Bonnie M. Ashe
Merck & Co., Inc., Rahway, NJ, USA (United States)(US)
Publications by Year
Research Areas
Protease and Inhibitor Mechanisms, Synthesis of β-Lactam Compounds, Peptidase Inhibition and Analysis, Enzyme Production and Characterization, Cell Adhesion Molecules Research
Most-Cited Works
- → Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the alpha 1-protease inhibitor reactive site.(1979)595 cited
- → Sensitive assays for trypsin, elastase, and chymotrypsin using new fluorogenic substrates(1977)264 cited
- → Cephalosporin antibiotics can be modified to inhibit human leukocyte elastase(1986)166 cited
- → Substrate specificity of the elastase and the chymotrypsin-like enzyme of the human granulocyte(1977)99 cited
- → Direct fluorescent assay of urokinase and plasminogen activators of normal and malignant cells: kinetics and inhibitor profiles.(1978)98 cited
- → Orally Active .beta.-Lactam Inhibitors of Human Leukocyte Elastase. 3. Stereospecific Synthesis and Structure-Activity Relationships for 3,3-Dialkylazetidin-2-ones(1995)89 cited
- → Specific inhibition of human granulocyte elastase by cis-unsaturated fatty acids and activation by the corresponding alcohols(1977)79 cited
- → Inhibition of human leukocyte elastase. 1. Inhibition by C-7-substituted cephalosporin tert-butyl esters(1990)73 cited
- → Orally active .beta.-lactam inhibitors of human leukocyte elastase-1. Activity of 3,3-diethyl-2-azetidinones(1992)68 cited
- → Characterization of an endopeptidase involved in pre-protein processing.(1979)64 cited