S-Homoadenosyl-l-cysteine and S-Homoadenosyl-l-homocysteine. Synthesis and Binding Studies of Non-Hydrolyzed Substrate Analogues with S-Adenosyl-l-homocysteine Hydrolase1
Author:
Affiliation:
1. Department of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602-5700, and Department of Pharmaceutical Chemistry, The University of Kansas, Lawrence, Kansas 66047 morris_robins@byu.edu
Publisher
American Chemical Society (ACS)
Subject
Organic Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jo020478g
Reference38 articles.
1. Correlation between the antiviral activity of acyclic and carbocyclic adenosine analogues in murine L929 cells and their inhibitory effect on L929 cell S-adenosylhomocysteine hydrolase
2. (a) Yuan, C.S.; Liu, S.; Wnuk, S. F.; Robins, M. J.; Borchardt, R. T. InAdvances in Antiviral Drug Design; De Clercq, E., Ed.; JAI Press: Greenwich, 1996; Vol. 2, pp 41−88.
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