Activation of Protein Kinase Cζ by Peroxynitrite Regulates LKB1-dependent AMP-activated Protein Kinase in Cultured Endothelial Cells

Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action

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Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase

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AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism

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Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase

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The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress

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Complexes between the LKB1 tumor suppressor, STRADα/β and MO25α/β are upstream kinases in the AMP-activated protein kinase cascade

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LKB1 is the upstream kinase in the AMP-activated protein kinase cascade

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Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMP-activated protein kinase

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THE AMP-ACTIVATED/SNF1 PROTEIN KINASE SUBFAMILY: Metabolic Sensors of the Eukaryotic Cell?

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Ca2+/calmodulin-dependent protein kinase kinase-β acts upstream of AMP-activated protein kinase in mammalian cells

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Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex

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LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR‐1

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Characterization of the AMP-activated Protein Kinase Kinase from Rat Liver and Identification of Threonine 172 as the Major Site at Which It Phosphorylates AMP-activated Protein Kinase

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The AMP-activated protein kinase pathway – new players upstream and downstream

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The LKB1 tumor suppressor negatively regulates mTOR signaling

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The Anti-diabetic Drugs Rosiglitazone and Metformin Stimulate AMP-activated Protein Kinase through Distinct Signaling Pathways

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The Ca2+/Calmodulin-dependent Protein Kinase Kinases Are AMP-activated Protein Kinase Kinases

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Adiponectin Stimulates Production of Nitric Oxide in Vascular Endothelial Cells

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Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia

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Activation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases

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High Rates of Fatty Acid Oxidation during Reperfusion of Ischemic Hearts Are Associated with a Decrease in Malonyl-CoA Levels Due to an Increase in 5’-AMP-activated Protein Kinase Inhibition of Acetyl-CoA Carboxylase

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Deficiency of LKB1 in skeletal muscle prevents AMPK activation and glucose uptake during contraction

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AMP-activated protein kinase, super metabolic regulator

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The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells

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AMPK, the metabolic syndrome and cancer

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AMP-activated protein kinase is activated by low glucose in cell lines derived from pancreatic β cells, and may regulate insulin release

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Contraction-induced Changes in Acetyl-CoA Carboxylase and 5′-AMP-activated Kinase in Skeletal Muscle

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Phosphorylation of the Protein Kinase Mutated in Peutz-Jeghers Cancer Syndrome, LKB1/STK11, at Ser431 by p90RSK and cAMP-dependent Protein Kinase, but Not Its Farnesylation at Cys433, Is Essential for LKB1 to Suppress Cell Growth*

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The Regulation of AMP-Activated Protein Kinase by H2O2

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New roles for the LKB1→AMPK pathway

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LKB1, a novel serine/threonine protein kinase and potential tumour suppressor, is phosphorylated by cAMP-dependent protein kinase (PKA) and prenylated in vivo

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AMP-activated protein kinase: balancing the scales

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LKB1, a protein kinase regulating cell proliferation and polarity

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Modulation by Peroxynitrite of Akt- and AMP-activated Kinase-dependent Ser1179 Phosphorylation of Endothelial Nitric Oxide Synthase

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Activation of the ERK Pathway and Atypical Protein Kinase C Isoforms in Exercise- and Aminoimidazole-4-carboxamide- 1-β-d-riboside (AICAR)-stimulated Glucose Transport

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Regulation of 5′-AMP-activated Protein Kinase Activity by the Noncatalytic β and γ Subunits

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Mammalian AMP-activated protein kinase: functional, heterotrimeric complexes by co-expression of subunits in Escherichia coli.

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Functional analysis of Peutz–Jeghers mutations reveals that the LKB1 C-terminal region exerts a crucial role in regulating both the AMPK pathway and the cell polarity

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Differential Regulation of Matrix Metalloproteinase-2 and -9 Expression and Activity in Adult Rat Cardiac Fibroblasts in Response to Interleukin-1β

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Thrombin Stimulation of Vascular Adhesion Molecule-1 in Endothelial Cells Is Mediated by Protein Kinase C (PKC)-δ-NF-κB and PKC-ζ-GATA Signaling Pathways

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AMP-activated protein kinase (AMPK) regulates the insulin-induced activation of the nitric oxide synthase in human platelets

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Roles of the Snf1/Rkin1/AMP-activated protein kinase family in the response to environmental and nutritional stress

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Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability

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Signalling by protein kinase C isoforms in the heart

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And now for something completely different?

