Evidence map›Paper›PMID 27852823›Full record

ArticleThe Journal of biological chemistry2017

Phosphorylation of Human Retinoid X Receptor α at Serine 260 Impairs Its Subcellular Localization, Receptor Interaction, Nuclear Mobility, and 1α,25-Dihydroxyvitamin D3-dependent DNA Binding in Ras-transformed Keratinocytes.

Sylvester Jusu, John F Presley, Richard Kremer

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

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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

3 authors at 2 institutions in 1 country.

Sylvester JusuFrom the Department of Medicine, Calcium Research Laboratory, Royal Victoria Hospital, McGill University, Montreal, Quebec H4A 3J1.
John F Presleythe Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 0C7, and.
Richard KremerFrom the Department of Medicine, Calcium Research Laboratory, Royal Victoria Hospital, McGill University, Montreal, Quebec H4A 3J1, richard.kremer@mcgill.ca.
McGill University · CAMcGill University Health Centre · CA

Funding

CIHR MOP10839
6 · The paper itself

Abstract

Human retinoid X receptor α (hRXRα) plays a critical role in DNA binding and transcriptional activity through heterodimeric association with several members of the nuclear receptor superfamily, including the human vitamin D receptor (hVDR). We previously showed that hRXRα phosphorylation at serine 260 through the Ras-Raf-MAPK ERK1/2 activation is responsible for resistance to the growth inhibitory effects of 1α,25-dihydroxyvitamin D

Indexed as

Active Transport, Cell NucleusAmino Acid SubstitutionCalcitriolCell Line, TransformedCell NucleusExtracellular Signal-Regulated MAP KinasesHumansKeratinocytesMutation, MissensePhosphorylationras ProteinsRetinoid X Receptor alphaSerineCalcitriolExtracellular Signal-Regulated MAP Kinasesras ProteinsRetinoid X Receptor alphaSerinefluorescence loss in photobleaching (FLIP)fluorescence resonance energy transfer (FRET)mitogen-activated protein kinase (MAPK)phosphorylationretinoidretinoid X receptorvitamin Dvitamin D receptor

Identifiers

PMID27852823
PMCPMC5270490
OpenAlexW2552675883

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.