An N-terminal fragment of mouse DGAT1 binds different acyl-CoAs with varying affinity-Reference-Cited by-同舟云学术

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An N-terminal fragment of mouse DGAT1 binds different acyl-CoAs with varying affinity

Published:2008-08 Issue:3 Volume:373 Page:350-354
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Siloto Rodrigo M.P.,Madhavji Milan,Wiehler William B.,Burton Tracy L.,Boora Parveen S.,Laroche André,Weselake Randall J.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference29 articles.

1. Regulation of triglyceride metabolism. I. Eurkaryoticneutral lipid synthesis: Many ways to skin ACAT or a DGAT;Turkish;Am. J. Physiol. Gastrointest. Liver Physiol.,2007

2. DGAT:novel therapeutic target for obesity and type 2 diabetes mellitus;Subauste;Curr. Drug Targets Immune Endocr. Metabol. Disord.,2003

3. Suppression of diacylglycerol acyltransferase-2 (DGAT2) but not DGAT1 with antisense oligonucleotides reverses diet-induced hepatic steatosis and insulin resistance;Choi;J. Biol. Chem.,2007

4. Biosynthesis of triacylglycerols;Lehner;Prog. Lipid Res.,1996

5. Identification of a gene encoding an acyl CoA:diacylglycerol acyltransferase, a key enzyme in triacylglycerol synthesis;Cases;Proc. Natl. Acad. Sci. USA,1998

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