Role of AMP-activated protein kinase in mechanism of metformin action.
By Gaochao Zhou, R. W. Myers, Ying Li, Yuli Chen, Xiaolan Shen, J. Fenyk-Melody, Margaret S. Wu, J. Ventre, T. Doebber, N. Fujii and 4 more. Journal of Clinical Investigation, 2001
5,645 citations recorded by the source corpus.
Subfields: Endocrinology, Diabetes and Metabolism, Molecular Biology, Surgery
View Paper: https://www.semanticscholar.org/paper/10fcc433ae3acd5d5e15590be424e81ea907ea07
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Endocrinology, Diabetes and Metabolism
- D. Hardie
- R. Shaw
- David M. Sabatini
- D. Shackelford
- S. Hawley
- M. Laplante
- Michael Pollak
- Ralph DeFronzo
In Molecular Biology
In Surgery
Citations in the corpus
- Cellular and molecular mechanisms of metformin: an overview. (2012, background): “Thus, AMPK activation by metformin induces the phosphorylation and inactivation of acetyl CoA carboxylase (ACC), an important rate-controlling enzyme for the synthesis of malonylCoA, which is both a critical precursor for the biosynthesis of fatty acids and a potent inhibitor of mitochondrial fatty ”
- Butyrate enhances the intestinal barrier by facilitating tight junction assembly via activation of AMP-activated protein kinase in Caco-2 cell monolayers. (2009, background): “Furthermore, compound C, a cell-permeable competitive specific AMPK inhibitor (30,31), inhibits the butyrate-induced activation of AMPK.”
- Regulation of the TSC pathway by LKB1: evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome. (2004, background): “To determine the functional significance of AMPK in the regulation of S6K by LKB1, a pharmacological inhibitor of AMPK was tested (Zhou et al. 2001).”
- AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism. (2005, background): “Antidiabetic drugs Further interest in the potential role of the AMPK pathway in the treatment of Type 2 diabetes was generated by findings that AMPK is activated indirectly by metformin (Zhou et al., 2001) and thiazolidinediones (Fryer et al.”
- AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy (2007, neutral): “cgi?id=125853">type 2 diabetes (including metformi”
- Metformin Induces a Dietary Restriction–Like State and the Oxidative Stress Response to Extend C. elegans Healthspan via AMPK, LKB1, and SKN-1 (2010, background): “In mammals, energy sensor AMPK is activated by metformin [20,21], and metformin-activated AMPK increases glucose uptake in muscle and inhibits gluconeogenesis in hepatocytes [19].”
- Obesity and Diabetes: The Increased Risk of Cancer and Cancer-Related Mortality. (2015, background): “lac, had been used to treat diabetes for many years, the mechanism of action was elusive until it was discovered that metformin led to decreased hepatic gluconeogenesis by activating or phosphorylating AMP kinase (AMPK) in the liver (216).”
- Use of Cells Expressing γ Subunit Variants to Identify Diverse Mechanisms of AMPK Activation (2010, background): “, 2006); (2) the antidiabetic biguanides, metformin (Zhou et al., 2001) and phenformin (Hawley et al.”
- Metformin, Independent of AMPK, Inhibits mTORC1 In a Rag GTPase-Dependent Manner (2010, background): “As metformin treatment is known to induce glucose uptake in skeletal muscle (Sakamoto et al., 2005; Zhou et al., 2001), it was hypothesized that, at least in part, these effects are mediated by metformin-induced activation of the AMPK-TSC1/2 axis and inhibition of mTORC1/S6K1 phosphorylation of IRS1”
- p53 target genes sestrin1 and sestrin2 connect genotoxic stress and mTOR signaling. (2008, positive): “To further examine the role of AMPK in Sestrin-modulated mTOR inhibition, we used compound C, an AMPK inhibitor (Zhou et al., 2001).”
- Molecular mediators of hepatic steatosis and liver injury. (2004, neutral): “In the absence of SCD-1, AMPK is activated (49), resulting in phosphorylation and inhibition of both ACC (50) and ChREBP (51) as well as a reduction in the expression levels of SREBP-1c (52).”