kim and Erwin J. G. Peterman and Christoph F Schmidt and Tarun M Kapoor},
  journal={Nature chemical biology},
  year={2006},
  volume={2 9},
  pages={480-5}
}
Small-molecule inhibitors of kinesin-5 (refs. 1-3), a protein essential for eukaryotic cell division, represent alternatives to antimitotic agents that target tubulin. While tubulin is needed for multiple intracellular processes, the known functions of kinesin-5 are limited to dividing cells, making it likely that kinesin-5 inhibitors would have fewer side effects than do tubulin-targeting drugs. Kinesin-5 inhibitors, such as monastrol, act through poorly understood allosteric mechanisms, not… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 56 extracted citations

Metaphase Spindle Assembly

Biology • 2017
View 2 Excerpts

Biased Brownian motion as a mechanism to facilitate nanometer-scale exploration of the microtubule plus end by a kinesin-8.

Proceedings of the National Academy of Sciences of the United States of America • 2015

Similar Papers

Loading similar papers…