A Novel Domain in AMP-Activated Protein Kinase Causes Glycogen Storage Bodies Similar to Those Seen in Hereditary Cardiac Arrhythmias

AMP‐activated protein kinase: the energy charge hypothesis revisited

Hardie, D. G., & Hawley, S. A. (2001) · BioEssays · doi:10.1002/bies.10009 · Cited by 794

A Mutation in PRKAG3 Associated with Excess Glycogen Content in Pig Skeletal Muscle

Milan, D., Jeon, J., Looft, C., Amarger, V., Robic, A., Thelander, M., Rogel-Gaillard, C., Paul, S., Iannuccelli, N., Rask, L., et al. (2000) · Science · doi:10.1126/science.288.5469.1248 · Cited by 733

Identification of a gene responsible for familial Wolff-Parkinson-White syndrome

Gollob, M. H., Green, M. S., Tang, A. S.-L., Gollob, T., Karibe, A., Hassan, A.-S., Ahmad, F., Lozado, R., Shah, G., Fananapazir, L., et al. (2001) · New England Journal of Medicine · doi:10.1056/nejm200106143442403 · Cited by 671

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

Constitutively active AMP kinase mutations cause glycogen storage disease mimicking hypertrophic cardiomyopathy

Arad, M., Benson, D. W., Pérez‐Atayde, A. R., McKenna, W. J., Sparks, E. A., Kanter, R. J., McGarry, K., Seidman, J. G., & Seidman, C. E. (2002) · Journal of Clinical Investigation · doi:10.1172/jci14571 · Cited by 545

Mutations in the gamma2 subunit of AMP-activated protein kinase cause familial hypertrophic cardiomyopathy: evidence for the central role of energy compromise in disease pathogenesis

Blair, E. M. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.11.1215 · Cited by 531

The AMP-activated protein kinase α2 catalytic subunit controls whole-body insulin sensitivity

Viollet, B., Andreelli, F., Jørgensen, S. B., Perrin, C., Geloen, A., Flamez, D., Mu, J., Lenzner, C., Baud, O., Bennoun, M., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci16567 · Cited by 499

AMP-activated protein kinase: greater AMP dependence, and preferential nuclear localization, of complexes containing the α2 isoform

Salt, I. P., Celler, J. W., Hawley, S. A., Prescott, A. R., Woods, A., Carling, D., & Hardie, D. G. (1998) · Biochemical Journal · doi:10.1042/bj3340177 · Cited by 437

AMPK β Subunit Targets Metabolic Stress Sensing to Glycogen

Polekhina, G., Gupta, A., Michell, B. J., van Denderen, B., Murthy, S., Feil, S. C., Jennings, I. G., Campbell, D. J., Witters, L. A., Parker, M. W., et al. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00292-6 · Cited by 423

Regulation of 5′AMP-activated protein kinase activity and substrate utilization in exercising human skeletal muscle

Wojtaszewski, J. F. P., MacDonald, C., Nielsen, J. N., Hellsten, Y., Hardie, D. G., Kemp, B. E., Kiens, B., & Richter, E. A. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00436.2002 · Cited by 348

Skeletal muscle AMPK is not activated during 2 h of moderate intensity exercise at ∼65% in endurance trained men

McConell, G. K., Wadley, G. D., Plastrier, K. L., & Linden, K. C. (2020) · The Journal of Physiology · doi:10.1113/jp277619 · Cited by 34

Towards Kinase Inhibitor Therapies for Fragile X Syndrome: Tweaking Twists in the Autism Spectrum Kinase Signaling Network

D’Incal, C., Broos, J., Torfs, T., Kooy, R. F., & Vanden Berghe, W. (2022) · Cells · doi:10.3390/cells11081325 · Cited by 29

Increased glycogen stores due to γ-AMPK overexpression protects against ischemia and reperfusion damage

Ofir, M., Arad, M., Porat, E. E., Freimark, D., Chepurko, Y., Vidne, B. A., Seidman, C. E., Seidman, J. G., Kemp, B. E., & Hochhauser, E. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.12.011 · Cited by 29

Amino Acid Trafficking and Skeletal Muscle Protein Synthesis: A Case of Supply and Demand

