ReviewPharmaceuticals (Basel, Switzerland)2015
Antimicrobial Peptides from Plants.
Review in Pharmaceuticals (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 217 papers, 1 of them a synthesis that pooled it.
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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
217 citing papers in PubMed, 1 synthesis or guideline pooled it, 482 citations in OpenAlex.
- Defensins of Grasses: A Systematic Review.Biomolecules · 2020Pooled it
- Article
- Article
- Plant Antimicrobial Peptides and Bacteriocins: Emerging Strategies Against Biofilms.Probiotics and antimicrobial proteins · 2026Review
- Sequence-Derived and Molecular Descriptors for Interpretable Modeling of Molecular Systems: Insights from Peptide Hemolysis.Journal of chemical information and modeling · 2026Article
- Plant-Derived Peptide-Polymer Therapeutics for Cutaneous Infections and Inflammation: Mechanistic Basis, Delivery Design and Translational Considerations.Pharmaceutics · 2026Review
- The Snakin Family of Antimicrobial Peptides: Promising Alternatives to Conventional Antibiotics.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Antimicrobial Potential of Defensin-DerivedInternational journal of molecular sciences · 2026Article
- Characterization and Biofungicide Potential of a Novel Antifungal defensin, K4CBP6, from Solanum lycopersicum L.Probiotics and antimicrobial proteins · 2026Article
- Antimicrobial peptides: An important link in the game theory between plants and pathogens.Journal of advanced research · 2026Review
- The Rana sylvatica skin-secreted antimicrobial peptide (AMP) gene repertoire highlights broader patterns in anuran AMP evolution.Scientific reports · 2026Article
- Bioactive peptides in Endodontic infections: The Good, The Bad, and The Ugly.Probiotics and antimicrobial proteins · 2026Review
- Transgenic Tobacco Plants Expressing Synthetic Peptides: A Functional and Structural Analysis for Pathogen Resistance.Plant biotechnology journal · 2026Article
- Arabidopsis phospholipid modifications mediate cellulase-induced resistance to a fungal peptide antibiotic by imposing cell polarity.The New phytologist · 2026Article
- Integrative computational-experimental discovery and translation of antifungal peptides for multidrug-resistant fungi.Frontiers in microbiology · 2026Review
- Overexpression ofFrontiers in plant science · 2026Article
- Antifungal peptides: From modes of action to synergistic and immunologic potential.Cell stress · 2026Article
- Antimicrobial Peptides: Current Status, Mechanisms of Action, and Strategies to Overcome Therapeutic Limitations.Microorganisms · 2025Review
- Bioactive Plant Peptides: Physicochemical Features, Structure-Function Insights and Mechanism of Action.Molecules (Basel, Switzerland) · 2025Review
- PDF gene family in four Cucurbitaceae species: genome-wide identification, classification and expression in response to biotic stress.BMC plant biology · 2025Article
157 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plant antimicrobial peptides (AMPs) have evolved differently from AMPs from other life forms. They are generally rich in cysteine residues which form multiple disulfides. In turn, the disulfides cross-braced plant AMPs as cystine-rich peptides to confer them with extraordinary high chemical, thermal and proteolytic stability. The cystine-rich or commonly known as cysteine-rich peptides (CRPs) of plant AMPs are classified into families based on their sequence similarity, cysteine motifs that determine their distinctive disulfide bond patterns and tertiary structure fold. Cystine-rich plant AMP families include thionins, defensins, hevein-like peptides, knottin-type peptides (linear and cyclic), lipid transfer proteins, α-hairpinin and snakins family. In addition, there are AMPs which are rich in other amino acids. The ability of plant AMPs to organize into specific families with conserved structural folds that enable sequence variation of non-Cys residues encased in the same scaffold within a particular family to play multiple functions. Furthermore, the ability of plant AMPs to tolerate hypervariable sequences using a conserved scaffold provides diversity to recognize different targets by varying the sequence of the non-cysteine residues. These properties bode well for developing plant AMPs as potential therapeutics and for protection of crops through transgenic methods. This review provides an overview of the major families of plant AMPs, including their structures, functions, and putative mechanisms.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.