JA Villena, B Viollet, F Andreelli, A Kahn, S Vaulont, HS … - Diabetes, 2004 - Am Diabetes Assoc AMP-activated protein kinase (AMPK) is considered as a cellular energy sensor that regulates
glucose and lipid metabolism by phosphorylating key regulatory enzymes. Despite the major
role of adipose tissue in regulating energy partitioning in the organism, the role of AMPK ... Cited by 51 - Related articles - BL Direct - All 6 versions
- ►nih.gov B Viollet, F Andreelli, SB Jørgensen, C … - Journal of Clinical …, 2003 - Am Soc Clin Investig AMP-activated protein kinase (AMPK) is viewed as a fuel sensor for glucose and lipid
metabolism. To better understand the physiological role of AMPK, we generated a knockout mouse
model in which the AMPKα2 catalytic subunit gene was inactivated. AMPKα2 –/– mice ... Cited by 207 - Related articles - BL Direct - All 11 versions
M Daval, F Diot-Dupuy, R Bazin, I Hainault, B … - Journal of Biological …, 2005 - ASBMB Despite its importance in terms of energy homeostasis, the role of AMP-activated protein kinase
in adipose tissue remains controversial. Initial studies have described an anti-lipolytic role for
AMP-activated protein kinase, whereas more recent studies have suggested the ... Cited by 59 - Related articles - All 5 versions
- ►endojournals.org F Andreelli, M Foretz, C Knauf, PD Cani, C Perrin, MA … - Endocrinology, 2006 - Endocrine Soc The AMP-activated kinase (AMPK) is a serine threonine kinase that functions as a fuel sensor
to regulate energy balance at both cellular and whole-body levels. Here we studied how hepatic
AMPK 2 isoform affects hepatic glucose production and peripheral glucose uptake in vivo. ... Cited by 62 - Related articles - All 3 versions
- ►jbc.org EK Kim, I Miller, S Aja, LE Landree, M Pinn, J … - Journal of Biological …, 2004 - ASBMB Energy homeostasis and feeding are regulated by the central nervous system. C75, a fatty acid
synthase (FAS) inhibitor, causes weight loss and anorexia, implying a novel central nervous
system pathway(s) for sensing energy balance. AMP-activated protein kinase (AMPK), a ... Cited by 135 - Related articles - BL Direct - All 4 versions
BR Barnes, S Marklund, TL Steiler, M Walter, G … - Journal of Biological …, 2004 - ASBMB 5′-AMP-activated protein kinase (AMPK) is a metabolic stress sensor present in all
eukaryotes. A dominant missense mutation (R225Q) in pig PRKAG3, encoding the muscle-specific
γ3 isoform, causes a marked increase in glycogen content. To determine the functional ... Cited by 96 - Related articles - BL Direct - All 5 versions
W Yin, J Mu, MJ Birnbaum - Journal of Biological Chemistry, 2003 - ASBMB AMP-activated protein kinase (AMPK) is a phylogenetically conserved intracellular energy sensor
that has been implicated as a major regulator of glucose and lipid metabolism in mammals.
However, its possible role in mediating or influencing the adrenergic control of lipolysis in ... Cited by 86 - Related articles - BL Direct - All 6 versions
SB Jørgensen, B Viollet, F Andreelli, C Frøsig, JB … - Journal of Biological …, 2004 - ASBMB We investigated the importance of the two catalytic α-isoforms of the 5′-AMP-activated protein
kinase (AMPK) in 5-aminoimidazole-4-carboxamide-1-β-4-ribofuranoside (AICAR) and
contraction-induced glucose uptake in skeletal muscle. Incubated soleus and EDL ... Cited by 190 - Related articles - BL Direct - All 4 versions
M Horikoshi, K Hara, J Ohashi, K Miyake, K Tokunaga, … - Diabetes, 2006 - Am Diabetes Assoc AMP-activated protein kinase (AMPK) acts as a fuel gauge for glucose and lipid metabolism.
The gene encoding the α2 isoform of the catalytic subunit of AMPK (PRKAA2) is located at one
of the Japanese type 2 diabetes loci mapped by our previous genome scan (1p36-32). ... Cited by 20 - Related articles - BL Direct - All 4 versions
N Sambandam, M Steinmetz, A Chu, JY Altarejos, … - FEBS Journal, 2004 - ingentaconnect.com Malonyl-CoA, a potent inhibitor of carnitine pamitoyl transferase-I (CPT-I), plays a pivotal role
in fuel selection in cardiac muscle. Malonyl-CoA decarboxylase (MCD) catalyzes the degradation
of malonyl-CoA, removes a potent allosteric inhibition on CPT-I and thereby increases ... Cited by 21 - Related articles - All 3 versions
