Design, Synthesis, and Enzymatic Evaluation of Multisubstrate Analogue Inhibitors of Escherichia coli Thymidine Phosphorylase-Reference-Cited by-同舟云学术

Design, Synthesis, and Enzymatic Evaluation of Multisubstrate Analogue Inhibitors of Escherichia coli Thymidine Phosphorylase

Published:2000-02-11 Issue:5 Volume:43 Page:971-983
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Esteban-Gamboa Antonio¹,Balzarini Jan¹,Esnouf Robert¹,De Clercq Erik¹,Camarasa María-José¹,Pérez-Pérez María-Jesús¹

Affiliation:

1. Instituto de Química Médica, C.S.I.C., Juan de la Cierva 3, 28006 Madrid, Spain, and Rega Institute for Medical Research, Katholieke Universiteit Leuven, B-3000 Leuven, Belgium

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm9911377

Reference43 articles.

1. Phosphorolysis of (E)-5-(2-bromovinyl)-2'-deoxyuridine (BVDU) and other 5-substituted-2'-deoxyuridines by purified human thymidine phosphorylase and intact blood platelets

2. Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity

3. Thymidine Phosphorylase Activity Associated with Platelet-Derived Endothelial Cell Growth Factor1

4. Angiogenic activity of enzymes

5. Thymidine phosphorylase is angiogenic and promotes tumor growth.

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