L L Johnson
Affiliation: Parke-Davis Pharmaceutical Research
- Matrix metalloproteinasesL L Johnson
Department of Biochemistry, Parke Davis Pharmaceutical Research, Division of Warner Lambert Company, Ann Arbor, MI 48105, USA
Curr Opin Chem Biol 2:466-71. 1998..In addition, more selective inhibitors with improved pharmacokinetic profiles have entered clinical trials, allowing the assessment of the safety and efficacy of this strategy...
- Effect of species differences on stromelysin-1 (MMP-3) inhibitor potency. An explanation of inhibitor selectivity using homology modeling and chimeric proteinsL L Johnson
Department of Cancer Research, Parke Davis Pharmaceutical Research, Division of Warner Lambert Company, Ann Arbor, Michigan 48105, USA
J Biol Chem 274:24881-7. 1999..Homology modeling provides a tool to identify key differences in isoforms that can significantly affect native enzyme activity...
- A rationalization of the acidic pH dependence for stromelysin-1 (Matrix metalloproteinase-3) catalysis and inhibitionL L Johnson
Department of Cancer Research, Parke Davis Pharmaceutical Research, Division of Warner Lambert Co, Ann Arbor, Michigan 48105, USA
J Biol Chem 275:11026-33. 2000..The striking acidic profile of stromelysin-1 defined by the combined ionization of Glu(202) and His(224) allows the design of highly selective inhibitors...
- X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivityA G Pavlovsky
Department of Chemistry, Parke Davis Pharmaceutical Research, Division of Warner Lambert Company, Ann Arbor, Michigan 48105, USA
Protein Sci 8:1455-62. 1999..An analysis of the unique binding mode predicts structural modifications to design improved MMP inhibitors...
- Structure-activity relationships and pharmacokinetic analysis for a series of potent, systemically available biphenylsulfonamide matrix metalloproteinase inhibitorsP M O'Brien
Department of Chemistry, Parke Davis Pharmaceutical Research, Division of Warner Lambert Company, 2800 Plymouth Road, Ann Arbor, Michigan 48105, USA
J Med Chem 43:156-66. 2000....
- X-ray structure of a hydroxamate inhibitor complex of stromelysin catalytic domain and its comparison with members of the zinc metalloproteinase superfamilyV Dhanaraj
Department of Crystallography, Birkbeck College, London, UK
Structure 4:375-86. 1996..Matrixins play key roles in diseases as diverse as arthritis and cancer and hence are important targets for therapeutic intervention...
- Complete amino acid sequence of human serum cholinesteraseO Lockridge
J Biol Chem 262:549-57. 1987..The sequence of human serum cholinesterase is 53.8% identical with the sequence of acetylcholinesterase from Torpedo californica and 28% identical with the carboxyl-terminal portion of bovine thyroglobulin...