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Biochemistry|January 11, 1994
Single peptide bond hydrolysis/resynthesis in squash inhibitors of serine proteinases. 1. Kinetics and thermodynamics of the interaction between squash inhibitors and bovine beta-trypsinJ Otlewski, T ZbyrytJournal of Molecular Biology|March 8, 1996
Thermodynamic stability effects of single peptide bond hydrolysis in protein inhibitors of serine proteinasesI Krokoszyńska, J OtlewskiEuropean Journal of Biochemistry|August 1, 1994
Denaturation of free and complexed bovine trypsinogen with the calcium ion, dipeptide Ile-Val and basic pancreatic trypsin inhibitor (Kunitz)G Bulaj, J OtlewskiActa Biochimica Polonica|January 1, 1997
Structural and energetic aspects of protein-protein recognitionJ Otlewski, W ApostolukBiological Chemistry Hoppe-Seyler|April 1, 1991
Interaction between squash inhibitors and bovine trypsinogenT Zbyryt, J OtlewskiProtein Science : a Publication of the Protein Society|March 29, 2001
Amino-acid substitutions at the fully exposed P1 site of bovine pancreatic trypsin inhibitor affect its stabilityD Krowarsch, J OtlewskiJournal of Molecular Biology|April 7, 1995
Ligand-induced changes in the conformational stability of bovine trypsinogen and their implications for the protein functionG Bulaj, J OtlewskiActa Biochimica Polonica|January 1, 1985
The serine proteinase inhibitor from summer squash (Cucurbita pepo): some structural features, stability and proteolytic degradationJ Otlewski, T WiluszActa Biochimica Polonica|January 1, 1996
Squash inhibitor family of serine proteinasesJ Otlewski, D KrowarschEuropean Journal of Biochemistry|April 2, 1999
Structural and energetic determinants of the S1-site specificity in serine proteasesH Czapinska, J OtlewskiPageof 7