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Konvalinka Jan

Born January 21, 1963 in Chomutov

  • Biochemistry and molecular biology
  • Member of Learned Society since 2003

Educational and professional preparation:

  • 1981, graduate, academic secondary school, Litvínov;
  • 1986, study of biochemistry, Faculty of Science, Charles University;
  • 1987-1991, post-graduate studies, Institute of Organic Chemistry and Biochemistry, AS CR; defended thesis Substrate specificity of retroviral proteases (supervisor Petr Štrop, PhD);
  • 2003, Associate Professor of biochemistry, FS CU

Employment and academic positions:

  • 1987-1991, internal PhD. Student, IOCB CSAS and AS CR;
  • 1991-1997, junior scientist, IOCB CSAS and AS CR;
  • 1997-present, senior scientist, IOCB, AS CR;
  • 1999-present, Head, Proteases of Human Pathogens Group, Department of the Biochemistry of Proteins, IOCB, AS CR;
  • 1996-1999, assistant lecturer, Department of Biochemistry, FS CU (half-time);
  • 2004-present, Associate Professor

Membership in selected domestic scientific bodies:

  • Member, Society for Biochemistry and Molecular Biology;
  • 1996-present, Secretary, Czech National Committee for Biochemistry and Molecular Biology;
  • 1996-1998, Chairman, Council for Molecular Biology and Biochemistry, Grant Agency of AS CR;
  • 1990-1992, 1996-2000, member, Scientific Council of IOCB, AS CR;
  • 2002-present, Chairman, Scientific Council, IOCB, AS CR;
  • 1998-present, external member, Scientific Council, Institute of Molecular Genetics, AS CR

Notable awards:

  • 1997, Award, Learned Society (for biochemistry)
  • 2002, Otto Wichterle Premium, Academic Council, AS CR
  • 2003, Award, Minister of Health

Selected publications:

  • Bařinka C., Šácha P., Sklenář J., Man P., Bezouška K., Slusher B.S. and Kon-valinka J: Identification of the N-glycosylation Sites on Glutamate Carboxy-peptidase II Necessary for Proteolytic Activity. Protein Sci. 13, 1627-1635 (2004).
  • Stříšovský K., Jirásková J., Bařinka C., Majer P., Rojas C., Slusher B.S. and Konvalinka J.: Mouse brain serine racemase catalyzes specific elimination of L-Ser to pyruvate. FEBS Lett. 535, 44-48 (2003).
  • Weber J., Mesters J. R., Lepšík M., Prejdová J., Švec M., Šponarová J., Mlčochová P., Stříšovský K., Uhlíková T., Souček M., Machala M., Staňková M., Vondrášek J., Klimkait T., Kraeusslich H.-G., Hilgenfeld R. and Konvalinka J.: Unusual binding mode of an HIV-1 protease inhibitor explains its potency against multi-drug-resistant virus strains. J. Mol. Biol. 324, 739-754 (2002).
  • Bařinka C., Rinnová M., Šácha P., Rojas C., Majer P., Slusher B.S. and Konvalinka J.: Substrate Specificity, Inhibition and Enzymological Analysis of Recombinant Human Glutamate Carboxypeptidase II. J. Neurochem. 80 (3), 477-488 (2002).
  • Rinnová M. Hradilek M., Bařinka C., Weber J., Souček M., Vondrášek J., Klimkait T. and Konvalinka J.: A picomolar inhibitor of resistant strains of HIV PR identified by a combinatorial approach. Arch. Biochem. Biophys. 382, 22-30 (2000).
  • Konvalinka J., Litera J., Weber J., Vondrášek J., Hradilek M., Souček M., Pichová I., Majer P., Štrop P., Sedláček J., Heuser A.-M., Kottler H. and Kraeusslich H.-G.: Configurations of diastereomeric hydroxyethylene isosteres strongly afect biological activities of a series of specific inhibitors of human-immunodeficiency-virus proteinase. Eur. J. Biochem. 250, 559-566 (1997).
  • Konvalinka J., Loechelt M., Zentgraf H., Fluegel R. and Kraeusslich H.-G.: Active Foamy Virus Proteinase is Essential for Virus Infectivity but Not for Formation of a Pol Polyprotein. J. Virol. 69, 7264-7268 (1995).
  • Konvalinka J., Literst M.A., Welker R., Rippman F., Heuser A.-M. and Kraeusslich H.-G.: An active site mutation in the HIV-1 proteinase (PR) causes reduced PR activity and loss of PR mediated cytotoxicity without apparent effect on virus maturation and infectivity. J. Virol. 69, 7180-7186 (1995).
  • Konvalinka J., Hořejší M., Andreánsky M., Novek P., Pichová I., Bláha I., Fábry M., Sedláček J., Foundling S. and Štrop P.: A retroviral proteinase from myeloblastosis associated virus acquires pH dependence and substrate specificity of the HIV-1 proteinase. EMBO J. 11, 1141-1144 (1992).
  • Richards A.D., Phylip L.H., Farmerie W.G., Scarborough P.E., Alvarez A., Dunn B.M., Herve-Hirel Ph., Konvalinka J., Strop P., Pavlickova L., Kostka V. and Kay J.: Sensitive, soluble chromogenic substrates for HIV-1 proteinase. J. Biol. Chem. 265, 7733-7736 (1990).

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