1H NMR structure of an antifungal γ-thionin protein SIα1: Similarity to scorpion toxins-Reference-Cited by-同舟云学术

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1H NMR structure of an antifungal γ-thionin protein SIα1: Similarity to scorpion toxins

Published:1998-08-15 Issue:3 Volume:32 Page:334-349
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Genetics
language:en
Short-container-title:Proteins

Author:

Bloch Carlos,Patel Sunil U.,Baud Franck,Zvelebil Marketa J.J.M.,Carr Mark D.,Sadler Peter J.,Thornton Janet M.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference81 articles.

1. Antimicrobial Peptides from Plants

2. Plant Defensins: Novel Antimicrobial Peptides as Components of the Host Defense System

3. Plant chitinases are potent inhibitors of fungal growth

4. Comparison of some molecular, enzymatic and antifungal properties of chitinases from thorn-apple, tobacco and wheat

5. Isolation and partial characterization of two antifungal proteins from barley

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1. Genome-wide investigation of defensin genes in peanut (Arachis hypogaea L.) reveals AhDef2.2 conferring resistance to bacterial wilt;The Crop Journal;2021-11

2. Antimicrobial Peptides from Fruits and Their Potential Use as Biotechnological Tools—A Review and Outlook;Frontiers in Microbiology;2017-01-10

3. Polar Characterization of Antifungal Peptides from APD2 Database;Cell Biochemistry and Biophysics;2014-07-01

4. Nematode-derived drosomycin-type antifungal peptides provide evidence for plant-to-ecdysozoan horizontal transfer of a disease resistance gene;Nature Communications;2014-01-17

5. Structural and Functional Studies of a Phosphatidic Acid-Binding Antifungal Plant Defensin MtDef4: Identification of an RGFRRR Motif Governing Fungal Cell Entry;PLoS ONE;2013-12-04

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