Abstract |
A newly-constructed antibody-like molecule containing the gp120-binding domain of the receptor for human immunodeficiency virus blocks HIV-1 infection of T cells and monocytes. Its long plasma half-life, other antibody-like properties, and potential to block all HIV isolates, make it a good candidate for therapeutic use.
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Authors | D J Capon, S M Chamow, J Mordenti, S A Marsters, T Gregory, H Mitsuya, R A Byrn, C Lucas, F M Wurm, J E Groopman |
Journal | Nature
(Nature)
Vol. 337
Issue 6207
Pg. 525-31
(Feb 09 1989)
ISSN: 0028-0836 [Print] England |
PMID | 2536900
(Publication Type: Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Adjuvants, Immunologic
- Antigens, Surface
- Cell Adhesion Molecules
- HIV Envelope Protein gp120
- Immunoglobulin G
- Receptors, Complement
- Receptors, Fc
- Receptors, HIV
- Receptors, Virus
- Retroviridae Proteins
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Topics |
- Acquired Immunodeficiency Syndrome
(immunology, metabolism, therapy)
- Adjuvants, Immunologic
(chemical synthesis, metabolism, pharmacokinetics)
- Animals
- Antigens, Surface
(administration & dosage, chemical synthesis, immunology)
- Binding Sites, Antibody
- Binding, Competitive
- Cell Adhesion Molecules
- Cell Line
- Drug Design
- HIV Envelope Protein gp120
- Half-Life
- Humans
- Immunoglobulin G
(administration & dosage, metabolism)
- Mice
- Rabbits
- Receptors, Complement
(analysis)
- Receptors, Fc
(analysis)
- Receptors, HIV
- Receptors, Virus
(administration & dosage, immunology)
- Retroviridae Proteins
(metabolism)
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