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

The protein kinase complement of the human genome

Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145

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

Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., Wu, M., Ventre, J., Doebber, T., Fujii, N., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13505 · Cited by 5,652

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

Hawley, S. A., Boudeau, J., Reid, J. L., Mustard, K. J., Udd, L., Mäkelä, T. P., Alessi, D. R., & Hardie, D. G. (2003) · Journal of Biology · doi:10.1186/1475-4924-2-28 · Cited by 1,694

A serine/threonine kinase gene defective in Peutz–Jeghers syndrome

Hemminki, A., Markie, D., Tomlinson, I. P. M., Avizienyte, E., Roth, S., Loukola, A., Bignell, G. R., Warren, W., Aminoff, M., Höglund, P., et al. (1998) · Nature · doi:10.1038/34432 · Cited by 1,680

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

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5-Aminoimidazole-4-Carboxamide Ribonucleoside. A Specific Method for Activating AMP-Activated Protein Kinase in Intact Cells?

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Peutz-Jeghers syndrome is caused by mutations in a novel serine threoninekinase

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par-1, a gene required for establishing polarity in C. elegans embryos, encodes a putative Ser/Thr kinase that is asymmetrically distributed

Guo, S., & Kemphues, K. J. (1995) · Cell · doi:10.1016/0092-8674(95)90082-9 · Cited by 1,113

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

Fryer, L. G. D., Patel, A. P., & Carling, D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202489200 · Cited by 1,035

MARK, a Novel Family of Protein Kinases That Phosphorylate Microtubule-Associated Proteins and Trigger Microtubule Disruption

Drewes, G., Ebneth, A., Preuss, U., Mandelkow, E.-M., & Mandelkow, E. (1997) · Cell · doi:10.1016/s0092-8674(00)80208-1 · Cited by 878

AMP-activated protein kinase activators can inhibit the growth of prostate cancer cells by multiple mechanisms

Xiang, X., Saha, A. K., Wen, R., Ruderman, N. B., & Luo, Z. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.06.133 · Cited by 257

Hepatocyte polarity

Treyer, A., & Müsch, A. (2013) · Comprehensive Physiology · doi:10.1002/cphy.c120009 · Cited by 252

Activation of the mTOR pathway in sporadic angiomyolipomas and other perivascular epithelioid cell neoplasms

Kenerson, H. L., Folpe, A. L., Τakayama, T. K., & Yeung, R. S. W. (2007) · Human Pathology · doi:10.1016/j.humpath.2007.01.028 · Cited by 250

Signaling networks in immunometabolism

Saravia, J., Raynor, J. L., Chapman, N. M., Lim, S. A., & Chi, H. (2020) · Cell Research · doi:10.1038/s41422-020-0301-1 · Cited by 258

Cell cycle arrest in Metformin treated breast cancer cells involves activation of AMPK, downregulation of cyclin D1, and requires p27Kip1 or p21Cip1

Zhuang, Y., & Miskimins, W. K. (2008) · Journal of Molecular Signaling · doi:10.1186/1750-2187-3-18 · Cited by 251

Cellular metabolism regulates the differentiation and function of T-cell subsets

Ma, S., Ming, Y., Wu, J., & Cui, G. (2024) · Cellular and Molecular Immunology · doi:10.1038/s41423-024-01148-8 · Cited by 276

PGE2 Induces Macrophage IL-10 Production and a Regulatory-like Phenotype via a Protein Kinase A–SIK–CRTC3 Pathway

MacKenzie, K. F., Clark, K., Naqvi, S., McGuire, V. A., Nöehren, G., Kristariyanto, Y. A., van den Bosch, M., Mudaliar, M., McCarthy, P. C., Pattison, M. J., et al. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1202462 · Cited by 252

mTOR: A pathogenic signaling pathway in developmental brain malformations

Crino, P. B. (2011) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2011.07.008 · Cited by 266

A comprehensive map of the mTOR signaling network

Caron, É., Ghosh, S., Matsuoka, Y., Ashton‐Beaucage, D., Therrien, M., Lemieux, S., Perreault, C., Roux, P. P., & Kitano, H. (2010) · Molecular Systems Biology · doi:10.1038/msb.2010.108 · Cited by 248

The liver kinase B1 is a central regulator of T cell development, activation, and metabolism

MacIver, N. J., Blagih, J., Saucillo, D. C., Tonelli, L., Griss, T., Rathmell, J. C., & Jones, R. G. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100367 · Cited by 235

