The discovery of sulfonylated dipeptides as Potent VLA-4 antagonists-Reference-Cited by-同舟云学术

The discovery of sulfonylated dipeptides as Potent VLA-4 antagonists

Published:2001-10 Issue:20 Volume:11 Page:2709-2713
ISSN:0960-894X
Container-title:Bioorganic & Medicinal Chemistry Letters
language:en
Short-container-title:Bioorganic & Medicinal Chemistry Letters

Author:

Hagmann William K,Durette Philippe L,Lanza Thomas,Kevin Nancy Jo,de Laszlo Stephen E,Kopka Ihor E,Young David,Magriotis Plato A,Li Bing,Lin Linus S,Yang Ginger,Kamenecka Theodore,Chang Linda L,Wilson Jonathan,MacCoss Malcolm,Mills Sander G,Van Riper Gail,McCauley Ermengilda,Egger Linda A,Kidambi Usha,Lyons Kathryn,Vincent Stella,Stearns Ralph,Colletti Adria,Teffera Johannes,Tong Sharon,Fenyk-Melody Judy,Owens Karen,Levorse Dorothy,Kim Philip,Schmidt John A,Mumford Richard A

Publisher

Elsevier BV

Subject

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

Reference13 articles.

1. Structure of the Integrin VLA-4 and its Cell-Cell and Cell-Matrix Adhesion Functions

2. The crystal structure of an N-terminal two-domain fragment of vascular cell adhesion molecule 1 (VCAM-1): a cyclic peptide based on the domain 1 C-D loop can inhibit VCAM-1-alpha 4 integrin interaction.

3. The minimal essential sequence for a major cell type-specific adhesion site (CS1) within the alternatively spliced type III connecting segment domain of fibronectin is leucine-aspartic acid-valine

4. Adams, S. P.; Lobb, R. R. In Ann. Rep. Med. Chem.; Doherty, A. M., Ed.; Academic: New York, 1999; Vol. 34, p 179.

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