Warner-lambert Company

Donald John Hupe

Linda Lea Johnson

Qi-Zhuang Ye

Andrew David White

Joseph Armand Picard

John C Hodges

Gary Louis Bolton

Francis John Tinney

Claude Forsey Purchase, Jr

Daniel Fred Ortwine

Daniele Marie Leonard

Alfred Campbell

Tomi Sawyer

Vijaykumar M Baragi

Judith Sebolt-Leopold

Joan A Keiser

Richard Gowan

A process for the production of the catalytic domain, without propeptide, of a matrix metalloproteinase is described which comprises culturing transformed host cells carrying a DNA sequence encoding the catalytic domain as well as a method for screening for inhibitors of a matrix metalloproteinase; a method for determining the 3-dimensional structure of the catalytic domain of a matrix metalloproteinase; and pharmaceutical compositions of human stromelysin catalytic domain protein which are useful in treating herniated vertebral discs, dermal ulcers, modifying scar tissue formation, and joint diseases.

Process for the production of stromelysin catalytic domain protein

Aromatic keto-acids and their derivatives as inhibitors of matrix

Tricyclic compounds are described as well as methods for the preparation and pharmaceutical compositions of same, which are useful as inhibitors of matrix metalloproteinases, particularly gelatinase A (72 kD gelatinase) and stromelysin-1 and for the treatment of multiple sclerosis, atherosclerotic plaque rupture, aortic aneurism, heart failure, restenosis, periodontal disease, corneal ulceration, cancer metastasis, tumor angiogenesis, arthritis, or other autoimmune or inflammatory disorders dependent upon tissue invasion by leukocytes.

Tricyclic inhibitors of matrix metalloproteinases

Inhibitors of protein:farnesyl transferase enzyme are described, as well as methods for the preparation and pharmaceutical compositions of the same, which are useful in controlling tissue proliferative diseases, including cancer and restenosis.

Substituted tetra- and pentapeptide inhibitors of protein: farnesyl

Tricyclic compounds are described as well as methods for the preparation and pharmaceutical compositions of same, which are useful as inhibitors of matrix metalloproteinases, particularly gelatinase A (72 kD gelatinase) and stromelysin-1 and for the treatment of multiple sclerosis, atherosclerotic plaque rupture, aortic aneurism, heart failure, restenosis, periodontal disease, corneal ulceration, cancer metastasis, tumor angionenesis, arthritis, or other autoimmune or inflammatory disorders dependent upon tissue invasion by leukocytes.

A process for the production of the catalytic domain, without propeptide, C-terminal domain, and the fibronectin-like insert, of human gelatinases is described which comprises culturing transformed E. coli host cells carrying a synthetic DNA sequence encoding the catalytic domain as well as a method for screening for inhibitors of a gelatinase; a method for determining the 3-dimensional structure of the catalytic domain of a gelatinase; and pharmaceutical compositions of human gelatinase catalytic domain protein which are useful in treating herniated vertebral discs, dermal ulcers, modifying scar tissue formation, and joint diseases.

Process for the production of gelatinase catalytic domain protein

A tricyclic compound is described as well as pharmaceutical compositions of same, which is useful as an inhibitor of matrix metalloproteinases, particularly gelatinase A (72 kD gelatinase) for the treatment of multiple sclerosis or other autoimmune or inflammatory disorders dependent upon tissue invasion by leukocytes.

Tricyclic inhibitor of matrix metalloproteinases

Polyamines inhibit vascular smooth muscle proliferation and thus are useful in treating and preventing vascular proliferative disorders such as restenosis following balloon angioplasty.

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Ann Arbor, MI, United States of America

Donald John Hupe