ArticleJournal of chemical information and modeling2025
Multidimensional Decomposition and Ensemble Modeling of Histatin 1 and Its Siblings: Detailing Structure and Biological Function Using an Integrative Approach.
Article in Journal of chemical information and modeling, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
2 citing papers in PubMed.
- Physicochemical Principles Governing the Intrinsically Disordered Salivary Peptide Histatin 5: Ensemble Structure, Electrostatics, and Environmental Responsiveness.The journal of physical chemistry. B · 2026Review
- Design and TAG-Assisted Synthesis of the C-Terminal Amidated Antimicrobial Peptide NCBP-1 Derived from a Plant-Derived Noncanonical NCBP and Its Biological Activity.Protein and peptide letters · 2026Article
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.
Funding
Abstract
Histatins are a family of multifunctional, cationic histidine-rich saliva peptides. The most prominently represented are Histatin 1, Histatin 3, and Histatin 5. Despite considerable similarities in primary structure, the three members are known to display varied antimicrobial properties and healing abilities. This study aims to provide a detailed structural comparison of Histatin 1, Histatin 3, and Histatin 5, as well as a thorough investigation into the variation caused to the conformational ensemble of Histatin 1 upon phosphorylation. The study applies molecular dynamics simulation, small-angle X-ray scattering, circular dichroism, bioinformatics tools, and neutron reflectometry. A multidimensional decomposition technique and its connection to clustering methods are also presented. It was observed that the phosphorylation of Histatin 1 profoundly shifts the conformational ensemble and may act as a molecular switch that facilitates tooth enamel binding. Observations are provided on the killing mechanisms of Histatins concerning self-association and membrane rupturing.
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What Socratic 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 Socratic graph.