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

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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

Theaflavine inhibits hepatic stellate cell activation by modulating the PKA/LKB1/AMPK/GSK3β cascade and subsequently enhancing Nrf2 signaling

Shu, G., Sun, H. M., Zhang, T., Zhu, A., Xiao, L., Wang, C., Song, A., & Deng, X. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.175964 · Cited by 23

Faulty Epithelial Polarity Genes and Cancer

Tervonen, T. A., Partanen, J. I., Saarikoski, S. T., Myllynen, M., Marques, E., Paasonen, K., Moilanen, A., Wohlfahrt, G., Kovanen, P. E., & Klefström, J. T. (2011) · Advances in cancer research · doi:10.1016/b978-0-12-385524-4.00003-9 · Cited by 24

Liver kinase B1 regulates the centrosome via PLK1

Werle, K. D., Chen, J., Xu, H.-G., Zhao, R.-X., He, Q., Lu, C., Cui, R., Liang, J., Li, Y.-L., & Xu, Z.-X. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.135 · Cited by 22

A bird's-eye view of post-translational modifications in the spliceosome and their roles in spliceosome dynamics

McKay, S. L., & Johnson, T. (2010) · Molecular BioSystems · doi:10.1039/c002828b · Cited by 22

Marked phenotypic differences of endurance performance and exercise-induced oxygen consumption between AMPK and LKB1 deficiency in mouse skeletal muscle: changes occurring in the diaphragm

Miura, S., Kai, Y., Tadaishi, M., Tokutake, Y., Sakamoto, K., Bruce, C. R., Febbraio, M. A., Kita, K., Chohnan, S., & Ezaki, O. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00114.2013 · Cited by 23

Mark/Par-1 Marking the Polarity of Migrating Neurons

Reiner, O., & Sapir, T. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-7687-6_6 · Cited by 22

New Roles of Lkb1 in Regulating Adipose Tissue Development and Thermogenesis

Xu, Z., Liu, J., & Shan, T. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25643 · Cited by 22

Mechanistic Connections between Glucose/Lipid Disturbances and Weight Gain induced by Antipsychotic Drugs

Dwyer, D. S., Donohoe, D. R., Lu, X., & Aamodt, E. J. (2005) · International review of neurobiology · doi:10.1016/s0074-7742(04)65008-2 · Cited by 22

Lack of Salt-Inducible Kinase 2 (SIK2) Prevents the Development of Cardiac Hypertrophy in Response to Chronic High-Salt Intake

Popov, S., Takemori, H., Tokudome, T., Mao, Y., Otani, K., Mochizuki, N., Pires, N. M., Pinho, M. J., Franco‐Cereceda, A., Torielli, L., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095771 · Cited by 22

Transient activation of fission yeast AMPK is required for cell proliferation during osmotic stress

Schutt, K. L., & Moseley, J. B. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-04-0235 · Cited by 23

Post-translational regulation contributes to the loss of LKB1 expression through SIRT1 deacetylase in osteosarcomas

Presneau, N., Duhamel, L. A., Ye, H., Tirabosco, R., Flanagan, A. M., & Eskandarpour, M. (2017) · British Journal of Cancer · doi:10.1038/bjc.2017.174 · Cited by 23

Modulating Tumor Microenvironment: A Review on STK11 Immune Properties and Predictive vs Prognostic Role for Non-small-cell Lung Cancer Immunotherapy

Mazzaschi, G., Leonetti, A., Minari, R., Gnetti, L., Quaini, F., Tiseo, M., & Facchinetti, F. (2021) · Current Treatment Options in Oncology · doi:10.1007/s11864-021-00891-8 · Cited by 21

AICAR Ameliorates Non-Alcoholic Fatty Liver Disease via Modulation of the HGF/NF-κB/SNARK Signaling Pathway and Restores Mitochondrial and Endoplasmic Reticular Impairments in High-Fat Diet-Fed Rats

Zineldeen, D. H., Tahoon, N., & Sarhan, N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043367 · Cited by 21

BRSK2 is regulated by ER stress in protein level and involved in ER stress-induced apoptosis

Wang, Y., Wan, B., Li, D., Zhou, J., Li, R., Bai, M., Chen, F., & Yu, L. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.06.046 · Cited by 23

