205 related articles for article (PubMed ID: 17711304)
1. Characterization of the interaction of two peptides from the N terminus of the NHR domain of HIV-1 gp41 with phospholipid membranes.
Moreno MR; Guillén J; Pérez-Berna AJ; Amorós D; Gómez AI; Bernabeu A; Villalaín J
Biochemistry; 2007 Sep; 46(37):10572-84. PubMed ID: 17711304
[TBL] [Abstract][Full Text] [Related]
2. Functional and structural characterization of HIV-1 gp41 ectodomain regions in phospholipid membranes suggests that the fusion-active conformation is extended.
Korazim O; Sackett K; Shai Y
J Mol Biol; 2006 Dec; 364(5):1103-17. PubMed ID: 17045292
[TBL] [Abstract][Full Text] [Related]
3. Conformational stability and membrane interaction of the full-length ectodomain of HIV-1 gp41: implication for mode of action.
Lev N; Fridmann-Sirkis Y; Blank L; Bitler A; Epand RF; Epand RM; Shai Y
Biochemistry; 2009 Apr; 48(14):3166-75. PubMed ID: 19206186
[TBL] [Abstract][Full Text] [Related]
4. The role of the N-terminal heptad repeat of HIV-1 in the actual lipid mixing step as revealed by its substitution with distant coiled coils.
Wexler-Cohen Y; Sackett K; Shai Y
Biochemistry; 2005 Apr; 44(15):5853-61. PubMed ID: 15823044
[TBL] [Abstract][Full Text] [Related]
5. Interaction of a peptide derived from the N-heptad repeat region of gp41 Env ectodomain with model membranes. Modulation of phospholipid phase behavior.
Pascual R; Contreras M; Fedorov A; Prieto M; Villalaín J
Biochemistry; 2005 Nov; 44(43):14275-88. PubMed ID: 16245944
[TBL] [Abstract][Full Text] [Related]
6. Effect of nonpolar substitutions of the conserved Phe11 in the fusion peptide of HIV-1 gp41 on its function, structure, and organization in membranes.
Pritsker M; Rucker J; Hoffman TL; Doms RW; Shai Y
Biochemistry; 1999 Aug; 38(35):11359-71. PubMed ID: 10471286
[TBL] [Abstract][Full Text] [Related]
7. Interaction of a peptide from the pre-transmembrane domain of the severe acute respiratory syndrome coronavirus spike protein with phospholipid membranes.
Guillén J; Moreno MR; Pérez-Berna AJ; Bernabeu A; Villalaín J
J Phys Chem B; 2007 Dec; 111(49):13714-25. PubMed ID: 18020324
[TBL] [Abstract][Full Text] [Related]
8. Fatty acids can substitute the HIV fusion peptide in lipid merging and fusion: an analogy between viral and palmitoylated eukaryotic fusion proteins.
Lev N; Shai Y
J Mol Biol; 2007 Nov; 374(1):220-30. PubMed ID: 17919659
[TBL] [Abstract][Full Text] [Related]
9. Role of the fusion peptide and membrane-proximal domain in HIV-1 envelope glycoprotein-mediated membrane fusion.
Dimitrov AS; Rawat SS; Jiang S; Blumenthal R
Biochemistry; 2003 Dec; 42(48):14150-8. PubMed ID: 14640682
[TBL] [Abstract][Full Text] [Related]
10. The hydrophobic pocket contributes to the structural stability of the N-terminal coiled coil of HIV gp41 but is not required for six-helix bundle formation.
Dwyer JJ; Hasan A; Wilson KL; White JM; Matthews TJ; Delmedico MK
Biochemistry; 2003 May; 42(17):4945-53. PubMed ID: 12718536
[TBL] [Abstract][Full Text] [Related]
11. Development of a FRET assay for monitoring of HIV gp41 core disruption.
Xu Y; Hixon MS; Dawson PE; Janda KD
J Org Chem; 2007 Aug; 72(18):6700-7. PubMed ID: 17685571
[TBL] [Abstract][Full Text] [Related]
12. Identification of the HIV-1 gp41 core-binding motif--HXXNPF.
Huang JH; Liu ZQ; Liu S; Jiang S; Chen YH
FEBS Lett; 2006 Sep; 580(20):4807-14. PubMed ID: 16904109
[TBL] [Abstract][Full Text] [Related]
13. Interaction of fusion peptides from HIV gp41 with membranes: a time-resolved membrane binding, lipid mixing, and structural study.
Buzón V; Padrós E; Cladera J
Biochemistry; 2005 Oct; 44(40):13354-64. PubMed ID: 16201760
[TBL] [Abstract][Full Text] [Related]
14. A salt bridge between an N-terminal coiled coil of gp41 and an antiviral agent targeted to the gp41 core is important for anti-HIV-1 activity.
Jiang S; Debnath AK
Biochem Biophys Res Commun; 2000 Apr; 270(1):153-7. PubMed ID: 10733920
[TBL] [Abstract][Full Text] [Related]
15. Membrane-induced conformational change during the activation of HIV-1 gp41.
Kliger Y; Peisajovich SG; Blumenthal R; Shai Y
J Mol Biol; 2000 Aug; 301(4):905-14. PubMed ID: 10966795
[TBL] [Abstract][Full Text] [Related]
16. Biophysical characterization and membrane interaction of the most membranotropic region of the HIV-1 gp41 endodomain.
Moreno MR; Pérez-Berná AJ; Guillén J; Villalaín J
Biochim Biophys Acta; 2008 May; 1778(5):1298-307. PubMed ID: 18230333
[TBL] [Abstract][Full Text] [Related]
17. A template-assembled model of the N-peptide helix bundle from HIV-1 Gp-41 with high affinity for C-peptide.
Xu W; Taylor JW
Chem Biol Drug Des; 2007 Oct; 70(4):319-28. PubMed ID: 17937777
[TBL] [Abstract][Full Text] [Related]
18. The Tryptophan-Rich Motif of HIV-1 gp41 Can Interact with the N-Terminal Deep Pocket Site: New Insights into the Structure and Function of gp41 and Its Inhibitors.
Zhu Y; Ding X; Yu D; Chong H; He Y
J Virol; 2019 Dec; 94(1):. PubMed ID: 31619552
[TBL] [Abstract][Full Text] [Related]
19. 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; 329(2):319-27. PubMed ID: 15518811
[TBL] [Abstract][Full Text] [Related]
20. Characterization of the interacting domain of the HIV-1 fusion peptide with the transmembrane domain of the T-cell receptor.
Cohen T; Pevsner-Fischer M; Cohen N; Cohen IR; Shai Y
Biochemistry; 2008 Apr; 47(16):4826-33. PubMed ID: 18376816
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
