ArticleFrontiers in immunology2024
Alpha-1-antitrypsin as novel substrate for
Article in Frontiers in immunology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed.
- Circulating alpha-1 antitrypsin and its c-terminal peptides differentiate bacterial from viral community-acquired pneumonia.Journal of translational medicine · 2026Article
- C-terminal αERJ open research · 2026Article
- Protein Fragments: From Biomarkers to Therapeutic Targets-A Focus on α1-Antitrypsin-Derived Peptides.Mediators of inflammation · 2026Review
- The secreted proteasesVirulence · 2025Article
- Linking Virulence and Iron Limitation Response inJournal of proteome research · 2025Article
- Serum levels of C-terminal peptides of alpha-1 antitrypsin as potential biomarkers in non-small cell lung cancer.Translational lung cancer research · 2025Article
- pTripleTREP - A vector for tightly controlled expression and purification of virulence factors in Staphylococcus aureus.Microbial cell factories · 2025Article
- Circulating C-terminal peptides and polymers of alpha-1 antitrypsin as putative markers of pediatric Pi*ZZ liver disease.Frontiers in pediatrics · 2025Article
- Integrated genomic and proteomic analysis of the mouse-adaptedCurrent research in microbial sciences · 2025Article
Corrections and comments
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Authors and funding
13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background: The serine protease like (Spl) proteases of Methods: We used MALDI-TOF-MS to identify the cleavage site of Spl proteases within AAT's reactive center loop (RCL) and LC-MS/MS to quantify the resulting peptide cleavage product in Results: SplD, E and F, but not A or B, cleave AAT in its RCL, resulting in the release of a peptide consisting of AAT's C-terminal 36 amino acids (C36). Synthetic C36, as well as AAT-SplD/E/F-digestions exhibit NETosis inhibition. Only SplE, but not D or F, was partly inhibited by AAT, forming a covalent complex. Conclusion: We unraveled a new virulence trait of
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Registered trials
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