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

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

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

Corton, J. M., Gillespie, J. G., Hawley, S. A., & Hardie, D. G. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20498.x · Cited by 1,232

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

Jenne, D. E., Reomann, H., Nezu, J., Friedel, W., Loff, S., Jeschke, R., Müller, O., Back, W. E., & Zimmer, M. (1998) · Nature Genetics · doi:10.1038/ng0198-38 · Cited by 1,201

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

mRNA Translation and Energy Metabolism in Cancer: The Role of the MAPK and mTORC1 PathwaysPreprint

Topisirović, I., & Sonenberg, N. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010785 · Cited by 96

Pterosin B prevents chondrocyte hypertrophy and osteoarthritis in mice by inhibiting Sik3

Yahara, Y., Takemori, H., Okada, M., Kosai, A., Yamashita, A., Kobayashi, T., Fujita, K., Itoh, Y., Nakamura, M., Fuchino, H., et al. (2016) · Nature Communications · doi:10.1038/ncomms10959 · Cited by 91

LKB1 loss promotes endometrial cancer progression via CCL2-dependent macrophage recruitment

Peña, C. G., Nakada, Y., Saatcioglu, H. D., Aloisio, G. M., Cuevas, I., Zhang, S., Miller, D. S., Lea, J. S., Wong, K., DeBerardinis, R. J., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci82152 · Cited by 92

LKB1 deficiency-induced metabolic reprogramming in tumorigenesis and non-neoplastic diseases

Zhang, Y., Meng, Q., Sun, Q., Xu, Z., Zhou, H., & Wang, Y. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101131 · Cited by 91

Analysis of detergent-resistant membranes of Helicobacter pylori infected gastric adenocarcinoma cells reveals a role for MARK2/Par1b in CagA-mediated disruption of cellular polarity

Zeaiter, Z., Cohen, D., Müsch, A., Bagnoli, F., Covacci, A., & Stein, M. (2008) · Cellular Microbiology · doi:10.1111/j.1462-5822.2007.01084.x · Cited by 91

Dissecting the role of AMP-activated protein kinase in human diseases

Li, J., Zhong, L., Wang, F., & Zhu, H. (2017) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2016.12.003 · Cited by 90

Rosiglitazone Stimulates Nitric Oxide Synthesis in Human Aortic Endothelial Cells via AMP-activated Protein Kinase*

Boyle, J. G., Logan, P. J., Ewart, M., Reihill, J. A., Ritchie, S. A., Connell, J., Cleland, S. J., & Salt, I. P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710048200 · Cited by 89

Evidence of cancer‐promoting roles for AMPK and related kinases

Monteverde, T., Muthalagu, N., Port, J., & Murphy, D. J. (2015) · FEBS Journal · doi:10.1111/febs.13534 · Cited by 91

Hippocampal Salt-Inducible Kinase 2 Plays a Role in Depression via the CREB-Regulated Transcription Coactivator 1–cAMP Response Element Binding–Brain-Derived Neurotrophic Factor Pathway

Jiang, B., Wang, H., Wang, J., Wang, Y., Zhu, Q., Wang, C., Song, L., Gao, T., Wang, Y., Meng, G., et al. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2018.10.004 · Cited by 87

Resistance to Durvalumab and Durvalumab plus Tremelimumab Is Associated with Functional STK11 Mutations in Patients with Non–Small Cell Lung Cancer and Is Reversed by STAT3 Knockdown

Pore, N., Wu, S., Standifer, N., Jure-Kunkel, M., de los Reyes, M., Shrestha, Y., Halpin, R., Rothstein, R., Mulgrew, K., Blackmore, S., et al. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-1543 · Cited by 88

Metabolic activation of AMP kinase in vascular smooth muscle

Rubin, L. J., Magliola, L., Feng, X., JONES, A. W., & Hale, C. C. (2004) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00075.2004 · Cited by 90

Inhibition of SIK2 and SIK3 during differentiation enhances the anti-inflammatory phenotype of macrophages

Darling, N. J., Toth, R. L., Arthur, J. S. C., & Clark, K. (2016) · Biochemical Journal · doi:10.1042/bcj20160646 · Cited by 89

LKB 1 and AMPK : central regulators of lymphocyte metabolism and function

Blagih, J., Krawczyk, C. M., & Jones, R. G. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01157.x · Cited by 91

AMP-Activated Protein Kinase: A New Beta-Cell Glucose Sensor?

