The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
LKB1 Is the Upstream Kinase in the AMP-Activated Protein Kinase Cascade
Open accessAbstract
Inactivating mutations in the protein kinase LKB1 lead to a dominantly inherited cancer in humans termed Peutz-Jeghers syndrome. The role of LKB1 is unclear, and only one target for LKB1 has been identified in vivo [3]. AMP-activated protein kinase (AMPK) is the downstream component of a protein kinase cascade that plays a pivotal role in energy homeostasis. AMPK may have a role in protecting the body from metabolic diseases including type 2 diabetes, obesity, and cardiac hypertrophy. We previously reported the identification of three protein kinases (Elm1, Pak1, and Tos3 [9]) that lie upstream of Snf1, the yeast homologue of AMPK. LKB1 shares sequence similarity with Elm1, Pak1, and Tos3, and we demonstrated that LKB1 phosphorylates AMPK on the activation loop threonine (Thr172) within the catalytic subunit and activates AMPK in vitro [9]. Here, we have investigated whether LKB1 corresponds to the major AMPKK activity present in cell extracts. AMPKK purified from rat liver corresponds to LKB1, and blocking LKB1 activity in cells abolishes AMPK activation in response to different stimuli. These results identify a link between two protein kinases, previously thought to lie in unrelated, distinct pathways, that are associated with human diseases.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Liver kinase B 1 (LKB1) [32] and calcium/calmodulin-dependent protein kinase kinase (CAMKK) 2 [33,34] can be employed as the two main mammalian upstream molecules that phosphorylate AMPK.”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [32]
Citations
Cites
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
Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase
Minokoshi, Y., Kim, Y.-B., Peroni, O. D., Fryer, L. G. D., Müller, C., Carling, D., & Kahn, B. B. (2002) · Nature · doi:10.1038/415339a · Cited by 2,053
Self-citationA 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
THE AMP-ACTIVATED/SNF1 PROTEIN KINASE SUBFAMILY: Metabolic Sensors of the Eukaryotic Cell?
Hardie, D. G., Carling, D., & Carlson, M. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.821 · Cited by 1,440
Self-citationHawley, S. A., Davison, M., Woods, A., Davies, S. P., Beri, R. K., Carling, D., & Hardie, D. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27879 · Cited by 1,264
Self-citationPeutz-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
Fryer, L. G. D., Patel, A. P., & Carling, D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202489200 · Cited by 1,035
Self-citationAMP-activated protein kinase, a metabolic master switch: possible roles in Type 2 diabetes
Winder, W. W., & Hardie, D. G. (1999) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1999.277.1.e1 · Cited by 1,000
Characterization of AMP-activated protein kinase γ-subunit isoforms and their role in AMP binding
CHEUNG, P. C. F., SALT, I. P., DAVIES, S. P., HARDIE, D. G., & CARLING, D. (2000) · Biochemical Journal · doi:10.1042/bj3460659 · Cited by 637
Self-citationActivation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases
Hong, S. P., Leiper, F. C., Woods, A., Carling, D., & Carlson, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1533136100 · Cited by 617
Self-citation
Flagged first, then by citations
Research works printed but not linked: 1
- Winder, 1999, AMP-activated protein kinase, a metabolic master switch, Am. J. Physiol., 277, 1
Cited by
Sorted by citations
Items 701–800 of 1,001
Metformin, an Anti-diabetic Drug to Target Leukemia
Biondani, G., & Peyron, J. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00446 · Cited by 56
Adiponectin-mediated stimulation of AMP-activated protein kinase (AMPK) in pancreatic beta cells
Huypens, P., Moens, K., Heimberg, H., Ling, Z., PIPELEERS, D. G., & de Casteele, M. V. (2005) · Life Sciences · doi:10.1016/j.lfs.2005.03.008 · Cited by 54
The Mammalian Target of Rapamycin Pathway as a Potential Target for Cancer Chemoprevention
Kopelovich, L., Fay, J. R., Sigman, C. C., & Crowell, J. A. (2007) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-07-0045 · Cited by 54
