ArticleFrontiers in microbiology2016
Membrane-Active Epithelial Keratin 6A Fragments (KAMPs) Are Unique Human Antimicrobial Peptides with a Non-αβ Structure.
Article in Frontiers in microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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.
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Who cites it
19 citing papers in PubMed, 25 citations in OpenAlex.
- Antimicrobial peptides in anti-infective and immunomodulatory applications: Mechanisms, challenges, and emerging computational design.Zoological research · 2026Review
- TRPV1 Defends the Healthy Murine Cornea Against Staphylococcus aureus Adhesion Independently of Sensory Nerve Firing.Investigative ophthalmology & visual science · 2025Article
- Article
- Progress in the classification, optimization, activity, and application of antimicrobial peptides.Frontiers in microbiology · 2025Review
- Antimicrobial Peptides: Mechanisms, Applications, and Therapeutic Potential.Infection and drug resistance · 2025Review
- Current Understanding of Feather Keratin and Keratinase and Their Applications in Biotechnology.Biochemistry research international · 2025Review
- Antibacterial Activity and Multi-Targeted Mechanism of Action of Suberanilic Acid Isolated fromMolecules (Basel, Switzerland) · 2024Article
- Simultaneous control of infection and inflammation with keratin-derived antibacterial peptides targeting TLRs and co-receptors.Science translational medicine · 2023Article
- Proteomic Profiling Reveals Distinct Bacterial Extracellular Vesicle Subpopulations with Possibly Unique Functionality.Applied and environmental microbiology · 2023Article
- Evaluation of a Human Keratin Wound Matrix as an Effective Wound Healing Therapy in Difficult- to-Heal Venous Leg Ulcers.Eplasty · 2023Article
- Antimicrobial peptides for bone tissue engineering: Diversity, effects and applications.Frontiers in bioengineering and biotechnology · 2022Review
- Keratins as an Inflammation Trigger Point in Epidermolysis Bullosa Simplex.International journal of molecular sciences · 2021Review
- Antimicrobial Peptides: An Update on Classifications and Databases.International journal of molecular sciences · 2021Review
- Foundational concepts in the biology of bacterial keratitis.Experimental eye research · 2021Review
- Contact lens-related corneal infection: Intrinsic resistance and its compromise.Progress in retinal and eye research · 2020Review
- ITRAQ-based proteomic analysis reveals possible target-related proteins in human adrenocortical adenomas.BMC genomics · 2019Article
- A Commensal Dipeptidyl Aminopeptidase with Specificity for N-Terminal Glycine Degrades Human-Produced Antimicrobial Peptides in Vitro.ACS chemical biology · 2018Article
- Article
- Keratin 6a reorganization for ubiquitin-proteasomal processing is a direct antimicrobial response.The Journal of cell biology · 2018Article
Corrections and comments
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Authors and funding
4 authors at 4 institutions in 1 country.
Funding
Abstract
Antibiotic resistance is a pressing global health problem that threatens millions of lives each year. Natural antimicrobial peptides and their synthetic derivatives, including peptoids and peptidomimetics, are promising candidates as novel antibiotics. Recently, the C-terminal glycine-rich fragments of human epithelial keratin 6A were found to have bactericidal and cytoprotective activities. Here, we used an improved 2-dimensional NMR method coupled with a new protocol for structural refinement by low temperature simulated annealing to characterize the solution structure of these kerain-derived antimicrobial peptides (KAMPs). Two specific KAMPs in complex with membrane mimicking sodium dodecyl sulfate (SDS) micelles displayed amphipathic conformations with only local bends and turns, and a central 10-residue glycine-rich hydrophobic strip that is central to bactericidal activity. To our knowledge, this is the first report of non-αβ structure for human antimicrobial peptides. Direct observation of
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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.