LKB1: cancer, polarity, metabolism, and now fertility

Shaw, R. J. (2008) · Biochemical Journal · doi:10.1042/bj20082023 · Cited by 21

AMP-activated Protein Kinase α2 Protects against Liver Injury from Metastasized Tumors via Reduced Glucose Deprivation-induced Oxidative Stress

Qiu, S.-L., Xiao, Z., Piao, C., Xian, Y.-L., Jia, L., Qi, Y., Han, J., Zhang, Y., & Du, J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.543447 · Cited by 22

A novel mutation in STK11gene is associated with Peutz-Jeghers Syndrome in Indian patients

Thakur, N., Reddy, D. N., Rao, G. V., Mohankrishna, P., Singh, L., & Chandak, G. R. (2006) · BMC Medical Genetics · doi:10.1186/1471-2350-7-73 · Cited by 21

STK11 Mutation Identified in Thyroid Carcinoma

Wei, S., LiVolsi, V. A., Brose, M. S., Montone, K. T., Morrissette, J. J. D., & Baloch, Z. W. (2015) · Endocrine Pathology · doi:10.1007/s12022-015-9411-6 · Cited by 21

Risperidone Mitigates Enhanced Excitatory Neuronal Function and Repetitive Behavior Caused by an ASD-Associated Mutation of SIK1

Badawi, M., Mori, T., Kurihara, T., Yoshizawa, T., Nohara, K., Kouyama-Suzuki, E., Yanagawa, T., Shirai, Y., & Tabuchi, K. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.706494 · Cited by 21

Regulation of epithelial and endothelial junctions by PAR proteins

Ebnet, K. (2008) · Frontiers in bioscience · doi:10.2741/3172 · Cited by 22

Effects of 3-phosphoglycerate and other metabolites on the activation of AMP-activated protein kinase by LKB1-STRAD-MO25

Ellingson, W. J., Chesser, D. G., & Winder, W. W. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00322.2006 · Cited by 21

Cellular polarity in aging: role of redox regulation and nutrition

Soares, H., Marinho, H. S., Real, C., & Antunes, F. (2013) · Genes & Nutrition · doi:10.1007/s12263-013-0371-5 · Cited by 21

LKB1 loss of function studied in vivo

Shorning, B. Y., & Clarke, A. R. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.01.019 · Cited by 26

Comparative proteomic analysis of normal and gliotic PVR retina and contribution of Müller glia to this profile

Eastlake, K., Heywood, W., Banerjee, P., Bliss, E., Mills, K. A., Khaw, P. T., Charteris, D. G., & Limb, G. A. (2018) · Experimental Eye Research · doi:10.1016/j.exer.2018.08.016 · Cited by 21

The role of STK11/LKB1 in cancer biology: implications for ovarian tumorigenesis and progression

Kang, J., Gallucci, S., Pan, J., Oakhill, J. S., & Sanij, E. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1449543 · Cited by 21

Role of AMP-Activated Protein Kinase on Steroid Hormone Biosynthesis in Adrenal NCI-H295R Cells

Hirsch, A., Hahn, D., Kempná, P., Hofer, G., Mullis, P. E., Nuoffer, J., & Flück, C. E. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030956 · Cited by 20

Underexpression of tumour suppressor LKB1 in clear cell renal cell carcinoma is common and confers growth advantage in vitro and in vivo

Duivenvoorden, W., Beatty, L. K., Lhoták, Š., Hill, B., Mak, I. W. Y., Paulin, G. A., Gallino, D., Popović, S., Austin, R. C., & Pinthus, J. H. (2013) · British Journal of Cancer · doi:10.1038/bjc.2012.574 · Cited by 20

SIK1 Regulates CRTC2-Mediated Gluconeogenesis Signaling Pathway in Human and Mouse Liver Cells

Wang, C., Song, D., Fu, J., & Wen, X. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00580 · Cited by 20

Cell adhesion molecule IGPR-1 activates AMPK connecting cell adhesion to autophagy

Amraei, R., Alwani, T., Ho, R. X.-Y., Aryan, Z., Wang, S., & Rahimi, N. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014790 · Cited by 20