A role for LKB1 gene in human cancer beyond the Peutz–Jeghers syndrome

Sánchez‐Céspedes, M. (2007) · Oncogene · doi:10.1038/sj.onc.1210594 · Cited by 233

Resveratrol Prevents the Prohypertrophic Effects of Oxidative Stress on LKB1

Dolinsky, V. W., Chan, A. Y. M., Frayne, I. R., Light, P. E., Rosiers, C. D., & Dyck, J. R. B. (2009) · Circulation · doi:10.1161/circulationaha.108.787440 · Cited by 237

Staying alive

Valcourt, J. R., Lemons, J. M. S., Haley, E. M., Kojima, M. L., Demuren, O. O., & Coller, H. A. (2012) · Cell Cycle · doi:10.4161/cc.19879 · Cited by 240

LKB1; linking cell structure and tumor suppression

Hezel, A. F., & Bardeesy, N. M. (2008) · Oncogene · doi:10.1038/onc.2008.342 · Cited by 237

The tau of MARK: a polarized view of the cytoskeleton

Matenia, D., & Mandelkow, E. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.03.008 · Cited by 236

Control of AMPK-related kinases by USP9X and atypical Lys29/Lys33-linked polyubiquitin chains

Al-Hakim, A., Zagórska, A., Chapman, L., Deák, M., Peggie, M. W., & Alessi, D. R. (2008) · Biochemical Journal · doi:10.1042/bj20080067 · Cited by 224

Metformin attenuates ovarian cancer cell growth in an AMP‐kinase dispensable manner

Rattan, R., Giri, S., Hartmann, L. C., & Shridhar, V. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00954.x · Cited by 226

LKB1 and AMPK Family Signaling: The Intimate Link Between Cell Polarity and Energy Metabolism

Jansen, M., ten Klooster, J. P., Offerhaus, G. J. A., & Clevers, H. C. (2009) · Physiological Reviews · doi:10.1152/physrev.00026.2008 · Cited by 233

Deficiency of LKB1 in heart prevents ischemia-mediated activation of AMPKα2 but not AMPKα1

Sakamoto, K., Zarrinpashneh, E., Budas, G. R., Pouleur, A., Dutta, A., Prescott, A. R., Vanoverschelde, J., Ashworth, A., Jovanović, A., Alessi, D. R., et al. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00443.2005 · Cited by 224

AMP-activated protein kinase and the regulation of glucose transport

FUJII, N. L., Jessen, N., & Goodyear, L. J. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00207.2006 · Cited by 224

Metabolic control of the Treg/Th17 axis

Barbi, J. J., Pardoll, D. M., & Pan, F. (2013) · Immunological Reviews · doi:10.1111/imr.12029 · Cited by 227

Role of AMP‐activated protein kinase in the metabolic syndrome and in heart disease

Hardie, D. G. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.11.018 · Cited by 221

Phosphorylation by Akt within the ST loop of AMPK-α1 down-regulates its activation in tumour cells

Hawley, S. A., Ross, F. A., Gowans, G. J., Tibarewal, P., Leslie, N. R., & Hardie, D. G. (2014) · Biochemical Journal · doi:10.1042/bj20131344 · Cited by 229

WIPI3 and WIPI4 β-propellers are scaffolds for LKB1-AMPK-TSC signalling circuits in the control of autophagy

Bakula, D., Müller, A. J., Zuleger, T., Takács, Z., Franz‐Wachtel, M., Thost, A.-K., Brigger, D., Tschan, M. P., Frickey, T., Robenek, H., et al. (2017) · Nature Communications · doi:10.1038/ncomms15637 · Cited by 216

MicroRNA-451 Exacerbates Lipotoxicity in Cardiac Myocytes and High-Fat Diet-Induced Cardiac Hypertrophy in Mice Through Suppression of the LKB1/AMPK Pathway

Kuwabara, Y., Horie, T., Baba, O., Watanabe, S., Nishiga, M., Usami, S., Izuhara, M., Nakao, T., Nishino, T., Otsu, K., et al. (2014) · Circulation Research · doi:10.1161/circresaha.116.304707 · Cited by 214

Targeting Apoptosis in Cancer

Singh, P., & Lim, B. (2022) · Current Oncology Reports · doi:10.1007/s11912-022-01199-y · Cited by 222

