Paul Ortiz De Montellano, PhD
|School||UCSF School of Pharmacy|
|Address||600 16th St|
San Francisco CA 94158
|Massachusetts Institute of Technology||B.S.||1964||Chemistry|
|Harvard University||M.A., Ph.D.||1968||Chemistry|
|Eidgenossische Technische Hochschule, Zurich||Postdoc||1969||Chemistry|
||1968||NIH Graduate Fellowship|
||1969||NATO Postdoctoral Fellow|
||1992||Alfred P. Sloan Research Fellow|
|UCSF School of Pharmacy||1985||Joseph M. Long Foundation Prize for Excellence in Teaching|
|UCSF||1988||Academic Senate Award for Distinction in Teaching|
|UCSF||1990||125 Most Outstanding People|
|1990||International Society for Neutron Capture Therapy Award for Excellence in Research|
|1988||Elected Fellow, American Association for the Advancement of Scie|
||1999||MERIT Grant Award, National Institutes of Health|
|Université René Descartes, Paris, France||1993
|1994||Bernard B. Brodie Award in Drug Metabolism, American Society for Pharmacology and Experimental Thera|
|UCSF School of Pharmacy||2006
||2013||Dean’s Recognition for Excellence in Teaching|
|2003||Ingelheim Boehringer Lecture Award, Division of Chemical Toxicology, 226th American Chemical Society|
|2006||Volwiler Research Achievement Award, American Association of Colleges of Pharmacy|
|2007||RT Williams Distinguished Scientific Achievement Award, International Society for the Study of Xenob|
|UCSF||2009||Champion of Diversity Award|
Heme-containing proteins are critical for the function of essentially all life forms. In humans, they are involved in respiration, the synthesis of hormones and other vital molecules, the elimination of drugs, and various signaling pathways. My laboratory has investigated the structure, mechanism, biochemistry and role of heme proteins for many years. We have focused particularly on the human cytochrome P450, peroxidase, and heme oxygenase enzymes. Our contributions in this area include crystal structures of bacterial P450 enzymes and the human heme oxygenase, clarification of the mechanism of cytochrome P450 enzymes, the development of methods for the mechanism-based inactivation of P450 enzymes, and more recently studies of human cytochrome P450 enzymes that are selectively expressed in cancer cells and are potentially useful in the activation of anticancer drugs. We currently also work on two classes of heme proteins in Mycobacterium tuberculosis, the causative agent of tuberculosis: (a) the twenty cytochrome P450 enzymes, some of which potential targets for anti-tuberculosis drugs, and (b) the gas sensor that initiates the dormant, persistent stage of tuberculosis that is difficult to eradicate and which can be reactivated when the immune system is compromised.
The studies in my laboratory employ a diversity of techniques, including organic synthesis, molecular biology, enzymology, and multiple spectroscopic techniques. We frequently collaborate with laboratories that have complementary expertise in organic synthesis, X-ray crystallography, NMR, or resonance Raman spectroscopy.
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