1 40 1 Text A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text. URL Address <a href="http://doi.org/10.1021/jm300100d" target="_blank" rel="noreferrer noopener">http://doi.org/10.1021/jm300100d</a> Rights Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s). Pages 3425-3435 Issue 7 Volume 55 Search for Full-text Locate full-text within NEOMED Library's e-journal collections <p>Users with a NEOMED Library login can search for full-text journal articles at the following url: <a href="https://libraryguides.neomed.edu/home">https://libraryguides.neomed.edu/home</a></p> Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Identification of a Class of Novel Tubulin Inhibitors Publisher An entity responsible for making the resource available Journal of Medicinal Chemistry Date A point or period of time associated with an event in the lifecycle of the resource 2012 2012-04 Subject The topic of the resource agents; analog jcc76; biological evaluation; breast-cancer cells; halichondrin-b; heat-shock proteins; hsp27 phosphorylation; in-vivo; nimesulide; nonsteroidal antiinflammatory drugs; Pharmacology & Pharmacy; tumor-cells Creator An entity primarily responsible for making the resource Yi X; Zhong B; Smith K M; Geldenhuys W J; Feng Y; Pink J J; Dowlati A; Xu Y; Zhou A M; Su B Description An account of the resource We previously developed a series of anticancer agents based on cyclooxygenase-2 (COX-2) inhibitor nimesulide as a lead compound. However, the molecular targets of these agents still remain unclear. In this study, we synthesized a biotinylated probe based on a representative molecule of the compound library and performed protein pull-down assays to purify the anticancer targets of the compound. Via proteomic approaches, the major proteins bound to the probe were identified to be tubulin and heat shock protein 27 (Hsp27), and the compound inhibited tubulin polymerization by binding at the colchicine domain. However, the tubulin inhibitory effect of the compound activated the Hsp27 phosphorylation and possibly overrode the direct Hsp27 inhibitory effects, which made it difficult to solely validate the Hsp27 target. Taken together, the compound was a dual ligand of tubulin and Hsp27, inhibited tubulin polymerization, and had the potential to be a class of new chemotherapeutic agents. Identifier An unambiguous reference to the resource within a given context <a href="http://doi.org/10.1021/jm300100d" target="_blank" rel="noreferrer noopener">10.1021/jm300100d</a> Format The file format, physical medium, or dimensions of the resource Journal Article 2012 agents analog jcc76 biological evaluation breast-cancer cells Dowlati A Feng Y Geldenhuys W J halichondrin-b Heat-Shock Proteins hsp27 phosphorylation in-vivo Journal Article Journal of medicinal chemistry nimesulide nonsteroidal antiinflammatory drugs Pharmacology & Pharmacy Pink J J Smith K M Su B tumor-cells Xu Y Yi X Zhong B Zhou A M