Skeletal Muscle-Selective Knockout of LKB1 Increases Insulin Sensitivity, Improves Glucose Homeostasis, and Decreases TRB3

Koh, H.-J., Arnolds, D. E., Fujii, N., Tran, T. T., Rogers, M. J., Jessen, N., Li, Y., Liew, C. W., Ho, R. C., Hirshman, M. F., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00979-06 · Cited by 202

Metabolic regulator LKB1 is crucial for Schwann cell–mediated axon maintenance

Beirowski, B., Babetto, E., Golden, J. P., Chen, Y., Yang, K., Gross, R. W., Patti, G. J., & Milbrandt, J. (2014) · Nature Neuroscience · doi:10.1038/nn.3809 · Cited by 210

AMP-activated protein kinase: balancing the scales

Carling, D. (2004) · Biochimie · doi:10.1016/j.biochi.2004.10.017 · Cited by 202

Current understanding of metformin effect on the control of hyperglycemia in diabetes

An, H., & He, L. (2016) · Journal of Endocrinology · doi:10.1530/joe-15-0447 · Cited by 205

Impaired Activation of AMP-Kinase and Fatty Acid Oxidation by Globular Adiponectin in Cultured Human Skeletal Muscle of Obese Type 2 Diabetics

Chen, M. B., McAinch, A. J., Macaulay, S. L., Castelli, L. A., O’Brien, P. E., Dixon, J. B., Cameron‐Smith, D., Kemp, B. E., & Steinberg, G. R. (2005) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-1980 · Cited by 201

Genetic Analysis Reveals AMPK Is Required to Support Tumor Growth in Murine Kras-Dependent Lung Cancer Models

Eichner, L. J., Brun, S. N., Herzig, S., Young, N. P., Curtis, S. D., Shackelford, D. B., Shokhirev, M. N., Leblanc, M., Vera, L. I., Hutchins, A., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.10.005 · Cited by 194

The regulation and function of mammalian AMPK‐related kinases

Bright, N. J., Thornton, C., & Carling, D. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01971.x · Cited by 208

New Roles for the LKB1-NUAK Pathway in Controlling Myosin Phosphatase Complexes and Cell Adhesion

Zagórska, A., Deak, M., Campbell, D. G., Banerjee, S., Hirano, M., Aizawa, S., Prescott, A. R., & Alessi, D. R. (2010) · Science Signaling · doi:10.1126/scisignal.2000616 · Cited by 193

Maternal Embryonic Leucine Zipper Kinase/Murine Protein Serine-Threonine Kinase 38 Is a Promising Therapeutic Target for Multiple Cancers

Gray, D., Jubb, A. M., Hogue, D. A., Dowd, P., Kljavin, N. M., Yi, S., Bai, W., Frantz, G. D., Zhang, Z., Koeppen, H., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4531 · Cited by 193

Arabidopsis Protein Kinases GRIK1 and GRIK2 Specifically Activate SnRK1 by Phosphorylating Its Activation Loop

Shen, W., Reyes, M. I., & Hanley-Bowdoin, L. K. (2009) · PLANT PHYSIOLOGY · doi:10.1104/pp.108.132787 · Cited by 185

iPTMnet: an integrated resource for protein post-translational modification network discovery

Huang, H.-Z., Arighi, C., Ross, K. E., Ren, J., Li, G., Chen, S.-C., Wang, Q.-H., Cowart, J. E., Vijay-Shanker, K., & Wu, C. H. (2017) · Nucleic Acids Res. · doi:10.1093/nar/gkx1104 · Cited by 169

The Skp2 Pathway: A Critical Target for Cancer Therapy

Cai, Z., Moten, A., Peng, D., Hsu, C.-C., Pan, B., Manne, R., Li, H., & Lin, H. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.01.013 · Cited by 186

AMP-activated protein kinase (AMPK) is a tau kinase, activated in response to amyloid β-peptide exposure

Thornton, C., Bright, N. J., Sastre, M., Muckett, P. J., & Carling, D. (2011) · Biochemical Journal · doi:10.1042/bj20101485 · Cited by 193

Phosphorylation and 14‐3‐3 binding of Arabidopsis trehalose‐phosphate synthase 5 in response to 2‐deoxyglucose

