dc.contributor.author | Cai, Sumin | |
dc.contributor.author | Li, Qing-Shan | |
dc.contributor.author | Fang, Jianwen | |
dc.contributor.author | Borchardt, Ronald T. | |
dc.contributor.author | Kuczera, Krzysztof | |
dc.contributor.author | Middaugh, C. Russell | |
dc.contributor.author | Schowen, Richard L. | |
dc.date.accessioned | 2017-06-27T18:48:52Z | |
dc.date.available | 2017-06-27T18:48:52Z | |
dc.date.issued | 2009-05 | |
dc.identifier.citation | Cai, S., Li, Q.-S., Fang, J., Borchardt, R. T., Kuczera, K., Middaugh, C. R., & Schowen, R. L. (2009). The Rationale for Targeting the NAD/NADH Cofactor Binding Site of Parasitic S-Adenosyl-L-homocysteine Hydrolase for the Design of Anti-parasitic Drugs. Nucleosides, Nucleotides & Nucleic Acids, 28(5), 485–503. http://doi.org/10.1080/15257770903051031 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/24659 | |
dc.description | This is an Accepted Manuscript of an article published by Taylor & Francis in Nucleosides, Nucleotides and Nucleic Acids in May 2009, available online: http://www.tandfonline.com/10.1080/15257770903051031. | en_US |
dc.description.abstract | Trypanosomal S-adenoyl-L-homocysteine hydrolase (Tc-SAHH), considered as a target for treatment of Chagas disease, has the same catalytic mechanism as human SAHH (Hs-SAHH) and both enzymes have very similar X-ray structures. Efforts toward the design of selective inhibitors against Tc-SAHH targeting the substrate binding site have not to date shown any significant promise. Systematic kinetic and thermodynamic studies on association and dissociation of cofactor NAD/H for Tc-SAHH and Hs-SAHH provide a rationale for the design of anti-parasitic drugs directed toward cofactor-binding sites. Analogues of NAD and their reduced forms show significant selective inactivation of Tc-SAHH, confirming that this design approach is rational. | en_US |
dc.publisher | Taylor & Francis | en_US |
dc.title | The Rationale for Targeting the NAD/NADH Cofactor Binding Site of Parasitic S-Adenosyl-L-homocysteine Hydrolase for the Design of Anti-parasitic Drugs | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Cai, Sumin | |
kusw.kuauthor | Li, Qing-Shan | |
kusw.kuauthor | Fang, Jianwen | |
kusw.kuauthor | Borchardt, Ronald T. | |
kusw.kuauthor | Kuczera, Krzysztof | |
kusw.kuauthor | Middaugh, C. Russell | |
kusw.kuauthor | Schowen, Richard L. | |
kusw.kudepartment | Pharmaceutical Chemistry | en_US |
dc.identifier.doi | 10.1080/15257770903051031 | en_US |
kusw.oaversion | Scholarly/refereed, author accepted manuscript | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC4128003 | en_US |
dc.rights.accessrights | openAccess | |