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Mode of action of linear amphipathic alpha-helical antimicrobial peptides.
Oren Z, Shai Y. Oren Z, et al. Biopolymers. 1998;47(6):451-63. doi: 10.1002/(SICI)1097-0282(1998)47:6<451::AID-BIP4>3.0.CO;2-F. Biopolymers. 1998. PMID: 10333737 Review.
The consequence of sequence alteration of an amphipathic alpha-helical antimicrobial peptide and its diastereomers.
Papo N, Oren Z, Pag U, Sahl HG, Shai Y. Papo N, et al. Among authors: oren z. J Biol Chem. 2002 Sep 13;277(37):33913-21. doi: 10.1074/jbc.M204928200. Epub 2002 Jul 10. J Biol Chem. 2002. PMID: 12110678 Free article.
Structures and mode of membrane interaction of a short alpha helical lytic peptide and its diastereomer determined by NMR, FTIR, and fluorescence spectroscopy.
Oren Z, Ramesh J, Avrahami D, Suryaprakash N, Shai Y, Jelinek R. Oren Z, et al. Eur J Biochem. 2002 Aug;269(16):3869-80. doi: 10.1046/j.1432-1033.2002.03080.x. Eur J Biochem. 2002. PMID: 12180963 Free article.
2D-NMR and ATR-FTIR study of the structure of a cell-selective diastereomer of melittin and its orientation in phospholipids.
Sharon M, Oren Z, Shai Y, Anglister J. Sharon M, et al. Among authors: oren z. Biochemistry. 1999 Nov 16;38(46):15305-16. doi: 10.1021/bi991225t. Biochemistry. 1999. PMID: 10563816
In a previous study, a diastereomer ([D]-V(5,8),I(17),K(21)-melittin, D-amino acids at positions V(5,8),I(17),K(21)) of melittin was synthesized and its function was investigated [Oren, Z., and Shai, Y. (1997) Biochemistry 36, 1826-1835]. ...
In a previous study, a diastereomer ([D]-V(5,8),I(17),K(21)-melittin, D-amino acids at positions V(5,8),I(17),K(21)) of melittin was synthes …
Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity.
Oren Z, Lerman JC, Gudmundsson GH, Agerberth B, Shai Y. Oren Z, et al. Biochem J. 1999 Aug 1;341 ( Pt 3)(Pt 3):501-13. Biochem J. 1999. PMID: 10417311 Free PMC article.
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