Harthill, J. E., Meek, S. E. M., MORRICE, N. A., Peggie, M. W., Borch, J., Wong, B. H. C., & MacKintosh, C. (2006) · The Plant Journal · doi:10.1111/j.1365-313x.2006.02780.x · Cited by 182

The Metabolic Mechanisms of Breast Cancer Metastasis

Wang, L., Zhang, S., & Wang, X. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2020.602416 · Cited by 200

AMP-activated protein kinase: a cellular energy sensor with a key role in metabolic disorders and in cancer

Hardie, D. G. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390001 · Cited by 180

Silencing the constitutive active transcription factor CREB by the LKB1‐SIK signaling cascade

Katoh, Y., Takemori, H., Lin, X., Tamura, M., Muraoka, M., Satoh, T., Tsuchiya, Y., Li, M., Doi, J., Miyauchi, A., et al. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05291.x · Cited by 173

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

Xie, Z., Dong, Y., Zhang, M., Cui, M.-Z., Cohen, R. A., Riek, U., Neumann, D., Schlattner, U., & Zou, M.-H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511178200 · Cited by 172

Histological evaluation of AMPK signalling in primary breast cancer

Hadad, S. M., Baker, L., Quinlan, P., Robertson, K. E., Bray, S. E., Thomson, G., Kellock, D., Jordan, L. B., Purdie, C. A., Hardie, D. G., et al. (2009) · BMC Cancer · doi:10.1186/1471-2407-9-307 · Cited by 177

Rosiglitazone suppresses human lung carcinoma cell growth through PPARγ-dependent and PPARγ-independent signal pathways

Han, S., & Roman, J. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-05-0347 · Cited by 170

Identification of the sucrose non‐fermenting related kinase SNRK, as a novel LKB1 substrate

Jaleel, M., McBride, A., Lizcano, J. M., Deák, M., Toth, R. L., MORRICE, N. A., & Alessi, D. R. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.01.042 · Cited by 168

The AMPK-Related Kinases SIK1 and SIK3 Mediate Key Tumor-Suppressive Effects of LKB1 in NSCLC

Hollstein, P. E., Eichner, L. J., Brun, S. N., Kamireddy, A., Svensson, R. U., Vera, L. I., Ross, D. S., Rymoff, T. J., Hutchins, A., Galvez, H. M., et al. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-1261 · Cited by 168

AMP-activated protein kinase regulates CO2-induced alveolar epithelial dysfunction in rats and human cells by promoting Na,K-ATPase endocytosis

Vadász, I., Dada, L. A., Briva, A., Bittar, H. E. T., Welch, L. C., Chen, J., Tóth, P. T., Lecuona, E., Witters, L. A., Schumacker, P. T., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci29723 · Cited by 167

Control of YAP/TAZ Activity by Metabolic and Nutrient-Sensing Pathways

Santinon, G., Pocaterra, A., & Dupont, S. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.11.004 · Cited by 169

Epithelial cell extrusion: Pathways and pathologies

Gudipaty, S. A., & Rosenblatt, J. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.05.010 · Cited by 163

Salt-Inducible Kinase 2 Couples Ovarian Cancer Cell Metabolism with Survival at the Adipocyte-Rich Metastatic Niche

Miranda, F., Mannion, D., Liu, S., Zheng, Y., Mangala, L. S., Redondo, C., Herrero‐González, S., Xu, R., Taylor, C., Fotso, D. C., et al. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.06.020 · Cited by 167

Reelin and Stk25 Have Opposing Roles in Neuronal Polarization and Dendritic Golgi Deployment

Matsuki, T., Matthews, R. T., Cooper, J. A., van der Brug, M. P., Cookson, M., Hardy, J., Olson, E. C., & Howell, B. W. (2010) · Cell · doi:10.1016/j.cell.2010.10.029 · Cited by 172

AMP-Activated Protein Kinase: A Key Stress Signaling Pathway in the Heart

Young, L. H., Li, J., Baron, S. J., & Russell, R. R. (2005) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2005.04.005 · Cited by 165

AMP-activated protein kinase pathway: a potential therapeutic target in cardiometabolic disease

Wong, A., Howie, J., Petrie, J. R., & Lang, C. C. (2009) · Clinical Science · doi:10.1042/cs20080066 · Cited by 170

Cardiac-specific deletion of LKB1 leads to hypertrophy and dysfunction

Ikeda, Y., Sato, K., Pimentel, D. R., Sam, F., Shaw, R. J., Dyck, J. R. B., & Walsh, K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.057273 · Cited by 164