Leclerc, I., & Rutter, G. A. (2004) · Diabetes · doi:10.2337/diabetes.53.suppl_3.s67 · Cited by 91

Different prognostic impact ofSTK11mutations in non-squamous non-small-cell lung cancer

Pécuchet, N., Laurent‐Puig, P., Mansuet‐Lupo, A., Legras, A., Alifano, M., Pallier, K., Didelot, A., Gibault, L., Danel, C. J., Just, P., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.6379 · Cited by 91

KIN‐29 SIK regulates chemoreceptor gene expression via an MEF2 transcription factor and a class II HDAC

van der Linden, A. M., Nolan, K. M., & Sengupta, P. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601479 · Cited by 87

Loss of LKB1 disrupts breast epithelial cell polarity and promotes breast cancer metastasis and invasion

Li, J., Liu, J., Yang, J., Li, P., Mao, X., Li, W., & Liu, P. (2014) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-014-0070-0 · Cited by 90

Regulation of AMP‐activated protein kinase by LKB1 and CaMKK in adipocytes

Gormand, A., Henriksson, E., Ström, K., Jensen, T. E., Sakamoto, K., & Göransson, O. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23053 · Cited by 85

Regulation of AMP-activated protein kinase activity by G-protein coupled receptors: Potential utility in treatment of diabetes and heart disease

Hutchinson, D. S., Summers, R. J., & Bengtsson, T. (2008) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2008.05.008 · Cited by 88

An update on the genetics of colorectal cancer

Kemp, Z. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh247 · Cited by 87

STK11 (LKB1) mutations in metastatic NSCLC: Prognostic value in the real world

Shire, N. J., Klein, A. B., Golozar, A., Collins, J. M., Fraeman, K. H., Nordstrom, B. L., McEwen, R., Hembrough, T., & Rizvi, N. A. (2020) · PLOS ONE · doi:10.1371/journal.pone.0238358 · Cited by 85

Phosphorylation of microtubule‐associated protein tau by AMPK‐related kinases

Yoshida, H., & Goedert, M. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07523.x · Cited by 85

A new role of NUAK1: directly phosphorylating p53 and regulating cell proliferation

Hou, X., Liu, J.-E., Liu, W., Liu, C.-Y., Liu, Z., & Zy, S. (2011) · Oncogene · doi:10.1038/onc.2011.19 · Cited by 85

Characterization of the AMP-activated protein kinase pathway in chickens

Proszkowiec‐Weglarz, M., Richards, M. P., Ramachandran, R., & McMurtry, J. P. (2005) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2005.10.009 · Cited by 89

Regulation of CREB-mediated gene expression by salt inducible kinase

Takemori, H., & Okamoto, M. (2007) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2007.09.006 · Cited by 85

Salt-inducible kinase 2 regulates CRTCs, HDAC4 and glucose uptake in adipocytes

Henriksson, E., Säll, J., Gormand, A., Wasserström, S., Morrice, N. A., Fritzen, A. M., Foretz, M., Campbell, D. G., Sakamoto, K., Ekelund, M., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.153932 · Cited by 87

The PAR network: redundancy and robustness in a symmetry-breaking system

Motegi, F., & Seydoux, G. (2013) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2013.0010 · Cited by 85

AMPK Causes Cell Cycle Arrest in LKB1-Deficient Cells via Activation of CAMKK2

Fogarty, S., Ross, F. A., Vara‐Ciruelos, D., Gray, A., Gowans, G. J., & Hardie, D. G. (2016) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0479 · Cited by 90

LKB1 tumor suppressor regulates AMP kinase/mTOR-independent cell growth and proliferation via the phosphorylation of Yap

Nguyen, H. B., Babcock, J. T., Wells, C. D., & Quilliam, L. A. (2013) · Oncogene · doi:10.1038/onc.2012.431 · Cited by 84

Chemerin suppresses neuroinflammation and improves neurological recovery via CaMKK2/AMPK/Nrf2 pathway after germinal matrix hemorrhage in neonatal rats

Zhang, Y., Xu, N., Ding, Y. P., Zhang, Y., Li, Q., Flores, J. J., Haghighiabyaneh, M., Doycheva, D. M., Tang, J., & Zhang, J. H. (2018) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2018.02.015 · Cited by 84

Resveratrol-Induced Sirt1 Activation Derives from Sirt1 Phosphorylation by LKB1

Huang, Y., Lu, J., Li, Z., Wang, M., Shi, R., Yuan, X. N., Gao, X., Liu, X., Zang, J., Liu, W., et al. (2020) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100929 · Cited by 87

Activating AMP-Activated Protein Kinase without AMP

Birnbaum, M. J. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.07.012 · Cited by 81

Dynein Modifiers in C. elegans: Light Chains Suppress Conditional Heavy Chain Mutants

O'Rourke, S. M., Dorfman, M. D., Carter, J. C., & Bowerman, B. A. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030128 · Cited by 82

AID-Induced Genotoxic Stress Promotes B Cell Differentiation in the Germinal Center via ATM and LKB1 Signaling

Sherman, M. H., Kuraishy, A. I., Deshpande, C., Hong, J. S., Cacalano, N. A., Gatti, R. A., Manis, J. P., Damore, M. A., Pellegrini, M. A., & Teitell, M. A. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.019 · Cited by 87

AMPK: mediating the metabolic effects of salicylate-based drugs?

