Evidence map›Paper›PMID 17397945›Full record

ArticleBiochimica et biophysica acta2007

The direct p53 target gene, FLJ11259/DRAM, is a member of a novel family of transmembrane proteins.

Joanna S Kerley-Hamilton, Aimee M Pike, Justine A Hutchinson, Sarah J Freemantle, Michael J Spinella

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Knockdown of Transmembrane Protein 150A (Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2022
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  6. The fourth transmembrane helix is important for DRAM function.Acta biochimica et biophysica Sinica · 2016
    Article
  7. Autophagy in Diabetic Retinopathy.Current neuropharmacology · 2016
    Review
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  14. Article
  15. Article
  16. Article
  17. Inactivation of CDK2 is synthetically lethal to MYCN over-expressing cancer cells.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  18. Review
  19. 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

5 authors at 1 institution in 1 country.

Joanna S Kerley-HamiltonDepartment of Pharmacology and Toxicology, Dartmouth Medical School, Hanover, NH03755, USA.
Aimee M Pike
Justine A Hutchinson
Sarah J Freemantle
Michael J Spinella
Dartmouth College · US

Funding

Retinoid Tumor Differentiation MechanismsR01CA104312 · NCI · DARTMOUTH COLLEGE · PI SPINELLA, MICHAEL J · 2004 to 2008
$1.3M
NCI NIH HHS R01 CA104312NCI NIH HHS R01-CA104312
6 · The paper itself

Abstract

The tumor suppressor p53 regulates diverse biological processes primarily via activation of downstream target genes. Even though many p53 target genes have been described, the precise mechanisms of p53 biological actions are uncertain. In previous work we identified by microarray analysis a candidate p53 target gene, FLJ11259/DRAM. In this report we have identified three uncharacterized human proteins with sequence homology to FLJ11259, suggesting that FLJ11259 is a member of a novel family of proteins with six transmembrane domains. Several lines of investigation confirm FLJ11259 is a direct p53 target gene. p53 siRNA prevented cisplatin-mediated up-regulation of FLJ11259 in NT2/D1 cells. Likewise in HCT116 p53+/+ cells and MCF10A cells, FLJ11259 is induced by cisplatin treatment but to a much lesser extent in isogenic p53-suppressed cells. A functional p53 response element was identified 22.3 kb upstream of the first coding exon of FLJ11259 and is shown to be active in reporter assays. In addition, chromatin immunoprecipitation assays indicate that p53 binds directly to this element in vivo and that binding is enhanced following cisplatin treatment. Confocal microscopy showed that an FLJ-GFP fusion protein localizes mainly in a punctate pattern in the cytoplasm. Overexpression studies in Cos-7, Saos2, and NT2/D1 cells suggest that FLJ11259 is associated with increased clonal survival. In summary, we have identified FLJ11259/DRAM as a p53-inducible member of a novel family of transmembrane proteins. FLJ11259/DRAM may be an important modulator of p53 responses in diverse tumor types.

Indexed as

Cell LineCisplatinEnhancer Elements, GeneticGene Expression RegulationHumansMembrane ProteinsProteinsRNA, Small InterferingTumor Suppressor Protein p53CisplatinDRAM1 protein, humanMembrane ProteinsProteinsRNA, Small InterferingTumor Suppressor Protein p53

Identifiers

PMID17397945
PMCPMC1936437
OpenAlexW2153852986

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.