Evidence map›Paper›PMID 29042441›Full record

ArticleThe Journal of biological chemistry2017

Transcription factor 19 interacts with histone 3 lysine 4 trimethylation and controls gluconeogenesis via the nucleosome-remodeling-deacetylase complex.

Sabyasachi Sen, Sulagna Sanyal, Dushyant Kumar Srivastava, Dipak Dasgupta, Siddhartha Roy, Chandrima Das

Open access · hybridAbstract read
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 24 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 2 pooled it
1.7field-weighted citation impact, top 15% 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

24 citing papers in PubMed, 2 syntheses or guidelines pooled it, 37 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

6 authors at 2 institutions in 1 country.

Sabyasachi SenFrom the Biophysics and Structural Genomics Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, Kolkata-700064 and.
Sulagna SanyalFrom the Biophysics and Structural Genomics Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, Kolkata-700064 and.
Dushyant Kumar Srivastavathe Structural Biology and Bio-Informatics Division, CSIR-Indian Institute of Chemical Biology, 4 Raja S.C. Mullick Road, Kolkata-700032, India.
Dipak DasguptaFrom the Biophysics and Structural Genomics Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, Kolkata-700064 and.
Siddhartha Roythe Structural Biology and Bio-Informatics Division, CSIR-Indian Institute of Chemical Biology, 4 Raja S.C. Mullick Road, Kolkata-700032, India.
Chandrima DasFrom the Biophysics and Structural Genomics Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, Kolkata-700064 and chandrima.das@saha.ac.in.
Saha Institute of Nuclear Physics · INIndian Institute of Chemical Biology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transcription factor 19 (TCF19) has been reported as a type 1 diabetes-associated locus involved in maintenance of pancreatic β cells through a fine-tuned regulation of cell proliferation and apoptosis. TCF19 also exhibits genomic association with type 2 diabetes, although the precise molecular mechanism remains unknown. It harbors both a plant homeodomain and a forkhead-associated domain implicated in epigenetic recognition and gene regulation, a phenomenon that has remained unexplored. Here, we show that TCF19 selectively interacts with histone 3 lysine 4 trimethylation through its plant homeodomain finger. Knocking down TCF19 under high-glucose conditions affected many metabolic processes, including gluconeogenesis. We found that TCF19 overexpression represses

Indexed as

GluconeogenesisModels, MolecularProtein Processing, Post-TranslationalCell LineEpigenesis, GeneticGene Expression Regulation, EnzymologicHepatocytesHistonesHumansLysineMethylationMi-2 Nucleosome Remodeling and Deacetylase ComplexMolecular Docking SimulationMutagenesis, Site-DirectedMutationPeptide FragmentsCHD4 protein, humanHistonesLysineMi-2 Nucleosome Remodeling and Deacetylase ComplexPeptide FragmentsRecombinant ProteinsTCF19 protein, humanTranscription Factorsgene transcriptiongluconeogenesisglucose metabolismhistone deacetylationhistone H3 lysine 4 trimethylationhistone modificationnucleosome remodeling deacetylase (NuRD)PHD fingertranscription factortranscription repressor

Identifiers

PMID29042441
PMCPMC5733577
OpenAlexW2765942587

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.