User:Joshua S. Waitzman

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(Research interests)
(Useful links)
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==Useful links==
==Useful links==
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*Northwestern Medical Scientist Training Program[http://mstp.northwestern.edu/]
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*[http://mstp.northwestern.edu/ Northwestern Medical Scientist Training Program]
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*Northwestern Cellular and Molecular Basis of Disease Training Grant[http://www.biochem.northwestern.edu/cmbd/]
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*[http://www.biochem.northwestern.edu/cmbd/ Northwestern Cellular and Molecular Basis of Disease Training Grant]
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*Hertz Foundation[http://www.hertzfoundation.org/]
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*[http://www.hertzfoundation.org/ Hertz Foundation]

Revision as of 21:22, 9 July 2010

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. Duch J, Waitzman JS, and Amaral LA. . pmid:20585387. PubMed HubMed [Paper1]
    This work's been picked up by the Science [1] and Scientific American [2] podcasts!

  2. Bauer JH, Chang C, Morris SN, Hozier S, Andersen S, Waitzman JS, and Helfand SL. . pmid:17686972. PubMed HubMed [Paper2]
All Medline abstracts: PubMed HubMed

Useful links

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