Emil Martin, Ph.D.
Assistant Professor,
Center for Cell Signaling
phone 713.500.2441;
fax 713.500.2447
Emil.Martin@uth.tmc.edu
Dr. Martin's current research interests lie in understanding the molecular basis of nitric oxide/cGMP signaling in cells
Dr. Emil Martin received his M.S. in Genetics in 1989 from Moscow State University, Moscow, Russia and his Ph.D. in Molecular Genetics from the joint program at Columbia University and the Russian Academy of Sciences in 1993. He then pursued his postdoctoral training in the Division of Immunology/Oncology at Cornell University Medical School, New York. In 1998 he joined the faculty of the Department of Integrative Biology at the University of Texas Houston Medical School as Instructor. In 2006 he was appointed Assistant Professor of Molecular Medicine in the Center for Cell Signaling of the Brown Foundation Institute of Molecular Medicine for the Prevention of Human Diseases.
Dr. Martin's research interests are focused on biochemistry and cell biology of nitric oxide/cGMP signaling.
One direction of Dr. Martin’s research is focused on understanding the molecular mechanisms responsible for conversion of exogenous nitric oxide signal into an intracellular messenger molecule cGMP. He established a system of recombinant expression of active human soluble guanylyl cyclase (sGC), an enzyme responsible for this conversion process. Expressed sGC protein is used to understand the molecular events leading to activation of sGC by nitric oxide and various pharmaceuticals targeting the enzyme and to identify new leading compounds regulating sGC activity.Intracellular processes involved in regulation of sGC activation and function are also investigated. Several sGC-interacting proteins have been identified through yeast two-hybrid screening and their role in regulation of sGC activity and function are currently under investigation.
Dr. Martin’s research is also directed on investigation of cGMP-dependent regulation of gene transcription. Microarray gene expression profiles are employed to identify the genes responsive to variation in intracellular cGMP concentrations. Of particular interest are the genes regulated independently on cGMP-dependent protein kinase.
He is currently a member of the American Heart Association and American Society for Microbiology.
SELECTED PUBLICATIONS: E. Martin, V. Berka, E. Bogatenkova, F. Murad, A-L Tsai. Ligand selectivity of soluble guanylyl cyclase: effect of the hydrogen bonding tyrosine in the distal heme pocket on binding of oxygen, nitric oxide and carbon monoxide. J. Biol. Chem. 2006, V.281(38):27836-45
E. Martin, K. Czarnewski, V. Jayaraman, F. Murad, J. Kincaid. Resonance Raman and Infrared Spectroscopic studies of high-output forms of human soluble guanylyl cyclase. J. Am. Chem.Soc. 2005, 127(13):4625-31
K. Hanafy, E. Martin and F. Murad. CCTeta: A novel soluble guanylyl cyclase-interacting protein. J Biol Chem. 2004, 279: 46946-46953
Sharina IG, Martin E, Thomas A, Uray KL, Murad F. CCAAT-binding factor regulates expression of the beta1 subunit of soluble guanylyl cyclase gene in the BE2 human neuroblastoma cell line. Proc Natl Acad Sci U S A. 2003;100:11523-8.
Martin E, Sharina I, Kots A, Murad F. A constitutively activated mutant of human soluble guanylyl cyclase (sGC): implication for the mechanism of sGC activation. Proc Natl Acad Sci U S A. 2003 Aug 5;100(16):9208-13.
Martin E, Lee YC and Murad F. YC-1 activation of human soluble guanylyl Cyclase has both heme-dependent and heme-independent components. Proc Natl Acad Sci U S A. 98(23):12938-4Lee YC, Martin E, Murad F. Human recombinant soluble guanylyl cyclase: expression, purification, and regulation. Proc Natl Acad Sci U S A. 97(20): 10763-8, 2000 Sharina IG, Krumenacker JS, Martin E, Murad F. Genomic organization of alpha1 and beta1 subunits of the mammalian soluble guanylyl cyclase genes. Proc Natl Acad Sci U S A. 97(20): 10878-83, 2000Zaychikov E, Martin E, Denissova L, Kozlov M, Markovtsov V, Kashlev M, Heumann H, Nikiforov V, Goldfarb A, Mustaev A. Mapping of catalytic residues in the RNA polymerase active center. Science. 273(5271): 107-9, 1996Cho HJ, Martin E, Xie QW, Sassa S, Nathan C. Inducible nitric oxide synthase: identification of amino acid residues essential for dimerization and binding of tetrahydrobiopterin. Proc Natl Acad Sci U S A. 92(25): 11514-8, 1995Martin E, Nathan C, Xie QW. Role of interferon regulatory factor 1 in Induction of nitric oxide synthase. J. Exp. Medicine. 180(3): 977-84, 1994Martin E, Sagitov V, Burova E, Nikiforov V, Goldfarb A. Genetic dissection of the transcription cycle. A mutant RNA polymerase that cannot hold onto a promoter. J Biol Chem. 267(28): 20175-80, 1992REVIEWS AND BOOK CHAPTERS:
E. Martin, V. Berka, .A-L. Tsai and F. Murad. Soluble guanylyl cyclase: nitric oxide receptor. In Methods of Enzymology, (Nitric Oxide, part E.) 2005.
E. Martin, I. Sharina, A. Seminara, J. Krumenacker and F. Murad. NO cell signaling mediated by cGMP. In Nitric Oxide, Cell Signaling, and Gene Expression. Eds. E. Cadenas. 2005, Boca Raton, FlDavis. K., Martin E., Turko I., Murad F. Novel effects of Niric Oxide. Annual Review of Pharmacology and Toxicology. 41:203-36, 2001. Martin E, Davis K, Bian K, Lee YC, Murad F. Cellular signaling with Nitric Oxide and cyclic guanosine monophosphate. Seminars in Perinatology. 24(1): 2-6, 2000