|1.||Cao, Deliang: 5 articles (11/2011 - 02/2008)|
|2.||Lopaschuk, Gary D: 4 articles (08/2014 - 05/2002)|
|3.||Liao, Duan-Fang: 4 articles (11/2011 - 02/2008)|
|4.||Tong, Liang: 3 articles (10/2015 - 05/2008)|
|5.||Ma, Jun: 3 articles (06/2015 - 02/2008)|
|6.||López, Miguel: 3 articles (03/2015 - 07/2008)|
|7.||Igal, R Ariel: 3 articles (06/2011 - 01/2009)|
|8.||Wang, Chun: 3 articles (12/2010 - 07/2009)|
|9.||Brusselmans, Koen: 3 articles (09/2007 - 08/2005)|
|10.||Verhoeven, Guido: 3 articles (09/2007 - 08/2005)|
05/10/2002 - "Our results support recent studies that indicate that acetyl-CoA carboxylase may be a suitable target for an anti-obesity therapeutic."
01/01/2014 - "Maternal obesity reduces milk lipid production in lactating mice by inhibiting acetyl-CoA carboxylase and impairing fatty acid synthesis."
02/01/2013 - "Acetyl-CoA carboxylase (ACC) is a crucial metabolic enzyme that plays a vital role in obesity-induced type 2 diabetes and fatty acid metabolism. "
01/10/2013 - "Treatment of Obesity and Related Disorders with Acetyl-CoA Carboxylase Inhibitors."
12/01/2011 - "In conclusion, common polymorphisms of ACACB gene are associated with obesity and, independently, with type 2 diabetes in postmenopausal women, suggesting that the activity of acetyl-CoA carboxylase beta plays an important role in these disorders related to energy metabolism."
|2.||Body Weight (Weight, Body)
04/01/2008 - "Inhibition of acetyl-CoA carboxylase both inhibits fatty acid synthesis and stimulates fatty acid oxidation, and this may to contribute to the in vivo effect of galegine on body weight."
02/01/1992 - "Changes of body weights and hepatic acetyl-CoA carboxylase activities were measured in voles and mice treated with monosodium-L-aspartate (MSA). "
04/01/2011 - "The I3C treatment decreased body weight and fat accumulation and infiltrated macrophages in epididymal adipose tissue of DIO mice, and these reductions were associated with improved glucose tolerance and with modulated expression of adipokines and lipogenic-associated gene products, including acetyl coenzyme A carboxylase and peroxisome proliferator-activated receptor-γ."
07/01/2006 - "Recent data strongly implicate the AMPK-acetyl CoA carboxylase (ACC)-malonyl CoA pathway in the hypothalamus in the regulation of food intake, body weight and hepatic glucose production. "
10/01/1995 - "Feed efficiency, N utilization, the ratio of abdominal fat or liver to body weight, acetyl-coenzyme A carboxylase (EC 126.96.36.199) activity, liver and serum cholesterol contents were significantly lower in treatment groups, while fatty acid synthetase activity and serum cholesterol concentration were not significantly different, compared with the control group. "
08/01/2013 - "We suggest a regulatory role for miR-204-5p which was predicted to inhibit acetyl coenzyme A carboxylase β, a key fatty acid oxidation enzyme that has been shown to play a role in regulating body fat and insulin resistance in adipose tissue. "
05/01/2009 - "Inhibition of acetyl-CoA carboxylase (ACC) may prevent lipid-induced insulin resistance and type 2 diabetes, making the enzyme an attractive pharmaceutical target. "
11/01/2003 - "Decreased muscle acetyl-coenzyme A carboxylase 2 mRNA and insulin resistance in formerly obese subjects."
05/23/2008 - "Acetyl-CoA carboxylase 1 (ACC1) currently is being investigated as a target for treatment of obesity-associated dyslipidemia and insulin resistance. "
10/01/2009 - "Inhibition of the acetyl-CoA carboxylase (ACC) system, consisting of the isozymes ACC1 and ACC2, may be beneficial for treatment of insulin resistance and/or obesity by interfering with de novo lipogenesis and beta-oxidation. "
11/01/2004 - "Due to CLA-induced hepatomegaly, the overall capacity for both fatty acid oxidation and synthesis-as evidenced by the total hepatic activities of 3-hydroxy-acyl-CoA dehydrogenase, citrate synthase, acetyl-CoA carboxylase, and fatty acid synthase-was significantly greater in the CLA-fed group after 12 weeks, although the overall capacity for fatty acid synthesis had increased more than that for fatty acid oxidation. "
12/15/1991 - "Rapid inhibition of acetyl-CoA carboxylase (ACC) activity in rat liver in response to 6 h starvation and rapid re-activation in response to 2-6 h of re-feeding chow were shown to be due to changes in the expressed activity of existing enzyme. "
12/15/1991 - "The short-term regulation of hepatic acetyl-CoA carboxylase during starvation and re-feeding in the rat."
01/01/1991 - "3. Between 6 and 24 hr starvation, total and expressed activities of acetyl-CoA carboxylase decreased by 62 and 55%, respectively. "
07/01/1986 - "The greater extent of activation in extracts from 24 h-starved rats (200%) compared with fed controls (70%) implies that the decrease in acetyl-CoA carboxylase activity in response to 24 h starvation may involve increased phosphorylation of the enzyme. "
07/01/1986 - "The role of acetyl-CoA carboxylase phosphorylation in the control of mammary gland fatty acid synthesis during the starvation and re-feeding of lactating rats."
|1.||Fatty Acid Synthetase Complex (Fatty Acid Synthase)
|4.||stearoyl-coenzyme A (stearoyl-CoA)
|6.||Citrate (si)-Synthase (Synthase, Citrate)
|8.||Biological Markers (Surrogate Marker)
|9.||Messenger RNA (mRNA)
|2.||Fat-Restricted Diet (Diet, Fat Restricted)