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Calcineurin is required for translational control of protein synthesis in rat pancreatic acini

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Thrombin Rapidly Induces Protein Kinase D Phosphorylation, and Protein Kinase C δ Mediates the Activation

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The stimulation of heart glycolysis by increased workload does not require AMP‐activated protein kinase but a wortmannin‐sensitive mechanism

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Lkb1 and GSK3-beta: kinases at the center and poles of the action.

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Lkb1 and GSK3b: Kinases at the Center (and the poles) of the Action

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Peroxynitrite: biochemistry, pathophysiology and development of therapeutics

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Regulation and function of AMPK in physiology and diseases

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Hypoxic Pulmonary Vasoconstriction

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ATM signals to TSC2 in the cytoplasm to regulate mTORC1 in response to ROS

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Dissecting the Role of 5′-AMP for Allosteric Stimulation, Activation, and Deactivation of AMP-activated Protein Kinase

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eNOS activation by physical forces: from short-term regulation of contraction to chronic remodeling of cardiovascular tissues

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Molecular machinery and interplay of apoptosis and autophagy in coronary heart disease

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AMPK alterations in cardiac physiology and pathology: enemy or ally?

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Akt-dependent and -independent mechanisms of mTOR regulation in cancer

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Redox control of inflammation in macrophages

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Molecular Insights and Therapeutic Targets for Diabetic Endothelial Dysfunction

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Free Radicals, Mitochondria, and Oxidized Lipids

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AMPKα2 Deletion Causes Aberrant Expression and Activation of NAD(P)H Oxidase and Consequent Endothelial Dysfunction In Vivo: Role of 26S Proteasomes

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Activation and Signaling by the AMP-Activated Protein Kinase in Endothelial Cells

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AMPK, Mitochondrial Function, and Cardiovascular Disease

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AMP-activated protein kinase regulation and biological actions in the heart

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Phosphorylation of LKB1 at Serine 428 by Protein Kinase C-ζ Is Required for Metformin-Enhanced Activation of the AMP-Activated Protein Kinase in Endothelial Cells

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Reduction of AMP-Activated Protein Kinase α2 Increases Endoplasmic Reticulum Stress and Atherosclerosis In Vivo

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Nitric Oxide and Reactive Oxygen Species in the Pathogenesis of Preeclampsia

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Role of glutathione, glutathione transferase, and glutaredoxin in regulation of redox-dependent processes

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AMP-activated protein kinase, stress responses and cardiovascular diseases

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AMP-activated Protein Kinase Is Activated as a Consequence of Lipolysis in the Adipocyte

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Nrf2-p62 autophagy pathway and its response to oxidative stress in hepatocellular carcinoma

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Resveratrol Prevents the Prohypertrophic Effects of Oxidative Stress on LKB1

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LKB1; linking cell structure and tumor suppression

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Oxygen sensors in context

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Activation of AMP-activated Protein Kinase by Temozolomide Contributes to Apoptosis in Glioblastoma Cells via p53 Activation and mTORC1 Inhibition

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Neuroprotective Effects of Adenosine Monophosphate- Activated Protein Kinase Inhibition and Gene Deletion in Stroke

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Adiponectin Activates AMP-Activated Protein Kinase in Muscle Cells via APPL1/LKB1-Dependent and Phospholipase C/Ca2+/Ca2+/Calmodulin-Dependent Protein Kinase Kinase-Dependent Pathways

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Microglia: Multitasking Specialists of the Brain

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Redox implications of AMPK-mediated signal transduction beyond energetic clues

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AMPK, metabolism, and vascular function

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SIRT1 and AMPK in regulating mammalian senescence: A critical review and a working model

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Exercise-Stimulated ROS Sensitive Signaling Pathways in Skeletal Muscle

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The Role of Reactive Oxygen Species in the Life Cycle of the Mitochondrion

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Effects of Metformin in Experimental Stroke

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NR4A nuclear receptors are orphans but not lonesome

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Proposed mechanisms of (−)-epigallocatechin-3-gallate for anti-obesity

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The interplay between autophagy and apoptosis in the diabetic heart

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Role of AMPK activation in oxidative cell damage: Implications for alcohol-induced liver disease

