Evidence map›Paper›PMID 10411930›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Elevated retinoic acid receptor beta(4) protein in human breast tumor cells with nuclear and cytoplasmic localization.

K M Sommer, L I Chen, P M Treuting, L T Smith, K Swisshelm

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

12 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Insoluble, speckled cytosolic distribution of retinoic acid receptor alpha protein as a marker of hepatic stellate cell activation in vitro.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2009
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. 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.

K M SommerDepartment of Pathology, University of Washington, Seattle, WA 98195, USA.
L I Chen
P M Treuting
L T Smith
K Swisshelm
University of Washington · US

Funding

PILOT STUDY--CLINICAL NUTRITION RESEARCHP30DK035816 · NIDDK · UNIVERSITY OF WASHINGTON · PI Ellen A Schur · 1986 to 2026
$30.4M
GENETIC APPROACHES TO AGING RESEARCHT32AG000057 · NIA · UNIVERSITY OF WASHINGTON · PI RABINOVITCH, PETER S · 1985 to 2019
$14.2M
STRUCTURAL PROTEINS IN DISORDERS OF KERATINIZATIONP01AR021557 · NIAMS · UNIVERSITY OF WASHINGTON · PI STEPHENS, KAREN G · 1986 to 2001
$2.8M
COMPARATIVE MEDICINET32RR007019 · NCRR · UNIVERSITY OF WASHINGTON · PI LIGGITT, HARRY DENNY · 1985 to 2006
$2.1M
MOLECULAR TRAINING PROGRAM IN CANCER RESEARCH - COMPETINT32CA009437 · NCI · UNIVERSITY OF WASHINGTON · PI LOEB, LAWRENCE A · 1985 to 2001
$1.1M
NCI NIH HHS T32 CA009437NCI NIH HHS T32CA 09437NCRR NIH HHS T32 RR007019NCRR NIH HHS T32 RR07019NIAMS NIH HHS P01 AR021557NIA NIH HHS T32 AG000057NIDDK NIH HHS P30 DK035816NIDDK NIH HHS P30-DK35816
6 · The paper itself

Abstract

The transcription factor retinoic acid receptor beta(2) (RARbeta(2)) is a potent inhibitor of breast cancer cells in vitro, and studies suggest that RARbeta expression is lost in primary breast cancer. Although RARbeta(2) is selectively down-regulated at the mRNA level in breast tumor cells, we show that expression of an RARbeta protein is elevated in five of five breast tumor cell lines relative to normal human mammary epithelial cells. Subsequent analysis identified this protein as the translation product of the human RARbeta(4) transcript. Unlike the previously characterized mouse RARbeta(4) isoform, the human RARbeta(4) retains only half of a DNA-binding domain and lacks a ligand-independent transactivation domain at its N terminus. The RARbeta(4) protein localizes to the cytoplasm and to subnuclear compartments that resemble nuclear bodies. The structure and preliminary characterizations of human RARbeta(4), coupled with the observation that its expression is greatly elevated in breast tumor cell lines, support the hypothesis that RARbeta(4) functions as a dominant-negative repressor of RAR-mediated growth suppression.

Indexed as

Base SequenceBreast NeoplasmsCell NucleusCloning, MolecularCytoplasmGene Expression Regulation, NeoplasticHumansImmunohistochemistryMolecular Sequence DataNeoplasm ProteinsOpen Reading FramesProtein BiosynthesisReceptors, Retinoic AcidRepressor ProteinsRNA, MessengerTumor Cells, CulturedNeoplasm ProteinsReceptors, Retinoic AcidRepressor Proteinsretinoic acid receptor betaRNA, Messenger

Identifiers

PMID10411930
PMCPMC17571
OpenAlexW2083029854

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.