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Clinical Gastroenterology and Hepatology, 2018
BACKGROUND & AIMS: Increased de novo lipogenesis (DNL) contributes to the pathogenesis of nonalcoholic steatohepatitis (NASH). Acetyl‐CoA carboxylase catalyzes the rate‐limiting step in DNL.
E. Lawitz +20 more
semanticscholar +3 more sources
BACKGROUND & AIMS: Increased de novo lipogenesis (DNL) contributes to the pathogenesis of nonalcoholic steatohepatitis (NASH). Acetyl‐CoA carboxylase catalyzes the rate‐limiting step in DNL.
E. Lawitz +20 more
semanticscholar +3 more sources
Regulation of acetyl-CoA carboxylase.
Biochemical Society Transactions, 2006Acetyl-CoA carboxylase (ACC) catalyses the formation of malonyl-CoA, an essential substrate for fatty acid synthesis in lipogenic tissues and a key regulatory molecule in muscle, brain and other tissues. ACC contributes importantly to the overall control of energy metabolism and has provided an important model to explore mechanisms of enzyme control ...
R. Brownsey +4 more
semanticscholar +3 more sources
Expert Opinion on Investigational Drugs, 2019
Introduction: Acetyl-CoA Carboxylase (ACC) is an essential rate-limiting enzyme in fatty acid metabolism. For many years, ACC inhibitors have gained great attention for developing therapeutics for various human diseases including microbial infections ...
Leyuan Chen +7 more
semanticscholar +3 more sources
Introduction: Acetyl-CoA Carboxylase (ACC) is an essential rate-limiting enzyme in fatty acid metabolism. For many years, ACC inhibitors have gained great attention for developing therapeutics for various human diseases including microbial infections ...
Leyuan Chen +7 more
semanticscholar +3 more sources
Regulation of mammalian acetyl-CoA carboxylase.
Biochemical Society Transactions, 2002Acetyl-CoA carboxylase (ACC) plays a critical role in the regulation of fatty acid metabolism and its two isoforms, ACCα and ACCβ, appear to have distinct functions in the control of fatty acid synthesis and fatty acid oxidation, respectively. They are regulated by similar short-term mechanisms of allosteric activation by citrate, and reversible ...
M. Munday
semanticscholar +3 more sources
Structural basis for regulation of human acetyl-CoA carboxylase
Nature, 2018M. Hunkeler +6 more
semanticscholar +3 more sources
Regulation and structure of the heteromeric acetyl-CoA carboxylase.
Biochimica Et Biophysica Acta - Molecular and Cell Biology of Lipids, 2016Matthew J Salie, J. Thelen
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Plant Molecular Biology, 1993
The acetyl-CoA carboxylase present in both wheat germ and total wheat leaf protein contains ca. 220 kDa subunits. It is the major biotin-dependent carboxylase present in wheat chloroplasts. Active acetyl-CoA carboxylase purified from wheat germ is a homodimer with an apparent molecular mass of ca. 500 kDa.
P, Gornicki, R, Haselkorn
openaire +2 more sources
The acetyl-CoA carboxylase present in both wheat germ and total wheat leaf protein contains ca. 220 kDa subunits. It is the major biotin-dependent carboxylase present in wheat chloroplasts. Active acetyl-CoA carboxylase purified from wheat germ is a homodimer with an apparent molecular mass of ca. 500 kDa.
P, Gornicki, R, Haselkorn
openaire +2 more sources

