Evidence map›Paper›PMID 22926519›Full record

ReviewOncogene2013

Far upstream element binding protein 1: a commander of transcription, translation and beyond.

J Zhang, Q M Chen

Open access · greenAbstract readReview
In one paragraph

Review in Oncogene, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing 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.

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

77 citing papers in PubMed, 122 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. A dual effect of FUBP1 onRNA (New York, N.Y.) · 2025
    Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Landscape of NcRNAs involved in drug resistance of breast cancer.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

17 more citing papers are in PubMed but not listed here.

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.

J ZhangDepartment of Pharmacology, University of Arizona, Tucson, AZ 85724, USA.
Q M Chen
University of Arizona · US

Funding

Training in Environmental Toxicology of Human DiseaseT32ES007091 · NIEHS · UNIVERSITY OF ARIZONA · PI Nathan J Cherrington · 1985 to 2026
$10.7M
Steroid As Cytoprotectants against Oxidative ToxicityR01HL076530 · NHLBI · UNIVERSITY OF ARIZONA · PI CHEN, QIN M · 2004 to 2007
$1.5M
Translational Control of Oxidative Stress in Myocardial InfarctionR01HL089958 · NHLBI · UNIVERSITY OF ARIZONA · PI CHEN, QIN M · 2009 to 2010
$908k
Nrf2 Protein Translation in Oxidative StressR21ES017473 · NIEHS · UNIVERSITY OF ARIZONA · PI CHEN, QIN M · 2009 to 2010
$414k
NHLBI NIH HHS R01 HL 076530NHLBI NIH HHS R01 HL076530NHLBI NIH HHS R01 HL089958NIEHS NIH HHS R21 ES017473NIEHS NIH HHS R21ES017473NIEHS NIH HHS T32 ES007091
6 · The paper itself

Abstract

The far upstream binding protein 1 (FBP1) was first identified as a DNA-binding protein that regulates c-Myc gene transcription through binding to the far upstream element (FUSE) in the promoter region 1.5 kb upstream of the transcription start site. FBP1 collaborates with TFIIH and additional transcription factors for optimal transcription of the c-Myc gene. In recent years, mounting evidence suggests that FBP1 acts as an RNA-binding protein and regulates mRNA translation or stability of genes, such as GAP43, p27(Kip) and nucleophosmin. During retroviral infection, FBP1 binds to and mediates replication of RNA from Hepatitis C and Enterovirus 71. As a nuclear protein, FBP1 may translocate to the cytoplasm in apoptotic cells. The interaction of FBP1 with p38/JTV-1 results in FBP1 ubiquitination and degradation by the proteasomes. Transcriptional and post-transcriptional regulations by FBP1 contribute to cell proliferation, migration or cell death. FBP1 association with carcinogenesis has been reported in c-Myc dependent or independent manner. This review summarizes biochemical features of FBP1, its mechanism of action, FBP family members and the involvement of FBP1 in carcinogenesis.

Indexed as

Protein BiosynthesisTranscription, GeneticAnimalsDNA-Binding ProteinsDNA HelicasesGene Expression RegulationHumansRNA-Binding ProteinsDNA-Binding ProteinsDNA HelicasesFUBP1 protein, humanRNA-Binding Proteins

Identifiers

PMID22926519
PMCPMC4968413
OpenAlexW2028056951

What OpenQuestion holds

Textmetadata
LicenceTDM
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.