S
Sharon M. Rinzel
Researcher at Eli Lilly and Company
Publications - 4
Citations - 423
Sharon M. Rinzel is an academic researcher from Eli Lilly and Company. The author has contributed to research in topics: In vivo & Bicyclic molecule. The author has an hindex of 4, co-authored 4 publications receiving 413 citations.
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Journal ArticleDOI
A dideazatetrahydrofolate analog lacking a chiral center at C-6: N-[4-[2-(2-amino-3,4-dihydro-4-oxo-7H-pyrrolo[2,3-d]pyrimidin-5yl)ethyl[benzoyl]-L-glutamic acid is an inhibitor of thymidylate synthase
Edward C. Taylor,Dietmar G Kuhnt,Chuan Shih,Sharon M. Rinzel,Gerald B. Grindey,Julio C. Barredo,Mehrdad Jannatipour,Richard G. Moran +7 more
TL;DR: L-glutamic acid (15), prepared in five steps from 2-pivaloyl-7-deazaguanine, has been found to be an antitumor agent with its primary site of action at thymidylate synthase rather than purine synthesis.
Journal ArticleDOI
Sulfonimidamide analogs of oncolytic sulfonylureas.
John E. Toth,Gerald B. Grindey,William J. Ehlhardt,James Edward Ray,George B. Boder,Jesse R. Bewley,Kim K. Klingerman,Susan B. Gates,Sharon M. Rinzel,Richard M. Schultz,Leonard C. Weir,John F. Worzalla +11 more
TL;DR: Several sulfonimidamide analogs demonstrated excellent growth inhibitory activity in the 6C3HED model when dosed orally or intraperitoneally and a correlative structure-activity relationship to the oncolytic sulfonylureas was not apparent.
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Effects of diarylsulfonylurea antitumor agents on the function of mitochondria isolated from rat liver and GC3/c1 cells
TL;DR: The mechanism of antitumor activity does not appear to be the result of uncoupled as no correlation was evident between inhibition of cell growth and uncoupling action of a variety of active and inactive diarylsulfonylureas.
Journal ArticleDOI
Synthesis and biological activity of acyclic analogues of 5,10-dideaza-5,6,7,8-tetrahydrofolic acid.
Chuan Shih,Lynn S. Gossett,John F. Worzalla,Sharon M. Rinzel,Gerald B. Grindey,Philip M. Harrington,Edward C. Taylor +6 more
TL;DR: Inhibition and cell culture reversal studies against isolated enzymes suggest the mode of action of these compounds, which were less efficient substrates for the enzyme folylpolyglutamate synthetase (FPGS) compared with their bicyclic counterparts.