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| WEIPING ZHENG |
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The James L. and Martha J. Foght Assistant Professor
B.S., 1987, Zhejiang Normal University
M.S., 1990, Shanghai Institute of Materia Medica, Academy of Sciences
Ph.D., 1999, The University of Tennessee
Postdoctoral fellow, 1999-2002, Johns Hopkins University School of Medicine
Research Associate, 2002-2004, Johns Hopkins University School of Medicine |
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Office: KNCL 406
(330) 972-2193 |
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Lab: KNCL 408
(330) 972-6982 |
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| Email: wzheng@uakron.edu |
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| Website: http://gozips.uakron.edu/~wzheng |
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| Research Interest |
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| Protein post-translational modifications (PTMs) have been increasingly regarded, especially in the post-genomic era, as biological approaches that play a significant role in amplifying the genetic information in higher eukaryotic species including humans through conferring extra level of structural and functional modulation onto proteins. Therefore, the identification of the modifying enzymes and the understanding of the mechanism, specificity, and function of PTMs undoubtedly represent a forefront in the post-genomic research arena. These efforts are not only able to unravel fundamental biological mechanisms, but also are critical to developing pharmacological interventions of therapeutic interests. We are employing our research expertise in organic/peptide chemistry, mechanistic enzymology, molecular biology, and protein chemistry to design, synthesize, and characterize bioactive molecules which may serve as molecular probes as well as potential therapeutics. Our initial research endeavors are primarily on the following two specific systems: human p53 protein which is the major tumor suppressor protein and human histone deacetylases which are intimately engaged in epigenetic transcriptional control. |
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| Schematic representation of cellular stress-induced p53 post-translational modifications. (P: phosphate on Ser or Thr residues; A: acetyl on Lys residues.) |
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| Selected Publications |
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Jamonnak, Nuttara; Fatkins, David G.; Wei, Lanlan; Zheng, Weiping. NƒÕ-methanesulfonyllysine as a non-hydrolyzable functional surrogate for NƒÕ-acetyl-lysine. Org. Biomol. Chem. 2007, 5, 892-896.
Zhang, Xiaodong; Guo, Ailan; Yu, Jianshi; Anthony Possemato, Yueting Chen, Zheng, Weiping; Polakiewicz, Roberto D.; Kinzler, Kenneth W.; Vogelstein, Bert; Velculescu, Victor E.; Wang, Zhenghe John. Identification of STAT3 as a substrate of receptor protein tyrosine phosphatase T. Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 4060-4064.
"Mechanistic studies on the alkyltransferase activity of serotonin N-acetyltransferase," Zheng, W.; Scheibner, K.A.; Ho, A.K.; and Cole, P.A., Chem. & Biol. 2001, 8, 379.
"Serotonin N-acetyltransferase: mechanism and inhibition," Zheng, W., and Cole, P.A.,
Curr. Med. Chem. 2002, 9, 1187.
"Novel bisubstrate analog inhibitors of serotonin N-acetyltransferase: the importance of being neutral," Zheng, W., and Cole, P.A., Bioorg. Chem. 2003, 31, 398.
"Cellular stabilization of the melatonin rhythm enzyme induced by non-hydrolyzable phosphonate incorporation," Zheng, W.; Zhang, Z.; Ganguly, S.; Weller, J.L.; Klein, D.C.; and Cole, P.A., Nat. Struct. Biol. 2003, 10, 1054.
"Bisubstrate analog structure-activity-relationships for p300 histone acetyltransferase inhibitors," Sagar, V.; Zheng, W.; Thompson P.R.; and Cole, P.A., Bioorg. & Med. Chem. 2004, 12, 3383.
"Cellular Stability of Serotonin N-acetyltransferase Conferred by Phosphono-difluoromethylene Alanine (Pfa) Substitution for Ser205," Zheng, W.; Schwarzer, D.; LeBeau, A.; Weller, J.L.; Klein, D.C.; and Cole, P.A. Journal of Biological Chemistry 2005, 280, 10462-10467.
¡§Negative regulation of a protein tyrosine phosphatase by tyrosine phosphorylation.¡¨ Schwarzer, D., Zhang, Z., Zheng, W., and Cole, P. A., The Journal of the American Chemical Society 2006, 128, 4192-4193.
¡§N(epsilon)-Thioacetyl-lysine: A multi-facet functional probe for enzymatic protein lysine N(epsilon)-deacetylation.¡¨ Fatkins, D. G., Monnot, A. D., and Zheng, W., Bioorganic & Medicinal Chemistry Letters 2006, 16, 3651-3656.
¡§N(epsilon)-methanesulfonyl-lysine as a non-hydrolyzable functional surrogate for N(epsilon)-acetyl-lysine.¡¨ Jamonnak, N., Fatkins, D. G., Wei, L., and Zheng, W., 2006 submitted).
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