Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity - Wikidata - wikimedia - TriplyDB

Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity

Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity

http://www.wikidata.org/entity/Q27678587

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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 Structural and functional studies of a phosphatidic acid-binding antifungal plant defensin MtDef4: identification of an RGFRRR motif governing fungal cell entry NMR Solution Structure and Condition-Dependent Oligomerization of the Antimicrobial Peptide Human Defensin 5 Phosphoinositide-mediated oligomerization of a defensin induces cell lysis The Tomato Defensin TPP3 Binds Phosphatidylinositol (4,5)-Bisphosphate via a Conserved Dimeric Cationic Grip Conformation To Mediate Cell Lysis.Human β-defensin 3 contains an oncolytic motif that binds PI(4,5)P2 to mediate tumour cell permeabilisation.Binding of phosphatidic acid by NsD7 mediates the formation of helical defensin-lipid oligomeric assemblies and membrane permeabilization.The C-terminal propeptide of a plant defensin confers cytoprotective and subcellular targeting functions.Role of Homeodomain leucine zipper (HD-Zip) IV transcription factors in plant development and plant protection from deleterious environmental factors.Defensins: antifungal lessons from eukaryotes Antifungal defensins and their role in plant defense.Field resistance to Fusarium oxysporum and Verticillium dahliae in transgenic cotton expressing the plant defensin NaD1.The phospholipid code: a key component of dying cell recognition, tumor progression and host-microbe interactions Antifungal plant defensins: increased insight in their mode of action as a basis for their use to combat fungal infections.Nicotiana alata Defensin Chimeras Reveal Differences in the Mechanism of Fungal and Tumor Cell Killing and an Enhanced Antifungal Variant.Agp2p, the plasma membrane transregulator of polyamine uptake, regulates the antifungal activities of the plant defensin NaD1 and other cationic peptides.Convergent evolution of defensin sequence, structure and function.The Defensins Consist of Two Independent, Convergent Protein Superfamilies.In silico identification, structural characterization, and phylogenetic analysis of MdesDEF-2: a novel defensin from the Hessian fly, Mayetiola destructor.Structure of the defensin NsD7 in complex with PIP2 reveals that defensin : lipid oligomer topologies are dependent on lipid type.Interaction of Scots Pine Defensin with Model Membrane by Coarse-Grained Molecular Dynamics.X-ray structure of a carpet-like antimicrobial defensin-phospholipid membrane disruption complex.

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P2860

Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity

http://www.wikidata.org/entity/Q27678587

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2012 nî lūn-bûn

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2012 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2012 թվականի հունիսին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年论文

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Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity

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Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity

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Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity

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Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity

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Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity

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Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity

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prefLabel

Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity

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Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity

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Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity

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JBC.M111.331009

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Journal of Biological Chemistry

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Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity

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Amy A Baxter

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Con Dogovski

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Grant D Mills

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Ivan K H Poon

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Nathan P Cowieson

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Nicole L van der Weerden

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Nigel Kirby

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P2860

Primary structures of three human neutrophil defensins

Defensins. Natural peptide antibiotics of human neutrophils

Trp-26 imparts functional versatility to human alpha-defensin HNP1

Crystal structures of human alpha-defensins HNP4, HD5, and HD6

PHENIX: a comprehensive Python-based system for macromolecular structure solution

The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance

The structure of human beta-defensin-2 shows evidence of higher order oligomerization

The NMR structure of human beta-defensin-2 reveals a novel alpha-helical segment

The structure of human beta-defensin-1: new insights into structural properties of beta-defensins

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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19961-72

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scholarly article

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10.1074/JBC.M111.331009

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24

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287

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Matthew A Perugini

Marilyn Anderson

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2012-06-08T00:00:00Z

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224285089

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22511788

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3370180

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