Evidence map›Paper›PMID 42319436›Full record

ReviewJournal of molecular medicine (Berlin, Germany)2026

Molecular regulation of PGC-1α: from protein-protein interactions and post-translational modifications to pharmacological modulation.

William Q Rios, Carlos M Silva, Rita Ferreira, José R B Gomes

Abstract readReview
In one paragraph

Review in Journal of molecular medicine (Berlin, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Article
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

4 authors.

William Q RiosDepartment of Chemistry, CICECO-Aveiro Institute of Materials, University of Aveiro, Aveiro, 3810-193, Portugal.ORCID http://orcid.org/0000-0001-5600-8771
Carlos M SilvaDepartment of Chemical Engineering, Faculty of Sciences and Technology, CERES, University of Coimbra, Rua Sílvio Lima, Polo II, Coimbra, 3030-790, Portugal.ORCID http://orcid.org/0000-0002-9310-2457
Rita FerreiraDepartment of Chemistry, LAQV-REQUIMTE, University of Aveiro, Aveiro, 3810-193, Portugal. ritaferreira@ua.pt.ORCID http://orcid.org/0000-0002-6872-4051
José R B GomesDepartment of Chemistry, CICECO-Aveiro Institute of Materials, University of Aveiro, Aveiro, 3810-193, Portugal.ORCID http://orcid.org/0000-0001-5993-1385

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxisome proliferator-activated receptor gamma coactivator 1α (PGC-1α) is a master transcriptional coactivator responsible for regulating cellular energy metabolism and mitochondrial biogenesis across high-energy tissues such as the heart, skeletal muscle, and brown adipose tissue. To orchestrate its regulatory functions, PGC-1α interacts with a diverse array of transcription factors such as peroxisome proliferator-activated receptors (PPARs), estrogen-related receptors (ERRs), and nuclear respiratory factors (NRFs), which is facilitated by its dynamic three-dimensional structure, the presence of distinct functional domains, and the ability to be modulated via post-translational modifications. This review examines the protein's interactions with key nuclear receptors and the biological consequences of these complexes, including the regulation of thermogenesis, gluconeogenesis, and fatty acid oxidation. Furthermore, we discuss the extensive post-translational modifications-including phosphorylation, acetylation, methylation, O-GlcNAcylation, and ubiquitination-that tightly regulate PGC-1α stability and coactivation efficiency. Finally, this review highlights recent progress in the identification of small molecule modulators, such as the activator ZLN005 and the inhibitor SR18292, evaluating their physiological outcomes and potential as therapeutic agents for metabolic disorders and cancer, while addressing the challenges posed by the protein's structural disorder in drug discovery.

Indexed as

Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaProtein Processing, Post-TranslationalAnimalsEnergy MetabolismHumansProtein BindingPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaEnergy metabolismIntrinsically disordered proteinPost-translational controlTranscriptional coactivator

Identifiers

PMID42319436
PMCPMC13282225

What OpenQuestion holds

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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.