@article {8103,
	title = {Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids},
	journal = {Nat Chem Biol},
	volume = {7},
	year = {2011},
	note = {Long, Jonathan ZCisar, Justin SMilliken, DavidNiessen, SherryWang, ChuTrauger, Sunia ASiuzdak, GaryCravatt, Benjamin FCA132630/CA/NCI NIH HHS/R01 CA132630-04/CA/NCI NIH HHS/Nat Chem Biol. 2011 Sep 18;7(11):763-5. doi: 10.1038/nchembio.659.
},
	month = {Nov},
	pages = {763-5},
	type = {Research Support, N.I.H., ExtramuralResearch Support, Non-U.S. Gov{\textquoteright}t},
	edition = {2011/09/20},
	abstract = {All organisms, including humans, possess a huge number of uncharacterized enzymes. Here we describe a general cell-based screen for enzyme substrate discovery by untargeted metabolomics and its application to identify the protein alpha/beta-hydrolase domain-containing 3 (ABHD3) as a lipase that selectively cleaves medium-chain and oxidatively truncated phospholipids. Abhd3(-/-) mice possess elevated myristoyl (C14)-phospholipids, including the bioactive lipid C14-lysophosphatidylcholine, confirming the physiological relevance of our substrate assignments.
},
	isbn = {1552-4469 (Electronic)1552-4450 (Linking)},
	url = {http://www.ncbi.nlm.nih.gov/pubmed/21926997},
	author = {Long, J. Z. and Cisar, J. S. and Milliken, D. and Niessen, S. and Wang, C. and Trauger, S. A. and Siuzdak, G. and Cravatt, B. F.}
}
