Evidence map›Paper›PMID 9001221›Full record

ArticleMolecular and cellular biology1997

The intracisternal A-particle proximal enhancer-binding protein activates transcription and is identical to the RNA- and DNA-binding protein p54nrb/NonO.

A Basu, B Dong, A R Krainer, C C Howe

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

43 citing papers in PubMed, 100 citations in OpenAlex.

  1. NONO regulates mJournal of experimental & clinical cancer research : CR · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. ArcRNAs and the formation of nuclear bodies.Mammalian genome : official journal of the International Mammalian Genome Society · 2022
    Review
  7. Article
  8. Frontiers in molecular biosciences · 2022
    Article
  9. Article
  10. NONO and tumorigenesis: More than splicing.Journal of cellular and molecular medicine · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Simvastatin reduces melanoma progression in a murine model.International journal of oncology · 2013
    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

4 authors at 2 institutions in 1 country.

A BasuThe Wistar Institute, Philadelphia, Pennsylvania 19104, USA.
B Dong
A R Krainer
C C Howe
Cold Spring Harbor Laboratory · USThe Wistar Institute · US

Funding

Tumor Microenvironment and MetastasisP30CA010815 · NCI · WISTAR INSTITUTE · PI Luis J Montaner · 1985 to 2026
$75.9M
GENE EXPRESSION AND MAMMALIAN DEVELOPMENTR01GM037762 · NIGMS · WISTAR INSTITUTE · PI HOWE, CHIN C · 1987 to 1994
–
DNA METHYLATION AND DEVELOPMENTR01GM047421 · NIGMS · WISTAR INSTITUTE · PI HOWE, CHIN C · 1992 to 1995
–
NCI NIH HHS CA10815NIGMS NIH HHS GM37762NIGMS NIH HHS GM47421
6 · The paper itself

Abstract

The long terminal repeats of murine intracisternal A particles (IAPs) contain an IAP proximal enhancer (IPE) element that is inactive in murine F9 embryonal carcinoma cells and active in the parietal endoderm cell line PYS-2. The element binds efficiently to a 60-kDa IPE-binding protein (IPEB) present in PYS-2 cells but poorly to F9 proteins, suggesting a role for IPEB in regulating IAP expression. We have purified calf thymus IPEB, which binds to the IPE and transactivates a reporter gene in HeLa cell extracts. Based on the peptide sequence of the purified calf IPEB, we have cloned a 420-bp cDNA and showed that the encoded protein is the homolog of human p54nrb and mouse NonO, which are characterized by the presence of two RNA recognition motifs. We show that p54nrb is an IPE-binding transcription activator with its DNA-binding and activation domains in the N- and C-terminal halves, respectively. The activation domain of p54nrb is active in HeLa, PYS-2, and F9 cells, whereas p54nrb as a whole molecule is active in HeLa and PYS-2 cells but not in F9 cells. Thus, the lack of activity of p54nrb in F9 cells is due to an ineffective DNA-binding domain. We demonstrate that p54nrb also binds to a pre-mRNA. Based on the close sequence relatedness of this protein to PSF, which is required for pre-mRNA splicing in vitro, we discuss the possibility that p54nrb has dual roles in transcription and splicing.

Indexed as

Nuclear Matrix-Associated ProteinsAnimalsCattleCell LineCloning, MolecularCyclin D1DNA-Binding ProteinsEnhancer Elements, GeneticGenes, Intracisternal A-ParticleHeLa CellsHumansMiceMolecular WeightNuclear ProteinsOctamer Transcription FactorsProto-Oncogene ProteinsCyclin D1DNA-Binding ProteinsNONO protein, humanNuclear Matrix-Associated ProteinsNuclear ProteinsOctamer Transcription FactorsProto-Oncogene ProteinsRecombinant Fusion ProteinsRNA-Binding ProteinsRNA PrecursorsTrans-Activators

Identifiers

PMID9001221
PMCPMC231793
OpenAlexW2159591573

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.