Hardie, D. G. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010819 · Cited by 55
Braun, K. A., Vaga, S., Dombek, K. M., Fang, F., Palmisano, S., Aebersold, R. H., & Young, E. T. (2014) · Science Signaling · doi:10.1126/scisignal.2005000 · Cited by 54
Kim, M., Park, I. J., Yun, H., Kang, I., Choe, W., Kim, S. S., & Ha, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.085456 · Cited by 53
Houde, V. P., Ritorto, M. S., Gourlay, R., Varghese, J., Davies, P., Shpiro, N., Sakamoto, K., & Alessi, D. R. (2013) · Biochemical Journal · doi:10.1042/bj20131324 · Cited by 61
Nguyễn, P. H., Rehman, G., Hwang, S.-L., Đào, T. T., Park, D. C., Kim, J. E., Song, H., Huh, T. L., & Oh, W. K. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.09.013 · Cited by 53
Sid, V., Wu, N., Sarna, L. K., Siow, Y. L., House, J. D., & Karmin, O. (2015) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00260.2015 · Cited by 54
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
Shirra, M. K., Rogers, S. E., Alexander, D. E., & Arndt, K. M. (2005) · Genetics · doi:10.1534/genetics.104.038075 · Cited by 53
The AMPK Pathway: Molecular Rejuvenation of Metabolism and Mitochondria
Malik, N., & Shaw, R. J. (2025) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-120420-094431 · Cited by 57
Zhang, L., Jouret, F., Rinehart, J., Sfakianos, J., Mellman, I., Lifton, R. P., Young, L. H., & Caplan, M. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.186932 · Cited by 55
Deletion of Lkb1 in Pro-Opiomelanocortin Neurons Impairs Peripheral Glucose Homeostasis in Mice
Claret, M., Smith, M. A., Knauf, C., Al‐Qassab, H., Woods, A., Heslegrave, A., Piipari, K., Emmanuel, J. J., Colom, A., Valet, P., et al. (2011) · Diabetes · doi:10.2337/db10-1055 · Cited by 52
Self-citationNew insights into antidiabetic drugs: Possible applications in cancer treatment
Shafiei‐Irannejad, V., Samadi, N., Salehi, R., Yousefi, B., & Zarghami, N. (2017) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13013 · Cited by 52
Maeda, A., Shirao, T., Shirasaya, D., Yoshioka, Y., Yamashita, Y., Akagawa, M., & Ashida, H. (2018) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201800086 · Cited by 52
LKB1 and Tumor Metabolism: The Interplay of Immune and Angiogenic Microenvironment in Lung Cancer
Bonanno, L., Zulato, E., Pavan, A., Attili, I., Pasello, G., Conte, P., & Indraccolo, S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081874 · Cited by 53
Current Status and Challenges Associated with Targeting mTOR for Cancer Therapy
Dowling, R. J. O., Pollak, M., & Sonenberg, N. (2009) · BioDrugs · doi:10.2165/00063030-200923020-00002 · Cited by 52
Jin, H., Hong, S., Choi, M., Maeng, H., Kim, D., Chung, S., & Shim, C. (2008) · Pharmaceutical Research · doi:10.1007/s11095-008-9770-5 · Cited by 53
Suzuki, A., Kusakai, G.-I., Shimojo, Y., Chen, J., Ogura, T., Kobayashi, M., & Esumi, H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503714200 · Cited by 52
Lu, L., Zhang, X., Zhang, B., Wu, J., & Zhang, X. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.08.007 · Cited by 51
LKB 1 and AMP ‐activated protein kinase: regulators of cell polarity
Nakano, A., & Takashima, S. (2012) · Genes to Cells · doi:10.1111/j.1365-2443.2012.01629.x · Cited by 63
The Dictyostelium model for mitochondrial disease
Francione, L. M., Annesley, S. J., Carilla-Latorre, S., Escalante, R., & Fisher, P. R. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.11.004 · Cited by 51
AICAR induces Nrf2 activation by an AMPK-independent mechanism in hepatocarcinoma cells
Sid, B., Glorieux, C., Valenzuela, M., Rommelaere, G., Najimi, M., Dejeans, N., Renard, P., Verrax, J., & Calderón, P. B. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.07.010 · Cited by 51
Contraction-related stimuli regulate GLUT4 traffic in C2C12-GLUT4mycskeletal muscle cells
Niu, W., Bilan, P. J., Ishikura, S., Schertzer, J. D., Contreras‐Ferrat, A. E., Fu, Z., Liu, J., Boguslavsky, S., Foley, K. P., Liu, Z., et al. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00773.2009 · Cited by 51
mTOR: more targets of resveratrol?
