Loenarz, Christoph - University of Nottingham

个人简介

Christoph Loenarz completed his PhD in Biochemistry in 2011 at the University of Oxford as a Rhodes Scholar under the supervision of Prof. Chris Schofield FRS. His PhD research investigated molecular mechanisms by which cells respond to changes in oxygen levels. In 2010, Dr. Loenarz was elected to the William R Miller Junior Research Fellowship in Molecular Aspects of Biology, where he identified novel oxygen-sensitive pathways regulating cellular protein synthesis which are conserved from mammals to bacteria. In collaboration with colleagues in Cambridge, he investigated how specific virus proteins modulate the host cell's hypoxic response. In 2012, Dr. Loenarz was awarded a Leverhulme Trust Early Career Fellowship and elected to a Fellowship by Special Election at St Edmund Hall, Oxford. In 2015, he was appointed Assistant Professor in Chemical Biology at the University of Nottingham, where his research principally focuses on (i) pushing the frontiers in epigenetics research by investigating connections between post-translational modifications such as histone lysine methylation and metabolic pathways of pathophysiological relevance, and (ii) extending his recent high profile identification of an oxygen-dependent mechanism that enables modulation of the accuracy of protein synthesis. The Loenarz lab is based within

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HORITA S, SCOTTI JS, THINNES C, MOTTAGHI-TAROMSARI YS, THALHAMMER A, GE W, AIK W, LOENARZ C, SCHOFIELD CJ and MCDONOUGH MA, 2015. Structure of the Ribosomal Oxygenase OGFOD1 Provides Insights into the Regio- and Stereoselectivity of Prolyl Hydroxylases. Structure (London, England : 1993). 23(4), 639-52 LONGBOTHAM JE, LEVY C, JOHANNISSEN LO, TARHONSKAYA H, JIANG S, LOENARZ C, FLASHMAN E, HAY S, SCHOFIELD CJ and SCRUTTON NS, 2015. Structure and Mechanism of a Viral Collagen Prolyl Hydroxylase. Biochemistry. 54(39), 6093-105 DAVYDOVA E, HO AYY, MALECKI J, MOEN A, ENSERINK JM, JAKOBSSON ME, LOENARZ C and FALNES P?, 2014. Identification and characterization of a novel evolutionarily conserved lysine-specific methyltransferase targeting eukaryotic translation elongation factor 2 (eEF2). The Journal of biological chemistry. 289(44), 30499-510 KATZ MJ, ACEVEDO JM, LOENARZ C, GALAGOVSKY D, LIU-YI P, PéREZ-PEPE M, THALHAMMER A, SEKIRNIK R, GE W, MELANI M, THOMAS MG, SIMONETTA S, BOCCACCIO GL, SCHOFIELD CJ, COCKMAN ME, RATCLIFFE PJ and WAPPNER P, 2014. Sudestada1, a Drosophila ribosomal prolyl-hydroxylase required for mRNA translation, cell homeostasis, and organ growth. Proceedings of the National Academy of Sciences of the United States of America. 111(11), 4025-30 LOENARZ C, SEKIRNIK R, THALHAMMER A, GE W, SPIVAKOVSKY E, MACKEEN MM, MCDONOUGH MA, COCKMAN ME, KESSLER BM, RATCLIFFE PJ, WOLF A and SCHOFIELD CJ, 2014. Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy. Proceedings of the National Academy of Sciences of the United States of America. 111(11), 4019-24 SINGLETON RS, LIU-YI P, FORMENTI F, GE W, SEKIRNIK R, FISCHER R, ADAM J, POLLARD PJ, WOLF A, THALHAMMER A, LOENARZ C, FLASHMAN E, YAMAMOTO A, COLEMAN ML, KESSLER BM, WAPPNER P, SCHOFIELD CJ, RATCLIFFE PJ and COCKMAN ME, 2014. OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation. Proceedings of the National Academy of Sciences of the United States of America. 111(11), 4031-6 MAZZON M, PETERS NE, LOENARZ C, KRYSZTOFINSKA EM, EMBER SWJ, FERGUSON BJ and SMITH GL, 2013. A mechanism for induction of a hypoxic response by vaccinia virus. Proceedings of the National Academy of Sciences of the United States of America. 110(30), 12444-9 GE W, WOLF A, FENG T, HO C, SEKIRNIK R, ZAYER A, GRANATINO N, COCKMAN ME, LOENARZ C, LOIK ND, HARDY AP, CLARIDGE TDW, HAMED RB, CHOWDHURY R, GONG L, ROBINSON CV, TRUDGIAN DC, JIANG M, MACKEEN MM, MCCULLAGH JS, GORDIYENKO Y, THALHAMMER A, YAMAMOTO A, YANG M, LIU-YI P, ZHANG Z, SCHMIDT-ZACHMANN M, KESSLER BM, RATCLIFFE PJ, PRESTON GM, COLEMAN ML and SCHOFIELD CJ, 2012. Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans. Nature chemical biology. 