Evidence map›Paper›PMID 26457522›Full record

ArticleActa crystallographica. Section F, Structural biology communications2015

Structural analysis of SepL, an enteropathogenic Escherichia coli type III secretion-system gatekeeper protein.

Brianne J Burkinshaw, Sergio A Souza, Natalie C J Strynadka

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

11 citing papers in PubMed, 12 citations in OpenAlex.

  1. Oligomeric assembly of the gatekeeper InvE orchestrates hierarchical type III protein secretion inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. BopN is a Gatekeeper of theMicrobiology spectrum · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016
    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

3 authors at 1 institution in 1 country.

Brianne J BurkinshawDepartment of Biochemistry and Molecular Biology, University of British Columbia, Health Sciences Mall, Vancouver, BC V6T 1Z3, Canada.
Sergio A SouzaDepartment of Biochemistry and Molecular Biology, University of British Columbia, Health Sciences Mall, Vancouver, BC V6T 1Z3, Canada.
Natalie C J StrynadkaDepartment of Biochemistry and Molecular Biology, University of British Columbia, Health Sciences Mall, Vancouver, BC V6T 1Z3, Canada.
University of British Columbia · CA

Funding

Canadian Institutes of Health ResearchHoward Hughes Medical Institute
6 · The paper itself

Abstract

During infection, enteropathogenic Escherichia coli assembles a complex multi-protein type III secretion system that traverses the bacterial membranes and targets the host cell membrane to directly deliver virulence or effector proteins to the host cytoplasm. As this secretion system is composed of more than 20 proteins, many of which form oligomeric associations, its assembly must be tightly regulated. A protein called the gatekeeper, or SepL, ensures that the secretion of the translocon component, which inserts into the host membrane, occurs before the secretion of effectors. The crystal structure of the gatekeeper SepL was determined and compared with the structures of SepL homologues from other bacterial pathogens in order to identify SepL residues that may be critical for its role in type III secretion-system assembly.

Indexed as

Bacterial Secretion SystemsAmino Acid SequenceCrystallizationCrystallography, X-RayEnteropathogenic Escherichia coliEscherichia coli ProteinsModels, MolecularMolecular Sequence DataProtein Structure, TertiarySolutionsStructural Homology, ProteinBacterial Secretion SystemsEscherichia coli ProteinsSepL protein, E coliSolutionsbacterial pathogenesisprotein secretion

Identifiers

PMID26457522
PMCPMC4601595
OpenAlexW2172486832

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.