Evidence map›Paper›PMID 8887632›Full record

ArticleMolecular and cellular biology1996

RIP-140 interacts with multiple nuclear receptors by means of two distinct sites.

F L'Horset, S Dauvois, D M Heery, V Cavaillès, M G Parker

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 1 pooled it
8.8field-weighted citation impact, top 2% 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

41 citing papers in PubMed, 1 synthesis or guideline pooled it, 130 citations in OpenAlex.

  1. Pooled it
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  11. Structural and Functional Diversity of Estrogen Receptor Ligands.Current topics in medicinal chemistry · 2015
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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.

F L'HorsetMolecular Endocrinology Laboratory, Imperial Cancer Research Fund, London, United Kingdom.
S Dauvois
D M Heery
V Cavaillès
M G Parker
The Honourable Society of Lincoln's Inn · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have characterized two distinct binding sites, called site 1 and site 2, in the nuclear protein RIP-140 which interact with the ligand binding domain of the estrogen receptor both in solution and when the receptor is bound to DNA. Both sites are capable of independently interacting with other nuclear receptors, including the thyroid hormone and retinoic acid receptors, but they are not identical since the interaction with retinoid X receptor is mediated primarily by site 1. The interaction is enhanced by agonists but not by antagonists, and the in vitro binding activities to a number of mutant receptors correlate with their abilities to stimulate transcription in vivo. When RIP-140 is fused to heterologous DNA binding domains, it is able to stimulate the transcription of reporter genes in both yeast and mammalian cells. Thus, RIP-140 is likely to function as a bridging protein between receptors and the basal transcription machinery and thereby stimulate the transcription of target genes.

Indexed as

Transcription, GeneticAdaptor Proteins, Signal TransducingAnimalsBinding SitesCell LineDNAGenes, ReporterGlutathione TransferaseHumansLigandsMammalsNuclear ProteinsNuclear Receptor Interacting Protein 1Receptors, Cytoplasmic and NuclearReceptors, EstrogenReceptors, Retinoic AcidAdaptor Proteins, Signal TransducingDNAGlutathione TransferaseLigandsNuclear ProteinsNuclear Receptor Interacting Protein 1Receptors, Cytoplasmic and NuclearReceptors, EstrogenReceptors, Retinoic AcidReceptors, Thyroid HormoneRecombinant Fusion Proteins

Identifiers

PMID8887632
PMCPMC231605
OpenAlexW1864394606

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.