Evidence map›Paper›PMID 20833800›Full record

ArticleJournal of bacteriology2010

SepL resembles an aberrant effector in binding to a class 1 type III secretion chaperone and carrying an N-terminal secretion signal.

Rasha Younis, Lewis E H Bingle, Sarah Rollauer, Diana Munera, Stephen J Busby, Steven Johnson, Janet E Deane, Susan M Lea, Gad Frankel, Mark J Pallen

Abstract read
In one paragraph

Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. BopN is a Gatekeeper of theMicrobiology spectrum · 2023
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016
    Review
  12. Article
  13. Structural analysis of SepL, an enteropathogenic Escherichia coli type III secretion-system gatekeeper protein.Acta crystallographica. Section F, Structural biology communications · 2015
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. 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

10 authors.

Rasha YounisSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham, United Kingdom.
Lewis E H Bingle
Sarah Rollauer
Diana Munera
Stephen J Busby
Steven Johnson
Janet E Deane
Susan M Lea
Gad Frankel
Mark J Pallen

Funding

Biotechnology and Biological Sciences Research Council BB/D010195/1Biotechnology and Biological Sciences Research Council BB/E020860/1Biotechnology and Biological Sciences Research Council BBE0208601
6 · The paper itself

Abstract

Here we show that the type III secretion gatekeeper protein SepL resembles an aberrant effector protein in binding to a class 1 type III secretion chaperone (Orf12, here renamed CesL). We also show that short N-terminal fragments (≤70 amino acids) from SepL are capable of targeting fusion proteins for secretion and translocation.

Indexed as

Amino Acid SequenceEscherichia coliEscherichia coli ProteinsMolecular ChaperonesMolecular Sequence DataProtein BindingProtein Sorting SignalsProtein TransportSequence AlignmentSequence Homology, Amino AcidEscherichia coli ProteinsMolecular ChaperonesProtein Sorting SignalsSepL protein, E coli

Identifiers

PMID20833800
PMCPMC2976445

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.