Veronika Harmat
Ph.D., assistant professor

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H-1117 Budapest, Pázmány Péter sétány 1/A
Room 5.123
1518 Budapest 112, Pf.: 32
veronika at chem.elte.hu
+36-1-372-2500 ext. 6547
+36-1-372-2592

Short CV:

Born:
  • 24 April 1973, Budapest
Current status:
  • Assistant Professor, Institute of Chemistry, Eötvös University, Budapest, Hungary

Education:
  • Ph.D. in structural chemistry, Eötvös Loránd University, 2003
  • M.Sc. in chemistry Eötvös Loránd University, 1996
Research activities:
  • Hungarian Academy of Sciences - Eötvös Loránd University, Protein Modeling Research Group, associate research fellow 2003-
  • Bolyai János Research Fellowship 2001-2004
  • Demonstrator at Eötvös Loránd University 2001-2002
Teaching activity:
  • Protein crystallography, special course in chemistry and biology major, 2006-
  • X-ray crystallography, semi-optional course in chemistry 1999-
  • X-ray crystallography laboratory practice 2000-
  • General chemistry laboratory practical, 2001-2002, 2008-
  • Inorganic chemistry laboratory practical, 2009-
Research interest
  • Macromolecular and small molecular crystallography
  • Molecular recognition in protein-ligand and protein-protein complexes
  • Member of the Protein Crystallography Laboratory, Department of Theoretical Chemistry, Eötvös Loránd University 1995-
Awards:
  • Young Scientist Award of the Hungarian Academy of Sciences 2006
Selected publications [full list (pdf)]
  • Harmat V, Domokos K, Menyhard DK, Pallo A, Szeltner Z, Szamosi I, Beke-Somfai T, Naray-Szabo G, Polgar L. Structure and catalysis of acylaminoacyl peptidase: closed and open subunits of a dimer oligopeptidase. J BIOL CHEM 2010 Nov 16. [Epub ahead of print] PMID: 21084296
  • Pecsi I, Leveles I, Harmat V, Vertessy BG, Toth J. Aromatic stacking between nucleobase and enzyme promotes phosphate ester hydrolysis in dUTPase. NUCLEIC ACIDS RES 38:7179-7186 (2010)
    [abstract]
  • Kovacs E, Harmat V, Tóth J, Vértessy BG, Módos K, Kardos J, Liliom K. Structure and mechanism of calmodulin binding to a signaling sphingolipid reveal new aspects of lipid-protein interactions. FASEB J. 24:3829-3839 (2010)
    [abstract]
  • Dobó J, Harmat V, Beinrohr L, Sebestyén E, Závodszky P, Gál P MASP-1, a Promiscuous Complement Protease: Structure of Its Catalytic Region Reveals the Basis of Its Broad Specificity JOURNAL OF IMMUNOLOGY 183: 1207-1214 (2009)
    [abstract]
  • Beinrohr L, Harmat V, Dobo J, Lorincz Z, Gal P, Zavodszky P. C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease, JOURNAL OF BIOLOGICAL CHEMISTRY 282: 21100 - 21109 (2007)
    [abstract]
  • Fodor K, Harmat V, Hetenyi C, Kardos J, Antal J, Perczel A, Patthy A, Katona G, Graf L Extended intermolecular interactions in a serine protease-canonical inhibitor complex account for strong and highly specific inhibition J. Mol. Biol. 350: 156-169 (2005)
    [abstract]
  • Horvath I, Harmat V, Perczel A, Palfi V, Nyitray L, Nagy A, Hlavanda E, Naray-Szabo G, Ovadi J The structure of the complex of calmodulin with KAR-2 - A novel mode of binding explains the unique pharmacology of the drug J. Biol. Chem 280: 8266-8274 (2005)
    [abstract]


last modified: Mon Feb 07 15:00:00 CET 2011