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Biochimica Et Biophysica Acta|May 31, 1990
pH-dependent salting-out effect in enzyme-catalyzed reaction kineticsT KesvateraBiochimica Et Biophysica Acta|May 9, 2001
Comparison of salt effects on the reactions of acetylcholinesterase with cationic and anionic inhibitorsV Tõugu, T KesvateraBiochimica Et Biophysica Acta|November 14, 1996
Role of ionic interactions in cholinesterase catalysisV Tõugu, T KesvateraEuropean Journal of Biochemistry|August 16, 1976
Structure-activity relationships in acetylcholinesterase reactions. Hydrolysis of non-ionic acetic estersJ Järv, T Kesvatera, A AavisksaarProteins|September 20, 2001
Focusing of the electrostatic potential at EF-hands of calbindin D(9k): titration of acidic residuesT Kesvatera, B Jönsson, E Thulin, et al.Proteins|August 19, 1999
Ionization behavior of acidic residues in calbindin D(9k)T Kesvatera, B Jönsson, E Thulin, et al.Biochemistry|November 29, 1994
Binding of Ca2+ to calbindin D9k: structural stability and function at high salt concentrationT Kesvatera, B Jönsson, E Thulin, et al.Journal of Molecular Biology|June 21, 1996
Measurement and modelling of sequence-specific pKa values of lysine residues in calbindin D9kT Kesvatera, B Jönsson, E Thulin, et al.FEBS Letters|December 10, 1987
Acetylcholinesterase as polyelectrolyte in reaction with cationic substratesV Tóugu, A Pedak, T Kesvatera, et al.Biochimica Et Biophysica Acta|June 11, 1993
Acetylcholinesterase as polyelectrolyte: interaction with multivalent cationic inhibitorsV Tõugu, T Kesvatera, A Lääne, et al.Pageof 2