Peptides Trap the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Fusion Intermediate at Two Sites
Author:
Affiliation:
1. Center for Biologics Evaluation and Research, Food and Drug Administration
2. National Institute for Arthritis and Musculoskeletal Diseases, National Institutes of Health, Bethesda, Maryland 20892
Abstract
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/JVI.77.3.1666-1671.2003
Reference28 articles.
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2. Bewley C. A. J. M. Louis R. Ghirlando and G. M. Clore. 2002. Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41. J. Biol. Chem.
3. Caffrey, M., M. Cai, J. Kaufman, S. J. Stahl, P. T. Wingfield, D. G. Covell, A. M. Gronenborn, and G. M. Clore. 1998. Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41. EMBO J. 17 : 4572-4584.
4. Caffrey, M., J. Kaufman, S. Stahl, P. Wingfield, A. M. Gronenborn, and G. M. Clore. 1999. Monomer-trimer equilibrium of the ectodomain of SIV gp41: insight into the mechanism of peptide inhibition of HIV infection. Protein Sci. 8 : 1904-1907.
5. Calderone, T. L., R. D. Stevens, and T. G. Oas. 1996. High-level misincorporation of lysine for arginine at AGA codons in a fusion protein expressed in Escherichia coli. J. Mol. Biol. 262 : 407-412.
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