Evidence map›Paper›PMID 19636396›Full record

ReviewNuclear receptor signaling2009

Naturally occurring C-terminal splice variants of nuclear receptors.

Michiel van der Vaart, Marcel J M Schaaf

Open access · hybridAbstract readReview
In one paragraph

Review in Nuclear receptor signaling, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

16 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Non-coding RNA crosstalk with nuclear receptors in liver disease.Biochimica et biophysica acta. Molecular basis of disease · 2021
    Review
  3. Glucocorticoid Receptor β (GRβ): Beyond Its Dominant-Negative Function.International journal of molecular sciences · 2021
    Review
  4. Review
  5. Article
  6. Review
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  9. Review
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  11. PPAR gamma, bioactive lipids, and cancer progression.Frontiers in bioscience (Landmark edition) · 2012
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
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.

Michiel van der VaartMolecular Cell Biology, Institute of Biology (IBL), Leiden University, Leiden, The Netherlands.
Marcel J M Schaaf
Leiden University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alternative mRNA splicing in the region encoding the C-terminus of nuclear receptors results in receptor variants lacking the entire ligand-binding domain (LBD), or a part of it, and instead contain a sequence of splice variant-specific C-terminal amino acids. A total of thirteen such splice variants have been shown to occur in vertebrates, and at least nine occur in humans. None of these receptor variants appear to be able to bind endogenous ligands and to induce transcription on promoters containing the response element for the respective canonical receptor variant. Interestingly, ten of these C-terminal splice variants have been shown to display dominant-negative activity on the transactivational properties of their canonical equivalent. Research on most of these splice variants has been limited, and the dominant-negative effect of these receptor variants has only been demonstrated in reporter assays in vitro, using transiently transfected receptors and reporter constructs. Therefore, the in vivo function and relevance of most C-terminal splice variants remains unclear. By reviewing the literature on the human glucocorticoid receptor beta-isoform (hGRbeta), we show that the dominant-negative effect of hGRbeta is well established using more physiologically relevant readouts. The hGR beta-isoform may alter gene transcription independent from the canonical receptor and increased hGRbeta levels correlate with glucocorticoid resistance and the occurrence of several immune-related diseases. Thus, available data suggests that C-terminal splice variants of nuclear receptors act as dominant-negative inhibitors of receptor-mediated signaling in vivo, and that aberrant expression of these isoforms may be involved in the pathogenesis of a variety of diseases.

Indexed as

RNA SplicingAmino Acid SequenceAnimalsGene Expression RegulationHumansMolecular Sequence DataProtein Structure, TertiaryReceptors, Cytoplasmic and NuclearReceptors, Glucocorticoidglucocorticoid receptor betaReceptors, Cytoplasmic and NuclearReceptors, Glucocorticoid

Identifiers

PMID19636396
PMCPMC2716050
OpenAlexW1605078883

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.