User: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]]
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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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==Research interests==
==Research interests==
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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, Eg5 and other mitotic motor proteins are promising drug targets for cancer therapy, and ispinesib, a specific inhibitor of Eg5, is in Phase II FDA trials for non-small cell lung cancer and glioblastoma multiforme.  
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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.  
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Eg5 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 Eg5. Our group uses Electron Paramagnetic Resonance (EPR) spectroscopy to monitor the freedom of movement of different parts of the Eg5 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 Eg5 and may be able to guide future drug discovery efforts.  
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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==
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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>
==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]

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

Useful links

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