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Gastrodin Ameliorates Oxidative Stress and Proinflammatory Response in Nonalcoholic Fatty Liver Disease through the AMPK/Nrf2 Pathway

Qu, L., Yu, B., Li, Z., Jiang, W., Jiang, J., & Kong, W. (2015) · Phytotherapy Research · doi:10.1002/ptr.5541 · Cited by 131 · see citing works

Deletion of Lkb1 in Renal Tubular Epithelial Cells Leads to CKD by Altering Metabolism

Han, S. H., Málaga-Diéguez, L., Chinga, F., Kang, H. M., Tao, J., Reidy, K. J., & Suszták, K. (2015) · Journal of the American Society of Nephrology · doi:10.1681/asn.2014121181 · Cited by 130 · see citing works

An essential role of the aPKC–Aurora A–NDEL1 pathway in neurite elongation by modulation of microtubule dynamics

Mori, D., Yamada, M., Mimori‐Kiyosue, Y., Shirai, Y., Suzuki, A., Ohno, S., Saya, H., Wynshaw-Boris, A. J., & Hirotsune, S. (2009) · Nature Cell Biology · doi:10.1038/ncb1919 · Cited by 130 · see citing works

Redox basis of exercise physiology

Margaritelis, N. V., Paschalis, V., Theodorou, A. A., Kyparos, A., & Nikolaidis, M. G. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101499 · Cited by 129 · see citing works

AMP-activated protein kinase agonists increase mRNA content of the muscle-specific ubiquitin ligases MAFbx and MuRF1 in C2C12 cells.

Krawiec, B., Nystrom, G. J., Frost, R., Jefferson, L., & Lang, C. H. (2007) · American Journal of Physiology. Endocrinology and Metabolism · doi:10.1152/ajpendo.00622.2006 · Cited by 129 · see citing works

The protective role of AMP-activated protein kinase in alpha-synuclein neurotoxicity in vitro

Dulović, M., Jovanović, M., Xilouri, M., Stefanis, L., Harhaji-Trajkovic, L. M., Kravic‐Stevovic, T., Paunović, V., Ardah, M. T., El‐Agnaf, O. M. A., Kostić, V., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.11.002 · Cited by 123 · see citing works

AMPK in cardiovascular health and disease

Shirwany, N. A., & Zou, M. (2010) · Acta Pharmacologica Sinica · doi:10.1038/aps.2010.139 · Cited by 121 · see citing works

Regulation of NAD(P)H oxidases by AMPK in cardiovascular systems

Song, P., & Zou, M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.01.025 · Cited by 119 · see citing works

AMPK activation prevents excess nutrient-induced hepatic lipid accumulation by inhibiting mTORC1 signaling and endoplasmic reticulum stress response

Li, H., Min, Q., Ouyang, C., Lee, J., He, C., Zou, M., & Xie, Z. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.07.002 · Cited by 117 · see citing works

AMP‐ACTIVATED PROTEIN KINASE ACTIVATION AS A STRATEGY FOR PROTECTING VASCULAR ENDOTHELIAL FUNCTION

Zou, M., & Wu, Y. (2007) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2007.04851.x · Cited by 115 · see citing works

AMPK and vasculoprotection

Ewart, M., & Kennedy, S. (2010) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2010.11.002 · Cited by 110 · see citing works

Nutrient-sensing mTORC1: Integration of metabolic and autophagic signals

Tan, V. P., & Miyamoto, S. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.01.005 · Cited by 110 · see citing works

The LKB1 tumor suppressor kinase in human disease

Katajisto, P., Vallenius, T., Vaahtomeri, K., Ekman, N., Udd, L., Tiainen, M., & Mäkelä, T. P. (2006) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2006.08.003 · Cited by 107 · see citing works

Autophagy and ethanol-induced liver injury

Donohue, T. M. (2009) · World Journal of Gastroenterology · doi:10.3748/wjg.15.1178 · Cited by 107 · see citing works

Empagliflozin attenuates ischemia and reperfusion injury through LKB1/AMPK signaling pathway

Lü, Q., Liu, J., Li, X., Sun, X., Zhang, J., Ren, D., Tong, N., & Li, J. (2019) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2019.110642 · Cited by 105 · see citing works

Honokiol activates AMP-activated protein kinase in breast cancer cells via an LKB1-dependent pathway and inhibits breast carcinogenesis