Adapt and conquer: Metabolic flexibility in cancer growth, invasion and evasion

Kreuzaler, P. A., Panina, Y., Segal, J., & Yuneva, M. O. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.08.021 · Cited by 170

Analysis of the LKB1-STRAD-MO25 complex

Boudeau, J., Scott, J. W., Resta, N., Deák, M., Kieloch, A., Komander, D., Hardie, D. G., Prescott, A. R., van Aalten, D. M. F., & Alessi, D. R. (2004) · Journal of Cell Science · doi:10.1242/jcs.01571 · Cited by 161

The LKB1-salt-inducible kinase pathway functions as a key gluconeogenic suppressor in the liver

Patel, K., Foretz, M., Marion, A., Campbell, D. G., Gourlay, R., Boudaba, N., Tournier, E., Titchenell, P. M., Peggie, M. W., Deák, M., et al. (2014) · Nature Communications · doi:10.1038/ncomms5535 · Cited by 171

Molecular Pathways: Is AMPK a Friend or a Foe in Cancer?

Hardie, D. G. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-3300 · Cited by 166

LKB1, Salt-Inducible Kinases, and MEF2C Are Linked Dependencies in Acute Myeloid Leukemia

Tarumoto, Y., Lu, B., Somerville, T. D. D., Huang, Y., Milazzo, J. P., Wu, X., Klingbeil, O., Demerdash, O. E., Shi, J., & Vakoc, C. R. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.02.011 · Cited by 154

Dysregulation of HIF and VEGF is a unifying feature of the familial hamartoma syndromes

Brugarolas, J., & Kaelin, W. G. (2004) · Cancer Cell · doi:10.1016/j.ccr.2004.06.020 · Cited by 165

SIK1 Couples LKB1 to p53-Dependent Anoikis and Suppresses Metastasis

Cheng, H.-L. M., Liu, P., Wang, Z. C., Zou, L., Santiago, S., Garbitt, V. M., Gjoerup, O. V., Iglehart, J. D., Miron, A., Richardson, A. L., et al. (2009) · Science Signaling · doi:10.1126/scisignal.2000369 · Cited by 162

miR-204-5p and miR-211-5p Contribute to BRAF Inhibitor Resistance in Melanoma

Díaz‐Martínez, M., Benito-Jardón, L., Alonso, L., Koetz‐Ploch, L., Hernando, E., & Teixidó, J. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-1318 · Cited by 162

Physiological functions of peroxisome proliferator-activated receptor β

Neels, J. G., & Grimaldi, P. A. (2014) · Physiological Reviews · doi:10.1152/physrev.00027.2013 · Cited by 161

Mst4 and Ezrin Induce Brush Borders Downstream of the Lkb1/Strad/Mo25 Polarization Complex

ten Klooster, J. P., Jansen, M., Yuan, J., Oorschot, V. M. J., Begthel, H., Giacomo, V. D., Colland, F., de Koning, J., Maurice, M. M., Hornbeck, P. V., et al. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.01.016 · Cited by 161

Maternal embryonic leucine zipper kinase is a key regulator of the proliferation of malignant brain tumors, including brain tumor stem cells

Nakano, I., Masterman-Smith, M. D., Saigusa, K., Paucar, A. A., Horvath, S., Shoemaker, L. D., Watanabe, M., Negro, A., Bajpai, R., Howes, A. L., et al. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21471 · Cited by 155

Targeting AMPK: A new therapeutic opportunity in breast cancer

Hadad, S. M., Fleming, S., & Thompson, A. M. (2008) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2008.01.007 · Cited by 158

A protein interaction landscape of breast cancer

Kim, M., Park, J., Bouhaddou, M., Kim, K., Rojc, A., Modak, M., Soucheray, M., McGregor, M., O’Leary, P. C., Wolf, D. M., et al. (2021) · Science · doi:10.1126/science.abf3066 · Cited by 160

Metabolism Controls the Balance of Th17/T-Regulatory Cells

Sun, L., Fu, J., & Zhou, Y. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01632 · Cited by 167

Tamoxifen-Induced Anorexia Is Associated With Fatty Acid Synthase Inhibition in the Ventromedial Nucleus of the Hypothalamus and Accumulation of Malonyl-CoA

