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Самый цитируемый биологический институт РФ *

Швядас Витаутас-Юозапас Каятоно

зав.отделом, профессор, доктор биологических наук
  1. Shcherbakova T.A., Panin N.V., Suplatov D.A., Shapovalova I.V., Svedas V.K. (2015) The beta D484N mutant of penicillin acylase from Escherichia coli is more resistant to inactivation by substrates and can effectively perform peptide synthesis in aqueous medium. J. Mol. Catal. B-Enzym., 112: 66-68. >>

  2. Grigorenko B.L., Khrenova M.G., Nilov D.K., Nemukhin A.V., Svedas V.K. (2014) Catalytic Cycle of Penicillin Acylase from Escherichia coli: QM/MM Modeling of Chemical Transformations in the Enzyme Active Site upon Penicillin G Hydrolysis. ACS Catal., 4 (8): 2521-2529. >>

  3. Novikov F.N., Stroganov O.V., Khaliullin I.G., Panin N.V., Shapovalova I.V., Chilov G.G., Svedas V.K. (2013) Molecular modeling of different substrate-binding modes and their role in penicillin acylase catalysis. FEBS J., 280 (1): 115-126. >>

  4. Suplatov D.A., Besenmatter W., Svedas V.K., Svendsen A. (2012) Bioinformatic analysis of alpha/beta-hydrolase fold enzymes reveals subfamily-specific positions responsible for discrimination of amidase and lipase activities. Protein Eng. Des. Sel., 25 (11): 689-697. >>

  5. Romanova N.N., Rybalko I.I., Tallo T.G., Zyk N.V., Svedas V.K. (2012) Synthesis of Schiff bases from 3-amino-3-arylpropionic acid esters in aqueous medium. Russ. J. Organ. Chem., 48 (6): 860-863. >>

  6. Guranda D.T., Ushakov G.A., Yolkin P.G., Svedas V.K. (2012) Thermodynamics of phenylacetamides synthesis: Linear free energy relationship with the pK of amine. J. Mol. Catal. B-Enzym., 74 (1): 48-53. >>

  7. Zakharenko A.L., Sukhanova M.V., Khodyreva S.N., Novikov F.N., Stroylov V.S., Nilov D.K., Chilov G.G., Svedas V.K., Lavrik O.I. (2011) Improved procedure of the search for poly(ADP-Ribose) polymerase-1 potential inhibitors with the use of the molecular docking approach. Molecular Biology, 45 (3): 517-521.

  8. Nilov D.K., Shabalin I.G., Popov V.O., Svedas V.K. (2011) Investigation of Formate Transport through the Substrate Channel of Formate Dehydrogenase by Steered Molecular Dynamics Simulations. Biochemistry-Moscow, 76 (2): 172-174.

  9. Chernorizov K.A., Elkina J.L., Semenyuk P.I., Svedas V.K., Muronetz V.I. (2010) Novel Inhibitors of Glyceraldehyde-3-phosphate Dehydrogenase: Covalent Modification of NAD-Binding Site by Aromatic Thiols. Biochemistry-Moscow, 75 (12): 1444-1449.

  10. Gardossi L., Poulsen P.B., Ballesteros A., Hult K., Svedas V.K., Vasic-racki D., Carrea G., Magnusson A., Schmid A., Wohlgemuth R., Halling P.J. (2010) Guidelines for reporting of biocatalytic reactions. Trends in Biotechnology, 28 (4): 171-180.

  11. Pchelintsev N.A., Youshko M.I., Svedas V.K. (2009) Quantitative characteristic of the catalytic properties and microstructure of cross-linked enzyme aggregates of penicillin acylase. Journal of Molecular Catalysis B-Enzymatic, 56 (4): 202-207.

  12. Grinberg V.Y., Burova T.V., Grinberg N.V., Shcherbakova T.A., Guranda D.T., Chilov G.G., Svedas V.K. (2008) Thermodynamic and kinetic stability of penicillin acylase from Escherichia coli. Biochimica et Biophysica Acta-Proteins and Proteomics, 1784 (5): 736-746.

  13. Chernobrovkin M.G., Shapovalova E.N., Guranda D.T., Kudryavtsev P.A., Svedas V.K., Shpigun O.A. (2007) Chiral high-performance liquid chromatography analysis of alpha-amino acid mixtures using a novel SH reagent-N-R-mandelyl-L-cysteine and traditional enantiomeric thiols for precolumn derivatization. Journal of Chromatography A, 1175 (1): 89-95.

  14. Chilov G.G., Sidorova A.V., Svedas V.K. (2007) Quantum chemical studies of the catalytic mechanism of N-terminal nucleophile hydrolase. Biochemistry-Moscow, 72 (5): 495-500.