Nagalingam, A., Arbiser, J. L., Bonner, M. Y., Saxena, N. K., & Sharma, D. (2012) · Breast Cancer Research · doi:10.1186/bcr3128 · Cited by 105 · see citing works

Inhibition of AMP-activated Protein Kinase α (AMPKα) by Doxorubicin Accentuates Genotoxic Stress and Cell Death in Mouse Embryonic Fibroblasts and Cardiomyocytes

Wang, S., Song, P., & Zou, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.315812 · Cited by 104 · see citing works

Metformin affects macrophages’ phenotype and improves the activity of glutathione peroxidase, superoxide dismutase, catalase and decreases malondialdehyde concentration in a partially AMPK-independent manner in LPS-stimulated human monocytes/macrophages

Bułdak, Ł., Łabuzek, K., Bułdak, R. J., Kozłowski, M., Machnik, G., Liber, S., Suchy, D., Duława, A., & Okopień, B. (2014) · Pharmacological Reports · doi:10.1016/j.pharep.2013.11.008 · Cited by 104 · see citing works

Suppression of nitrative damage by metallothionein in diabetic heart contributes to the prevention of cardiomyopathy

Cai, L. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.06.007 · Cited by 99 · see citing works

AMP‐activated protein kinase: a core signalling pathway in the heart

Kim, A. S., Miller, E. J., & Young, L. H. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01978.x · Cited by 98 · see citing works

AICAR and metformin, but not exercise, increase muscle glucose transport through AMPK-, ERK-, and PDK1-dependent activation of atypical PKC

Sajan, M. P., Bandyopadhyay, G. K., Miura, A., Standaert, M. L., Nimal, S., Longnus, S., OBBERGHEN, E. V., Hainault, I., Foufelle, F., Kahn, R. C., et al. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00392.2009 · Cited by 98 · see citing works

Identification of the Serine 307 of LKB1 as a Novel Phosphorylation Site Essential for Its Nucleocytoplasmic Transport and Endothelial Cell Angiogenesis

Xie, Z., Dong, Y., Zhang, J., Scholz, R., Neumann, D., & Zou, M. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01417-08 · Cited by 98 · see citing works

Tankyrase disrupts metabolic homeostasis and promotes tumorigenesis by inhibiting LKB1-AMPK signalling

Li, N., Wang, Y., Neri, S., Zhen, Y., Fong, L. W. R., Qiao, Y., Li, X., Chen, Z., STEPHAN, C. C., Deng, W., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12377-1 · Cited by 95 · see citing works

Structural Properties of AMP-activated Protein Kinase

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Arsenic Inhibits Neurite Outgrowth by Inhibiting the LKB1–AMPK Signaling Pathway

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Protein kinase C (PKC) participates in acetaminophen hepatotoxicity through c-jun-N-terminal kinase (JNK)-dependent and -independent signaling pathways

Saberi, B., Ybanez, M. D., Johnson, H. S., Gaarde, W. A., Han, D., & Kaplowitz, N. (2014) · Hepatology · doi:10.1002/hep.26625 · Cited by 88 · see citing works

AMPKα2 deficiency exacerbates long-term PM2.5 exposure-induced lung injury and cardiac dysfunction

Wang, H., Shen, X., Tian, G., Shi, X., Huang, W., Wu, Y., Sun, L., Peng, C., Liu, S., Huang, Y., et al. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.008 · Cited by 87 · see citing works

Thromboxane receptor activates the AMP-activated protein kinase in vascular smooth muscle cells via hydrogen peroxide

Zhang, M., Dong, Y., Xu, J., Xie, Z., Wu, Y., Song, P., Guzman, M., Wu, J., & Zou, M.-H. (2008) · Circulation Research · doi:10.1161/circresaha.107.163253 · Cited by 82 · see citing works

In the regulation of cytochrome P450 genes, phenobarbital targets LKB1 for necessary activation of AMP-activated protein kinase

Blättler, S. M., Rencurel, F., Kaufmann, M., & Meyer, U. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610216104 · Cited by 82 · see citing works

Inhibition of AMP-Activated Protein Kinase Accentuates Lipopolysaccharide-Induced Lung Endothelial Barrier Dysfunction and Lung Injury in Vivo

Xing, J., Wang, Q., Coughlan, K. A., Viollet, B., Moriasi, C. M., & Zou, M. (2013) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.11.022 · Cited by 79 · see citing works