8(12), 960-2 HILLRINGHAUS L, YUE WW, ROSE NR, NG SS, GILEADI C, LOENARZ C, BELLO SH, BRAY JE, SCHOFIELD CJ and OPPERMANN U, 2011. Structural and evolutionary basis for the dual substrate selectivity of human KDM4 histone demethylase family. The Journal of biological chemistry. 286(48), 41616-25 KAWAMURA A, LOENARZ C and SCHOFIELD CJ, 2011. Mutations to metabolic enzymes in cancer herald a need to unify genetics and biochemistry. Cell cycle (Georgetown, Tex.). 10(17), 2819-20 THALHAMMER A, BENCOKOVA Z, POOLE R, LOENARZ C, ADAM J, O'FLAHERTY L, SCH?DEL J, MOLE D, GIASLAKIOTIS K, SCHOFIELD CJ, HAMMOND EM, RATCLIFFE PJ and POLLARD PJ, 2011. Human AlkB homologue 5 is a nuclear 2-oxoglutarate dependent oxygenase and a direct target of hypoxia-inducible factor 1α (HIF-1α). PloS one. 6(1), e16210 ROTILI D, ALTUN M, HAMED RB, LOENARZ C, THALHAMMER A, HOPKINSON RJ, TIAN Y, RATCLIFFE PJ, MAI A, KESSLER BM and SCHOFIELD CJ, 2011. Photoactivable peptides for identifying enzyme-substrate and protein-protein interactions. Chemical communications (Cambridge, England). 47(5), 1488-90 LOENARZ C, COLEMAN ML, BOLEININGER A, SCHIERWATER B, HOLLAND PWH, RATCLIFFE PJ and SCHOFIELD CJ, 2011. The hypoxia-inducible transcription factor pathway regulates oxygen sensing in the simplest animal, Trichoplax adhaerens. EMBO reports. 12(1), 63-70 THALHAMMER A, MECINOVI? J, LOENARZ C, TUMBER A, ROSE NR, HEIGHTMAN TD and SCHOFIELD CJ, 2011. Inhibition of the histone demethylase JMJD2E by 3-substituted pyridine 2,4-dicarboxylates. Organic & biomolecular chemistry. 9(1), 127-35 LOENARZ C and SCHOFIELD CJ, 2011. Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases. Trends in biochemical sciences. 36(1), 7-18 THALHAMMER, ARMIN, BENCOKOVA, ZUZANA, POOLE, RACHEL, LOENARZ, CHRISTOPH, ADAM, JULIE, O'FLAHERTY, LINDA, SCHOEDEL, JOHANNES, MOLE, DAVID, GIASLAKIOTIS, KONSTANTINOS, SCHOFIELD, CHRISTOPHER J., HAMMOND, ESTER M., RATCLIFFE, PETER J. and POLLARD, PATRICK J., 2011. Human AlkB Homologue 5 Is a Nuclear 2-Oxoglutarate Dependent Oxygenase and a Direct Target of Hypoxia-Inducible Factor 1 alpha ( HIF-1 alpha) PLOS ONE. 6(1), MCDONOUGH MA, LOENARZ C, CHOWDHURY R, CLIFTON IJ and SCHOFIELD CJ, 2010. Structural studies on human 2-oxoglutarate dependent oxygenases. Current opinion in structural biology. 20(6), 659-72 CONEJO-GARCIA A, MCDONOUGH MA, LOENARZ C, MCNEILL LA, HEWITSON KS, GE W, LIéNARD BM, SCHOFIELD CJ and CLIFTON IJ, 2010. Structural basis for binding of cyclic 2-oxoglutarate analogues to factor-inhibiting hypoxia-inducible factor. Bioorganic & medicinal chemistry letters. 20(20), 6125-8 ILLINGWORTH CJR, LOENARZ C, SCHOFIELD CJ and DOMENE C, 2010. Chemical basis for the selectivity of the von Hippel Lindau tumor suppressor pVHL for prolyl-hydroxylated HIF-1alpha. Biochemistry. 49(32), 6936-44 YUE WW, HOZJAN V, GE W, LOENARZ C, COOPER CDO, SCHOFIELD CJ, KAVANAGH KL, OPPERMANN U and MCDONOUGH MA, 2010. Crystal structure of the PHF8 Jumonji domain, an Nepsilon-methyl lysine demethylase. FEBS letters. 584(4), 825-30 LOENARZ C, GE W, COLEMAN ML, ROSE NR, COOPER CDO, KLOSE RJ, RATCLIFFE PJ and SCHOFIELD CJ, 2010. PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an Nepsilon-dimethyl lysine demethylase. Human molecular genetics. 19(2), 217-22 MECINOVI? J, LOENARZ C, CHOWDHURY R and SCHOFIELD CJ, 2009. 2-Oxoglutarate analogue inhibitors of prolyl hydroxylase domain 2. Bioorganic & medicinal chemistry letters. 19(21), 6192-5 CHOWDHURY R, MCDONOUGH MA, MECINOVI? J, LOENARZ C, FLASHMAN E, HEWITSON KS, DOMENE C and SCHOFIELD CJ, 2009. Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases. Structure (London, England : 1993). 17(7), 981-9 LOENARZ C and SCHOFIELD CJ, 2009. Oxygenase catalyzed 5-methylcytosine hydroxylation. Chemistry & biology. 16(6), 580-3 STUBBS CJ, LOENARZ C, MECINOVI? J, YEOH KK, HINDLEY N, LIéNARD BM, SOBOTT F, SCHOFIELD CJ and FLASHMAN E, 2009. Application of a proteolysis/mass spectrometry method for investigating the effects of inhibitors on hydroxylase structure. Journal of medicinal chemistry. 52(9), 2799-805