Monastrol stabilises an attached low-friction mode of Eg5
- 1 June 2004
- journal article
- magazine
- Published by Elsevier in Current Biology
- Vol. 14 (11), R411-R412
- https://doi.org/10.1016/j.cub.2004.05.030
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Inhibition of a Mitotic Motor Protein: Where, How, and Conformational ConsequencesJournal of Molecular Biology, 2004
- Interaction of the Mitotic Inhibitor Monastrol with Human Kinesin Eg5Biochemistry, 2002
- Evidence that Monastrol Is an Allosteric Inhibitor of the Mitotic Kinesin Eg5Chemistry & Biology, 2002
- Direct Long-Term Observation of Kinesin Processivity at Low LoadCurrent Biology, 2002
- Switch-based mechanism of kinesin motorsNature, 2001
- Probing Spindle Assembly Mechanisms with Monastrol, a Small Molecule Inhibitor of the Mitotic Kinesin, Eg5The Journal of cell biology, 2000
- Mechanism of the single-headed processivity: Diffusional anchoring between the K-loop of kinesin and the C terminus of tubulinProceedings of the National Academy of Sciences, 2000
- Small Molecule Inhibitor of Mitotic Spindle Bipolarity Identified in a Phenotype-Based ScreenScience, 1999
- Kinetic evidence for low chemical processivity in ncd and Eg5Journal of Molecular Biology, 1997
- Kinetics and Motility of the Eg5 Microtubule MotorBiochemistry, 1996