Evidence map›Paper›PMID 28216659›Full record

ReviewNature reviews. Microbiology2017

The β-barrel assembly machinery in motion.

Nicholas Noinaj, James C Gumbart, Susan K Buchanan

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
130citing papers in PubMed, 1 pooled it
22.7field-weighted citation impact, top 1% of its field
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

130 citing papers in PubMed, 1 synthesis or guideline pooled it, 197 citations in OpenAlex.

  1. Drug-resistantClinical microbiology reviews · 2025
    Pooled it
  2. Review
  3. Article
  4. ThemBio · 2026
    Article
  5. Membrane-Associated Biomolecules for Synthetic Cell Signalling.Chembiochem : a European journal of chemical biology · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Repurposing a drug to punish carbapenem-resistantProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Type IV pili ofEcoSal Plus · 2024
    Review
  18. Article
  19. Article
  20. Article

70 more citing papers are in PubMed but not listed here.

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 at 3 institutions in 1 country.

Nicholas NoinajMarkey Center for Structural Biology, Department of Biological Sciences and the Purdue Institute for Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, Indiana 47907, USA.
James C GumbartSchool of Physics, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.
Susan K BuchananNational Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892, USA.
Georgia Institute of Technology · USNational Institute of Diabetes and Digestive and Kidney Diseases · USPurdue University West Lafayette · US

Funding

structural characterization of bacterial secretion channelsZIADK036139 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2025
$19.3M
The role of BamA in the biogenesis of beta-barrel membrane proteinsK22AI113078 · NIAID · PURDUE UNIVERSITY · PI NOINAJ, NICHOLAS · 2015 to 2016
$267k
Intramural NIH HHS ZIA DK036139NIAID NIH HHS K22 AI113078
6 · The paper itself

Abstract

In Gram-negative bacteria, the biogenesis of β-barrel outer membrane proteins (OMPs) is mediated by the β-barrel assembly machinery (BAM) complex. During the past decade, structural and functional studies have collectively contributed to advancing our understanding of the structure and function of the BAM complex; however, the exact mechanism that is involved remains elusive. In this Progress article, we discuss recent structural studies that have revealed that the accessory proteins may regulate essential unprecedented conformational changes in the core component BamA during function. We also detail the mechanistic insights that have been gained from structural data, mutagenesis studies and molecular dynamics simulations, and explore two emerging models for the BAM-mediated biogenesis of OMPs in bacteria.

Indexed as

Protein FoldingBacterial Outer Membrane ProteinsEscherichia coliEscherichia coli ProteinsLipid-Linked ProteinsModels, MolecularMolecular Dynamics SimulationProtein DomainsProtein Structure, SecondaryBacterial Outer Membrane ProteinsBamA protein, E coliBamB protein, E coliBamC protein, E coliBamD protein, E coliEscherichia coli ProteinsLipid-Linked Proteins

Identifiers

PMID28216659
PMCPMC5455337
OpenAlexW2589042007

What OpenQuestion holds

Textmetadata
LicenceTDM
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.