Concept and connotation of oxidative stress in preeclampsia

Al-Kuraishy, H. M., Al-Gareeb, A. I., & Al-Maiahy, T. J. (2018) · Journal of Laboratory Physicians · doi:10.4103/jlp.jlp_26_18 · Cited by 76 · see citing works

SUMOylation regulates LKB1 localization and its oncogenic activity in liver cancer

Zubiete‐Franco, I., García‐Rodríguez, J. L., Lopitz‐Otsoa, F., Serrano‐Maciá, M., Simón, J., Fernández‐Tussy, P., Barbier‐Torres, L., Fernández‐Ramos, D., Gutiérrez-de-Juan, V., de Davalillo, S. L., et al. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2018.12.031 · Cited by 76 · see citing works

Controlling the master—upstream regulation of the tumor suppressor LKB1

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Glutathione S-Transferases Interact with AMP-Activated Protein Kinase: Evidence for S-Glutathionylation and Activation In Vitro

Klaus, A., Zorman, S., Berthier, A., Polge, C., Ramírez‐Ríos, S., Michelland, S., Sève, M., Vertommen, D., Rider, M. H., Lentze, N., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062497 · Cited by 75 · see citing works

Fluid Shear Stress and NO Decrease the Activity of the Hydroxy-Methylglutaryl Coenzyme A Reductase in Endothelial Cells via the AMP-Activated Protein Kinase and FoxO1

Fißlthaler, B., Fleming, I., Keserü, B., Walsh, K., & Busse, R. (2007) · Circulation Research · doi:10.1161/01.res.0000257747.74358.1c · Cited by 75 · see citing works

Recent Progress on Liver Kinase B1 (LKB1): Expression, Regulation, Downstream Signaling and Cancer Suppressive Function

Gan, R., & Li, H. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150916698 · Cited by 72 · see citing works

Principles for integrating reactive species into in vivo biological processes: Examples from exercise physiology

Margaritelis, N. V., Cobley, J. N., Paschalis, V., Veskoukis, A. S., Theodorou, A. A., Kyparos, A., & Nikolaidis, M. G. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.12.011 · Cited by 71 · see citing works

SIK inhibition in human myeloid cells modulates TLR and IL-1R signaling and induces an anti-inflammatory phenotype

Lombardi, M. S., Gilliéron, C., Dietrich, D., & Gabay, C. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.2a0715-307r · Cited by 68 · see citing works

Endothelial Cell–Specific Liver Kinase B1 Deletion Causes Endothelial Dysfunction and Hypertension in Mice In Vivo

Zhang, W., Wang, Q., Wu, Y., Moriasi, C. M., Liu, Z., Dai, X., Wang, Q., Liu, W., Yuan, Z., & Zou, M. (2014) · Circulation · doi:10.1161/circulationaha.113.004146 · Cited by 69 · see citing works

Dapagliflozin as an autophagic enhancer via LKB1/AMPK/SIRT1 pathway in ovariectomized/d-galactose Alzheimer’s rat model

Ibrahim, W. W., Kamel, A. S. E. D., Wahid, A. M., & Abdelkader, N. F. (2022) · Inflammopharmacology · doi:10.1007/s10787-022-00973-5 · Cited by 68 · see citing works

An in vitro comparative study of the antioxidant activity and SIRT1 modulation of natural compounds

Fusi, J., Bianchi, S. E., Daniele, S., Pellegrini, S., Martini, C., Galetta, F., Giovannini, L., & Franzoni, F. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.03.006 · Cited by 67 · see citing works

Mycobacterium tuberculosislipoprotein-induced association of TLR2 with protein kinase C ζ in lipid rafts contributes to reactive oxygen species-dependent inflammatory signalling in macrophages

Shin, D., Yang, C., Lee, J., Lee, S. J., Choi, H.-H., Lee, H. M., Yuk, J., Harding, C. V., & Jo, E. (2008) · Cellular Microbiology · doi:10.1111/j.1462-5822.2008.01179.x · Cited by 66 · see citing works

Blocking a vicious cycle nNOS/peroxynitrite/AMPK by S-nitrosoglutathione: implication for stroke therapy

Khan, M., Dhammu, T. S., Matsuda, F., Singh, A. K., & Singh, I. (2015) · BMC Neuroscience · doi:10.1186/s12868-015-0179-x · Cited by 64 · see citing works