Steinberg, G. R., Dandapani, M., & Hardie, D. G. (2013) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.06.002 · Cited by 85

Characterization of WZ4003 and HTH-01-015 as selective inhibitors of the LKB1-tumour-suppressor-activated NUAK kinases

Banerjee, S., Buhrlage, S. J., Huang, H., Deng, X., Zhou, W., Wang, J., Traynor, R., Prescott, A. R., Alessi, D. R., & Gray, N. S. (2013) · Biochemical Journal · doi:10.1042/bj20131152 · Cited by 85

Regulation of microtubule (MT)-based cytoskeleton in the seminiferous epithelium during spermatogenesis

Tang, E. I., Mruk, D. D., & Cheng, C. Y. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.01.004 · Cited by 86

Structure of the Catalytic and Ubiquitin-Associated Domains of the Protein Kinase MARK/Par-1

Panneerselvam, S., Marx, A., Mandelkow, E., & Mandelkow�, E. (2006) · Structure · doi:10.1016/j.str.2005.09.022 · Cited by 82

MELK promotes Endometrial carcinoma progression via activating mTOR signaling pathway

Xu, Q., Ge, Q., Zhou, Y., Yang, B., Yang, Q., Jiang, S., Jiang, R., Ai, Z., Zhang, Z., & Teng, Y. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2019.102609 · Cited by 83

DAPK activates MARK1/2 to regulate microtubule assembly, neuronal differentiation, and tau toxicity

Wu, P.-R., Tsai, P.-I., Chen, G., Chou, H.-J., Huang, Y.-P., Chen, Y. H., Lin, M.-Y., Kimchi, A., Chien, C.-T., & Chen, R.-H. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.2 · Cited by 82

LKB1 Is Necessary for Akt-Mediated Phosphorylation of Proapoptotic Proteins

Zhong, D., Liu, X., Khuri, F. R., Sun, S., Vertino, P. M., & Zhou, W. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-1484 · Cited by 87

AMPK mediates curcumin-induced cell death in CaOV3 ovarian cancer cells

Di (1994) · Oncology Reports · doi:10.3892/or_00000179 · Cited by 83

Pseudokinases: Update on Their Functions and Evaluation as New Drug Targets

Byrne, D. P., Foulkes, D. M., & Eyers, P. A. (2017) · Future Medicinal Chemistry · doi:10.4155/fmc-2016-0207 · Cited by 84

Dissecting the Crosstalk between NRF2 Signaling and Metabolic Processes in Cancer

DeBlasi, J. M., & DeNicola, G. M. (2020) · Cancers · doi:10.3390/cancers12103023 · Cited by 82

Regulation of LKB1/STRAD Localization and Function by E-Cadherin

Sebbagh, M., Santoni, M.-J., Hall, B., Borg, J., & Schwartz, M. A. (2008) · Current Biology · doi:10.1016/j.cub.2008.11.033 · Cited by 93

LKB1 Deficiency Sensitizes Mice to Carcinogen-Induced Tumorigenesis

Gurumurthy, S., Hezel, A. F., Berger, J. H., Bosenberg, M., & Bardeesy, N. M. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-3225 · Cited by 82

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 85

New insights into the molecular mechanisms specifying neuronal polarity in vivo

Barnes, A. P., Solecki, D. J., & Polleux, F. (2008) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2008.05.003 · Cited by 85

Convergence of Hormones, Inflammation, and Energy-Related Factors: A Novel Pathway of Cancer Etiology

Slattery, M. L., & Fitzpatrick, F. A. (2009) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-08-0191 · Cited by 82

Activation of PAR-1 Kinase and Stimulation of Tau Phosphorylation by Diverse Signals Require the Tumor Suppressor Protein LKB1

Wang, J.-W., Imai, Y., & Lu, B. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.5094-06.2007 · Cited by 80

GSK-3β controls autophagy by modulating LKB1-AMPK pathway in prostate cancer cells