Widlund, A. L., Baur, J. A., & Vang, O. (2013) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2013.11 · Cited by 51
Rao, Y., Yu, H., Gao, L., Lu, Y., Zhao, X. D., Liu, H., Gu, L., Ye, J., & Huang, Z. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13855 · Cited by 51
Zheng, X., Chi, J., Zhi, J., Zhang, H., Yue, D., Zhao, J., Li, D., Li, Y., Gao, M., & Guo, J. (2017) · Oncogene · doi:10.1038/onc.2017.354 · Cited by 51
Interplay between adenylate metabolizing enzymes and AMP‐activated protein kinase
Camici, M., Allegrini, S., & Tozzi, M. G. (2018) · FEBS Journal · doi:10.1111/febs.14508 · Cited by 52
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 52
Wallimann, T., Hall, C. H. T., Colgan, S. P., & Glover, L. E. (2021) · Nutrients · doi:10.3390/nu13051429 · Cited by 50
Self-citationResveratrol ameliorates high glucose-induced protein synthesis in glomerular epithelial cells
Lee, M.-J., Féliers, D., Sataranatarajan, K., Mariappan, M. M., Li, M., Barnes, J. L., Choudhury, G. G., & Kasinath, B. S. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.09.011 · Cited by 50
AMPK supports growth in Drosophila by regulating muscle activity and nutrient uptake in the gut
Bland, M. L., Lee, R. J., Magallanes, J. M., Foskett, J. K., & Birnbaum, M. J. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2010.05.010 · Cited by 51
de Llera, A. H., Martín‐Hidalgo, D., Gil, M. C., Garcı́a, L. J., & Bragado, M. J. (2014) · Biology of Reproduction · doi:10.1095/biolreprod.113.112797 · Cited by 50
Zhang, Y., Chen, S., Wei, C., Chen, J., & Ye, X. (2016) · Journal of Functional Foods · doi:10.1016/j.jff.2016.12.030 · Cited by 50
AMPK phosphorylates GBF1 for mitotic Golgi disassembly
Mao, L., Li, N., Guo, Y., Xu, X., Gao, L., Xu, Y., Zhou, L., & Liu, W. (2013) · Journal of Cell Science · doi:10.1242/jcs.121954 · Cited by 50
Wan, X., Huo, Y., Johns, M. S., Piper, E., Mason, J. C., Carling, D., Haskard, D. O., & Boyle, J. J. (2013) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.113.300986 · Cited by 53
Self-citationTang, G., Wang, H., Wang, J.-Y., Lee, C.-C., Tseng, H., Wu, Y.-L., Shyue, S., Lee, T., & Kou, Y. R. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.02.030 · Cited by 49
Lee, J., Jeong, J., & Park, S.-Y. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.07.072 · Cited by 49
Ahtiainen, J. P., Walker, S., Silvennoinen, M., Kyröläinen, H., Nindl, B. C., Häkkinen, K., Nyman, K., Selänne, H., & Hulmi, J. J. (2015) · European Journal of Applied Physiology · doi:10.1007/s00421-015-3155-3 · Cited by 52
Oestrogen receptors interact with the α-catalytic subunit of AMP-activated protein kinase
Lipovka, Y., Chen, H., Vagner, J., Price, T. J., Tsao, T.-S., & Konhilas, J. P. (2015) · Bioscience Reports · doi:10.1042/bsr20150074 · Cited by 49
Nakatsu, Y., Matsunaga, Y., Yamamotoya, T., Ueda, K., Inoue, Y., Mori, K., Sakoda, H., Fujishiro, M., Ono, H., Kushiyama, A., et al. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17091495 · Cited by 50
Klotho ameliorates diabetic nephropathy via LKB1-AMPK-PGC1α-mediated renal mitochondrial protection
Lee, J., Tsogbadrakh, B., Yang, S., Ryu, H., Kang, E., Kang, M., Kang, H. G., Ahn, C., & Oh, K. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.10.040 · Cited by 49
Shen, Q. W., Gerrard, D. E., & Du, . (2007) · Meat Science · doi:10.1016/j.meatsci.2007.06.023 · Cited by 49
Ma, Y., Fuzhen, Y., Wang, Y., Du, Z., Liu, D.-H., Guo, H., Shen, J., & Peng, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047900 · Cited by 49
Gaskin, F. S., Kamada, K., Yusof, M., & Korthuis, R. J. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00744.2006 · Cited by 49
Cytokine Regulation of AMPK signalling
Steinberg, G. R. (2009) · Frontiers in bioscience · doi:10.2741/3350 · Cited by 49
AMP-activated protein kinase regulation of kidney tubular transport
Pastor‐Soler, N. M., & Hallows, K. R. (2012) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0b013e3283562390 · Cited by 49
Metformin: Its emerging role in oncology
Micić, D., Cvijović, G., Trajković, V., Duntas, L. H., & Polovina, S. P. (2011) · HORMONES · doi:10.14310/horm.2002.1288 · Cited by 48
Structure and Regulation of AMPK
Kurumbail, R. G., & Calabrese, M. F. (2016) · Proceedings of the Fourth International Symposium on Polarization Phenomena in Nuclear Reactions · doi:10.1007/978-3-319-43589-3_1 · Cited by 48
Tim-4 Inhibits NLRP3 Inflammasome via the LKB1/AMPKα Pathway in Macrophages
Liu, W., Bai, F., Wang, H., Liang, Y., Du, X., Liu, C., Cai, D., Peng, J., Zhong, G., Liang, X., et al. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1900117 · Cited by 49
Minireview: Obesity and LipOdystrophy—Where Do the Circles Intersect?
