Evidence map›Paper›PMID 22864569›Full record

ArticleNature communications2012

Proteomic screen reveals Fbw7 as a modulator of the NF-κB pathway.

Azadeh Arabi, Karim Ullah, Rui M M Branca, Johan Johansson, Daniel Bandarra, Moritz Haneklaus, Jing Fu, Ingrid Ariës, Peter Nilsson, Monique L Den Boer and 6 more

Registry-linked trialOpen access · hybridAbstract read
In one paragraph

Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT07765251 (Smoking is Associated With Angiogenesis Through the Expression of FBXW7 and KLF2 in Periodontal Disease), which is not on this map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
3.9field-weighted citation impact, top 6% 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.

NCT07765251 completednot on this mapstarted 2024, after this paper: background citation

Smoking is Associated With Angiogenesis Through the Expression of FBXW7 and KLF2 in Periodontal Disease

TypeobservationalSponsorInonu UniversityRan2024 to 2024Enrolled114ConditionsGingivitis
3 · Its place in the literature

Who cites it

59 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
  2. Article
  3. The ubiquitin ligase FBXW7 regulates epithelial pyroptosis in severe asthma.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Article
  4. Article
  5. Epidermal growth factor receptor (EGFR) is a target of the tumor-suppressor E3 ligase FBXW7.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Tumor Suppressor FBXW7 and Its Regulation of DNA Damage Response and Repair.Frontiers in cell and developmental biology · 2021
    Review
  16. Article
  17. Review
  18. Review
  19. Review
  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

16 authors at 6 institutions in 4 countries.

Azadeh ArabiDepartment of Cell and Molecular Biology, Karolinska Institutet, 171 77 Stockholm, Sweden. azadeh.arabi@ki.se
Karim Ullah
Rui M M Branca
Johan Johansson
Daniel Bandarra
Moritz Haneklaus
Jing Fu
Ingrid Ariës
Peter Nilsson
Monique L Den Boer
Katja Pokrovskaja
Dan Grandér
Gutian Xiao
Sonia Rocha
Janne Lehtiö
Olle Sangfelt
Karolinska Institutet · SERotterdam University of Applied Sciences · NLScience for Life Laboratory · SEUniversity of Dundee · GBUniversity of Pittsburgh · USSwedish Defence University · SE

Funding

HTLV deregulation of NF-kappaB2 p100 processing in tumorR01CA116616 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI XIAO, GUTIAN · 2006 to 2010
$1.1M
Cancer Research UK 12918Cancer Research UK A12918NCI NIH HHS R01 CA116616
6 · The paper itself

Abstract

Fbw7 is a ubiquitin-ligase that targets several oncoproteins for proteolysis, but the full range of Fbw7 substrates is not known. Here we show that by performing quantitative proteomics combined with degron motif searches, we effectively screened for a more complete set of Fbw7 targets. We identify 89 putative Fbw7 substrates, including several disease-associated proteins. The transcription factor NF-κB2 (p100/p52) is one of the candidate Fbw7 substrates. We show that Fbw7 interacts with p100 via a conserved degron and that it promotes degradation of p100 in a GSK3β phosphorylation-dependent manner. Fbw7 inactivation increases p100 levels, which in the presence of NF-κB pathway stimuli, leads to increased p52 levels and activity. Accordingly, the apoptotic threshold can be increased by loss of Fbw7 in a p100-dependent manner. In conclusion, Fbw7-mediated destruction of p100 is a regulatory component restricting the response to NF-κB2 pathway stimulation.

Indexed as

Cell Cycle ProteinsCell LineCell Line, TumorComputational BiologyF-Box ProteinsF-Box-WD Repeat-Containing Protein 7Glycogen Synthase Kinase 3HumansImmunoblottingImmunoprecipitationNF-kappa B p52 SubunitPhosphorylationProteomicsSignal TransductionTandem Mass SpectrometryUbiquitin-Protein LigasesCell Cycle ProteinsF-Box ProteinsF-Box-WD Repeat-Containing Protein 7FBXW7 protein, humanGlycogen Synthase Kinase 3NF-kappa B p52 SubunitUbiquitin-Protein Ligases

Identifiers

PMID22864569
PMCPMC4354031
OpenAlexW2021056570

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

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.