Sun, A., Li, C., Chen, R., Huang, Y., Chen, Q., Cui, X., Liu, H., Thrasher, J. B., & Li, B. (2015) · The Prostate · doi:10.1002/pros.23106 · Cited by 83

LKB1 and AMPK differentially regulate pancreatic β‐cell identity

Kone, M., Pullen, T. J., Sun, G., Ibberson, M. R., Martínez-Sánchez, A., Sayers, S. R., Nguyen‐Tu, M., Kantor, C., Swisa, A., Dor, Y., et al. (2014) · The FASEB Journal · doi:10.1096/fj.14-257667 · Cited by 84

A novel short splice variant of the tumour suppressor LKB1 is required for spermiogenesis

Towler, M. C., Fogarty, S., Hawley, S. A., Pan, D. A., Martin, D. M. A., Morrice, N. A., McCarthy, A., Galardo, M. N., Meroni, S. B., Cigorraga, S. B., et al. (2008) · Biochemical Journal · doi:10.1042/bj20081447 · Cited by 91

Inactivation of MARK4, an AMP-activated Protein Kinase (AMPK)-related Kinase, Leads to Insulin Hypersensitivity and Resistance to Diet-induced Obesity

Sun, C., Liang, T., Nie, J., Zhang, H., Han, X., & Shi, Y. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.388934 · Cited by 82

Role of Individual MARK Isoforms in Phosphorylation of Tau at Ser262 in Alzheimer’s Disease

Gu, G. J., Lund, H., Wu, D., Blokzijl, A., Classon, C., von Euler, G., Landegren, U. D., Sunnemark, D., & Kamali‐Moghaddam, M. (2013) · NeuroMolecular Medicine · doi:10.1007/s12017-013-8232-3 · Cited by 82

LKB1 Regulates Lipid Oxidation During Exercise Independently of AMPK

Jeppesen, J. F., Maarbjerg, S., Jordy, A. B., Fritzen, A. M., Pehmøller, C. K., Sylow, L., Serup, A. K., Jessen, N., Thorsen, K., Prats, C., et al. (2013) · Diabetes · doi:10.2337/db12-1160 · Cited by 82

Activation of NAD(P)H:Quinone Oxidoreductase 1 Prevents Arterial Restenosis by Suppressing Vascular Smooth Muscle Cell Proliferation

Kim, S.-Y., Jeoung, N. H., Oh, C. J., Choi, Y., Lee, H., Kim, H., Kim, J., Hwang, J. H., Tadi, S., Yim, Y., et al. (2009) · Circulation Research · doi:10.1161/circresaha.108.189837 · Cited by 80

The microtubule affinity regulating kinase MARK4 promotes axoneme extension during early ciliogenesis

Kuhns, S., Schmidt, K. N., Reymann, J., Gilbert, D. F., Neuner, A., Hub, B., Carvalho, R., Wiedemann, P., Zentgraf, H., Erfle, H., et al. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201206013 · Cited by 87

LKB1 and AMPK and the regulation of skeletal muscle metabolism

Koh, H.-J., Brandauer, J., & Goodyear, L. J. (2008) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/mco.0b013e3282fb7b76 · Cited by 78

Citrus Tangeretin Improves Skeletal Muscle Mitochondrial Biogenesis via Activating the AMPK-PGC1-α Pathway In Vitro and In Vivo: A Possible Mechanism for Its Beneficial Effect on Physical Performance

Kou, G., Li, Z., Wu, C., Liu, Y., Hu, Y., Guo, L., Xu, X., & Zhou, Z. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b04124 · Cited by 78

A single phosphorylation site of SIK3 regulates daily sleep amounts and sleep need in mice

Honda, T., Fujiyama, T., Miyoshi, C., Ikkyu, A., Hotta-Hirashima, N., Kanno, S., Mizuno, S., Sugiyama, F., Takahashi, S., Funato, H., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1810823115 · Cited by 76

Involvement of SIK3 in Glucose and Lipid Homeostasis in Mice

Uebi, T., Itoh, Y., Hatano, O., Kumagai, A., Sanosaka, M., Sasaki, T., Sasagawa, S., Doi, J., Tatsumi, K., Mitamura, K., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037803 · Cited by 79

Maternal Embryonic Leucine Zipper Kinase Is Upregulated and Required in Mammary Tumor-Initiating Cells In vivo

Hebbard, L., Maurer, J., Miller, A., Lesperance, J., Hassell, J. A., Oshima, R. G., & Terskikh, A. V. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-1295 · Cited by 82

Proteasome Failure Promotes Positioning of Lysosomes around the Aggresome via Local Block of Microtubule-Dependent Transport