Neuroprotection by Radical Avoidance: Search for Suitable Agents

Hardeland, R. (2009) · Molecules · doi:10.3390/molecules14125054 · Cited by 64 · see citing works

Redox Characterization of Functioning Skeletal Muscle

Zuo, L., & Pannell, B. K. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00338 · Cited by 60 · see citing works

Effect of ethanol on hydrogen peroxide-induced AMPK phosphorylation

Liangpunsakul, S., Wou, S.-E., Zeng, Y., Ross, R. A., Jayaram, H. N., & Crabb, D. W. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90349.2008 · Cited by 52 · see citing works

Bradykinin stimulates endothelial cell fatty acid oxidation by CaMKK-dependent activation of AMPK

Mount, P. F., Lane, N., Venkatesan, S., Steinberg, G. R., Fraser, S. A., Kemp, B. E., & Power, D. A. (2008) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2007.12.003 · Cited by 51 · see citing works

Hypoxia exposure induces the emergence of fibroblasts lacking replication repressor signals of PKC in the pulmonary artery adventitia

Das, M., Burns, N. C., Wilson, S. J., Zawada, W. M., & Stenmark, K. R. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn014 · Cited by 51 · see citing works

Tight junction proteins and signal transduction pathways in hepatocytes.

Kojima, T., Murata, M., Yamamoto, T., Lan, M., Imamura, M., Son, S., Takano, K., Yamaguchi, H., Ito, T., Tanaka, S., et al. (2009) · PubMed · doi:10.14670/hh-24.1463 · Cited by 51 · see citing works

Suppression of oxidative stress and improvement of liver functions in mice by ursolic acid via LKB 1‐ AMP ‐activated protein kinase signaling

Yang, Y., Zhao, Z., Liu, Y., Kang, X., Zhang, H., & Meng, M. (2014) · Journal of Gastroenterology and Hepatology · doi:10.1111/jgh.12723 · Cited by 50 · see citing works

AMPK α2 subunit is involved in platelet signaling, clot retraction, and thrombus stability

Randriamboavonjy, V., Isaak, J., Frömel, T., Viollet, B., Fißlthaler, B., Preissner, K. T., & Fleming, I. (2010) · Blood · doi:10.1182/blood-2010-04-279612 · Cited by 47 · see citing works

Does LKB1 Mediate Activation of Hepatic AMP-Protein Kinase (AMPK) and Sirtuin1 (SIRT1) After Roux-en-Y Gastric Bypass in Obese Rats?

Peng, Y., Rideout, D. A., Rakita, S., Gower, W. R., You, M., & Murr, M. M. (2009) · Journal of Gastrointestinal Surgery · doi:10.1007/s11605-009-1102-5 · Cited by 47 · see citing works

AMPK

Andersen, M. N., & Rasmussen, H. B. (2012) · Communicative & Integrative Biology · doi:10.4161/cib.21200 · Cited by 47 · see citing works

1 REGULATION OF LKB1-DEPENDENT ADENOSINE MONOPHOSPHATE-ACTIVATED PROTEIN KINASE BY PROTEIN KINASE C-z R.

Xie, Z., Davis, B., Zhang, M., & Zou, M.-H. (2006) · Journal of Investigative Medicine · doi:10.2310/6650.2005.x0008

Protein kinase C ζ‐dependent LKB1 phosphorylation at serine 428 induces LKB1 nuclear export and apoptosis in endothelial cells

Song, P., Xie, Z., Wu, Y., Xu, J., Dong, Y., & Zou, M. (2008) · The FASEB Journal · doi:10.1096/fasebj.22.1_supplement.648.12

Modulation by Peroxynitrite of Akt- and AMP-activated Kinase-dependent Ser1179 Phosphorylation of Endothelial Nitric Oxide Synthase

Zou, M., Hou, X., Shi, C., Nagata, D., Walsh, K., & Cohen, R. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204512200 · Cited by 189 · see citing works

eNOS activation mediated by AMPK after stimulation of endothelial cells with histamine or thrombin is dependent on LKB1

Thors, B., Halldórsson, H., & Þorgeirsson, G. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.12.001 · Cited by 45 · see citing works

Activation of the AMP-Activated Protein Kinase (AMPK) by Nitrated Lipids in

Cells, E., Wu, Y., Dong, Y., Song, P., & Zou, M. (2012)