ArticleExperimental & molecular medicine2026
Cardiomyocyte-enriched OTUD5 alleviates pathological myocardial hypertrophy by deubiquitinating STAT3 and modulating the STAT3-PGC-1α axis.
Article in Experimental & molecular medicine, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors.
Funding
Abstract
Pathological cardiac hypertrophy presents a important public health challenge, particularly in aging populations, highlighting the urgent need for novel therapeutic targets. This study investigates the role and molecular mechanisms of OTUD5 in pathological cardiac hypertrophy. OTUD5 expression is greatly increased in cardiomyocytes from hypertrophic hearts. Deleting cardiomyocyte-specific OTUD5 exacerbates myocardial hypertrophy induced by angiotensin II (Ang II) and transverse aortic constriction (TAC). By contrast, targeted overexpression of OTUD5 in cardiomyocytes alleviates Ang II-induced pathological hypertrophy. Mechanistically, we demonstrate that OTUD5 regulates STAT3 activity by removing the K63-linked ubiquitin chain at lysine 283 (K283) on STAT3 through its C224 residue. This process inhibits both phosphorylation and nuclear translocation of STAT3, effectively relieving its transcriptional repression of PGC1α and enhancing mitochondrial function within cardiomyocytes. Our research uncovers a new OTUD5-STAT3-PGC1α axis that modulates mitochondrial bioenergetics, suggesting it as a potential therapeutic target for pathological cardiac hypertrophy.
Identifiers
42888217What OpenQuestion holds
Registered trials
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.