Zaarur, N., Meriin, A. B., Bejarano, E., Xu, X., Gabai, V. L., Cuervo, A. M., & Sherman, M. Y. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00103-14 · Cited by 82

Salt‐inducible kinase‐1 represses cAMP response element‐binding protein activity both in the nucleus and in the cytoplasm

Katoh, Y., Takemori, H., Li, M., Muraoka, M., Doi, J., Horike, N., & Okamoto, M. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04372.x · Cited by 77

Structure and regulation of MARK, a kinase involved in abnormal phosphorylation of Tau protein

Timm, T., Marx, A., Panneerselvam, S., Mandelkow�, E., & Mandelkow, E. (2008) · BMC Neuroscience · doi:10.1186/1471-2202-9-s2-s9 · Cited by 78

AMPK promotes osteogenesis and inhibits adipogenesis through AMPK-Gfi1-OPN axis

Wang, Y., Qu, X., Yang, Y., Han, X., Wang, L., Qiao, H., Fan, Q., Tang, T., & Dai, K. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.06.004 · Cited by 76

Loss of the Par-1b/MARK2 polarity kinase leads to increased metabolic rate, decreased adiposity, and insulin hypersensitivity in vivo

Hurov, J., Huang, M., White, L. S., Lennerz, J. K., Choi, C. S., Cho, Y.-R., Kim, H., Prior, J. L., Piwnica-Worms, D., Cantley, L. C., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701179104 · Cited by 81

Interplay between cancer cell cycle and metabolism: Challenges, targets and therapeutic opportunities

Roy, D., Sheng, G. Y., Semukunzi, H., de Carvalho, E. L., Mahanty, A., Yuan, S., & Sun, L. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.01.019 · Cited by 76

Metformin-induced ablation of microRNA 21-5p releases Sestrin-1 and CAB39L antitumoral activities

Pulito, C., Mori, F., Sacconi, A., Goeman, F., Ferraiuolo, M. A., Pasanisi, P., Campagnoli, C., Berrino, F., Fanciulli, M., Ford, R. J., et al. (2017) · Cell Discovery · doi:10.1038/celldisc.2017.22 · Cited by 75

A signalling pathway for transcriptional regulation of sleep amount in mice

Zhou, R., Wang, G., Li, Q., Meng, F., Liu, C., Gan, R., Ju, D., Liao, M., Xu, J., Sang, D., et al. (2022) · Nature · doi:10.1038/s41586-022-05510-6 · Cited by 76

HDAC3 is critical in tumor development and therapeutic resistance in Kras -mutant non–small cell lung cancer

Eichner, L. J., Curtis, S. D., Brun, S. N., McGuire, C. K., Gushterova, I., Baumgart, J. T., Trefts, E., Ross, D. S., Rymoff, T. J., & Shaw, R. J. (2023) · Science Advances · doi:10.1126/sciadv.add3243 · Cited by 81

Downregulation of SIK2 expression promotes the melanogenic program in mice

Horike, N., Kumagai, A., Shimono, Y., Onishi, T., Itoh, Y., Sasaki, T., Kitagawa, K., Hatano, O., Takagi, H., Susumu, T., et al. (2010) · Pigment Cell & Melanoma Research · doi:10.1111/j.1755-148x.2010.00760.x · Cited by 78

Molecular mechanisms of tumor suppression by LKB1

Vaahtomeri, K., & Mäkelä, T. P. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.12.034 · Cited by 78

Lkb1 Deficiency Causes Prostate Neoplasia in the Mouse

Pearson, H. B., McCarthy, A., Collins, C. M. P., Ashworth, A., & Clarke, A. R. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-5169 · Cited by 82

LKB1 Regulated Pathways in Lung Cancer Invasion and Metastasis

Marcus, A. I., & Zhou, W. (2010) · Journal of Thoracic Oncology · doi:10.1097/jto.0b013e3181fbc28a · Cited by 76

The regulation and function of the NUAK family

Sun, X., Gao, L., Chien, H.-Y., Li, W., & Zhao, J. (2013) · Journal of Molecular Endocrinology · doi:10.1530/jme-13-0063 · Cited by 77

MEX-5 asymmetry in one-cell C. elegans embryos requires PAR-4-and PAR-1-dependent phosphorylation

Tenlen, J. R., Molk, J. N., London, N., Page, B. D., & Priess, J. R. (2008) · Development · doi:10.1242/dev.027060 · Cited by 71

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Metformin impairs the growth of liver kinase B1-intact cervical cancer cells

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Stromal Lkb1 deficiency leads to gastrointestinal tumorigenesis involving the IL-11–JAK/STAT3 pathway

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COMMENTARY The

(2013)

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

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

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