Sirtuins in Health and Disease: Volume 154 (Progress in Molecular Biology and Translational Science)

Sirtuins in Health and Disease: Volume 154 (Progress in Molecular Biology and Translational Science)

By: Weiping Zheng (volume_editor)Hardback

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Sirtuins in Health and Disease, Volume 154 presents the reactions catalyzed by sirtuins in terms of their unique coenzyme NAD+-dependent catalytic mechanisms, the ways to elucidate these mechanisms, and the design of the inhibitory compounds against the sirtuin-catalyzed reactions as potential therapeutic agents for human diseases. Sections cover the concepts and chemical tools in sirtuin research, SIRT4 and SIRT7, the regulatory effects of NAD metabolic pathways on sirtuin activity, sirtuins as modifiers of Huntington's Disease (HD) pathology, parasite sirtuins as targets for novel chemotherapeutic agents, targeting sirtuins - substrate specificity and inhibitor design, and chemical probes in sirtuin research. This book focuses on the outstanding issues in the sirtuin field and implications for future sirtuin research.

About Author

Weiping Zheng received a Ph.D. in 1999 in medicinal chemistry from University of Tennessee, USA. He was a Postdoctoral Research Fellow (1999-2002) and a Research Associate (2002-2004) in bioorganic chemistry at Johns Hopkins University School of Medicine, USA. He was the James L. and Martha J. Foght Assistant Professor (tenure-track) in biochemistry at Department of Chemistry of University of Akron, USA (2004-2011). Since 2012, he has been a Professor at School of Pharmacy of Jiangsu University, China. His research interests are in medicinal chemistry: to develop catalytic mechanism-based enzyme inhibitors; to develop activity-based chemical probes for enzyme-catalyzed reactions and to explore the applications of the developed probes in biology and medicinal chemistry; to develop novel "peptide stapling" methodologies and to explore the applications of the developed methodologies in medicinal chemistry. Given these research interests, his research group has been the first in the world to start developing the catalytic mechanism-based inhibitors for the sirtuin-catalyzed protein acyl-lysine deacylation, with the identification of the first and the up-to-date most efficacious catalytic mechanism-based inhibitory warhead (i.e. N(epsilon)-thioacetyl-lysine) for the sirtuin-catalyzed deacetylation (Ref: Fatkins, David G.; Monnot, Andrew D.; Zheng, Weiping*. N(epsilon)-thioacetyl-lysine: a multi-facet functional probe for enzymatic protein lysine N(epsilon)-deacetylation. Bioorganic & Medicinal Chemistry Letters 2006, 16, 3651-3656). In collaboration with Prof. Zhenghe Wang's research group (Case Western Reserve University, USA), they recently identified a protein-protein interaction uniquely present in certain cancer cells, which opened up a new avenue for developing novel anti-cancer therapeutics (Ref: Hao, Yujun; Wang, Chao; Cao, Bo; Hirsch, Brett M.; Song, Jing; Markowitz, Sanford D.; Ewing, Rob M.; Sedwick, David; Liu, Lili; Zheng, Weiping*; Wang, Zhenghe*. Gain of interaction with IRS1 by p110alpha helical domain mutants is crucial for their oncogenic functions. Cancer Cell 2013, 23, 583-593). While traditional peptide stapling methodology, i.e. the all-hydrocarbon stapling, was employed in this study to construct stapled peptides used as pharmacological probes, his research group intended to develop novel superior peptide stapling methodologies and to explore the applications of the developed methodologies in this particular case and in medicinal chemistry in general.


Chemical Probes in Sirtuin Research Xiao Hu and Weiping Zheng Targeting Sirtuins: Substrate Specificity and Inhibitor Design Nima Rajabi, Iacopo Galleano, Andreas S. Madsen and Christian A. Olsen Regulatory Effects of NAD+ Metabolic Pathways on Sirtuin Activity Ning Zhang and Anthony A. Sauve Sirtuins as Modifiers of Huntington's Disease (HD) Pathology Sin Hui Neo and Bor Luen Tang Mammalian Sirtuins SIRT4 and SIRT7 Shengchao Li and Weiping Zheng

Product Details

  • ISBN13: 9780128122617
  • Format: Hardback
  • Number Of Pages: 186
  • ID: 9780128122617
  • weight: 450
  • ISBN10: 0128122617

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