  15. Pchelintsev N.A., Youshko M.I., Svedas V.K. (2006) A new method for spectrophotometric assay of activity of cross-linked penicillin acylase aggregates. Biochemistry-Moscow, 71 (3): 315-319.

  16. Guranda D.T., Kudryavtsev P.A., Khimiuk A.Y., Svedas V.K. (2005) Efficient enantiomeric analysis of primary amines and amino alcohols by high-performance liquid chromatography with precolumn derivatization using novel chiral SH-reagent N-(R)-mandelyl-(S)-cysteine. Journal of Chromatography A, 1095 (1): 89-93.

  17. Pertsovich S.I., Guranda D.T., Podchernyaev D.A., Yanenko A.S., Svedas V.K. (2005) Aliphatic amidase from Rhodococcus rhodochrous M8 is related to the nitrilase/cyanide hydratase family. Biochemistry-Moscow, 70 (11): 1280-1287.

  18. Guranda D.T., Volovik T.S., Svedas V.K. (2004) pH stability of penicillin acylase from Escherichia coli. Biochemistry-Moscow, 69 (12): 1386-1390.

  19. Shcherbakova T.A., Korennykh A.V., Van Langen L.M., Sheldon R.A., Svedas V.K. (2004) Use of high acyl donor concentrations leads to penicillin acylase inactivation in the course of peptide synthesis. Journal of Molecular Catalysis B-Enzymatic, 31 (1): 63-65.

  20. Guranda D.T., Khimiuk A.I., Van Langen L.M., Van Rantwijk F., Sheldon R.A., Svedas V.K. (2004) An 'easy-on, easy-off' protecting group for the enzymatic resolution of (+/-)-1-phenylethylamine in an aqueous medium. Tetrahedron-Asymmetry, 15 (18): 2901-2906.

  21. Guranda D.T., Shapovalova I.V., Svedas V.K. (2004) A new N-acyl derivative of (S)-cysteine for quantitative determination of enantiomers of amino compounds by HPLC with a precolumn modification with o-phthalaldehyde. Russian Journal of Bioorganic Chemistry, 30 (5): 403-408.

  22. Youshko M.I., Van Langen L.M., Sheldon R.A., Svedas V.K. (2004) Application of aminoacylase I to the enantioselective resolution of alpha-amino acid esters and amides. Tetrahedron-Asymmetry, 15 (12): 1933-1936.

  23. Youshko M.I., Moody H.M., Bukhanov A.L., Boosten W.H.J., Svedas V.K. (2004) Penicillin acylase-catalyzed synthesis of beta-lactam antibiotics in highly condensed aqueous systems: Beneficial impact of kinetic substrate supersaturation. Biotechnology and Bioengineering, 85 (3): 323-329.

  24. Khimiuk A.Y., Korennykh A.V., Van Langen L.M., Van Rantwijk F., Sheldon R.A., Svedas V.K. (2003) Penicillin acylase-catalyzed peptide synthesis in aqueous medium: a chemo-enzymatic route to stereoisomerically pure diketopiperazines. Tetrahedron-Asymmetry, 14 (20): 3123-3128.

  25. Chilov G.G., Moody H.M., Boesten W.H.J., Svedas V.K. (2003) Resolution of (RS)-phenylglycinonitrile by penicillin acylase-catalyzed acylation in aqueous medium. Tetrahedron-Asymmetry, 14 (17): 2613-2617.

  26. Stroganov O.V., Chilov G.G., Svedas V.K. (2003) Force field parametrization for 6-aminopenicillanic acid. Journal of Molecular Structure-Theochem, 631: 117-125.

  27. Youshko M.I., Bukhanov A.L., Svedas V.K. (2003) Study of nucleophile binding in the penicillin acylase active center. Kinetic analysis. Biochemistry-Moscow, 68 (3): 334-338.

  28. Youshko M.I., Chilov G.G., Shcherbakova T.A., Svedas V.K. (2002) Quantitative characterization of the nucleophile reactivity in penicillin acylase-catalyzed acyl transfer reactions. Biochimica et Biophysica Acta-Proteins and Proteomics, 1599 (1): 134-140.

  29. Youshko M.I., Svedas V.K. (2002) Penicillin acylase-catalyzed solid-state ampicillin synthesis. Catalysis, 344 (8): 894-898.

  30. Van Langen L.M., Janssen M.H.A., Oosthoek N.H.P., Pereira S.R.M., Svedas V.K., Van Rantwijk F., Sheldon R.A. (2002) Active site titration as a tool for the evaluation of immobilization procedures of penicillin acylase. Biotechnology and Bioengineering, 79 (2): 224-228.

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