Refined three-dimensional solution structure of insect defensin A (Q27729857)

2

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C Hetru

3

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J A Hoffmann

4

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M Ptak

5

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F Vovelle

Insect defensins: inducible antibacterial peptides

6

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publication date

15 May 1995

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published in

Structure

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volume

3

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issue

5

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page(s)

435-48

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Determination of disulfide bridges in natural and recombinant insect defensin A.

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Mode of action of sapecin, a novel antibacterial protein of Sarcophaga peregrina (flesh fly).

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Two-dimensional 1H NMR study of recombinant insect defensin A in water: resonance assignments, secondary structure and global folding

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Progress in multidimensional NMR investigations of peptide and protein 3-D structures in solution. From structure to functional aspects

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1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin

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Coiling of beta-pleated sheets.

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Standard structures in proteins

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Nuclear magnetic resonance solution structure of dendrotoxin K from the venom of Dendroaspis polylepis polylepis

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Inhibition of the Ca(2+)-activated K(+)-channel by sapecin B, an insect antibacterial protein

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A novel insect defensin mediates the inducible antibacterial activity in larvae of the dragonfly Aeschna cyanea (Paleoptera, Odonata).

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Alpha plus beta folds revisited: some favoured motifs

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Thionins: plant peptides that modify membrane permeability in cultured mammalian cells

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Solution conformation of a heptadecapeptide comprising the DNA binding helix F of the cyclic AMP receptor protein of Escherichia coli. Combined use of 1H nuclear magnetic resonance and restrained molecular dynamics.

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Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding

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Refined Structure of Charybdotoxin: Common Motifs in Scorpion Toxins and Insect Defensins

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Proton nuclear magnetic resonance and distance geometry/simulated annealing studies on the variant-1 neurotoxin from the New World scorpion Centruroides sculpturatus Ewing

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Solution structure of .gamma.1-H and .gamma.1-P thionins from barley and wheat endosperm determined by proton NMR: a structural motif common to toxic arthropod proteins

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

3912811

3912811

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference