Evidence map›Paper›PMID 26299785›Full record

ReviewNature reviews. Microbiology2015

Structure and function of Fic proteins.

Craig R Roy, Jacqueline Cherfils

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Science advances · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Structural basis for selective AMPylation of Rac-subfamily GTPases byProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. The Impact ofFrontiers in microbiology · 2021
    Review
  12. Article
  13. Article
  14. Pathogens (Basel, Switzerland) · 2019
    Article
  15. Article
  16. A CaNature communications · 2019
    Article
  17. Article
  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

2 authors at 1 institution in 1 country.

Craig R RoyYale University School of Medicine, New Haven, Connecticut 06536, USA.
Jacqueline CherfilsLaboratoire de Biologie et Pharmacologie Appliquée, Centre National de la Recherche Scientifique-Ecole Normale Supérieure Cachan, 61 Avenue du Président Wilson, 94235 Cachan, France.
Yale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fic proteins are a family of proteins characterized by the presence of a conserved FIC domain that is involved in the modification of protein substrates by the addition of phosphate-containing compounds, including AMP and other nucleoside monophosphates, phosphocholine and phosphate. Fic proteins are widespread in bacteria, and various pathogenic species secrete Fic proteins as toxins that mediate post-translational modifications of host cell proteins, to interfere with cytoskeletal, trafficking, signalling or translation pathways in the host cell. In this Review, we discuss the current knowledge of the structure, function and regulation of Fic proteins and consider important areas for future research.

Indexed as

BacteriaBacterial ProteinsCoenzymesEscherichia coli ProteinsProtein Structure, TertiarySubstrate SpecificityBacterial ProteinsCoenzymesEscherichia coli Proteinsfic protein, E coli

Identifiers

PMID26299785
OpenAlexW1186606388

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.