ArticleThe Journal of biological chemistry2012
Invariant gly residue is important for α-defensin folding, dimerization, and function: a case study of the human neutrophil α-defensin HNP1.
Article in The Journal of biological chemistry, 2012. 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
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
19 citing papers in PubMed, 32 citations in OpenAlex.
- Human alpha-defensin 5 stabilizes the enterovirus A71 capsid and blocks infection.bioRxiv : the preprint server for biology · 2026Article
- Advances in the chemical synthesis of human proteoforms.Science China. Life sciences · 2025Review
- HNP-1: From Structure to Application Thanks to Multifaceted Functions.Microorganisms · 2025Review
- Review
- Mechanisms and regulation of defensins in host defense.Signal transduction and targeted therapy · 2023Review
- Mouse α-Defensins: Structural and Functional Analysis of the 17 Cryptdin Isoforms Identified from a Single Jejunal Crypt.Infection and immunity · 2023Article
- Using an Ensemble to Identify and Classify Macroalgae Antimicrobial Peptides.Interdisciplinary sciences, computational life sciences · 2021Article
- High-Throughput Quantification of Bacterial-Cell Interactions Using Virtual Colony Counts.Frontiers in cellular and infection microbiology · 2018Article
- Targeting and inactivation of bacterial toxins by human defensins.Biological chemistry · 2017Review
- Defensins, lectins, mucins, and secretory immunoglobulin A: microbe-binding biomolecules that contribute to mucosal immunity in the human gut.Critical reviews in biochemistry and molecular biology · 2017Review
- Guardians of the Gut: Enteric Defensins.Frontiers in microbiology · 2017Review
- Thermodynamic instability of viral proteins is a pathogen-associated molecular pattern targeted by human defensins.Scientific reports · 2016Article
- Quantification of polysaccharides fixed to Gram stained slides using lactophenol cotton blue and digital image processing.F1000Research · 2015Article
- Human defensins facilitate local unfolding of thermodynamically unstable regions of bacterial protein toxins.Immunity · 2014Article
- Discovery and characterization of a disulfide-locked C(2)-symmetric defensin peptide.Journal of the American Chemical Society · 2014Article
- β-Bulges: extensive structural analyses of β-sheets irregularities.Protein science : a publication of the Protein Society · 2013Article
- Article
- NMR solution structure and condition-dependent oligomerization of the antimicrobial peptide human defensin 5.Biochemistry · 2012Article
- Functional determinants of human enteric α-defensin HD5: crucial role for hydrophobicity at dimer interface.The Journal of biological chemistry · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
The human α-defensins (HNP) are synthesized in vivo as inactive prodefensins, and contain a conserved glycine, Gly(17), which is part of a β-bulge structure. It had previously been shown that the glycine main chain torsion angles are in a D-configuration, and that d-amino acids but not L-alanine could be substituted at that position to yield correctly folded peptides without the help of a prodomain. In this study, the glycine to L-alanine mutant defensin was synthesized in the form of a prodefensin using native chemical ligation. The ligation product folded correctly and yielded an active peptide upon CNBr cleavage. The L-Ala(17)-HNP1 crystal structure depicted a β-bulge identical to wild-type HNP1. However, dimerization was perturbed, causing one monomer to tilt with respect to the other in a dimerization model. Inhibitory activity against the anthrax lethal factor showed a 2-fold reduction relative to wild-type HNP1 as measured by the inhibitory concentration IC(50). Self-association was slightly reduced, as detected by surface plasmon resonance measurements. According to the results of the virtual colony count assay, the antibacterial activity against Escherichia coli, Staphylococcus aureus, and Bacillus cereus exhibited a less than 2-fold reduction in virtual lethal dose values. Prodefensins with two other L-amino acid substitutions, Arg and Phe, at the same position did not fold, indicating that only small side chains are tolerable. These results further elucidate the factors governing the region of the β-bulge structure that includes Gly(17), illuminating why glycine is conserved in all mammalian α-defensins.
Indexed as
Identifiers
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.