López, M., Lelliott, C. J., Tovar, S. A., Kimber, W. L., Gallego, R., Virtue, S., Blount, M., Vazquez, M. J., Finer, N., Powles, T. J., et al. (2006) · Diabetes · doi:10.2337/db05-1356 · Cited by 151

Pancreatic Lkb1 Deletion Leads to Acinar Polarity Defects and Cystic Neoplasms

Hezel, A. F., Gurumurthy, S., Granot, Z., Swisa, A., Chu, G. C., Bailey, G., Dor, Y., Bardeesy, N. M., & DePinho, R. A. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01621-07 · Cited by 161

ATP and MO25α Regulate the Conformational State of the STRADα Pseudokinase and Activation of the LKB1 Tumour Suppressor

Zeqiraj, E., Filippi, B., Goldie, S. P., Navratilova, I. H., Boudeau, J., Deák, M., Alessi, D. R., & van Aalten, D. M. F. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000126 · Cited by 147

Calorie Restriction and Dietary Restriction Mimetics: A Strategy for Improving Healthy Aging and Longevity

Testa, G., Biasi, F., Poli, G., & Chiarpotto, E. (2014) · Current Pharmaceutical Design · doi:10.2174/13816128113196660699 · Cited by 153

The 14-3-3 proteins in regulation of cellular metabolism

Kleppe, R., Martı́nez, A., Døskeland, S. O., & Haavik, J. (2011) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2011.08.008 · Cited by 150

Skeletal muscle and heart LKB1 deficiency causes decreased voluntary running and reduced muscle mitochondrial marker enzyme expression in mice.

Thomson, D. M., Porter, B. B., Tall, J. H., Kim, H.-J., Barrow, J. R., & Winder, W. W. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00366.2006 · Cited by 146

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

Forcet, C., Etienne‐Manneville, S., Gaude, H., Fournier, L., Debilly, S., Salmi, M., Baas, A. F., Olschwang, S., Clevers, H. C., & Billaud, M. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi139 · Cited by 157

Molecular Physiology of SPAK and OSR1: Two Ste20-Related Protein Kinases Regulating Ion Transport

Gagnon, K. B., & Delpire, E. J. (2012) · Physiological Reviews · doi:10.1152/physrev.00009.2012 · Cited by 148

Metformin Activates AMP-Activated Protein Kinase by Promoting Formation of the αβγ Heterotrimeric Complex

Meng, S., Cao, J., He, Q., Xiong, L., Chang, E., Radovick, S., Wondisford, F. E., & He, L. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.604421 · Cited by 146

Cellular energy sensing and signaling by AMP-activated protein kinase

Winder, W. W., & Thomson, D. M. (2007) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-007-0008-7 · Cited by 142

The role of LKB1 and AMPK in cellular responses to stress and damage

Alexander, A., & Walker, C. L. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.03.010 · Cited by 145

Exercise-induced AMPK activity in skeletal muscle: Role in glucose uptake and insulin sensitivity

Friedrichsen, M., Mortensen, B., Pehmøller, C., Birk, J. B., & Wojtaszewski, J. F. P. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.06.013 · Cited by 143

MO25 is a master regulator of SPAK/OSR1 and MST3/MST4/YSK1 protein kinases

Filippi, B., Heros, P. D. L., Mehellou, Y., Navratilova, I. H., Gourlay, R., Deák, M., Plater, L., Toth, R. L., Zeqiraj, E., & Alessi, D. R. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.78 · Cited by 144

Calmodulin-dependent protein kinase kinase-β activates AMPK without forming a stable complex: synergistic effects of Ca2+ and AMP

Fogarty, S., Hawley, S. A., Green, K. A., Saner, N., Mustard, K. J., & Hardie, D. G. (2009) · Biochemical Journal · doi:10.1042/bj20091372 · Cited by 146

Salt-Inducible Kinases: Physiology, Regulation by cAMP, and Therapeutic Potential

Wein, M. N., Foretz, M., Fisher, D. E., Xavier, R. J., & Kronenberg, H. M. (2018) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2018.08.004 · Cited by 138

Telmisartan prevention of LPS-induced microglia activation involves M2 microglia polarization via CaMKKβ-dependent AMPK activation

Xu, Y., Xu, Y., Wang, Y., Wang, Y., He, L., Jiang, Z., Huang, Z., Liao, H., Li, J., Saavedra, J. M., et al. (2015) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2015.07.015 · Cited by 140

