Single, double and quadruple alanine substitutions at oligomeric interfaces identify hydrophobicity as the key determinant of human neutrophil alpha defensin HNP1 function (Q21132446)

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scientific article published on 13 November 2013

Single, Double and Quadruple Alanine Substitutions at Oligomeric Interfaces Identify Hydrophobicity as the Key Determinant of Human Neutrophil Alpha Defensin HNP1 Function

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English	Single, double and quadruple alanine substitutions at oligomeric interfaces identify hydrophobicity as the key determinant of human neutrophil alpha defensin HNP1 function	scientific article published on 13 November 2013	Single, Double and Quadruple Alanine Substitutions at Oligomeric Interfaces Identify Hydrophobicity as the Key Determinant of Human Neutrophil Alpha Defensin HNP1 Function

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Single, double and quadruple alanine substitutions at oligomeric interfaces identify hydrophobicity as the key determinant of human neutrophil alpha defensin HNP1 function (English)

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13 November 2013

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Invariant gly residue is important for α-defensin folding, dimerization, and function: a case study of the human neutrophil α-defensin HNP1

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Sometimes it takes two to tango: contributions of dimerization to functions of human α-defensin HNP1 peptide

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Primary structures of three human neutrophil defensins

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Human -Defensin 6 Promotes Mucosal Innate Immunity Through Self-Assembled Peptide Nanonets

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Resonance Assignment and Three-Dimensional Structure Determination of a Human α-Defensin, HNP-1, by Solid-State NMR

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Retrocyclin-2: structural analysis of a potent anti-HIV theta-defensin

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The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus

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Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent

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Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization

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Defensins: antimicrobial peptides of innate immunity

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NMR studies of defensin antimicrobial peptides. 1. Resonance assignment and secondary structure determination of rabbit NP-2 and human HNP-1

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10.1371/JOURNAL.PONE.0078937

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