Role of ARK5 in cancer and other diseases (Review)

Mo, G., Zhang, B., & Jiang, Q. (2021) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2021.10129 · Cited by 21

Salt-Inducible Kinase 1 is a potential therapeutic target in Desmoplastic Small Round Cell Tumor

Hartono, A. B., Kang, H., Shi, L., Phipps, W. E., Ungerleider, N., Giardina, A., Chen, W., Spraggon, L., Somwar, R., Moroz, K., et al. (2022) · Oncogenesis · doi:10.1038/s41389-022-00395-6 · Cited by 21

MARK3 kinase: Regulation and physiologic roles

Yang, J., Niu, H., Pang, S., Liu, M., Chen, F., Li, Z., He, L., Mo, J., Yi, H., Xiao, J., et al. (2022) · Cellular Signalling · doi:10.1016/j.cellsig.2022.110578 · Cited by 20

Sleep need, the key regulator of sleep homeostasis, is indicated and controlled by phosphorylation of threonine 221 in salt-inducible kinase 3

Li, Y., Li, C., Liu, Y., Yu, J., Yang, J., Cui, Y., Wang, T. V., Li, C., Jiang, L., Song, M., et al. (2023) · Genetics · doi:10.1093/genetics/iyad136 · Cited by 20

Structural insights into regulatory mechanisms of MO25-mediated kinase activation

Qian, H., Feng, M., Shi, Z., Li, C., Chen, M., Wang, W., Zhang, M., Jiao, S., & Zhou, Z. (2014) · Journal of Structural Biology · doi:10.1016/j.jsb.2014.04.005 · Cited by 20

Association of AMP-Activated Protein Kinase with Risk and Progression of Non–Hodgkin Lymphoma

Hoffman, A. E., Demanelis, K., Fu, A., Zheng, T., & Zhu, Y. L. (2013) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-12-1014 · Cited by 20

A protein interaction map for cell-cell adhesion regulators identifies DUSP23 as a novel phosphatase for β-catenin

Gallegos, L. L., Ng, M. R., Sowa, M. E., Selfors, L. M., White, A., Zervantonakis, I. K., Singh, P., Dhakal, S., Harper, J. W., & Brugge, J. S. (2016) · Scientific Reports · doi:10.1038/srep27114 · Cited by 20

Epigenetic mechanism in search for the pathomechanism of diabetic neuropathy development in diabetes mellitus type 1 (T1DM)

Gastoł, J., Kapusta, P., Polus, A., Pitera, E., Sordyl, M., Wołkow, P. P., Pawliński, Ł., & Kieć‐Wilk, B. (2020) · Endocrine · doi:10.1007/s12020-019-02172-9 · Cited by 22

Zhenqing recipe attenuates non-alcoholic fatty liver disease by regulating the SIK1/CRTC2 signaling in experimental diabetic rats

Song, D., Yin, L., Wang, C., & Wen, X. (2020) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-019-2811-2 · Cited by 20

Salt-inducible kinase 3 protects tumor cells from cytotoxic T-cell attack by promoting TNF-induced NF-κB activation

Sorrentino, A., Menevse, A. N., Michels, T., Volpin, V., Durst, F. C., Sax, J., Xydia, M., Hussein, A., Stamova, S., Spoerl, S., et al. (2022) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2021-004258 · Cited by 21

Nuclear localization of SNARK; its impact on gene expression

Kuga, W., Tsuchihara, K., Ogura, T., Kanehara, S., Saito, M., Suzuki, A., & Esumi, H. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.10.143 · Cited by 20

Biological Activities, Pharmacokinetics and Toxicity of Nootkatone: A Review

Sahu, B. D., Jha, A. K., Gairola, S., Kundu, S., Doye, P., Syed, A. M., Ram, C., Kulhari, U., Kumar, N., & Murty, U. S. (2022) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557522666220214092005 · Cited by 19

Dendritic cell–intrinsic LKB1-AMPK/SIK signaling controls metabolic homeostasis by limiting the hepatic Th17 response during obesity

van der Zande, H. J. P., Brombacher, E. C., Lambooij, J. M., Pelgrom, L. R., Zawistowska‐Deniziak, A., Patente, T. A., Heieis, G. A., Otto, F., Ozir‐Fazalalikhan, A., Yazdanbakhsh, M., et al. (2023) · JCI Insight · doi:10.1172/jci.insight.157948 · Cited by 17

