Human Tryptases α and β/II Are Functionally Distinct Due, in Part, to a Single Amino Acid Difference in One of the Surface Loops That Forms the Substrate-binding Cleft

This publication has 37 references indexed in Scilit:

• Cloning of the Human Homolog of Mouse Transmembrane Tryptase
  International Archives of Allergy and Immunology, 1999
• The Tryptase, Mouse Mast Cell Protease 7, Exhibits Anticoagulant Activity in Vivo and in Vitro Due to Its Ability to Degrade Fibrinogen in the Presence of the Diverse Array of Protease Inhibitors in Plasma
  Journal of Biological Chemistry, 1997
• A novel heparin-dependent processing pathway for human tryptase. Autocatalysis followed by activation with dipeptidyl peptidase I.
  Journal of Clinical Investigation, 1996
• Packaging of Proteases and Proteoglycans in the Granules of Mast Cells and Other Hematopoietic Cells
  Journal of Biological Chemistry, 1995
• Conversion of the substrate specificity of mouse proteinase granzyme B
  Nature Structural & Molecular Biology, 1994
• Expression of a Mast Cell Tryptase in the Human Monocytic Cell Lines U‐937 and Mono Mac 6
  Scandinavian Journal of Immunology, 1993
• Mast cell tryptases: Examination of unusual characteristics by multiple sequence alignment and molecular modeling
  Protein Science, 1992
• Cloning and characterization of a second complementary DNA for human tryptase.
  Journal of Clinical Investigation, 1990
• Molecular cloning of dog mast cell tryptase and a related protease: structural evidence of a unique mode of serine protease activation
  Biochemistry, 1989
• On the disordered activation domain in trypsinogen: chemical labelling and low-temperature crystallography
  Acta Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1982