Evidence map›Paper›PMID 41853578›Full record

ArticleChemical science2026

Screening pertactin-specific antibodies and evaluating competitive epitope recognition by native mass spectrometry.

Mohamed I Gadallah, Kate A McConnell, Kelli M Hager, Virginia K James, Annalee W Nguyen, Jennifer A Maynard, Jennifer S Brodbelt

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chemical science, 2026. 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. Article
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

7 authors.

Mohamed I GadallahDepartment of Chemistry, The University of Texas at Austin Austin TX 78712 USA jbrodbelt@cm.utexas.edu.ORCID https://orcid.org/0000-0003-4913-7668
Kate A McConnellDepartment of Molecular Biosciences, The University of Texas at Austin Austin TX 78712 USA.
Kelli M HagerDepartment of Molecular Biosciences, The University of Texas at Austin Austin TX 78712 USA.
Virginia K JamesDepartment of Chemistry, The University of Texas at Austin Austin TX 78712 USA jbrodbelt@cm.utexas.edu.
Annalee W NguyenDepartment of Chemical Engineering, The University of Texas at Austin Austin TX 78712 USA.
Jennifer A MaynardDepartment of Chemical Engineering, The University of Texas at Austin Austin TX 78712 USA.
Jennifer S BrodbeltDepartment of Chemistry, The University of Texas at Austin Austin TX 78712 USA jbrodbelt@cm.utexas.edu.ORCID https://orcid.org/0000-0003-3207-0217

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structural characterization of antigen-antibody interactions is critical for understanding protective vaccine responses and development of therapeutic monoclonal antibodies (mAb). Traditional biophysical and biochemical techniques often require the immobilization of one binding partner or provide ensemble-averaged measurements, constraints which may limit the ability to probe multiple facets of antigen-antibody interactions. Native mass spectrometry (nMS) offers a versatile alternative, providing a comprehensive view of antigen-antibody complexes. Here, we utilized native MS to screen the interactions between a small panel of monoclonal antibodies (mAbs) and the

Identifiers

PMID41853578
PMCPMC12994607

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.