Evidence map›Paper›PMID 33329381›Full record

ArticleFrontiers in endocrinology2020

PPARγ S273 Phosphorylation Modifies the Dynamics of Coregulator Proteins Recruitment.

Marieli Mariano Gonçalves Dias, Fernanda Aparecida Heleno Batista, Thais Helena Tittanegro, André Gustavo de Oliveira, Albane Le Maire, Felipe Rafael Torres, Helder Veras Ribeiro Filho, Leonardo Reis Silveira, Ana Carolina Migliorini Figueira

Open access · goldAbstract read
In one paragraph

Article in Frontiers in endocrinology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

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  2. GαMetabolites · 2026
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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

9 authors at 4 institutions in 2 countries.

Marieli Mariano Gonçalves DiasBrazilian Biosciences National Laboratory (LNBio), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, Brazil.
Fernanda Aparecida Heleno BatistaBrazilian Biosciences National Laboratory (LNBio), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, Brazil.
Thais Helena TittanegroBrazilian Biosciences National Laboratory (LNBio), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, Brazil.
André Gustavo de OliveiraMitochondrial Molecular Biology Laboratory, Obesity and Comorbidities Research Center (OCRC), Campinas, Brazil.
Albane Le MaireBrazilian Biosciences National Laboratory (LNBio), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, Brazil.
Felipe Rafael TorresBrazilian Biosciences National Laboratory (LNBio), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, Brazil.
Helder Veras Ribeiro FilhoBrazilian Biosciences National Laboratory (LNBio), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, Brazil.
Leonardo Reis SilveiraMitochondrial Molecular Biology Laboratory, Obesity and Comorbidities Research Center (OCRC), Campinas, Brazil.
Ana Carolina Migliorini FigueiraBrazilian Biosciences National Laboratory (LNBio), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, Brazil.
Universidade Estadual de Campinas (UNICAMP) · BRBrazilian Biosciences National Laboratory · BRBrazilian Center for Research in Energy and Materials · BRUniversité de Montpellier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nuclear receptor PPARγ is essential to maintain whole-body glucose homeostasis and insulin sensitivity, acting as a master regulator of adipogenesis, lipid, and glucose metabolism. Its activation through natural or synthetic ligands induces the recruitment of coactivators, leading to transcription of target genes such as cytokines and hormones. More recently, post translational modifications, such as PPARγ phosphorylation at Ser273 by CDK5 in adipose tissue, have been linked to insulin resistance trough the dysregulation of expression of a specific subset of genes. Here, we investigate how this phosphorylation may disturb the interaction between PPARγ and some coregulator proteins as a new mechanism that may leads to insulin resistance. Through cellular and

Indexed as

3T3 CellsAdipocytesAnimalsChlorocebus aethiopsCOS CellsCyclin-Dependent Kinase 5HEK293 CellsHumansInsulin ResistanceMicePhosphorylationPPAR gammaSerineCDK5 protein, humanCyclin-Dependent Kinase 5PPAR gammaSerinecoactivatorcoregulator interactioncorepressorinsulin resistancenuclear receptorsPPARgammaSer273 phosphorylation

Identifiers

PMID33329381
PMCPMC7729135
OpenAlexW3110599697

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.