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Results: 1-11 |
Results: 11
Tryptophan rotamers that report the conformational dynamics of proteins
Authors: Fidy, J Laberge, M Ullrich, B Polgar, L Szeltner, Z Gallay, J Vincent, M
Citation: J. Fidy et al., Tryptophan rotamers that report the conformational dynamics of proteins, PUR A CHEM, 73(3), 2001, pp. 415-419
Structures of prolyl oligopeptidase substrate/inhibitor complexes - Use ofinhibitor binding for titration of the catalytic histidine residue
Authors: Fulop, V Szeltner, Z Renner, V Polgar, L
Citation: V. Fulop et al., Structures of prolyl oligopeptidase substrate/inhibitor complexes - Use ofinhibitor binding for titration of the catalytic histidine residue, J BIOL CHEM, 276(2), 2001, pp. 1262-1266
Thiolate-imidazolium ion pair is not an obligatory catalytic entity of cysteine peptidases: The active site of picornain 3C
Authors: Sarkany, Z Szeltner, Z Polgar, L
Citation: Z. Sarkany et al., Thiolate-imidazolium ion pair is not an obligatory catalytic entity of cysteine peptidases: The active site of picornain 3C, BIOCHEM, 40(35), 2001, pp. 10601-10606
Catalysis of serine oligopeptidases is controlled by a gating filter mechanism
Authors: Fulop, V Szeltner, Z Polgar, L
Citation: V. Fulop et al., Catalysis of serine oligopeptidases is controlled by a gating filter mechanism, EMBO REP, 1(3), 2000, pp. 277-281
Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase family
Authors: Szeltner, Z Renner, V Polgar, L
Citation: Z. Szeltner et al., Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase family, PROTEIN SCI, 9(2), 2000, pp. 353-360
Trp42 rotamers report reduced flexibility when the inhibitor acetyl-pepstatin is bound to HIV-1 protease
Authors: Ullrich, B Laberge, M Tolgyesi, F Szeltner, Z Polgar, L Fidy, J
Citation: B. Ullrich et al., Trp42 rotamers report reduced flexibility when the inhibitor acetyl-pepstatin is bound to HIV-1 protease, PROTEIN SCI, 9(11), 2000, pp. 2232-2245
The noncatalytic beta-propeller domain of prolyl oligopeptidase enhances the catalytic capability of the peptidase domain
Authors: Szeltner, Z Renner, V Polgar, L
Citation: Z. Szeltner et al., The noncatalytic beta-propeller domain of prolyl oligopeptidase enhances the catalytic capability of the peptidase domain, J BIOL CHEM, 275(20), 2000, pp. 15000-15005
Characterization of the active site thiol group of rhinovirus 2A proteinase
Authors: Sarkany, Z Skern, T Polgar, L
Citation: Z. Sarkany et al., Characterization of the active site thiol group of rhinovirus 2A proteinase, FEBS LETTER, 481(3), 2000, pp. 289-292
Results of the seventh joint pesticide testing programme carried out by the IOBC/WPRS-Working Group 'Pesticides and Beneficial Organisms'
Authors: Sterk, G Hassan, SA Baillod, M Bakker, F Bigler, F Blumel, S Bogenschutz, H Boller, E Bromand, B Brun, J Calis, JNM Coremans-Pelseneer, J Duso, C Garrido, A Grove, A Heimbach, U Hokkanen, H Jacas, J Lewis, G Moreth, L Polgar, L Roversti, L Samsoe-Peterson, L Sauphanor, B Schaub, L Staubli, A Tuset, JJ Vainio, A Van de Veire, M Viggiani, G Vinuela, E Vogt, H
Citation: G. Sterk et al., Results of the seventh joint pesticide testing programme carried out by the IOBC/WPRS-Working Group 'Pesticides and Beneficial Organisms', BIOCONTROL, 44(1), 1999, pp. 99-117
Oligopeptidase B: A new type of serine peptidase with a unique substrate-dependent temperature sensitivity
Authors: Polgar, L
Citation: L. Polgar, Oligopeptidase B: A new type of serine peptidase with a unique substrate-dependent temperature sensitivity, BIOCHEM, 38(47), 1999, pp. 15548-15555
Crystallization and preliminary X-ray analysis of porcine muscle prolyl oligopeptidase
Authors: Bocskei, Z Fuxreiter, M Naray-Szabo, G Szabo, E Polgar, L
Citation: Z. Bocskei et al., Crystallization and preliminary X-ray analysis of porcine muscle prolyl oligopeptidase, ACT CRYST D, 54, 1998, pp. 1414-1415
Risultati: 1-11 |