Phosphatidylcholine transfer protein interacts with thioesterase superfamily member 2 to attenuate insulin signaling
A functional variant in the transcriptional regulatory region of gene LOC344967 cosegregates with disease phenotype in familial nasopharyngeal carcinoma
Crystal structure of human thioesterase superfamily member 2
|Biochem. Biophys. Res. Commun.
BFIT, a unique acyl-CoA thioesterase induced in thermogenic brown adipose tissue: cloning, organization of the human gene and assessment of a potential link to obesity
The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis
The emerging role of acyl-CoA thioesterases and acyltransferases in regulating peroxisomal lipid metabolism
|Biochim. Biophys. Acta
New players on the metabolic stage: How do you like Them Acots?
Thioesterase superfamily member 2 (Them2) and phosphatidylcholine transfer protein (PC-TP) interact to promote fatty acid oxidation and control glucose utilization
|Mol. Cell. Biol.
Structural basis for regulation of the human acetyl-CoA thioesterase 12 and interactions with the steroidogenic acute regulatory protein-related lipid transfer (START) domain
|J. Biol. Chem.
Identification of fatty acid oxidation disorder patients with lowered acyl-CoA thioesterase activity in human skin fibroblasts
van Roermond, CW,
|Eur. J. Clin. Invest.
Functional and structural properties of mammalian acyl-coenzyme A thioesterases
|Prog. Lipid Res.
Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs
PC-TP/StARD2: Of membranes and metabolism
|Trends Endocrinol. Metab.