ArticleProceedings of the National Academy of Sciences of the United States of America2019
Unifying structural signature of eukaryotic α-helical host defense peptides.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 42 citations in OpenAlex.
- Retracing the origin and evolution of a cryptic antimicrobial peptide within mammalian lactoferrin.PLoS biology · 2026Article
- Virulence Phenotypes Differentiate Persistent vs. Resolving Isolates of HumanAntibiotics (Basel, Switzerland) · 2026Article
- Amphipathic Antimicrobial Peptides Illuminate a Reciprocal Relationship Between Self-assembly and Cytolytic Activity.Angewandte Chemie (International ed. in English) · 2025Article
- Viral afterlife: SARS-CoV-2 as a reservoir of immunomimetic peptides that reassemble into proinflammatory supramolecular complexes.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Krein support vector machine classification of antimicrobial peptides.Digital discovery · 2023Article
- Release of immunomodulatory peptides at bacterial membrane interfaces as a novel strategy to fight microorganisms.The Journal of biological chemistry · 2023Article
- Unraveling the Role of Antimicrobial Peptides in Insects.International journal of molecular sciences · 2023Review
- Antimicrobial peptides´ immune modulation role in intracellular bacterial infection.Frontiers in immunology · 2023Review
- Histidine-Mediated Ion Specific Effects Enable Salt Tolerance of a Pore-Forming Marine Antimicrobial Peptide.Angewandte Chemie (International ed. in English) · 2022Article
- Rationalisation of Antifungal Properties of α-Helical Pore-Forming Peptide, Mastoparan B.Molecules (Basel, Switzerland) · 2022Article
- Targeted Antimicrobial Agents as Potential Tools for Modulating the Gut Microbiome.Frontiers in microbiology · 2022Review
- Novel Antimicrobial Peptides from a Cecropin-Like Region of Heteroscorpine-1 fromMolecules (Basel, Switzerland) · 2021Article
- Characteristics and therapeutic applications of antimicrobial peptides.Biophysics reviews · 2021Review
- Identification of Candida glabrata Transcriptional Regulators That Govern Stress Resistance and Virulence.Infection and immunity · 2021Article
- PACAP is a pathogen-inducible resident antimicrobial neuropeptide affording rapid and contextual molecular host defense of the brain.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- How do cyclic antibiotics with activity against Gram-negative bacteria permeate membranes? A machine learning informed experimental study.Biochimica et biophysica acta. Biomembranes · 2020Article
- Chemokine CCL28 Is a Potent Therapeutic Agent for Oropharyngeal Candidiasis.Antimicrobial agents and chemotherapy · 2020Article
- Monitoring the Site-Specific Solid-State NMR Data in Oligopeptides.International journal of molecular sciences · 2020Article
- Strategies in Translating the Therapeutic Potentials of Host Defense Peptides.Frontiers in immunology · 2020Review
- Antimicrobial Peptides and Cell-Penetrating Peptides for Treating Intracellular Bacterial Infections.Frontiers in cellular and infection microbiology · 2020Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Diversity of α-helical host defense peptides (αHDPs) contributes to immunity against a broad spectrum of pathogens via multiple functions. Thus, resolving common structure-function relationships among αHDPs is inherently difficult, even for artificial-intelligence-based methods that seek multifactorial trends rather than foundational principles. Here, bioinformatic and pattern recognition methods were applied to identify a unifying signature of eukaryotic αHDPs derived from amino acid sequence, biochemical, and three-dimensional properties of known αHDPs. The signature formula contains a helical domain of 12 residues with a mean hydrophobic moment of 0.50 and favoring aliphatic over aromatic hydrophobes in 18-aa windows of peptides or proteins matching its semantic definition. The holistic α-core signature subsumes existing physicochemical properties of αHDPs, and converged strongly with predictions of an independent machine-learning-based classifier recognizing sequences inducing negative Gaussian curvature in target membranes. Queries using the α-core formula identified 93% of all annotated αHDPs in proteomic databases and retrieved all major αHDP families. Synthesis and antimicrobial assays confirmed efficacies of predicted sequences having no previously known antimicrobial activity. The unifying α-core signature establishes a foundational framework for discovering and understanding αHDPs encompassing diverse structural and mechanistic variations, and affords possibilities for deterministic design of antiinfectives.
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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 Socratic graph.