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Synthetic peptides and anti-peptide antibodies as probes to study interdomain interactions involved in virus assembly: the envelope of the human immunodeficiency virus (HIV-1).
Neurath AR, Strick N, Jiang S. Neurath AR, et al. Among authors: strick n. Virology. 1992 May;188(1):1-13. doi: 10.1016/0042-6822(92)90729-9. Virology. 1992. PMID: 1373549
Identification of N-phenyl-N'-(2,2,6,6-tetramethyl-piperidin-4-yl)-oxalamides as a new class of HIV-1 entry inhibitors that prevent gp120 binding to CD4.
Zhao Q, Ma L, Jiang S, Lu H, Liu S, He Y, Strick N, Neamati N, Debnath AK. Zhao Q, et al. Among authors: strick n. Virology. 2005 Sep 1;339(2):213-25. doi: 10.1016/j.virol.2005.06.008. Virology. 2005. PMID: 15996703 Free article.
Anti-HIV-1 activity of cellulose acetate phthalate: synergy with soluble CD4 and induction of "dead-end" gp41 six-helix bundles.
Neurath AR, Strick N, Jiang S, Li YY, Debnath AK. Neurath AR, et al. Among authors: strick n. BMC Infect Dis. 2002 Apr 30;2:6. doi: 10.1186/1471-2334-2-6. BMC Infect Dis. 2002. PMID: 11983022 Free PMC article.
Anti-HIV-1 activity of anionic polymers: a comparative study of candidate microbicides.
Neurath AR, Strick N, Li YY. Neurath AR, et al. Among authors: strick n. BMC Infect Dis. 2002 Nov 21;2:27. doi: 10.1186/1471-2334-2-27. Epub 2002 Nov 21. BMC Infect Dis. 2002. PMID: 12445331 Free PMC article.
3-Hydroxyphthaloyl beta-lactoglobulin. III. Antiviral activity against herpesviruses.
Neurath AR, Strick N, Li YY. Neurath AR, et al. Among authors: strick n. Antivir Chem Chemother. 1998 Mar;9(2):177-84. doi: 10.1177/095632029800900209. Antivir Chem Chemother. 1998. PMID: 9875389
Cellulose acetate phthalate, a common pharmaceutical excipient, inactivates HIV-1 and blocks the coreceptor binding site on the virus envelope glycoprotein gp120.
Neurath AR, Strick N, Li YY, Debnath AK. Neurath AR, et al. Among authors: strick n. BMC Infect Dis. 2001;1:17. doi: 10.1186/1471-2334-1-17. Epub 2001 Sep 25. BMC Infect Dis. 2001. PMID: 11602021 Free PMC article.
Inhibition of HIV-1 infection by a fusion domain binding peptide from the HIV-1 envelope glycoprotein GP41.
Jiang S, Lin K, Strick N, Neurath AR. Jiang S, et al. Among authors: strick n. Biochem Biophys Res Commun. 1993 Sep 15;195(2):533-8. doi: 10.1006/bbrc.1993.2078. Biochem Biophys Res Commun. 1993. PMID: 8373393
The peptide (637-666) selectively binds to the fusion domain at the N-terminus of gp41, suggesting that inhibition of HIV-1 infection is caused by blocking fusion of HIV-1 with cells or of infected cells with uninfected cells. ...
The peptide (637-666) selectively binds to the fusion domain at the N-terminus of gp41, suggesting that inhibition of HIV-1 infection …
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