Chehab, F. F. (2008) · Endocrinology · doi:10.1210/en.2007-1355 · Cited by 48
Peutz–Jeghers LKB1 mutants fail to activate GSK-3β, preventing it from inhibiting Wnt signaling
Lin-Marq, N., Borel, C., & Antonarakis, S. E. (2005) · Molecular Genetics and Genomics · doi:10.1007/s00438-005-1124-y · Cited by 50
Nuclear UHRF1 is a gate-keeper of cellular AMPK activity and function
Xu, X., Ding, G., Liu, C., Ding, Y., Chen, X. L., Huang, X., Zhang, C., Lu, S., Zhang, Y., Huang, Y., et al. (2021) · Cell Research · doi:10.1038/s41422-021-00565-y · Cited by 47
Andersen, M. N., & Rasmussen, H. B. (2012) · Communicative & Integrative Biology · doi:10.4161/cib.21200 · Cited by 47
At the crossroad of T cells, adipose tissue, and diabetes
Matarese, G., Procaccini, C., & Rosa, V. D. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01154.x · Cited by 47
Gaude, H., Aznar, N., Delay, A., Brès, A., Buchet-Poyau, K., Caillat, C., Vigouroux, A., Rogon, C., Woods, A., Vanacker, J.-M., et al. (2011) · Oncogene · doi:10.1038/onc.2011.342 · Cited by 55
Self-citationAMPK: opposing the metabolic changes in both tumour cells and inflammatory cells?
Dandapani, M., & Hardie, D. G. (2013) · Biochemical Society Transactions · doi:10.1042/bst20120351 · Cited by 47
Dogliotti, G., Kullmann, L., Dhumale, P., Thiele, C., Panichkina, O., Mendl, G., Houben, R., Haferkamp, S., Püschel, A. W., & Krahn, M. P. (2017) · Nature Communications · doi:10.1038/ncomms15747 · Cited by 49
Heat Shock Factor 1 Is a Direct Antagonist of AMP-Activated Protein Kinase
Su, K., Dai, S., Tang, Z., Xu, M., & Dai, C. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.08.021 · Cited by 47
Chou, H.-Y., Liu, L., Chen, C., Lin, I., Ali, D., Lee, A. Y., & Wang, H. (2021) · Food and Chemical Toxicology · doi:10.1016/j.fct.2021.112020 · Cited by 48
Negative regulation of mTOR activity by LKB1-AMPK signaling in non-small cell lung cancer cells
Dong, L., Sun, L., Zhang, X., Li, P., Lian, L., Chen, Z., & Zhong, D. (2012) · Acta Pharmacologica Sinica · doi:10.1038/aps.2012.143 · Cited by 47
Roles of the Glycogen-binding Domain and Snf4 in Glucose Inhibition of SNF1 Protein Kinase
Momcilovic, M., Iram, S. H., Liu, Y., & Carlson, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803624200 · Cited by 47
Self-citationRegulation of AMP‐activated protein kinase by a pseudosubstrate sequence on the γ subunit
Scott, J. W., Ross, F. A., Liu, J. K. D., & Hardie, D. G. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601542 · Cited by 50
Potential effects of metformin in DNA BER system based on oxidative status in type 2 diabetes
Dogan Turacli, I., Candar, T., Yuksel, E. B., Kalay, S., Oguz, A. K., & Demirtas, S. (2018) · Biochimie · doi:10.1016/j.biochi.2018.08.002 · Cited by 46
Sensing and responding to energetic stress: Evolution of the AMPK network
Craig, P. M., Moyes, C. D., & LeMoine, C. M. R. (2018) · Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2017.11.001 · Cited by 46
Cai, H., Zhang, Y., Han, T. K., Everett, R. S., & Thakker, D. R. (2016) · International Journal of Cancer · doi:10.1002/ijc.29965 · Cited by 46
Post-Translational Modifications of the Energy Guardian AMP-Activated Protein Kinase
Ovens, A. J., Scott, J. W., Langendorf, C. G., Kemp, B. E., Oakhill, J. S., & Smiles, W. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031229 · Cited by 50
Mayor, E. (2023) · Frontiers in Aging · doi:10.3389/fragi.2023.1161814 · Cited by 47
