M
Mehrdad Jannatipour
Researcher at University of Southern California
Publications - 7
Citations - 580
Mehrdad Jannatipour is an academic researcher from University of Southern California. The author has contributed to research in topics: Etoposide & Amsacrine. The author has an hindex of 7, co-authored 7 publications receiving 572 citations. Previous affiliations of Mehrdad Jannatipour include Children's Hospital Los Angeles.
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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 Article
Amsacrine and etoposide hypersensitivity of yeast cells overexpressing DNA topoisomerase II.
TL;DR: The results provide strong support of the hypothesis that the cellular target of these drugs is DNA topoisomerase II, and that these drugs kill cells by convertingDNA topoisomersase II into a DNA damaging agent.
Journal ArticleDOI
The top2-5 mutant of yeast topoisomerase II encodes an enzyme resistant to etoposide and amsacrine.
TL;DR: The results suggest that the top2-5 protein is altered in its sensitivity to anti-topoisomerase II agents, and several tightly clustered mutations have been identified.
Journal Article
Yeast Topoisomerase II Mutants Resistant to Anti-Topoisomerase Agents: Identification and Characterization of New Yeast Topoisomerase II Mutants Selected for Resistance to Etoposide
TL;DR: A system that allows us to easily isolate and characterize mutants in yeast topoisomerase II that are resistant to antitumor agents that target this enzyme is described, using yeast strains that are sensitive to those agents and that carry temperature-sensitive top2 mutations.
Journal Article
Functional expression of human topoisomerase IIα in yeast : mutations at amino acids 450 or 803 of topoisomerase IIα result in enzymes that can confer resistance to anti-topoisomerase II agents
Yuchu Hsiung,Mehrdad Jannatipour,Angela Rose,Jeannette McMahon,Dennis P. Duncan,John L. Nitiss +5 more
TL;DR: It is demonstrated that temperature-conditional yeast TOP2 mutants can be complemented by expression of wild-type human topoisomerase II alpha and that a human enzyme carrying both mutations confers a higher level of drug resistance than enzymes carrying either single mutation.