ArticleProbiotics and antimicrobial proteins2019
Gene Cloning, Expression, and Antifungal Activities of Permatin from Naked Oat (Avena nuda).
Article in Probiotics and antimicrobial proteins, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
5 citing papers in PubMed.
- Genome-Wide Identification and Expression Analysis of the Thaumatin-like Protein Genes inCurrent issues in molecular biology · 2026Article
- CtTLP13 Located in Extracellular Vesicles Enhances the Resistance of Safflower (Carthamus tinctorius) to Botrytis cinerea.Molecular plant pathology · 2026Article
- Thaumatin-like Proteins in Legumes: Functions and Potential Applications-A Review.Plants (Basel, Switzerland) · 2024Review
- Article
- Ginkgo Seed Proteins: Characteristics, Functional Properties and Bioactivities.Plant foods for human nutrition (Dordrecht, Netherlands) · 2021Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Thaumatin-like proteins (TLPs) are the products of a large, highly complex gene family involved in host defense. TLPs also belong to the pathogenesis-related family 5 (PR-5) of plant defense proteins. Most TLPs exhibit potential antifungal activities, and their accumulation in the plant is related to many physiological processes. In this study, a gene encoding TLP named permatin with an open reading frame of 678 bp encoding a protein of 225 amino acids with a calculated molecular mass of 23.5 kDa was cloned from naked oat leaves. Phylogenetic analysis revealed that permatin shares high homology with a number of other TLPs among diverse taxa. Model of structure by homology modeling showed that permatin consists of an acidic cleft region consistent with most TLPs. Recombinant NusA-permatin was overexpressed in Escherichia coli strain BL21 and purified by Heparin column combined with Sephacryl S-200 column. The protein exhibited antifungal activity to Fusarium oxysporum (half maximal inhibitory concentration, IC
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Registered trials
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