Evidence map›Paper›PMID 40854123›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

Structure of the

Norman Tran, Aaron Frenette, Todd Holyoak

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Norman Tran *Department of Biology, Faculty of Science, University of Waterloo, Waterloo, ON N2L 3G1, Canada.
Aaron Frenette *Department of Biology, Faculty of Science, University of Waterloo, Waterloo, ON N2L 3G1, Canada.
Todd HolyoakDepartment of Biology, Faculty of Science, University of Waterloo, Waterloo, ON N2L 3G1, Canada.ORCID 0000-0002-7329-1115

Funding

Training and OutreachP30GM124166 · NIGMS · CORNELL UNIVERSITY · PI RICHARD A. CERIONE · 2019 to 2026
$28.3M
Canadian Government | Natural Sciences and Engineering Research Council of Canada (NSERC) Discovery GrantIGAN Biosciences noneNIGMS NIH HHS P30 GM124166
6 · The paper itself

Abstract

Immunoglobulin A proteases (IgAPs) are a diverse group of enzymes secreted from bacteria that inhabit human mucosal tissues. These enzymes have convergently evolved to cleave human immunoglobulin A as a means of modulating and evading host immunity. Only two of three known IgAP families have been biochemically characterized beyond their initial discovery. Here, we show using solution-scattering, steady-state kinetic, and crystallographic approaches that the protease from

Indexed as

Bacterial ProteinsImmunoglobulin APeptide HydrolasesCrystallography, X-RayHumansKineticsModels, MolecularProtein ConformationSubstrate SpecificityBacterial ProteinsImmunoglobulin APeptide HydrolasesIgA proteaseimmunoglobulinmucosal immunityprotease structure

Identifiers

PMID40854123
PMCPMC12415215

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.