Evidence map›Paper›PMID 25796031›Full record

ReviewCurrent opinion in structural biology2015

The β-barrel membrane protein insertase machinery from Gram-negative bacteria.

Nicholas Noinaj, Sarah E Rollauer, Susan K Buchanan

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed.

  1. Review
  2. Article
  3. Total Synthesis of Dynobactin A.Journal of the American Chemical Society · 2024
    Article
  4. The Name Is Barrel, β-Barrel.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  5. Article
  6. Article
  7. Drug Binding to BamA Targets Its Lateral Gate.The journal of physical chemistry. B · 2023
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Interplay of protein primary sequence, lipid membrane, and chaperone in β-barrel assembly.Protein science : a publication of the Protein Society · 2021
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. The big BAM theory: An open and closed case?Biochimica et biophysica acta. Biomembranes · 2020
    Review
  20. 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

3 authors.

Nicholas NoinajMarkey Center for Structural Biology, Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, United States.
Sarah E RollauerNational Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, United States.
Susan K BuchananNational Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, United States. Electronic address: skbuchan@helix.nih.gov.

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 1K22AI113078-01NIAID NIH HHS K22 AI113078Wellcome TrustWellcome Trust 103040/Z/13/Z
6 · The paper itself

Abstract

The outer membranes (OM) of Gram-negative bacteria contain a host of β-barrel outer membrane proteins (OMPs) which serve many functions for cell survival and virulence. The biogenesis of these OMPs is mediated by the β-barrel assembly machinery (BAM) complex which is composed of five components including the essential core component called BamA that mediates the insertase function within the OM. The crystal structure of BamA has recently been reported from three different species, including a full-length structure from Neisseria gonorrhoeae. Mutagenesis and functional studies identified several conformational changes within BamA that are required for function, providing a significant advancement towards unraveling exactly how BamA and the BAM complex are able to fold and insert new OMPs in the OM.

Indexed as

Gram-Negative BacteriaBacterial Outer Membrane ProteinsProtein Structure, SecondaryBacterial Outer Membrane Proteins

Identifiers

PMID25796031
PMCPMC4476940

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.