Bremer, K., Kocha, K. M., Snider, T., & Moyes, C. D. (2015) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2015.09.005 · Cited by 46
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
Kim, N., Lee, J. O., Lee, H. J., Kim, H. I., Kim, J. K., Lee, S. K., Lee, S. K., Kim, S. J., Park, S. H., & Kim, H. S. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.657379 · Cited by 46
Global Reprogramming of Host Kinase Signaling in Response to Fungal Infection
Pandey, A., Ding, S. L., Qin, Q., Gupta, R., Gomez, G., Lin, F., Feng, X., da Costa, L. F., Chaki, S. P., Katepalli, M. P., et al. (2017) · Cell Host & Microbe · doi:10.1016/j.chom.2017.04.008 · Cited by 48
Dysregulation of mRNA translation and energy metabolism in cancer
Leibovitch, M., & Topisirović, I. (2017) · Advances in Biological Regulation · doi:10.1016/j.jbior.2017.11.001 · Cited by 46
Fenofibrate improves vascular endothelial function and contractility in diabetic mice
Xu, N., Wang, Q., Jiang, S., Wang, Q., Hu, W., Zhou, S., Zhao, L., Xie, L., Chen, J., Wellstein, A., et al. (2018) · Redox Biology · doi:10.1016/j.redox.2018.09.024 · Cited by 46
Basavarajappa, S. C., & Nandini, C. (2018) · Phytomedicine · doi:10.1016/j.phymed.2018.12.031 · Cited by 47
AMPK: Potential Therapeutic Target for Alzheimer's Disease
Yang, L., Jiang, Y., Shi, L., Zhong, D., Li, Y., Li, J., & Jin, R. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203720666190819142746 · Cited by 48
Seegmiller, A. C. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150916083 · Cited by 46
Ayasolla, K., Giri, S., Singh, A. K., & Singh, I. (2005) · Journal of Neuroinflammation · doi:10.1186/1742-2094-2-21 · Cited by 47
AMP‐activated protein kinase and the regulation of Ca2+ signalling in O2‐sensing cells
Evans, A. M. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.108381 · Cited by 47
The inherited genetics of pancreatic cancer and prospects for secondary screening
Vitone, L. J., Greenhalf, W., McFaul, C., Ghaneh, P., & Neoptolemos, J. P. (2006) · Best Practice & Research Clinical Gastroenterology · doi:10.1016/j.bpg.2005.10.007 · Cited by 46
Carbohydrate ingestion does not alter skeletal muscle AMPK signaling during exercise in humans
Lee-Young, R. S., Palmer, M. J., Linden, K. C., LePlastrier, K., Canny, B. J., Hargreaves, M., Wadley, G. D., Kemp, B. E., & McConell, G. K. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00023.2006 · Cited by 45
Mao, C., Lei, G., Horbath, A. D., Wang, M., Lu, Z., Yan, Y., Liu, X., Kondiparthi, L., Chen, X., Cheng, J., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.04.009 · Cited by 50
A Complex Containing SNF1-Related Kinase (SnRK1) and Adenosine Kinase in Arabidopsis
Mohannath, G., Jackel, J. N., Lee, Y., Buchmann, R. C., Wang, H., Patil, V., Adams, A. K., & Bisaro, D. M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087592 · Cited by 48
AMPK-associated signaling to bridge the gap between fuel metabolism and hepatocyte viability
Yang, Y. M. (2010) · World Journal of Gastroenterology · doi:10.3748/wjg.v16.i30.3731 · Cited by 46
Akhtar, N., Syed, D. N., Khan, M. I., Adhami, V. M., Mirza, B., & Mukhtar, H. (2015) · Oncotarget · doi:10.18632/oncotarget.6625 · Cited by 45
Aznar, N., Patel, A., Rohena, C. C., Dunkel, Y., Joosen, L., Taupin, V., Kufareva, I., Farquhar, M. G., & Ghosh, P. (2016) · eLife · doi:10.7554/elife.20795 · Cited by 46
Memmott, R. M., Gills, J. J., Hollingshead, M. G., Powers, M. C., Chen, Z., Kemp, B. E., Kozikowski, A. P., & Dennis, P. A. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-3091 · Cited by 46