NUAK2: an emerging acral melanoma oncogene

Namiki, T., Coelho, S. G., & Hearing, V. J. (2011) · Oncotarget · doi:10.18632/oncotarget.325 · Cited by 20

Cyclin CYB-3 controls both S-phase and mitosis and is asymmetrically distributed in the early C. elegans embryo

Michael, W. M. (2016) · Development · doi:10.1242/dev.141226 · Cited by 19

The Key Role of IP6K: A Novel Target for Anticancer Treatments?

Minini, M., Senni, A., Unfer, V., & Bizzarri, M. (2020) · Molecules · doi:10.3390/molecules25194401 · Cited by 21

Interaction between Salt-inducible Kinase 2 (SIK2) and p97/Valosin-containing Protein (VCP) Regulates Endoplasmic Reticulum (ER)-associated Protein Degradation in Mammalian Cells

Yang, F.-C., Lin, Y.-H., Chen, W., Huang, J., Chang, H.-Y., Su, S.-H., Wang, H.-T., Chiang, C.-Y., Hsu, P., Tsai, M., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.492199 · Cited by 19

Targeted Inactivation of GPR26 Leads to Hyperphagia and Adiposity by Activating AMPK in the Hypothalamus

Chen, D., Liu, X., Zhang, W., & Shi, Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040764 · Cited by 19

Expression and transcriptional profiling of the LKB1 tumor suppressor in cervical cancer cells

Zhang, X., Chen, H., Wang, X., Zhao, W., & Chen, J. J. (2014) · Gynecologic Oncology · doi:10.1016/j.ygyno.2014.04.050 · Cited by 19

LKB1 Mutations Frequently Detected in Mucinous Bronchioloalveolar Carcinoma

Osoegawa, A., Kometani, T., Nosaki, K., Ondo, K., Hamatake, M., Hirai, F., Takumi, S. E. T. O., Sugio, K., & Ichinose, Y. (2011) · Japanese Journal of Clinical Oncology · doi:10.1093/jjco/hyr102 · Cited by 19

AMP-Activated Protein Kinase

Hardie, D. G. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00073-5 · Cited by 19

Cell polarity proteins promote macropinocytosis in response to metabolic stress

Lambies, G., Lee, S.-W., Duong‐Polk, K., Aza‐Blanc, P., Maganti, S., Galapate, C. M., Deshpande, A. J., Deshpande, A. J., Scott, D. A., Dawson, D. W., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54788-9 · Cited by 18

Deletion of Stk11 and Fos in mouse BLA projection neurons alters intrinsic excitability and impairs formation of long-term aversive memory

Levitan, D., Liu, C., Yang, T. L., Shima, Y., Lin, J.-Y., Wachutka, J., Marrero-Garcia, Y., Ghoddousi, R. A. M., Beltrame, E. D. V., Richter, T. A., et al. (2020) · eLife · doi:10.7554/elife.61036 · Cited by 18

Loss of LKB1-NUAK1 signalling enhances NF-κB activity in a spheroid model of high-grade serous ovarian cancer

Buensuceso, A. V., Fritz, J. L., Collins, O. M., Valdés, Y. R., Borrelli, M. J., DiMattia, G. E., & Shepherd, T. G. (2022) · Scientific Reports · doi:10.1038/s41598-022-06796-2 · Cited by 18

Transient changes to metabolic homeostasis initiate mitochondrial adaptation to endurance exercise

Dent, J. R., Stocks, B., Campelj, D. G., & Philp, A. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.03.022 · Cited by 19

Nuciferine Ameliorates Nonesterified Fatty Acid-Induced Bovine Mammary Epithelial Cell Lipid Accumulation, Apoptosis, and Impaired Migration via Activating LKB1/AMPK Signaling Pathway

Li, J., Zhao, C., Liu, M., Chen, L., Zhu, Y., Gao, W., Du, X., Song, Y., Li, X., Liu, G., et al. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c06133 · Cited by 18

Metformin derivatives – Researchers’ friends or foes?

