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- Publisher Website: 10.1021/ja405199h
- Scopus: eid_2-s2.0-84883305317
- PMID: 23930594
- WOS: WOS:000323876300008
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Article: Site-specific chemistry on the microtubule polymer
Title | Site-specific chemistry on the microtubule polymer |
---|---|
Authors | |
Issue Date | 2013 |
Citation | Journal of the American Chemical Society, 2013, v. 135, n. 34, p. 12520-12523 How to Cite? |
Abstract | Microtubules are hollow tube-like biological polymers required for transport in diverse cellular contexts and are important drug targets. Microtubule function depends on interactions with associated proteins and post-translational modifications at specific sites located on its interior and exterior surfaces. However, we lack strategies to selectively perturb or probe these basic biochemical mechanisms. In this work, by combining amber suppression-mediated non-natural amino acid incorporation and tubulin overexpression in budding yeast, we demonstrate, for the first time, a general strategy for site-specific chemistry on microtubules. Probes and labels targeted to precise sites on the interior and exterior surfaces of microtubules will allow analysis and modulation of interactions with proteins and drugs, and elucidation of the functions of post-translational modifications. © 2013 American Chemical Society. |
Persistent Identifier | http://hdl.handle.net/10722/277624 |
ISSN | 2023 Impact Factor: 14.4 2023 SCImago Journal Rankings: 5.489 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Kleiner, Ralph E. | - |
dc.contributor.author | Ti, Shih Chieh | - |
dc.contributor.author | Kapoor, Tarun M. | - |
dc.date.accessioned | 2019-09-27T08:29:31Z | - |
dc.date.available | 2019-09-27T08:29:31Z | - |
dc.date.issued | 2013 | - |
dc.identifier.citation | Journal of the American Chemical Society, 2013, v. 135, n. 34, p. 12520-12523 | - |
dc.identifier.issn | 0002-7863 | - |
dc.identifier.uri | http://hdl.handle.net/10722/277624 | - |
dc.description.abstract | Microtubules are hollow tube-like biological polymers required for transport in diverse cellular contexts and are important drug targets. Microtubule function depends on interactions with associated proteins and post-translational modifications at specific sites located on its interior and exterior surfaces. However, we lack strategies to selectively perturb or probe these basic biochemical mechanisms. In this work, by combining amber suppression-mediated non-natural amino acid incorporation and tubulin overexpression in budding yeast, we demonstrate, for the first time, a general strategy for site-specific chemistry on microtubules. Probes and labels targeted to precise sites on the interior and exterior surfaces of microtubules will allow analysis and modulation of interactions with proteins and drugs, and elucidation of the functions of post-translational modifications. © 2013 American Chemical Society. | - |
dc.language | eng | - |
dc.relation.ispartof | Journal of the American Chemical Society | - |
dc.title | Site-specific chemistry on the microtubule polymer | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1021/ja405199h | - |
dc.identifier.pmid | 23930594 | - |
dc.identifier.scopus | eid_2-s2.0-84883305317 | - |
dc.identifier.volume | 135 | - |
dc.identifier.issue | 34 | - |
dc.identifier.spage | 12520 | - |
dc.identifier.epage | 12523 | - |
dc.identifier.eissn | 1520-5126 | - |
dc.identifier.isi | WOS:000323876300008 | - |
dc.identifier.f1000 | 718071484 | - |
dc.identifier.issnl | 0002-7863 | - |