Evidence map›Paper›PMID 28860194›Full record

ArticleThe Journal of biological chemistry2017

The bacterial arginine glycosyltransferase effector NleB preferentially modifies Fas-associated death domain protein (FADD).

Nichollas E Scott, Cristina Giogha, Georgina L Pollock, Catherine L Kennedy, Andrew I Webb, Nicholas A Williamson, Jaclyn S Pearson, Elizabeth L Hartland

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

29 citing papers in PubMed, 55 citations in OpenAlex.

  1. Mechanism of Bacterial ArginineACS catalysis · 2026
    Article
  2. Review
  3. Review
  4. Speaking the host language: howMicrobiology (Reading, England) · 2023
    Review
  5. Hybrid Vigor: Importance of Hybrid λ Phages in Early Insights in Molecular Biology.Microbiology and molecular biology reviews : MMBR · 2022
    Review
  6. FADD as a key molecular player in cancer progression.Molecular medicine (Cambridge, Mass.) · 2022
    Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Tubulin Folding Cofactor TBCB is a Target of theInternational journal of molecular sciences · 2020
    Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  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

8 authors at 1 institution in 1 country.

Nichollas E ScottFrom the Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne 3000, Australia, nichollas.scott@unimelb.edu.au.ORCID 0000-0003-2556-8316
Cristina GioghaFrom the Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne 3000, Australia.
Georgina L PollockFrom the Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne 3000, Australia.
Catherine L KennedyFrom the Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne 3000, Australia.
Andrew I WebbThe Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3052, Melbourne, Australia.
Nicholas A WilliamsonBio21 Molecular Science and Biotechnology Institute, University of Melbourne, Victoria 3010, Australia.
Jaclyn S PearsonFrom the Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne 3000, Australia.
Elizabeth L HartlandFrom the Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne 3000, Australia.ORCID 0000-0003-4254-2863
The University of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The inhibition of host innate immunity pathways is essential for the persistence of attaching and effacing pathogens such as enteropathogenic

Indexed as

ApoptosisProtein Processing, Post-TranslationalCitrobacter rodentiumEnteropathogenic Escherichia coliEscherichia coli InfectionsEscherichia coli ProteinsFas-Associated Death Domain ProteinGlycosyltransferasesHeLa CellsHumansProtein StabilityReceptor-Interacting Protein Serine-Threonine KinasesTNF Receptor-Associated Death Domain ProteinVirulence FactorsEscherichia coli ProteinsFADD protein, humanFas-Associated Death Domain ProteinGlycosyltransferasesNleB protein, E coliReceptor-Interacting Protein Serine-Threonine KinasesRIPK1 protein, humanTNF Receptor-Associated Death Domain ProteinVirulence Factorsbacterial effectorsEscherichia coli (E. coli)glycosylationinnate immunitypathogenesispost-translational modification (PTM)

Identifiers

PMID28860194
PMCPMC5655511
OpenAlexW2750786467

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.