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Inosine Monophosphate Dehydrogenases A Major Therapeutic Target (Acs Symposium Series) by

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Published by An American Chemical Society Publication .
Written in English

Subjects:

  • Pharmacology,
  • Technology,
  • Inhibitors,
  • Heterocyclic Chemistry,
  • Technology Of Organic Products,
  • Science,
  • Science/Mathematics,
  • Life Sciences - Biochemistry,
  • Science / Biochemistry,
  • Congresses,
  • Chemistry - Organic,
  • Engineering - Chemical & Biochemical,
  • IMP dehydrogenase

Book details:

Edition Notes

ContributionsKrzysztof W. Pankiewicz (Editor), Barry M. Goldstein (Editor)
The Physical Object
FormatHardcover
Number of Pages376
ID Numbers
Open LibraryOL8227082M
ISBN 100841237808
ISBN 109780841237803

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Inosine monophosphate dehydrogenase (IMPDH) is a key enzyme of de novo purine nucleotide biosynthesis and is viewed as an important target in the quest for discovery of drugs in the antiviral, antibacterial and anticancer therapeutic areas. This review focuses on the medicinal chemistry, drug discovery and chemical biology of by: Inosine Monophosphate Dehydrogenase: A Major Therpeutic Target provides a comphrensive look at the chemotherapeutic inosine monophosphate deydrogenase. In addition to an overview of the field, this volume examines the molecular biology and gentics, the structure and mechanisms of IMPDH, inhibitor design, clinical applications, and new trends for the future. Cell Metabolism Clinical and Translational Report Inosine Monophosphate Dehydrogenase Dependence in a Subset of Small Cell Lung Cancers Fang Huang,1,2 Min Ni,2 Milind D. Chalishazar,3 Kenneth E. Huffman,4 Jiyeon Kim,2 Ling Cai,2,5 Xiaolei Shi,2 Feng Cai,2 Lauren G. Zacharias,2 Abbie S. Ireland,3 Kailong Li,2 Wen Gu,2 Akash K. Kaushik,2 Xin Liu,2 Adi F. Gazdar,4 Trudy G. Oliver,3 John . Corpus ID: Inosine Monophosphate Dehydrogenase: The Molecular Target of Mycophenolate @inproceedings{BremerInosineMD, title={Inosine Monophosphate Dehydrogenase: The Molecular Target of Mycophenolate}, author={S. Bremer}, year={} }.

Inosine Monophosphate Dehydrogenase Dependence in a Subset of Small Cell Lung Cancers. Fang Huang. Fang Huang. Affiliations. Institute of Hematology, Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, Hubei , China. The CBS subdomain of inosine 5′-monophosphate dehydrogenase regulates purine nucleotide turnover. Molecular Microbiology , 68 (2), DOI: /jx. Maxim Pimkin, George D. Markham. The CBS subdomain of inosine 5'-monophosphate dehydrogenase regulates purine nucleotide turnover.   30 Shu Q, Nair V. Inosine monophosphate dehydrogenase (IMPDH) as a target in drug discovery. Med. Res. Rev. 28(2),– ().Crossref, Medline, CAS, Google Scholar; 31 Jain J, Almquist SJ, Ford PJ et al. Regulation of inosine monophosphate dehydrogenase type I and type II isoforms in human lymphocytes. Biochem. Pharmacol. 67(4),– Inosine monophosphate dehydrogenase. IMPDH is also tightly regulated and catalyzes the conversion of IMP into xanthosine 5′-monophosphate, which is the rate-limiting step in the de novo synthesis of guanine nucleotides (Fig. ) (Jackson et al., ; Weber et al., ).

Inosine Monophosphate Dehydrogenase: A Major Therpeutic Target provides a comphrensive look at the chemotherapeutic inosine monophosphate deydrogenase. In addition to an overview of the field, this volume examines the molecular biology and gentics, the structure and mechanisms of IMPDH, inhibitor design, clinical applications, and new trends. Inosine-5'-monophosphate dehydrogenase; This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism. View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism. Mary Ann Lim MD, Roy D. Bloom MD, in Chronic Kidney Disease, Dialysis, and Transplantation (Fourth Edition), Mycophenolic Acid. MPA is a noncompetitive inhibitor of the rate-limiting enzyme inosine monophosphate dehydrogenase in the de novo purine biosynthesis pathway (see Fig. ).Because lymphocytes cannot efficiently use the salvage pathway and are highly dependent on the de novo. Inosine Monophosphate Dehydrogenase 17 Biosynthetic pathways 17 Genes and regulation 19 IMPDH isoenzymes 23 Catalytic cycle 24 Protein structure 25 IMPDH and pathophysiology 26 Inhibitors of IMPDH 27 Mycophenolic Acid 29 Mechanisms of action