Sirtuins in Health and Disease - 1st Edition - ISBN: 9780128122617

Sirtuins in Health and Disease, Volume 154

1st Edition

Serial Volume Editors: Weiping Zheng
Hardcover ISBN: 9780128122617
Imprint: Academic Press
Published Date: 1st February 2018
Page Count: 300
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Table of Contents

1. Concepts and chemical tools in sirtuin research” and (2) “SIRT4 and SIRT7: the least known mammalian sirtuins
2. Regulatory effects of NAD metabolic pathways on sirtuin activity
3. Sirtuins as modifiers of Huntington’s disease (HD) pathology
4. Parasite sirtuins as targets for novel chemotherapeutic agents
5. Targeting Sirtuins – Substrate Specificity and Inhibitor Design
6. Chemical probes in sirtuin research


Description

Sirtuins refer to a family of physiologically and pathologically important enzymes present in all life forms on this planet. This book entitled "Sirtuins in Health and Disease" introduces to readers 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. This book is intended to focus on the outstanding issues in the sirtuin field with implications for future sirtuin research.

Key Features

  • Excellent subject, excellent structural organization, authoritative contributions from world-renowned scholars in the sirtuin field, and the excellent writing style

Readership

Those working on the biology (including biochemistry), physiology, medicinal chemistry, chemical biology, pharmacology, and bioorganic chemistry of sirtuins and the unique reactions they catalyze. This volume will also benefit researchers outside of the sirtuin field since the lessons learned from sirtuin studies will also be applicable in other fields of study


Details

No. of pages:
300
Language:
English
Copyright:
© Academic Press 2018
Published:
Imprint:
Academic Press
Hardcover ISBN:
9780128122617

About the Serial Volume Editors

Weiping Zheng Serial Volume Editor

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.