Associated Papers
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
Lipid droplet targeting of ABHD5 and PNPLA3 I148M is required to promote liver steatosis.
Teskey G et al.
Biorxiv : the Preprint Server for Biology, 2024
Identification of motifs and mechanisms for lipid droplet targeting of the lipolytic inhibitors G0S2 and HIG2.
Campbell LE et al.
Journal of Cell Science, 2022
Structural and functional insights into ABHD5, a ligand-regulated lipase co-activator.
Tseng YY et al.
Scientific Reports, 2022
Adipose Triglyceride Lipase in Hepatic Physiology and Pathophysiology.
Li T et al.
Biomolecules, 2021
Forcing ATGL expression in hepatocarcinoma cells imposes glycolytic rewiring through PPAR-α/p300-mediated acetylation of p53.
Di Leo L et al.
Oncogene, 2019
Molecular Basis of ABHD5 Lipolysis Activation.
Sanders MA et al.
Scientific Reports, 2017
Clinical and molecular characterization of a novel PLIN1 frameshift mutation identified in patients with familial partial lipodystrophy.
Kozusko K et al.
Diabetes, 2015
Identification of a novel phosphorylation site in adipose triglyceride lipase as a regulator of lipid droplet localization.
Xie X et al.
American Journal of Physiology. Endocrinology and Metabolism, 2014
Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover.
Olzmann JA et al.
Proceedings of the National Academy of Sciences of the United States of America, 2013
Contribution of novel ATGL missense mutations to the clinical phenotype of NLSD-M: a strikingly low amount of lipase activity may preserve cardiac function.
Tavian D et al.
Human Molecular Genetics, 2012
Human frame shift mutations affecting the carboxyl terminus of perilipin increase lipolysis by failing to sequester the adipose triglyceride lipase (ATGL) coactivator AB-hydrolase-containing 5 (ABHD5).
Gandotra S et al.
The Journal of Biological Chemistry, 2011
Interaction between the triglyceride lipase ATGL and the Arf1 activator GBF1.
Ellong EN et al.
Plos One, 2011
Differential control of ATGL-mediated lipid droplet degradation by CGI-58 and G0S2.
Lu X et al.
Cell Cycle (georgetown, Tex.), 2010
Characterization of desnutrin functional domains: critical residues for triacylglycerol hydrolysis in cultured cells.
Duncan RE et al.
Journal of Lipid Research, 2010
The lack of the C-terminal domain of adipose triglyceride lipase causes neutral lipid storage disease through impaired interactions with lipid droplets.
Kobayashi K et al.
The Journal of Clinical Endocrinology and Metabolism, 2008
The C-terminal region of human adipose triglyceride lipase affects enzyme activity and lipid droplet binding.
Schweiger M et al.
The Journal of Biological Chemistry, 2008