Evidence map›Paper›PMID 17880914›Full record

ReviewBiochimica et biophysica acta2008

Structural biology of membrane-intrinsic beta-barrel enzymes: sentinels of the bacterial outer membrane.

Russell E Bishop

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

76 citing papers in PubMed, 133 citations in OpenAlex.

  1. Article
  2. Lipid landscaping of the bacterial cell surface.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Immobile lipopolysaccharides and outer membrane proteins differentially segregate in growingProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Review
  11. Coordinated subdomain movements of MlaC regulate ligand binding and transport.Computational and structural biotechnology journal · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. A periplasmic phospholipase that maintains outer membrane lipid asymmetry inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Review
  17. Article
  18. Review
  19. Deletion of Yersinia pestisJournal of bacteriology · 2021
    Article
  20. Article

16 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

1 author at 1 institution in 1 country.

Russell E BishopDepartment of Biochemistry and Biomedical Sciences, 1200 Main Street West, Health Sciences Centre 4H19, McMaster University, Hamilton, ON, Canada L8N 3Z5. bishopr@mcmaster.ca
McMaster University Medical Centre · CA

Funding

CIHR 43886-1
6 · The paper itself

Abstract

The outer membranes of Gram-negative bacteria are replete with integral membrane proteins that exhibit antiparallel beta-barrel structures, but very few of these proteins function as enzymes. In Escherichia coli, only three beta-barrel enzymes are known to exist in the outer membrane; these are the phospholipase OMPLA, the protease OmpT, and the phospholipidColon, two colonslipid A palmitoyltransferase PagP, all of which have been characterized at the structural level. Structural details have also emerged for the outer membrane beta-barrel enzyme PagL, a lipid A 3-O-deacylase from Pseudomonas aeruginosa. Lipid A can be further modified in the outer membrane by two beta-barrel enzymes of unknown structure; namely, the Salmonella enterica 3'-acyloxyacyl hydrolase LpxR, and the Rhizobium leguminosarum oxidase LpxQ, which employs O(2) to convert the proximal glucosamine unit of lipid A into 2-aminogluconate. Structural biology now indicates how beta-barrel enzymes can function as sentinels that remain dormant when the outer membrane permeability barrier is intact. Host immune defenses and antibiotics that perturb this barrier can directly trigger beta-barrel enzymes in the outer membrane. The ensuing adaptive responses occur instantaneously and rapidly outpace other signal transduction mechanisms that similarly function to restore the outer membrane permeability barrier.

Indexed as

AcyltransferasesBacterial Outer Membrane ProteinsBacterial ProteinsCarboxylic Ester HydrolasesCell MembraneEscherichia coliEscherichia coli ProteinsGram-Negative BacteriaModels, BiologicalModels, MolecularPhospholipases A1PorinsProtein ConformationProtein Structure, SecondaryAcyltransferasesBacterial Outer Membrane ProteinsBacterial ProteinsCarboxylic Ester HydrolasesEscherichia coli ProteinsompT protein, bacteriaPhospholipases A1Porins

Identifiers

PMID17880914
PMCPMC5007122
OpenAlexW2124530114

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.