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Items: 1 to 20 of 78

1.

Reorientation of the helix of the tryptophan-rich gp41W peptide from HIV-1 at interfaces.

Matar G, Benichou E, Nasir MN, El Harfouch Y, Brevet PF, Besson F.

J Chem Phys. 2013 Dec 14;139(22):225105. doi: 10.1063/1.4841795.

PMID:
24329097
2.

Interfacial properties and structure stability of the gp41 tryptophan-rich peptide from HIV-1.

Matar G, Nasir MN, Besson F.

J Colloid Interface Sci. 2010 Dec 15;352(2):520-5. doi: 10.1016/j.jcis.2010.08.075. Epub 2010 Sep 17.

PMID:
20850757
3.

Influence of the lipid composition of biomimetic monolayers on the structure and orientation of the gp41 tryptophan-rich peptide from HIV-1.

Matar G, Besson F.

Biochim Biophys Acta. 2011 Oct;1808(10):2534-43. doi: 10.1016/j.bbamem.2011.06.003. Epub 2011 Jun 13.

4.
8.

Interhelical interactions in the gp41 core: implications for activation of HIV-1 membrane fusion.

Wang S, York J, Shu W, Stoller MO, Nunberg JH, Lu M.

Biochemistry. 2002 Jun 11;41(23):7283-92.

PMID:
12044159
9.
11.

The tryptophan-rich region of HIV gp41 and the promotion of cholesterol-rich domains.

Epand RF, Sayer BG, Epand RM.

Biochemistry. 2005 Apr 12;44(14):5525-31.

PMID:
15807546
12.

Protein design of a bacterially expressed HIV-1 gp41 fusion inhibitor.

Deng Y, Zheng Q, Ketas TJ, Moore JP, Lu M.

Biochemistry. 2007 Apr 10;46(14):4360-9. Epub 2007 Mar 20.

PMID:
17371053
13.

Structure of a fusion peptide analogue at the air-water interface, determined from surface activity, infrared spectroscopy and scanning force microscopy.

Taylor SE, Desbat B, Blaudez D, Jacobi S, Chi LF, Fuchs H, Schwarz G.

Biophys Chem. 2000 Sep 15;87(1):63-72.

PMID:
11036970
14.

A monomeric 3(10)-helix is formed in water by a 13-residue peptide representing the neutralizing determinant of HIV-1 on gp41.

Biron Z, Khare S, Samson AO, Hayek Y, Naider F, Anglister J.

Biochemistry. 2002 Oct 22;41(42):12687-96.

PMID:
12379111
15.

Identification of a human protein-derived HIV-1 fusion inhibitor targeting the gp41 fusion core structure.

Chao L, Lu L, Yang H, Zhu Y, Li Y, Wang Q, Yu X, Jiang S, Chen YH.

PLoS One. 2013 May 31;8(5):e66156. doi: 10.1371/journal.pone.0066156. Print 2013.

16.

Conserved residues in the coiled-coil pocket of human immunodeficiency virus type 1 gp41 are essential for viral replication and interhelical interaction.

Mo H, Konstantinidis AK, Stewart KD, Dekhtyar T, Ng T, Swift K, Matayoshi ED, Kati W, Kohlbrenner W, Molla A.

Virology. 2004 Nov 24;329(2):319-27.

18.
19.

Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection.

Wild CT, Shugars DC, Greenwell TK, McDanal CB, Matthews TJ.

Proc Natl Acad Sci U S A. 1994 Oct 11;91(21):9770-4.

20.

The LLSGIV stretch of the N-terminal region of HIV-1 gp41 is critical for binding to a model peptide, T20.

Trivedi VD, Cheng SF, Wu CW, Karthikeyan R, Chen CJ, Chang DK.

Protein Eng. 2003 Apr;16(4):311-7.

PMID:
12736375

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