Mucosal prolapse in the pathogenesis of Peutz-Jeghers polyposis

Jansen, M., de Leng, W. W. J., Baas, A. F., Myoshi, H., Mathus-Vliegen, L., Taketo, M. M., Clevers, H. C., Giardiello, F. M., & Offerhaus, G. J. A. (2005) · Gut · doi:10.1136/gut.2005.069062 · Cited by 140

Dysfunctional AMPK activity, signalling through mTOR and survival in response to energetic stress in LKB1-deficient lung cancer

Carretero, J., Medina, P. P., Blanco, R., Smit, L., Tang, M., Roncador, G., Maestre, L., Conde, E., López‐Ríos, F., Clevers, H. C., et al. (2006) · Oncogene · doi:10.1038/sj.onc.1209951 · Cited by 143

The strange case of AMPK and cancer: Dr Jekyll or Mr Hyde?

Vara‐Ciruelos, D., Russell, F. M., & Hardie, D. G. (2019) · Open Biology · doi:10.1098/rsob.190099 · Cited by 140

Glucose-Dependent Insulinotropic Polypeptide-Mediated Up-Regulation of β-Cell Antiapoptotic Bcl-2 Gene Expression Is Coordinated by Cyclic AMP (cAMP) Response Element Binding Protein (CREB) and cAMP-Responsive CREB Coactivator 2

Kim, S., Nian, C., Widenmaier, S. B., & McIntosh, C. H. S. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00325-07 · Cited by 138

LKB1 and AMPK in cell polarity and division

Williams, T., & Brenman, J. E. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.01.008 · Cited by 141

Fuel economy in food‐deprived skeletal muscle: signaling pathways and regulatory mechanisms

de Lange, P., Moreno, M., Silvestri, E., Lombardi, A., Goglia, F., & Lanni, A. (2007) · The FASEB Journal · doi:10.1096/fj.07-8527rev · Cited by 137

Cadmium induces autophagy through ROS-dependent activation of the LKB1–AMPK signaling in skin epidermal cells

Son, Y., Wang, X., Hitron, J. A., Zhang, Z., Cheng, S., Budhraja, A., Ding, S., Lee, J., & Shi, X. (2011) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2011.06.024 · Cited by 136

Regulation of the MEX-5 Gradient by a Spatially Segregated Kinase/Phosphatase Cycle

Griffin, E. E., Odde, D. J., & Seydoux, G. (2011) · Cell · doi:10.1016/j.cell.2011.08.012 · Cited by 135

The potent roles of salt-inducible kinases (SIKs) in metabolic homeostasis and tumorigenesis

Sun, Z., Jiang, Q., Li, J., & Guo, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00265-w · Cited by 132

MARKing tau for tangles and toxicity

Drewes, G. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.08.001 · Cited by 137

Mimicry of a Cellular Low Energy Status Blocks Tumor Cell Anabolism and Suppresses the Malignant Phenotype

Swinnen, J. V., Beckers, A., Brusselmans, K., Organe, S., Segers, J., Timmermans, L., Vanderhoydonc, F., Deboel, L., Derua, R., Waelkens, E., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3025 · Cited by 136

Nuts and bolts of the salt-inducible kinases (SIKs)

Darling, N. J., & Cohen, P. (2021) · Biochemical Journal · doi:10.1042/bcj20200502 · Cited by 134

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

Hawley, S. A., Boudeau, J., Reid, J. L., Mustard, K. J., Udd, L., Mäkelä, T. P., Alessi, D. R., & Hardie, D. G. (2003) · Journal of Biology · doi:10.1186/1475-4924-2-28 · Cited by 1,694

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

Woods, A., Johnstone, S. R., Dickerson, K., Leiper, F. C., Fryer, L. G. D., Neumann, D., Schlattner, U., Wallimann, T., Carlson, M., & Carling, D. (2003) · Current Biology · doi:10.1016/j.cub.2003.10.031 · Cited by 1,650

COMMENTARY The

(2013)

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

Shaw, R. J., Kosmatka, M., Bardeesy, N., Hurley, R. L., Witters, L. A., DePinho, R. A., & Cantley, L. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308061100 · Cited by 1,797

LKB1, an upstream AMPK kinase, regulates glucose and lipid metabolism in cultured liver and muscle cells

Imai, K., Inukai, K., Ikegami, Y., Awata, T., & Katayama, S. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.056 · Cited by 54