Torunoglu, S. T., Zajda, A., Tampio, J., Markowicz-Piasecka, M., & Huttunen, K. M. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115743 · Cited by 22

Therapeutic Approaches to Tuberous Sclerosis Complex: From Available Therapies to Promising Drug Targets

Conte, E., Boccanegra, B., Dinoi, G., Pusch, M., Luca, A. D., Liantonio, A., & Imbrici, P. (2024) · Biomolecules · doi:10.3390/biom14091190 · Cited by 19

STK11 is required for the normal program of ciliated cell differentiation in airways

Chu, Q., Yao, C., Qi, X., Stripp, B. R., & Tang, N. (2019) · Cell Discovery · doi:10.1038/s41421-019-0104-z · Cited by 20

Advances in defining signaling networks for the establishment of neuronal polarity

Funahashi, Y., Watanabe, T., & Kaibuchi, K. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.12.009 · Cited by 21

A Modular Mathematical Model of Exercise-Induced Changes in Metabolism, Signaling, and Gene Expression in Human Skeletal Muscle

Akberdin, I. R., Kiselev, I. N., Pintus, S. S., Sharipov, R., Vertyshev, A. Y., Виноградова, О. Л., Popov, D. V., & Kolpakov, F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910353 · Cited by 19

Deletion of Lkb1 in adult mice results in body weight reduction and lethality

Shan, T., Xiong, Y., & Kuang, S. (2016) · Scientific Reports · doi:10.1038/srep36561 · Cited by 19

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

Zhuang, Y., & Miskimins, W. K. (2008) · Cited by 18

An efficient expression system for the production of functionally active human LKB1

Martinez-Torrecuadrada, J. L., Romero, S., Núñez, A., Alfonso, P., Sánchez‐Céspedes, M., & Casal, J. I. (2004) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2004.07.011 · Cited by 18

Functional assessment of somatic STK11 variants identified in primary human non-small cell lung cancers

Donnelly, L. L., Hogan, T. C., Lenahan, S. M., Nandagopal, G., Eaton, J. G., Lebeau, M. A., McCann, C., Sarausky, H. M., Hampel, K. J., Armstrong, J. D., et al. (2021) · Carcinogenesis · doi:10.1093/carcin/bgab104 · Cited by 18

A Review on Metformin: Clinical Significance and Side Effects

Mazumder, A., & Ashini, S. (2021) · Research Journal of Pharmacy and Technology · doi:10.52711/0974-360x.2021.01070 · Cited by 22

Translation initiation factor eIF3a regulates glucose metabolism and cell proliferation via promoting small GTPase Rheb synthesis and AMPK activation

Ma, S., Dong, Z., Huang, Y., Liu, J., & Zhang, J. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102044 · Cited by 17

AMP-activated protein kinase — a journey from 1 to 100 downstream targets

Hardie, D. G. (2022) · Biochemical Journal · doi:10.1042/bcj20220255 · Cited by 17

Posttranslational regulation of liver kinase B1 in human cancer

Hu, L., Liu, M., Tang, B., Li, Q., Pan, B., Xu, C. S., & Lin, H. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104570 · Cited by 18

Roles of salt‑inducible kinases in cancer (Review)

Feng, S., Wei, F., Shi, H., Chen, S., Wang, B., Huang, D., & Luo, L. (2023) · International Journal of Oncology · doi:10.3892/ijo.2023.5566 · Cited by 18

Blocking AMPKαS496 phosphorylation improves mitochondrial dynamics and hyperglycemia in aging and obesity

Pearah, A., Ramatchandirin, B., Liu, T., Wolf, R. M., Ikeda, A., Radovick, S., Sesaki, H., Wondisford, F. E., O'Rourke, B. P., & He, L. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.09.017 · Cited by 19

NUAK: never underestimate a kinase

Skalka, G., Whyte, D., Lubawska, D., & Murphy, D. J. (2024) · Essays in Biochemistry · doi:10.1042/ebc20240005 · Cited by 18

NUAK1 activates STAT5/GLI1/SOX2 signaling to enhance cancer cell expansion and drives chemoresistance in gastric cancer

