Correlation of β-bend conformations of tetrapeptides with their activities in CD4-receptor binding assays
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1989.tb01582.x/fullpdf
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1. Octapeptides deduced from the neuropeptide receptor-like pattern of antigen T4 in brain potently inhibit human immunodeficiency virus receptor binding and T-cell infectivity.
2. CD4 receptor binding peptides that block HIV infectivity cause human monocyte chemotaxis
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4. A strong homology exists between the active T-cell binding gp120 octapeptide of human immunodeficiency virus and the subtilisin cleavage peptide of bovine ribonuclease A
5. Comparative X-ray crystallographic evidence for a ?-bend conformation as the active structure for peptide T in T4 receptor recognition
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