Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
2R01AI030411-06A2
Application #
2065607
Study Section
AIDS and Related Research Study Section 3 (ARRC)
Project Start
1990-09-30
Project End
2000-02-29
Budget Start
1996-03-01
Budget End
1997-02-28
Support Year
6
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Duke University
Department
Surgery
Type
Schools of Medicine
DUNS #
071723621
City
Durham
State
NC
Country
United States
Zip Code
27705
Chen, C H; Greenberg, M L; Bolognesi, D P et al. (2000) Monoclonal antibodies that bind to the core of fusion-active glycoprotein 41. AIDS Res Hum Retroviruses 16:2037-41
Rovinski, B; Dekaban, G A; Cao, S X et al. (1999) Engineering of noninfectious HIV-1-like particles containing mutant gp41 glycoproteins as vaccine candidates that allow vaccinees to be distinguished from HIV-1 infectees. Virology 257:438-48
Rimsky, L T; Shugars, D C; Matthews, T J (1998) Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J Virol 72:986-93
Shugars, D C; Wild, C T; Greenwell, T K et al. (1996) Biophysical characterization of recombinant proteins expressing the leucine zipper-like domain of the human immunodeficiency virus type 1 transmembrane protein gp41. J Virol 70:2982-91
Wild, C; Greenwell, T; Shugars, D et al. (1995) The inhibitory activity of an HIV type 1 peptide correlates with its ability to interact with a leucine zipper structure. AIDS Res Hum Retroviruses 11:323-5
Rovinski, B; Rodrigues, L; Cao, S X et al. (1995) Induction of HIV type 1 neutralizing and env-CD4 blocking antibodies by immunization with genetically engineered HIV type 1-like particles containing unprocessed gp160 glycoproteins. AIDS Res Hum Retroviruses 11:1187-95
Chen, C H; Matthews, T J; McDanal, C B et al. (1995) A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: implication for viral fusion. J Virol 69:3771-7
Wild, C; Dubay, J W; Greenwell, T et al. (1994) Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex. Proc Natl Acad Sci U S A 91:12676-80
Wild, C T; Shugars, D C; Greenwell, T K et al. (1994) Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc Natl Acad Sci U S A 91:9770-4
Matthews, T J; Wild, C; Chen, C H et al. (1994) Structural rearrangements in the transmembrane glycoprotein after receptor binding. Immunol Rev 140:93-104

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