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Items: 1 to 20 of 132

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Self-assembly molecular dynamics simulations shed light into the interaction of the influenza fusion Peptide with a membrane bilayer.

Victor BL, Lousa D, Antunes JM, Soares CM.

J Chem Inf Model. 2015 Apr 27;55(4):795-805. doi: 10.1021/ci500756v. Epub 2015 Apr 13.

PMID:
25826469
5.

Relationship between the infectivity of influenza virus and the ability of its fusion peptide to perturb bilayers.

Epand RM, Epand RF.

Biochem Biophys Res Commun. 1994 Aug 15;202(3):1420-5.

PMID:
8060322
6.

Single mutation effects on conformational change and membrane deformation of influenza hemagglutinin fusion peptides.

Li J, Das P, Zhou R.

J Phys Chem B. 2010 Jul 8;114(26):8799-806. doi: 10.1021/jp1029163.

PMID:
20552971
7.

Conformational sampling of influenza fusion peptide in membrane bilayers as a function of termini and protonation states.

Panahi A, Feig M.

J Phys Chem B. 2010 Jan 28;114(3):1407-16. doi: 10.1021/jp907366g.

PMID:
20043654
9.

Micelle-bound conformation of a hairpin-forming peptide: combined NMR and molecular dynamics study.

Dixon AM, Venable RM, Pastor RW, Bull TE.

Biopolymers. 2002 Nov 15;65(4):284-98.

PMID:
12382289
10.

H+-induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino-terminal fusion peptide but not the coiled coil region.

Durrer P, Galli C, Hoenke S, Corti C, Glück R, Vorherr T, Brunner J.

J Biol Chem. 1996 Jun 7;271(23):13417-21.

11.

Design and function of a conformationally restricted analog of the influenza virus fusion peptide.

Bertocco A, Formaggio F, Toniolo C, Broxterman QB, Epand RF, Epand RM.

J Pept Res. 2003 Jul;62(1):19-26.

PMID:
12787447
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Configuration of influenza hemagglutinin fusion peptide monomers and oligomers in membranes.

Sammalkorpi M, Lazaridis T.

Biochim Biophys Acta. 2007 Jan;1768(1):30-8. Epub 2006 Aug 22.

14.

Fusion peptide from influenza hemagglutinin increases membrane surface order: an electron-spin resonance study.

Ge M, Freed JH.

Biophys J. 2009 Jun 17;96(12):4925-34. doi: 10.1016/j.bpj.2009.04.015.

15.

Effect of lipid composition on the "membrane response" induced by a fusion peptide.

Volynsky PE, Polyansky AA, Simakov NA, Arseniev AS, Efremov RG.

Biochemistry. 2005 Nov 8;44(44):14626-37.

PMID:
16262262
16.

Interaction of the Dengue virus fusion peptide with membranes assessed by NMR: The essential role of the envelope protein Trp101 for membrane fusion.

Melo MN, Sousa FJ, Carneiro FA, Castanho MA, Valente AP, Almeida FC, Da Poian AT, Mohana-Borges R.

J Mol Biol. 2009 Sep 25;392(3):736-46. doi: 10.1016/j.jmb.2009.07.035. Epub 2009 Jul 17.

PMID:
19619560
17.

Structure-dependent charge density as a determinant of antimicrobial activity of peptide analogues of defensin.

Bai Y, Liu S, Jiang P, Zhou L, Li J, Tang C, Verma C, Mu Y, Beuerman RW, Pervushin K.

Biochemistry. 2009 Aug 4;48(30):7229-39. doi: 10.1021/bi900670d.

PMID:
19580334
18.

The SIV tilted peptide induces cylindrical reverse micelles in supported lipid bilayers.

El Kirat K, Dufrêne YF, Lins L, Brasseur R.

Biochemistry. 2006 Aug 1;45(30):9336-41.

PMID:
16866380
19.

Structural intermediates in influenza haemagglutinin-mediated fusion.

Chernomordik LV, Leikina E, Kozlov MM, Frolov VA, Zimmerberg J.

Mol Membr Biol. 1999 Jan-Mar;16(1):33-42. Review.

PMID:
10332735
20.

Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts.

Freitas MS, Gaspar LP, Lorenzoni M, Almeida FC, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL.

J Biol Chem. 2007 Sep 14;282(37):27306-14. Epub 2007 Jun 1.

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