Mass General Home
HMS MGH banner
Photo Strip
Research People Publications Links Tour Contact Us Home spacer
Jeffrey D. Macklis

 
Moshe Pritsker, Ph.D.

Moshe Pritsker, Ph.D.

Title Postdoctoral Fellow
Phone (617) 726-9132
Fax (617) 726-2310
Email Pritsker.moshe@mgh.harvard.edu
Location Massachusetts General Hospital- Main Campus
MGH-HMS Center for Nervous System Repair
50 Blossom Street, EDR-410
Boston, MA 02114

 

Research Overview

My current scientific interests are design of cell-based therapies and development of genomic technologies.

During my Ph.D. at Princeton, I established a novel approach for large-scale genetic screens in embryonic stem (ES) cells. Using this approach, I plan to initiate studies toward rational design of stem cell therapies in the neural system. My other projects included genome-wide studies of alternative splicing and bioinformatics analysis of transcriptional networks. Before, I finished a M.Sc. degree at the Weizmann Institute (Israel), studying HIV protein-mediated membrane fusion.

 

Previous Publications

  • Pritsker M, Doniger T, Kramer L, Westcot S, Lemischka I. (2005) Diversification of Stem Cell Molecular Repertoire by Alternative Splicing. Proceedings of National Academy of Science , 102(40), 14290-14295.
  • Pritsker M, Liu YC, Beer MA, Tavazoie S. (2004) Whole-genome discovery of transcription factor binding sites by network-level conservation. Genome Research 14(1), 99-108.
  • *Gerber D, * Pritsker M, Gunther-Ausborn S, Johnson B, Blumenthal R, Shai Y. (2004) Inhibition of HIV-1 envelope glycoprotein-mediated cell fusion by a D,L-amino acid-containing fusion peptide: possible recognition of the fusion complex. Journal of Biological Chemistry 279(46), 48224-48230. *Equal contribution.
  • Peisajovich S, Epand RF, Pritsker M, Shai Y, Epand RM (2000) The Polar Region Consecutive to the HIV Fusion Peptide Participates in Membrane Fusion. Biochemistry 39(7), 1826-1833.
  • Pritsker M, Rucker J, Hoffmann T, Doms RW, Shai Y (1999) Effect of nonpolar substitutions of the conserved Phe(11) in the fusion peptide of HIV-1 gp41 on its function, structure, and organization in membranes. Biochemistry 38(35), 11359-11371.
  • Pritsker M, Jones P, Blumenthal R, Shai Y (1998) A synthetic all D-amino acid peptide corresponding to the N-terminal sequence of HIV-1 gp41 recognizes the wild-type fusion peptide in the membrane and inhibits HIV-1 envelope glycoprotein-mediated cell fusion. Proceedings of National Academy of Science 95, 7287-7292.

 

 

Last Updated: May 26, 2006
© 2005 Jeffrey D. Maklis Lab - Massachusetts General Hospital. All Rights Reserved
Site design: Academic Web Pages
Contact us Click for a recent paper Click for a recent paper Click for a recent paper Click for a recent paper