Evidence map›Paper›PMID 8552662›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Retinoblastoma protein directly interacts with and activates the transcription factor NF-IL6.

P L Chen, D J Riley, S Chen-Kiang, W H Lee

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
10.1field-weighted citation impact, top 1% 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

88 citing papers in PubMed, 211 citations in OpenAlex.

  1. Article
  2. CDK6 activity in a recurring convergent kinase network motif.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023
    Article
  3. Review
  4. Review
  5. Arrhythmogenic Cardiomyopathy: the Guilty Party in Adipogenesis.Journal of cardiovascular translational research · 2017
    Review
  6. Article
  7. Cell Differentiation and Checkpoint.International journal of cancer research and molecular mechanisms · 2015
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. RB1, development, and cancer.Current topics in developmental biology · 2011
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

28 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

4 authors at 1 institution in 1 country.

P L ChenCenter for Molecular Medicine/Institute of Biotechnology, University of Texas Health Science Center at San Antonio 78245, USA.
D J Riley
S Chen-Kiang
W H Lee
The University of Texas Health Science Center at San Antonio · US

Funding

CANCER SUPPRESSION BY THE RETINOBLASTOMA GENER01CA058318 · NCI · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI LEE, WEN-HWA · 1992 to 2002
$825k
MOLECULAR MECHANISMS OF THE RETINOBLASTOMA FORMATIONR01EY005758 · NEI · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI LEE, WEN-HWA · 1985 to 2000
$367k
NCI NIH HHS CA58318NEI NIH HHS EY05758
6 · The paper itself

Abstract

The biological function of the retinoblastoma protein (RB) in the cell division cycle has been extensively documented, but its apparent role in differentiation remains largely unexplored. To investigate how RB is involved in differentiation, the U937 large-cell lymphoma line was induced to differentiate along a monocyte/macrophage lineage. During differentiation RB was found to interact directly through its simian virus 40 large tumor antigen (T antigen)-binding domain with NF-IL6, a member of the CAAT/enhancer-binding protein (C/EBP) family of transcription factors. NF-IL6 utilizes two distinct regions to bind to the hypophosphorylated form of RB in vitro and in cells. Wild-type but not mutant RB enhanced both binding activity of NF-IL6 to its cognate DNA sequences in vitro and promoter transactivation by NF-IL6 in cells. These findings indicate a novel biochemical function of RB: it activates, by an apparent chaperone-like activity, specific transcription factors important for differentiation. This contrasts with its sequestration and inactivation of other transcription factors, such as E2F-1, which promote progression of the cell cycle. Such disparate mechanisms may help to explain the dual role of RB in cell differentiation and the cell division cycle.

Indexed as

Amino Acid SequenceBase SequenceCCAAT-Enhancer-Binding ProteinsCell DifferentiationDNA-Binding ProteinsGene Expression RegulationHumansMolecular Sequence DataNuclear ProteinsOligodeoxyribonucleotidesPromoter Regions, GeneticProtein BindingRetinoblastoma ProteinSequence AlignmentSequence Homology, Amino AcidTranscription FactorsCCAAT-Enhancer-Binding ProteinsDNA-Binding ProteinsNuclear ProteinsOligodeoxyribonucleotidesRetinoblastoma ProteinTranscription Factors

Identifiers

PMID8552662
PMCPMC40259
OpenAlexW2029824360

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.