Evidence map›Paper›PMID 32675245›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

The gain-of-function allele

Elizabeth M Hart, Meera Gupta, Martin Wühr, Thomas J Silhavy

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. A mechanism for substrate quality control in outer membrane protein assembly.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Structures of folding intermediates on BAM show diverse substrates fold by a conserved mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. A fluorescent reporter and single-turnover kinetics reveal insight into BAM complex function.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Fighting Antimicrobial Resistance: Innovative Drugs in Antibacterial Research.Angewandte Chemie (International ed. in English) · 2025
    Review
  12. Review
  13. Native β-barrel substrates pass through two shared intermediates during folding on the BAM complex.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

4 authors.

Elizabeth M HartDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544.ORCID 0000-0003-0444-6547
Meera GuptaDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544.
Martin WührDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544.ORCID 0000-0002-0244-8947
Thomas J SilhavyDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544; tsilhavy@princeton.edu.

Funding

Biogenesis and maintenance of the outer membrane of Gram-negative bacteriaR35GM118024 · NIGMS · PRINCETON UNIVERSITY · PI SILHAVY, THOMAS J. · 2016 to 2025
$8.1M
GENETIC ANALYSIS OF PROTEIN EXPORTR01GM034821 · NIGMS · PRINCETON UNIVERSITY · PI SILHAVY, THOMAS J. · 1985 to 2015
$4.7M
Development of New Proteomics Technology and its Application to Study Cellular OrganizationR35GM128813 · NIGMS · PRINCETON UNIVERSITY · PI Martin Wühr · 2018 to 2026
$4.0M
Investigating the mycomembrane protein assembly pathwayK99AI190054 · NIAID · HARVARD MEDICAL SCHOOL · PI Elizabeth Mary Hart · 2025 to 2026
$227k
NIAID NIH HHS K99 AI190054NIGMS NIH HHS R01 GM034821NIGMS NIH HHS R35 GM118024NIGMS NIH HHS R35 GM128813
6 · The paper itself

Abstract

The outer membrane (OM) of gram-negative bacteria confers innate resistance to toxins and antibiotics. Integral β-barrel outer membrane proteins (OMPs) function to establish and maintain the selective permeability of the OM. OMPs are assembled into the OM by the β-barrel assembly machine (BAM), which is composed of one OMP-BamA-and four lipoproteins-BamB, C, D, and E. BamB, C, and E can be removed individually with only minor effects on barrier function; however, depletion of either BamA or BamD causes a global defect in OMP assembly and results in cell death. We have identified a gain-of-function mutation,

Indexed as

Bacterial Outer MembraneBacterial Outer Membrane ProteinsEscherichia coli ProteinsEscherichia coliGain of Function MutationBacterial Outer Membrane ProteinsBamA protein, E coliBamD protein, E coliEscherichia coli ProteinsBAM complexOMP assemblyouter membrane biogenesis

Identifiers

PMID32675245
PMCPMC7414184

What OpenQuestion holds

Textmetadata
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.