Sung, J. Y., & Choi, H. C. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.04.052 · Cited by 45
Doğan, S., Johannsen, A. C., Grande, J. P., & Cleary, M. P. (2011) · Nutrition and Cancer · doi:10.1080/01635581.2011.535968 · Cited by 45
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
Convergence of IPMK and LKB1-AMPK Signaling Pathways on Metformin Action
Bang, S., Chen, Y., Ahima, R. S., & Kim, S. F. (2014) · Molecular Endocrinology · doi:10.1210/me.2014-1134 · Cited by 45
Poly (ADP-ribose) polymerase 1 and neurodegenerative diseases: past, present, and future
Hu, M.-L., Pan, Y.-R., Yong, Y.-Y., Liu, Y., Yu, L., Qin, D.-L., Qiao, G., Law, B. Y.-K., Wu, J.-M., Zhou, X.-G., et al. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102078 · Cited by 44
Possible involvement of LKB1-AMPK signaling in non-homologous end joining
Ui, A., Ogiwara, H., Nakajima, S., Kanno, S.-I., Watanabe, R., Harata, M., Okayama, H., Harris, C. C., Yokota, J., Yasui, A., et al. (2013) · Oncogene · doi:10.1038/onc.2013.125 · Cited by 44
AMPK couples p73 with p53 in cell fate decision
Adamovich, Y., Adler, J., Meltser, V., Reuven, N. B., & Shaul, Y. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.60 · Cited by 44
Krishan, S., Richardson, D. R., & Sahni, S. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.09.011 · Cited by 45
5’-AMP-Activated Protein Kinase Regulates Goat Sperm Functions via Energy Metabolism In Vitro
Zhu, Z., Li, R., Ma, G., Bai, W.-J., Fan, X., Lv, Y., Luo, J., & Zeng, W. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000491616 · Cited by 44
How is AMPK activity regulated in skeletal muscles during exercise?
Jørgensen, S. B. (2008) · Frontiers in bioscience · doi:10.2741/3102 · Cited by 45
Characterization of an Alternative Splice Variant of LKB1
Denison, F. C., Hiscock, N. J., Carling, D., & Woods, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806153200 · Cited by 52
Self-citationDialogue Between LKB1 and AMPK: A Hot Topic at the Cellular Pole
Forcet, C., & Billaud, M. (2007) · Science s STKE · doi:10.1126/stke.4042007pe51 · Cited by 48
Metadata
- Authors
- Woods, A., Johnstone, S. R., Dickerson, K., Leiper, F. C., Fryer, L. G. D., Neumann, D., Schlattner, U., Wallimann, T., Carlson, M., & Carling, D.
- Affiliations
- Hammersmith Hospital (GB)
- ETH Zurich (CH)
- Columbia University (US)
- Corresponding author
- Carling, David
- Venue
- Current Biology
- Publisher
- Elsevier BV
- Published
- 2003-11
- Volume
- 13
- Issue
- 22
- Pages
- 2004-2008
- ISSN
- 0960-9822 (ISSN-L)
- OpenAlex
- W1990278643
- Cited by
- 1,650
- References
- 24
- Citations by year
- 2026: 40 · 2025: 26 · 2024: 47 · 2023: 51 · 2022: 60 · 2021: 86 · 2020: 64 · 2019: 62 · 2018: 83 · 2017: 85 · 2016: 75 · 2015: 85 · 2014: 86 · 2013: 96 · 2012: 90
- FWCI
- 25.86
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 3546 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Current Biology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (GM-34095)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- LKB1, AMPK, AMPK activation, upstream kinases, kinase cascade, Peutz-Jeghers syndrome, energy homeostasis, Snf1, PAK1, rat liver
- MeSH terms
- Animals, Chromatography, Ion Exchange, Enzyme Activation, Liver, Multienzyme Complexes, Precipitin Tests, Blotting, Western, Protein Serine-Threonine Kinases, Rats, AMP-Activated Protein Kinases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review