Cao, L., Lin, G., Fan, D.-H., Weng, K., Chen, Y., Wang, J., Li, P., Zheng, C., Huang, C., & Xie, J. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114446 · Cited by 17

Molecular control of the Wee1 regulatory pathway by the SAD kinase Cdr2

Guzmán-Vendrell, M., Rincón, S. A., Dingli, F., Loew, D., & Paoletti, A. (2015) · Journal of Cell Science · doi:10.1242/jcs.173146 · Cited by 17

Isozyme-Specific Role of SAD-A in Neuronal Migration During Development of Cerebral Cortex

Nakanishi, K., Niida, H., Tabata, H., Ito, T., Hori, Y., Hattori, M., Johmura, Y., Yamada, C., Ueda, T., Takeuchi, K., et al. (2018) · Cerebral Cortex · doi:10.1093/cercor/bhy253 · Cited by 21

LKB1 Mediates the Development of Conventional and Innate T Cells via AMP-Dependent Kinase Autonomous Pathways

Zarrouk, M., Rolf, J., & Cantrell, D. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060217 · Cited by 16

Identification of Stk25 as a Genetic Modifier of Tau Phosphorylation in Dab1-Mutant Mice

Matsuki, T., Zaka, M., Guerreiro, R. J., van der Brug, M. P., Cooper, J. A., Cookson, M., Hardy, J., & Howell, B. W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031152 · Cited by 17

MicroRNA-23a promotes colorectal cancer cell migration and proliferation by targeting at MARK1

Tang, X., Yang, M., Wang, Z., Wu, X., & Wang, D. (2019) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmz047 · Cited by 17

Crosstalk of cell polarity signaling pathways

Mazel, T. (2017) · PROTOPLASMA · doi:10.1007/s00709-017-1075-2 · Cited by 18

LKB1 signaling is altered in skeletal muscle of a Duchenne muscular dystrophy mouse model

Boccanegra, B., Mantuano, P., Conte, E., Cerchiara, A. G., Tulimiero, L., Quarta, R., Caputo, E., Sanarica, F., Forino, M., Spadotto, V., et al. (2023) · Disease Models & Mechanisms · doi:10.1242/dmm.049930 · Cited by 16

NUAK1 coordinates growth factor-dependent activation of mTORC2 and Akt signaling

Palma, M., Riffo, E. N., Farías, A., Coliboro-Dannich, V., Espinoza-Francine, L., Escalona, E., Amigo, R., Gutiérrez, J. L., Pincheira, R., & Castro, A. F. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-01185-2 · Cited by 17

Arrestin-3 interaction with maternal embryonic leucine-zipper kinase

Perry, N. A., Fialkowski, K. P., Kaoud, T. S., Kaya, A. İ., Chen, A. L., Taliaferro, J. M., Gurevich, V. V., Dalby, K. N., & Iverson, T. M. (2019) · Cellular Signalling · doi:10.1016/j.cellsig.2019.109366 · Cited by 16

PIM kinases inhibit AMPK activation and promote tumorigenicity by phosphorylating LKB1

Mung, K. L., Eccleshall, W. B., Santio, N. M., Rivero‐Müller, A., & Koskinen, P. J. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00749-4 · Cited by 16

NUAK Kinases: Brain–Ovary Axis

Molina, E., Hong, L., & Chefetz, I. (2021) · Cells · doi:10.3390/cells10102760 · Cited by 17

Syzygium aromaticum L. (Clove) Extract Regulates Energy Metabolism in Myocytes

Tu, Z., Moss‐Pierce, T., Ford, P. W., & Jiang, T. A. (2014) · Journal of Medicinal Food · doi:10.1089/jmf.2013.0175 · Cited by 16

BRSK2 is activated by cyclic AMP-dependent protein kinase A through phosphorylation at Thr260

Guo, Z., Tang, W., Yuan, J., Chen, X., Wan, B., Gu, X., Luo, K., Wang, Y., & Yu, L. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.06.178 · Cited by 16

Expression of Maternal Embryonic Leucine Zipper Kinase (MELK) Correlates to Malignant Potentials in Hepatocellular Carcinoma

