rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
4
|
pubmed:dateCreated |
2011-3-4
|
pubmed:abstractText |
NAmPRTase (PBEF/Visfatin) plays a pivotal role in the salvage pathway of NAD(+) biosynthesis. NAmPRTase has been an attractive target for anti-cancer agents that induce apoptosis of tumor cells via a declining plasma NAD(+) level. In this report, a series of structural analogs of FK866 (1), a known NAmPRTase inhibitor, was synthesized and tested for inhibitory activities against the proliferation of cancer cells and human NAmPRTase. Among them, compound 7 showed similar anti-cancer and enzyme inhibitory activities to compound 1. Further investigation of compound 7 with X-ray analysis revealed a co-crystal structure in complex with human NAmPRTase, suggesting that Asp219 in the active site of the enzyme could contribute to an additional interaction with the pyrrole nitrogen of compound 7.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
1768-3254
|
pubmed:author |
|
pubmed:copyrightInfo |
Copyright © 2011 Elsevier Masson SAS. All rights reserved.
|
pubmed:issnType |
Electronic
|
pubmed:volume |
46
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1153-64
|
pubmed:meshHeading |
pubmed-meshheading:21330015-Acrylamides,
pubmed-meshheading:21330015-Antineoplastic Agents,
pubmed-meshheading:21330015-Cell Line, Tumor,
pubmed-meshheading:21330015-Cell Survival,
pubmed-meshheading:21330015-Crystallography, X-Ray,
pubmed-meshheading:21330015-Drug Design,
pubmed-meshheading:21330015-Enzyme Assays,
pubmed-meshheading:21330015-Enzyme Inhibitors,
pubmed-meshheading:21330015-Humans,
pubmed-meshheading:21330015-Hydrogen Bonding,
pubmed-meshheading:21330015-Models, Molecular,
pubmed-meshheading:21330015-Nicotinamide Phosphoribosyltransferase,
pubmed-meshheading:21330015-Piperidines,
pubmed-meshheading:21330015-Protein Conformation,
pubmed-meshheading:21330015-Ribose
|
pubmed:year |
2011
|
pubmed:articleTitle |
Design, synthesis and X-ray crystallographic study of NAmPRTase inhibitors as anti-cancer agents.
|
pubmed:affiliation |
School of Life Science, Gwangju Institute of Science and Technology, Gwangju 500-712, Republic of Korea.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|