ATTENTION: The software behind KU ScholarWorks is being upgraded to a new version. Starting July 15th, users will not be able to log in to the system, add items, nor make any changes until the new version is in place at the end of July. Searching for articles and opening files will continue to work while the system is being updated.
If you have any questions, please contact Marianne Reed at mreed@ku.edu .
The Rationale for Targeting the NAD/NADH Cofactor Binding Site of Parasitic S-Adenosyl-L-homocysteine Hydrolase for the Design of Anti-parasitic Drugs
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 |