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Items: 1 to 20 of 153


ADS-J1 inhibits HIV-1 infection and membrane fusion by targeting the highly conserved pocket in the gp41 NHR-trimer.

Yu F, Lu L, Liu Q, Yu X, Wang L, He E, Zou P, Du L, Sanders RW, Liu S, Jiang S.

Biochim Biophys Acta. 2014 May;1838(5):1296-305. doi: 10.1016/j.bbamem.2013.12.022. Epub 2014 Jan 3.


HIV-1 variants with a single-point mutation in the gp41 pocket region exhibiting different susceptibility to HIV fusion inhibitors with pocket- or membrane-binding domain.

Lu L, Tong P, Yu X, Pan C, Zou P, Chen YH, Jiang S.

Biochim Biophys Acta. 2012 Dec;1818(12):2950-7. doi: 10.1016/j.bbamem.2012.07.020. Epub 2012 Jul 31.


ADS-J1 inhibits human immunodeficiency virus type 1 entry by interacting with the gp41 pocket region and blocking fusion-active gp41 core formation.

Wang H, Qi Z, Guo A, Mao Q, Lu H, An X, Xia C, Li X, Debnath AK, Wu S, Liu S, Jiang S.

Antimicrob Agents Chemother. 2009 Dec;53(12):4987-98. doi: 10.1128/AAC.00670-09. Epub 2009 Sep 28.


Peptide and non-peptide HIV fusion inhibitors.

Jiang S, Zhao Q, Debnath AK.

Curr Pharm Des. 2002;8(8):563-80. Review.


Identification of a critical motif for the human immunodeficiency virus type 1 (HIV-1) gp41 core structure: implications for designing novel anti-HIV fusion inhibitors.

He Y, Cheng J, Li J, Qi Z, Lu H, Dong M, Jiang S, Dai Q.

J Virol. 2008 Jul;82(13):6349-58. doi: 10.1128/JVI.00319-08. Epub 2008 Apr 16.


Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors.

Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.

J Virol. 2016 Dec 16;91(1). pii: e01445-16. Print 2017 Jan 1.


Mutations of Gln64 in the HIV-1 gp41 N-terminal heptad repeat render viruses resistant to peptide HIV fusion inhibitors targeting the gp41 pocket.

Yu X, Lu L, Cai L, Tong P, Tan S, Zou P, Meng F, Chen YH, Jiang S.

J Virol. 2012 Jan;86(1):589-93. doi: 10.1128/JVI.05066-11. Epub 2011 Oct 19.


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.


HIV gp41 C-terminal heptad repeat contains multifunctional domains. Relation to mechanisms of action of anti-HIV peptides.

Liu S, Jing W, Cheung B, Lu H, Sun J, Yan X, Niu J, Farmar J, Wu S, Jiang S.

J Biol Chem. 2007 Mar 30;282(13):9612-20. Epub 2007 Feb 2.


Membrane-anchored HIV-1 N-heptad repeat peptides are highly potent cell fusion inhibitors via an altered mode of action.

Wexler-Cohen Y, Shai Y.

PLoS Pathog. 2009 Jul;5(7):e1000509. doi: 10.1371/journal.ppat.1000509. Epub 2009 Jul 10.


Hydrophobic mutations in buried polar residues enhance HIV-1 gp41 N-terminal heptad repeat-C-terminal heptad repeat interactions and C-peptides' anti-HIV activity.

Zheng B, Wang K, Lu L, Yu F, Cheng M, Jiang S, Liu K, Cai L.

AIDS. 2014 Jun 1;28(9):1251-60. doi: 10.1097/QAD.0000000000000255.


Conserved residue Lys574 in the cavity of HIV-1 Gp41 coiled-coil domain is critical for six-helix bundle stability and virus entry.

He Y, Liu S, Jing W, Lu H, Cai D, Chin DJ, Debnath AK, Kirchhoff F, Jiang S.

J Biol Chem. 2007 Aug 31;282(35):25631-9. Epub 2007 Jul 6.


The stability of the intact envelope glycoproteins is a major determinant of sensitivity of HIV/SIV to peptidic fusion inhibitors.

Gallo SA, Sackett K, Rawat SS, Shai Y, Blumenthal R.

J Mol Biol. 2004 Jun 25;340(1):9-14.


Multimerized CHR-derived peptides as HIV-1 fusion inhibitors.

Nomura W, Hashimoto C, Suzuki T, Ohashi N, Fujino M, Murakami T, Yamamoto N, Tamamura H.

Bioorg Med Chem. 2013 Aug 1;21(15):4452-8. doi: 10.1016/j.bmc.2013.05.060. Epub 2013 Jun 5.


Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain.

Wexler-Cohen Y, Ashkenazi A, Viard M, Blumenthal R, Shai Y.

FASEB J. 2010 Nov;24(11):4196-202. doi: 10.1096/fj.09-151704. Epub 2010 Jul 6.


Molecular dynamics studies of the inhibitor C34 binding to the wild-type and mutant HIV-1 gp41: inhibitory and drug resistant mechanism.

Ma X, Tan J, Su M, Li C, Zhang X, Wang C.

PLoS One. 2014 Nov 13;9(11):e111923. doi: 10.1371/journal.pone.0111923. eCollection 2014.


Genetic Pathway of HIV-1 Resistance to Novel Fusion Inhibitors Targeting the Gp41 Pocket.

Su Y, Chong H, Xiong S, Qiao Y, Qiu Z, He Y.

J Virol. 2015 Dec;89(24):12467-79. doi: 10.1128/JVI.01741-15. Epub 2015 Oct 7.


ADS-J1 inhibits HIV-1 entry by interacting with gp120 and does not block fusion-active gp41 core formation.

González-Ortega E, Mena MP, Permanyer M, Ballana E, Clotet B, Esté JA.

Antimicrob Agents Chemother. 2010 Oct;54(10):4487-92. doi: 10.1128/AAC.00359-10. Epub 2010 Jul 19.


HIV entry inhibitors targeting gp41: from polypeptides to small-molecule compounds.

Liu S, Wu S, Jiang S.

Curr Pharm Des. 2007;13(2):143-62. Review.


Covalent fusion inhibitors targeting HIV-1 gp41 deep pocket.

Bai Y, Xue H, Wang K, Cai L, Qiu J, Bi S, Lai L, Cheng M, Liu S, Liu K.

Amino Acids. 2013 Feb;44(2):701-13. doi: 10.1007/s00726-012-1394-8. Epub 2012 Sep 9.


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