Design of orally active, non-peptide fibrinogen receptor antagonists. An evolutionary process from the RGD sequence to novel anti-platelet aggregation agents-Reference-Cited by-同舟云学术

Design of orally active, non-peptide fibrinogen receptor antagonists. An evolutionary process from the RGD sequence to novel anti-platelet aggregation agents

Published:1994-09 Issue:9 Volume:2 Page:881-895
ISSN:0968-0896
Container-title:Bioorganic & Medicinal Chemistry
language:en
Short-container-title:Bioorganic & Medicinal Chemistry

Author:

Bovy P.R.,Tjoeng F.S.,Rico J.G.,Rogers T.E.,Lindmark R.J.,Zablocki J.A.,Garland R.B.,McMackins D.E.,Dayringer H.,Tóth M.V.,Zupec M.E.,Rao S.,Panzer-Knodle S.G.,Nicholson N.S.,Salyers A.,Taite B.B.,Herin M.,Miyano M.,Feigen L.P.,Adams S.P.

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry

Reference31 articles.

1. The platelet membrane glycoprotein IIb-IIIa complex

2. Arginyl-glycyl-aspartic acid sequences and fibrinogen binding to platelets

3. Amino Acid Sequences in Fibrinogen Mediating Its Interaction with Its Platelet Receptor, GPIIbIIIa

4. Potent inhibitors of platelet aggregation based upon the Arg-Gly-Asp-Phe sequence of fibrinogen. A proposal on the nature of the binding interaction between the Asp-carboxylate of RGDX mimetics and the platelet GP IIb-IIIa receptor

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