Evidence map›Paper›PMID 40553494›Full record

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

In situ NMR reveals a pH sensor motif in an outer membrane protein that drives bacterial vesicle production.

Nicholas A Wood, Alyssa Kraft, Kyungsoo Shin, Tata Gopinath, Francesca M Marassi

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 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Solid-state NMR of membrane proteins in situ.Current opinion in structural biology · 2025
    Review
  5. Review
4 · The record

Corrections and comments

  • Update of
    2025
5 · Who and what money

Authors and funding

5 authors.

Nicholas A WoodDepartment of Biophysics, Medical College of Wisconsin, Milwaukee, WI 53226-3548.
Alyssa KraftDepartment of Biophysics, Medical College of Wisconsin, Milwaukee, WI 53226-3548.ORCID 0009-0008-7549-4064
Kyungsoo ShinDepartment of Biophysics, Medical College of Wisconsin, Milwaukee, WI 53226-3548.ORCID 0000-0003-4836-8798
Tata GopinathDepartment of Biophysics, Medical College of Wisconsin, Milwaukee, WI 53226-3548.
Francesca M MarassiDepartment of Biophysics, Medical College of Wisconsin, Milwaukee, WI 53226-3548.ORCID 0000-0003-2695-5844

Funding

Membrane Protein Effectors of Pathogen Interactions With HostR35GM118186 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Francesca M Marassi · 2016 to 2026
$8.5M
A 600 MHz NMR spectrometer upgrade for the Sanford Burnham Prebys Cancer CenterS10OD028716 · OD · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI MARASSI, FRANCESCA M · 2020 to 2020
$926k
Multi-disciplinary analysis of the role of PagC for outer membrane vesicle biogenesisF32AI188770 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI Nicholas A Wood · 2025 to 2026
$152k
HHS | NIH (NIH) AI188770HHS | NIH (NIH) GM118186HHS | NIH (NIH) OD028716NIAID NIH HHS F32 AI188770NIGMS NIH HHS R35 GM118186NIH HHS S10 OD028716
6 · The paper itself

Abstract

The outer membrane vesicles (OMVs) produced by diderm bacteria have important roles in cell envelope homeostasis, secretion, interbacterial communication, and pathogenesis. The facultative intracellular pathogen

Indexed as

Bacterial Outer Membrane ProteinsSalmonella typhimuriumAmino Acid MotifsEscherichia coliGene Expression Regulation, BacterialHydrogen-Ion ConcentrationMagnetic Resonance SpectroscopyBacterial Outer Membrane Proteinsouter membrane vesiclePagCSalmonellasolid-state NMR

Identifiers

PMID40553494
PMCPMC12232643

What OpenQuestion holds

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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.