User:Joshua S. Waitzman

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(Contact Info)
Current revision (15:45, 1 February 2012) (view source)
(Publications)
 
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*Joshua S. Waitzman
*Joshua S. Waitzman
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<br>Ward 8-321
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*Ward 8-321
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<br>Department of Cell and Molecular Biology
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*Department of Cell and Molecular Biology
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<br>Feinberg School of Medicine, Northwestern University
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*Feinberg School of Medicine, Northwestern University
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<br>Chicago, IL, USA 60611
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*Chicago, IL, USA 60611
*[[Special:Emailuser/Joshua S. Waitzman|Email me through OpenWetWare]]
*[[Special:Emailuser/Joshua S. Waitzman|Email me through OpenWetWare]]
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I'm an MD/PhD student working in the Rice Lab at Northwestern
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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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<biblio>
<biblio>
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#Paper1 pmid=20585387  
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#Paper1 pmid=22261065
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#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!
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#Paper2 pmid=17686972  
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#Paper3 pmid=17686972  
</biblio>
</biblio>

Current revision

Contents

Contact Info

Joshua S. Waitzman
Joshua S. Waitzman
  • 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

  1. Waitzman JS, Larson AG, Cochran JC, Naber N, Cooke R, Jon Kull F, Pate E, and Rice SE. . pmid:22261065. PubMed HubMed [Paper1]
  2. Duch J, Waitzman JS, and Amaral LA. . pmid:20585387. PubMed HubMed [Paper2]
    This work's been picked up by the Science [1] and Scientific American [2] podcasts!

  3. Bauer JH, Chang C, Morris SN, Hozier S, Andersen S, Waitzman JS, and Helfand SL. . pmid:17686972. PubMed HubMed [Paper3]
All Medline abstracts: PubMed HubMed

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