User:Joshua S. Waitzman: Difference between revisions
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==Contact Info== | ==Contact Info== | ||
[[Image: | [[Image:Waitzman.jpg|thumb|right|Joshua S. Waitzman]] | ||
*Joshua S. Waitzman | *Joshua S. Waitzman | ||
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*[[Special:Emailuser/Joshua S. Waitzman|Email me through OpenWetWare]] | *[[Special:Emailuser/Joshua S. Waitzman|Email me through OpenWetWare]] | ||
I'm an MD/PhD student working in the Rice Lab at Northwestern | I'm an MD/PhD student working in the [http://openwetware.org/wiki/Rice_Lab Rice Lab] at Northwestern | ||
==Education== | ==Education== | ||
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==Research interests== | ==Research interests== | ||
In order to divide and proliferate, a single cell must distribute its chromsomes equally to daughter cells by establishing a microtubule-based spindle. Kinesin-5 is a microtubule motor protein that plays an essential role in aligning this spindle structure. As a hallmark of cancer cells is their increased ability to divide, kinesin-5 and other mitotic motor proteins are promising drug targets for cancer therapy, and ispinesib, a specific inhibitor of kinesin-5, is in Phase II FDA trials for non-small cell lung cancer and glioblastoma multiforme. | |||
Kinesin-5 is believed to be regulated by phosphorylation by both M-Cdk and Wee1, kinases known to play roles in the cell cycle. However, the structural mechanisms of this phospho-regulation are unknown. My work uses structural biology and biochemistry approaches to determine the phosphorylation-dependent changes in kinesin-5. Our group uses Electron Paramagnetic Resonance (EPR) spectroscopy to monitor the freedom of movement of different parts of the kinesin-5 protein, as well as kinetic measurements of the protein's activity. By combining these approaches, we hope to clarify the relationships between structure and activity in kinesin-5 and may be able to guide future drug discovery efforts. | |||
==Publications== | ==Publications== | ||
<!-- Replace the PubMed ID's ("pmid=#######") below with the PubMed ID's for your publications. You can add or remove lines as needed --> | <!-- Replace the PubMed ID's ("pmid=#######") below with the PubMed ID's for your publications. You can add or remove lines as needed --> | ||
<biblio> | <biblio> | ||
#Paper1 pmid=20585387 | #Paper1 pmid=22261065 | ||
#Paper2 pmid=20585387 | |||
// This work's been picked up by the Science [http://podcasts.aaas.org/science_news/SciencePodcast_100618_ScienceNOW.mp3] and Scientific American [http://www.scientificamerican.com/podcast/episode.cfm?id=soccer-players-ranked-with-network-10-06-17] podcasts! | // This work's been picked up by the Science [http://podcasts.aaas.org/science_news/SciencePodcast_100618_ScienceNOW.mp3] and Scientific American [http://www.scientificamerican.com/podcast/episode.cfm?id=soccer-players-ranked-with-network-10-06-17] podcasts! | ||
# | #Paper3 pmid=17686972 | ||
</biblio> | </biblio> | ||
==Useful links== | ==Useful links== | ||
*[[ | *[http://mstp.northwestern.edu/ Northwestern Medical Scientist Training Program] | ||
*[ | *[http://www.biochem.northwestern.edu/cmbd/ Northwestern Cellular and Molecular Basis of Disease Training Grant] | ||
*[http://www.hertzfoundation.org/ Hertz Foundation] |
Latest revision as of 12:45, 1 February 2012
Contact Info
- Joshua S. Waitzman
- Ward 8-321
- Department of Cell and Molecular Biology
- Feinberg School of Medicine, Northwestern University
- Chicago, IL, USA 60611
- Email me through OpenWetWare
I'm an MD/PhD student working in the Rice Lab at Northwestern
Education
- 2007, Sc.B. with Honors in Biophysics, magna cum laude, Brown University
Research interests
In order to divide and proliferate, a single cell must distribute its chromsomes equally to daughter cells by establishing a microtubule-based spindle. Kinesin-5 is a microtubule motor protein that plays an essential role in aligning this spindle structure. As a hallmark of cancer cells is their increased ability to divide, kinesin-5 and other mitotic motor proteins are promising drug targets for cancer therapy, and ispinesib, a specific inhibitor of kinesin-5, is in Phase II FDA trials for non-small cell lung cancer and glioblastoma multiforme.
Kinesin-5 is believed to be regulated by phosphorylation by both M-Cdk and Wee1, kinases known to play roles in the cell cycle. However, the structural mechanisms of this phospho-regulation are unknown. My work uses structural biology and biochemistry approaches to determine the phosphorylation-dependent changes in kinesin-5. Our group uses Electron Paramagnetic Resonance (EPR) spectroscopy to monitor the freedom of movement of different parts of the kinesin-5 protein, as well as kinetic measurements of the protein's activity. By combining these approaches, we hope to clarify the relationships between structure and activity in kinesin-5 and may be able to guide future drug discovery efforts.
Publications
- Waitzman JS, Larson AG, Cochran JC, Naber N, Cooke R, Jon Kull F, Pate E, and Rice SE. The loop 5 element structurally and kinetically coordinates dimers of the human kinesin-5, Eg5. Biophys J. 2011 Dec 7;101(11):2760-9. DOI:10.1016/j.bpj.2011.10.032 |
- Duch J, Waitzman JS, and Amaral LA. Quantifying the performance of individual players in a team activity. PLoS One. 2010 Jun 16;5(6):e10937. DOI:10.1371/journal.pone.0010937 |
- Bauer JH, Chang C, Morris SN, Hozier S, Andersen S, Waitzman JS, and Helfand SL. Expression of dominant-negative Dmp53 in the adult fly brain inhibits insulin signaling. Proc Natl Acad Sci U S A. 2007 Aug 14;104(33):13355-60. DOI:10.1073/pnas.0706121104 |