Robin V. Ward
Pfizer (United Kingdom)(GB)
Publications by Year
Research Areas
Protease and Inhibitor Mechanisms, Alzheimer's disease research and treatments, Peptidase Inhibition and Analysis, Computational Drug Discovery Methods, Blood Coagulation and Thrombosis Mechanisms
Most-Cited Works
- → Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP)(1991)452 cited
- → Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response(2000)272 cited
- → The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases(1992)266 cited
- → Intermolecular Autolytic Cleavage Can Contribute to the Activation of Progelatinase A by Cell Membranes(1995)244 cited
- → Tissue inhibitor of metalloproteinases-2 inhibits the activation of 72 kDa progelatinase by fibroblast membranes(1991)199 cited
- → The purification of tissue inhibitor of metalloproteinases-2 from its 72 kDa progelatinase complex. Demonstration of the biochemical similarities of tissue inhibitor of metalloproteinases-2 and tissue inhibitor of metalloproteinases-1(1991)165 cited
- → Fractionation and characterization of oligomeric, protofibrillar and fibrillar forms of β-amyloid peptide(2000)150 cited
- → Gingival fibroblasts degrade type I collagen films when stimulated with tumor necrosis factor and interleukin 1: Evidence that breakdown is mediated by metal loproteinases(1989)148 cited
- Common structural features determine the effectiveness of carvedilol, daunomycin and rolitetracycline as inhibitors of Alzheimer beta-amyloid fibril formation.(1999)
- → Cell surface-mediated activation of progelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts(1994)88 cited