Structural Basis of New Allosteric Inhibition in Kinesin Spindle Protein Eg5
Author:
Affiliation:
1. Department of Physical Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 422-8526, Japan
2. Center for Drug Discovery, Graduate School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 422-8526, Japan
Funder
Ministry of Education, Culture, Sports, Science, and Technology
Pharma Valley Center
Japan Society for the Promotion of Science
Publisher
American Chemical Society (ACS)
Subject
Molecular Medicine,General Medicine,Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/cb500939x
Reference37 articles.
1. Analysis of the kinesin superfamily: insights into structure and function
2. Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo
3. Induction of apoptosis by an inhibitor of the mitotic kinesin KSP requires both activation of the spindle assembly checkpoint and mitotic slippage
4. Mitotic Kinesin Inhibitors Induce Mitotic Arrest and Cell Death in Taxol-resistant and -sensitive Cancer Cells
5. Antitumor Activity of a Kinesin Inhibitor
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