Hiwatashi, K., Ueno, S., Sakoda, M., Iino, S., Minami, K., Yonemori, K., Nishizono, Y., Kurahara, H., Mataki, Y., Maemura, K., et al. (2016) · Anticancer Research · doi:10.21873/anticanres.11088 · Cited by 16

Phosphatases Generate Signal Specificity Downstream of Ssp1 Kinase in Fission Yeast

Deng, L., Lee, M. E., Schutt, K. L., & Moseley, J. B. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00494-16 · Cited by 16

Caenorhabditis elegans CES-1 Snail Represses pig-1 MELK Expression To Control Asymmetric Cell Division

Wei, H., Yan, B., Gagneur, J., & Conradt, B. (2017) · Genetics · doi:10.1534/genetics.117.202754 · Cited by 16

Dysregulation of microRNAs and renin-angiotensin system in high salt diet-induced cardiac dysfunction in uninephrectomized rats

Amara, V. R., Surapaneni, S. K., & Tikoo, K. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180490 · Cited by 16

Adipocyte-specific DKO of Lkb1 and mTOR protects mice against HFD-induced obesity, but results in insulin resistance

Xiong, Y., Xu, Z., Wang, Y., Kuang, S., & Shan, T. (2018) · Journal of Lipid Research · doi:10.1194/jlr.m081463 · Cited by 16

C-terminal phosphorylation of SPAK and OSR1 kinases promotes their binding and activation by the scaffolding protein MO25

Mehellou, Y., Alamri, M. A., Dhiani, B. A., & Kadri, H. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.07.128 · Cited by 15

PKIS deep dive yields a chemical starting point for dark kinases and a cell active BRSK2 inhibitor

Tamir, T. Y., Drewry, D. H., Wells, C. I., Major, M. B., & Axtman, A. D. (2020) · Scientific Reports · doi:10.1038/s41598-020-72869-9 · Cited by 15

Impact of diabetes on the increased risk of hepatic cancer: An updated review of biological aspects

Das, B. K., & Gadad, P. C. (2021) · Diabetes Epidemiology and Management · doi:10.1016/j.deman.2021.100025 · Cited by 15

Metabolomic Analysis of the Takifugu Obscurus Gill under Acute Hypoxic Stress

Zhang, H., Hu, Z., Li, R., Wang, Y., Zhou, J., Xu, H., Wang, G., Qiu, X., & Wang, X. (2022) · Animals · doi:10.3390/ani12192611 · Cited by 15

NUAK1 governs centrosome replication in pancreatic cancer via MYPT1 / PP1β and GSK3β ‐dependent regulation of PLK4

Whyte, D., Skalka, G., Walsh, P. J., Wilczynska, A., Paul, N. R., Mitchell, C. A., Nixon, C., Clarke, W., Bushell, M., Morton, J. P., et al. (2023) · Molecular Oncology · doi:10.1002/1878-0261.13425 · Cited by 15

Shifting the selectivity of pyrido[2,3-d]pyrimidin-7(8H)-one inhibitors towards the salt-inducible kinase (SIK) subfamily

Rak, M., Tesch, R., Berger, L. M., Shevchenko, E., Raab, M., Tjaden, A., Zhubi, R., Balourdas, D.-I., Joerger, A. C., Poso, A., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115347 · Cited by 15

The LKB1–TSSK1B axis controls YAP phosphorylation to regulate the Hippo–YAP pathway

Kim, C.-L., Lim, S.-B., Choi, S.-H., Kim, D. H., Sim, Y. E., Jo, E.-H., Kim, K., Lee, K., Park, H.-S., Lim, S. B., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06465-4 · Cited by 16

Role of MARK2 in the nervous system and cancer

Lei, Y., Zhang, R., & Cai, F. (2024) · Cancer Gene Therapy · doi:10.1038/s41417-024-00737-z · Cited by 15

Effect of metformin on residual cells after chemotherapy in a human lung adenocarcinoma cell line

Kitazono, S., Takiguchi, Y., Ashinuma, H., Kitazono, M., Kitamura, A., Chiba, T., Sakaida, E., Sekine, I., Tada, Y., Kurosu, K., et al. (2013) · International Journal of Oncology · doi:10.3892/ijo.2013.2120 · Cited by 16

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