Structure−Activity Relationships of Boronic Acid Inhibitors of Dipeptidyl Peptidase IV. 1. Variation of the P2 Position of Xaa-boroPro Dipeptides

Author:

Coutts Simon J.1,Kelly Terence A.1,Snow Roger J.1,Kennedy Charles A.1,Barton Randall W.1,Adams Julian1,Krolikowski Dale A.1,Freeman Dorothy M.1,Campbell Scot J.1,Ksiazek John F.1,Bachovchin William W.1

Affiliation:

1. Research and Development Center, Boehringer Ingelheim Pharmaceuticals Inc., 900 Ridgebury Road, P.O. Box 368, Ridgefield, Connecticut 06877, and Department of Biochemistry, Tufts University School of Medicine, 136 Harrison Avenue, Boston, Massachusetts 02111

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Reference38 articles.

1. For general reviews on DPP IV, see:  (a)Dipeptidyl Peptidase IV−General and Applied Aspects; Barth, A., Schowen, R. L., Eds.; Institüt für Pharmakologische Forschung:  Berlin, 1990; Vol. 38.

2. (b) McDonald, J. K.; Barrett, A. J.Mammalian Proteases:  a Glossary and Bibliography; Academic Press:  London, 1986; Vol. 2, pp 132−144.

3. The role of dipeptidyl peptidase IV in human T lymphocyte activation. Inhibitors and antibodies against dipeptidyl peptidase IV suppress lymphocyte proliferation and immunoglobulin synthesisin vitro

4. Dipeptidyl Peptidase IV in Human T Lymphocytes.

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