Associated Papers
PNPLA3-I148M is a neomorph that interferes with two primary hepatic triglyceride clearance pathways.
Sherman DJ et al.
Cell Reports, 2025
PNPLA3(148M) is a gain-of-function mutation that promotes hepatic steatosis by inhibiting ATGL-mediated triglyceride hydrolysis.
Wang Y et al.
Journal of Hepatology, 2025
Unlocking the influence of PNPLA3 mutations on lipolysis: Insights into lipid droplet formation and metabolic dynamics in metabolic dysfunction-associated steatotic liver disease.
Roy A et al.
Biochimica Et Biophysica Acta. General Subjects, 2025
Lipid droplet targeting of the lipase coactivator ABHD5 and the fatty liver disease-causing variant PNPLA3 I148M is required to promote liver steatosis.
Teskey G et al.
The Journal of Biological Chemistry, 2025
PNPLA3 is a triglyceride lipase that mobilizes polyunsaturated fatty acids to facilitate hepatic secretion of large-sized very low-density lipoprotein.
Johnson SM et al.
Nature Communications, 2024
Substrate-Specific Function of PNPLA3 Facilitates Hepatic VLDL-Triglyceride Secretion During Stimulated Lipogenesis.
Johnson S et al.
Biorxiv : the Preprint Server for Biology, 2023
ABHD5-A Regulator of Lipid Metabolism Essential for Diverse Cellular Functions.
Schratter M et al.
Metabolites, 2022
Modeling PNPLA3-Associated NAFLD Using Human-Induced Pluripotent Stem Cells.
Tilson SG et al.
Hepatology (baltimore, Md.), 2021
The PNPLA3-I148M Variant Confers an Antiatherogenic Lipid Profile in Insulin-resistant Patients.
Luukkonen PK et al.
The Journal of Clinical Endocrinology and Metabolism, 2021
Discovery and Targeting of the Signaling Controls of PNPLA3 to Effectively Reduce Transcription, Expression, and Function in Pre-Clinical NAFLD/NASH Settings.
Schwartz BE et al.
Cells, 2020
The PNPLA3-I148M variant increases polyunsaturated triglycerides in human adipose tissue.
Qadri S et al.
Liver International : Official Journal of the International Association for the Study of the Liver, 2020
Human PNPLA3-I148M variant increases hepatic retention of polyunsaturated fatty acids.
Luukkonen PK et al.
Jci Insight, 2019
PNPLA3, CGI-58, and Inhibition of Hepatic Triglyceride Hydrolysis in Mice.
Wang Y et al.
Hepatology (baltimore, Md.), 2019
Missense Mutant Patatin-Like Phospholipase Domain Containing 3 Alters Lipid Droplet Turnover in Partnership With CGI-58.
McHenry S et al.
Hepatology (baltimore, Md.), 2019
Accumulation of PNPLA3 on lipid droplets is the basis of associated hepatic steatosis.
BasuRay S et al.
Proceedings of the National Academy of Sciences of the United States of America, 2019
Dynamic interactions of ABHD5 with PNPLA3 regulate triacylglycerol metabolism in brown adipocytes.
Yang A et al.
Nature Metabolism, 2019
Patatin-like phospholipase domain–containing protein 3 promotes transfer of essential fatty acids from triglycerides to phospholipids in hepatic lipid droplets.
Mitsche MA et al.
The Journal of Biological Chemistry, 2018
The PNPLA3 variant associated with fatty liver disease (I148M) accumulates on lipid droplets by evading ubiquitylation.
BasuRay S et al.
Hepatology (baltimore, Md.), 2017
Transcriptional regulation of PNPLA3 and its impact on susceptibility to nonalcoholic fatty liver Disease (NAFLD) in humans.
Liu W et al.
Aging, 2016
PNPLA3 genetic variation in alcoholic steatosis and liver disease progression.
Stickel F et al.
Hepatobiliary Surgery and Nutrition, 2015
Pnpla3I148M knockin mice accumulate PNPLA3 on lipid droplets and develop hepatic steatosis.
Smagris E et al.
Hepatology (baltimore, Md.), 2015
NAFLD. PNPLA3 variant and hepatic steatosis.
Ray K
Nature Reviews. Gastroenterology & Hepatology, 2014
PNPLA3/adiponutrin functions in lipid droplet formation.
Chamoun Z et al.
Biology of the Cell, 2013
Expression and characterization of a PNPLA3 protein isoform (I148M) associated with nonalcoholic fatty liver disease.
Huang Y et al.
The Journal of Biological Chemistry, 2011
Recent progress in phospholipase A₂ research: from cells to animals to humans.
Murakami M et al.
Progress in Lipid Research, 2011
Pnpla3/Adiponutrin deficiency in mice does not contribute to fatty liver disease or metabolic syndrome.
Basantani MK et al.
Journal of Lipid Research, 2011
A sequence variation (I148M) in PNPLA3 associated with nonalcoholic fatty liver disease disrupts triglyceride hydrolysis.
He S et al.
The Journal of Biological Chemistry, 2010
Suppressed Fat Mobilization Due to PNPLA3 rs738409 -Associated Liver Damage in Heavy Drinkers: The Liver Damage Feedback Hypothesis.
Rausch V et al.
Advances in Experimental Medicine and Biology, 0