Bivalent inhibition of human beta-tryptase.
Selective inhibition of human mast cell tryptase by gabexate mesylate, an antiproteinase drug.
The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities.
The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition.
Human tryptase fibrinogenolysis is optimal at acidic pH and generates anticoagulant fragments in the presence of the anti-tryptase monoclonal antibody B12.
Oxyanion-mediated inhibition of serine proteases.
Inhibitors of tryptase for the treatment of mast cell-mediated diseases.
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore.
Bovine mast cell tryptase inactivation: effect of temperature.
Generation of catalytically active granzyme K from Escherichia coli inclusion bodies and identification of efficient granzyme K inhibitors in human plasma.
The structure of the human betaII-tryptase tetramer: fo(u)r better or worse.
Extrapancreatic trypsin-2 cleaves proteinase-activated receptor-2.
Granzymes (lymphocyte serine proteases): characterization with natural and synthetic substrates and inhibitors.
The human mast cell tryptase tetramer: a fascinating riddle solved by structure.
Formation of enzymatically active, homotypic, and heterotypic tetramers of mouse mast cell tryptases. Dependence on a conserved Trp-rich domain on the surface.
Mast cell tryptases and airway remodeling.
Human tryptase epsilon (PRSS22), a new member of the chromosome 16p13.3 family of human serine proteases expressed in airway epithelial cells.
Induction of rapid histone degradation by the cytotoxic T lymphocyte protease Granzyme A.
Diverse stability and catalytic properties of human tryptase alpha and beta isoforms are mediated by residue differences at the S1 pocket.
The crystal structure of human alpha1-tryptase reveals a blocked substrate-binding region.
Cyclotheonamide E4 and E5, new potent tryptase inhibitors from an Ircinia species of sponge.
This enzyme belongs to the peptidase family-S1. According to the literature [6], this enzyme has got a similar catalytic triad (Ser/His/Asp) to that of trypsin, suggesting a similar mechanism.