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AICA riboside increases AMP-activated protein kinase, fatty acid oxidation, and glucose uptake in rat muscle.
- G. Merrill, E. Kurth, D. Hardie, W. Winder
- Biology, Medicine
- American journal of physiology. Endocrinology and…
- 1 December 1997
5-Aminoimidazole-4-carboxamide ribonucleoside (AICAR) has previously been reported to be taken up into cells and phosphorylated to form ZMP, an analog of 5'-AMP. This study was designed to determine… Expand
AMP-activated protein kinase, a metabolic master switch: possible roles in Type 2 diabetes.
Adenosine 5'-monophosphate-activated protein kinase (AMPK) now appears to be a metabolic master switch, phosphorylating key target proteins that control flux through metabolic pathways of hepatic… Expand
Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise.
Malonyl-CoA, an inhibitor of fatty acid oxidation in skeletal muscle mitochondria, decreases in rat skeletal muscle during exercise or in response to electrical stimulation. Regulation of rat… Expand
Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle.
- W. Winder, B. Holmes, D. S. Rubink, E. B. Jensen, M. Chen, J. Holloszy
- Biology, Medicine
- Journal of applied physiology
- 1 June 2000
Muscle contraction causes an increase in activity of 5'-AMP-activated protein kinase (AMPK). This study was designed to determine whether chronic chemical activation of AMPK will increase… Expand
Chronic activation of 5'-AMP-activated protein kinase increases GLUT-4, hexokinase, and glycogen in muscle.
- B. Holmes, E. J. Kurth-Kraczek, W. Winder
- Biology, Medicine
- Journal of applied physiology
- 1 November 1999
This study was designed to determine whether chronic chemical activation of AMP-activated protein kinase (AMPK) would increase glucose transporter GLUT-4 and hexokinase in muscles similarly to… Expand
Evidence for 5′AMP-Activated Protein Kinase Mediation of the Effect of Muscle Contraction on Glucose Transport
- T. Hayashi, M. Hirshman, E. Kurth, W. Winder, L. Goodyear
- Biology, Medicine
- Diabetes
- 1 August 1998
The intracellular signaling proteins that lead to exercise-stimulated glucose transport in skeletal muscle have not been identified, although it is clear that there are separate signaling mechanisms… Expand
Phosphorylation-activity relationships of AMPK and acetyl-CoA carboxylase in muscle.
- S. H. Park, S. R. Gammon, J. Knippers, S. Paulsen, D. S. Rubink, W. Winder
- Biology, Medicine
- Journal of applied physiology
- 1 June 2002
AMP-activated protein kinase (AMPK) is activated during muscle contraction in response to the increase in AMP and decrease in phosphocreatine (PCr). Once activated, AMPK has been proposed to… Expand
Energy-sensing and signaling by AMP-activated protein kinase in skeletal muscle.
- W. Winder
- Biology, Medicine
- Journal of applied physiology
- 1 September 2001
AMP-activated protein kinase (AMPK) is emerging as an important energy-sensing/signaling system in skeletal muscle. This kinase is activated allosterically by 5'-AMP and inhibited allosterically by… Expand
5' AMP-activated protein kinase activation causes GLUT4 translocation in skeletal muscle.
- E. J. Kurth-Kraczek, M. Hirshman, L. Goodyear, W. Winder
- Biology, Medicine
- Diabetes
- 1 August 1999
It has previously been reported that exercise causes an increase in glucose uptake in skeletal muscle and also an increase in 5' AMP-activated protein kinase (AMPK) activity.… Expand
AMP-activated protein kinase phosphorylates transcription factors of the CREB family.
- D. M. Thomson, S. Herway, +4 authors W. Winder
- Biology, Medicine
- Journal of applied physiology
- 1 February 2008
AMP-activated protein kinase (AMPK) has been identified as a regulator of gene transcription, increasing mitochondrial proteins of oxidative metabolism as well as hexokinase expression in skeletal… Expand
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