The DOI matches its Crossref record; 197 of the 197 references it cites were found in a registry or an index.
Drugs that target dynamic microtubules: A new molecular perspective
Open accessAbstract
Microtubules have long been considered an ideal target for anticancer drugs because of the essential role they play in mitosis, forming the dynamic spindle apparatus. As such, there is a wide variety of compounds currently in clinical use and in development that act as antimitotic agents by altering microtubule dynamics. Although these diverse molecules are known to affect microtubule dynamics upon binding to one of the three established drug domains (taxane, vinca alkaloid, or colchicine site), the exact mechanism by which each drug works is still an area of intense speculation and research. In this study, we review the effects of microtubule‐binding chemotherapeutic agents from a new perspective, considering how their mode of binding induces conformational changes and alters biological function relative to the molecular vectors of microtubule assembly or disassembly. These “biological vectors” can thus be used as a spatiotemporal context to describe molecular mechanisms by which microtubule‐targeting drugs work. © 2011 Wiley Periodicals, Inc. Med Res Rev, 31, No. 3, 443‐481, 2011
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Cell death response to anti-mitotic drug treatment in cell culture, mouse tumor model and the clinic
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Impact of taxanes on androgen receptor signaling
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Microtubule inhibitor, SP-6-27 inhibits angiogenesis and induces apoptosis in ovarian cancer cells
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Metadata
- Authors
- Stanton, R. A., Gernert, K. M., Nettles, J. H., & Aneja, R.
- Venue
- Medicinal Research Reviews
- Publisher
- Wiley
- Published
- 2011-03-04
- Volume
- 31
- Issue
- 3
- Pages
- 443-481
- ISSN
- 0198-6325 (ISSN-L)
- 1098-1128
- OpenAlex
- W1988263368
- Cited by
- 526
- References
- 197
- FWCI
- 10.89
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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