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A structural model for monastrol inhibition of dimeric kinesin Eg5

✍ Scribed by Krzysiak, Troy C; Wendt, Thomas; Sproul, Lisa R; Tittmann, Peter; Gross, Heinz; Gilbert, Susan P; Hoenger, Andreas


Book ID
110031495
Publisher
Nature Publishing Group
Year
2006
Tongue
English
Weight
751 KB
Volume
25
Category
Article
ISSN
0261-4189

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The conformational features of the mitotic kinesin Eg5 inhibitor monastrol were investigated by computational (AM1, HF/3-21G ‫ؑ‬ ), X-ray diffraction, and NMR studies showing that monastrol is a conformationally highly flexible molecule. Racemic monastrol was resolved by direct enantioselective HPLC

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## Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a β€œFull Text” option. The original article is trackable v