Novel Interactions of Fluorinated Nucleotide Derivatives Targeting Orotidine 5′-Monophosphate Decarboxylase-Reference-Cited by-同舟云学术

Novel Interactions of Fluorinated Nucleotide Derivatives Targeting Orotidine 5′-Monophosphate Decarboxylase

Published:2011-03-21 Issue:8 Volume:54 Page:2891-2901
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Lewis Melissa¹,Meza-Avina Maria Elena¹²,Wei Lianhu¹,Crandall Ian E.³,Bello Angelica Mara¹,Poduch Ewa¹,Liu Yan⁴,Paige Christopher J.⁵⁶,Kain Kevin C.⁷,Pai Emil F.¹⁵⁴,Kotra Lakshmi P.¹³⁷

Affiliation:

1. Center for Molecular Design and Preformulations and Division of Cellular and Molecular Biology, Toronto General Research Institute, University Health Network, Toronto, Ontario, M5G 1L7 Canada

2. Department of Chemistry and Biochemistry, The University of North Carolina at Greensboro, Greensboro, North Carolina 27412, United States

3. Departments of Pharmaceutical Sciences and Chemistry, University of Toronto, Toronto, Ontario, Canada

4. Departments of Biochemistry and Molecular Genetics, University of Toronto, 1 King’s College Circle, Toronto, Ontario, Canada

5. Department of Medical Biophysics, Ontario Cancer Institute, Princess Margaret Hospital, 620 University Avenue, Toronto, Ontario, M5G 2M9, Canada

6. Department of Immunology, University of Toronto, Toronto, Ontario, Canada

7. McLaughlin Center for Molecular Medicine, University of Toronto, Toronto, Ontario, Canada

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm101642g

Reference45 articles.

1. No Metal Cofactor in Orotidine 5′-Monophosphate Decarboxylase

2. Orotidylate decarboxylase: insights into the catalytic mechanism from substrate specificity studies

3. Purification and characterization of orotidine-5'-phosphate decarboxylase from Escherichia coli K-12.

4. Orotate phosphoribosyltransferase and orotidylate decarboxylase from Crithidia luciliae: Subcellular location of the enzymes and a study of substrate channeling

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