ReviewCellular and molecular life sciences : CMLS2011
Proline-rich antimicrobial peptides: converging to a non-lytic mechanism of action.
Review in Cellular and molecular life sciences : CMLS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 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
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
114 citing papers in PubMed, 255 citations in OpenAlex.
- Musical Peptide: Fragmentation of Musical Protein for AI-driven Bioactive Peptide Discovery Based on a New DeepPepQSAR Pipeline.Interdisciplinary sciences, computational life sciences · 2026Article
- Time-resolved phenotyping at subcellular resolution reveals shared principles and key trade-offs across antimicrobial peptide activities.bioRxiv : the preprint server for biology · 2026Article
- Bacterial Acyl Carrier Proteins Are a Cytoplasmic Target for Different Cationic Antimicrobial and Antibiofilm Peptides.International journal of molecular sciences · 2026Article
- Characterization of Proline-Rich Antimicrobial Peptides with SbmA Transporter-Dependent and Independent Antimicrobial Activity towardACS infectious diseases · 2026Article
- Shared structural mechanisms of alternating access between the secondary peptide transporter SbmA and ABC transporters.Nature communications · 2026Article
- Antimicrobial peptides-based strategies at the frontline in battling the escalating menace of methicillin-resistant Staphylococcus aureus biofilms.European journal of microbiology & immunology · 2026Review
- Review
- Recombinant Expression and Antimicrobial Mechanism of Cysteine-Rich Antimicrobial Peptides fromMarine drugs · 2026Article
- Study of Human Antimicrobial Peptides Active Against Some Bacteroidota Species of the Oral Cavity.Antibiotics (Basel, Switzerland) · 2026Article
- Mechanistic Divergence and Differential Antibacterial Potency of the Proline-Rich Antimicrobial Peptide B7-005 Across ESKAPE + E Pathogens.Probiotics and antimicrobial proteins · 2026Article
- AI-driven antimicrobial peptide characterization unveils novel motifs for drug design.Scientific reports · 2025Article
- Reinforcement learning with low-rank adaptation for targeted antimicrobial peptide design.Briefings in bioinformatics · 2025Article
- Bioactive peptides fromFood chemistry: X · 2025Article
- Unlocking Antimicrobial Peptides from Marine Invertebrates: A Comprehensive Review of Antimicrobial Discovery.Antibiotics (Basel, Switzerland) · 2025Review
- Interactions ofInternational journal of molecular sciences · 2025Article
- Antimicrobial Peptide-Peptoid Macrocycles from the Polymyxin B2 Chemical Space.Angewandte Chemie (International ed. in English) · 2025Article
- The structure of the Vibrio natriegens 70S ribosome in complex with the proline-rich antimicrobial peptide Bac5(1-17).Nucleic acids research · 2025Article
- The importance role of central proline to the antimicrobial potency and selectivity of indolicidin.Archives of microbiology · 2025Article
- Proline-Modified (RW)ACS omega · 2025Article
- Aquatic Invertebrate Antimicrobial Peptides in the Fight Against Aquaculture Pathogens.Microorganisms · 2025Review
54 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
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proline-rich antimicrobial peptides are a group of cationic host defense peptides of vertebrates and invertebrates characterized by a high content of proline residues, often associated with arginine residues in repeated motifs. Those isolated from some mammalian and insect species, although not evolutionarily related, use a similar mechanism to selectively kill Gram-negative bacteria, with a low toxicity to animals. Unlike other types of antimicrobial peptides, their mode of action does not involve the lysis of bacterial membranes but entails penetration into susceptible cells, where they then act intracellularly. Some aspects of the transport system and cytoplasmic targets have been elucidated. These features make them attractive both as anti-infective lead compounds and as a new class of potential cell-penetrating peptides capable of internalising membrane-impermeant drugs into both bacterial and eukaryotic cells.
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What OpenQuestion holds
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.