White, J. P. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.656604 · Cited by 29

Chemical genetic screen identifies Gapex-5/GAPVD1 and STBD1 as novel AMPK substrates

Ducommun, S., Deák, M., Zeigerer, A., Göransson, O., Seitz, S., Collodet, C., Madsen, A. B., Jensen, T. E., Viollet, B., Foretz, M., et al. (2019) · Cellular Signalling · doi:10.1016/j.cellsig.2019.02.001 · Cited by 30

A Renaissance of Metabolite Sensing and Signaling: From Modular Domains to Riboswitches

Templeton, G. W., & Moorhead, G. B. G. (2004) · The Plant Cell · doi:10.1105/tpc.104.160930 · Cited by 28

Structural and functional basis for starch binding in the SnRK1 subunits AKINβ2 and AKINβγ

Ávila-Castañeda, A., Gutiérrez-Granados, N., Ruiz‐Gayosso, A., Sosa‐Peinado, A., Martínez‐Barajas, E., & Coello, P. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00199 · Cited by 27

Targeting AMPK Signaling by Dietary Polyphenols in Cancer Prevention

Hu, Z., Li, M., Cao, Y., Akan, O. D., Guo, T., & Luo, F. (2021) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202100732 · Cited by 28

Sanguinarine is an allosteric activator of AMP-activated protein kinase

Choi, J., He, N., Sung, M., Yang, Y. D., & Yoon, S. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.08.081 · Cited by 27

Allosteric regulation of AMP-activated protein kinase by adenylate nucleotides and small-molecule drugs

Matos, A. L. D. S. A., Oakhill, J. S., Moreira, J. M. A., Loh, K., Galić, S., & Scott, J. W. (2019) · Biochemical Society Transactions · doi:10.1042/bst20180625 · Cited by 28

Homo-oligomerization and Activation of AMP-activated Protein Kinase Are Mediated by the Kinase Domain αG-Helix

Scholz, R., Suter, M., Weimann, T., Polge, C., Konarev, P. V., Thali, R. F., Tuerk, R. D., Viollet, B., Wallimann, T., Schlattner, U., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.047670 · Cited by 27

At the crossroads: AMP-activated kinase and the LKB1 tumor suppressor link cell proliferation to metabolic regulation.

Kyriakis, J. M. (2003) · Journal of Biology · doi:10.1186/1475-4924-2-26 · Cited by 26

Role of AMP-Activated Protein Kinase for Regulating Post-exercise Insulin Sensitivity

Kjøbsted, R., Wojtaszewski, J. F. P., & Treebak, J. T. (2016) · Proceedings of the Fourth International Symposium on Polarization Phenomena in Nuclear Reactions · doi:10.1007/978-3-319-43589-3_5 · Cited by 26

α-Catalytic subunits of 5′AMP-activated protein kinase display fiber-specific expression and are upregulated by chronic low-frequency stimulation in rat muscle

Putman, C. T., Martins, K. J. B., Gallo, M. E., Lopaschuk, G. D., Pearcey, J. A., MacLean, I. M., Saranchuk, R. J., & Pette, D. (2007) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00609.2006 · Cited by 25

Pharmacological Targeting of AMP-Activated Protein Kinase and Opportunities for Computer-Aided Drug Design: Miniperspective

Miglianico, M., Nicolaes, G. A. F., & Neumann, D. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01201 · Cited by 24

Gene expression profiling of mice with genetically modified muscle glycogen content

Parker, G. E., Pederson, B. A., Obayashi, M., Schroeder, J. M., Harris, R. A., & Roach, P. J. (2006) · Biochemical Journal · doi:10.1042/bj20051456 · Cited by 23

Glycogen at the Crossroad of Stress Resistance, Energy Maintenance, and Pathophysiology of Aging

Gusarov, I., & Nudler, E. (2018) · BioEssays · doi:10.1002/bies.201800033 · Cited by 24

Constitutive expression of a novel isoamylase from Bacillus lentus in Pichia pastoris for starch processing

Li, Y., Zhang, L., Ding, Z., & Shi, G. (2013) · Process Biochemistry · doi:10.1016/j.procbio.2013.07.001 · Cited by 21

Maize AKINβγ dimerizes through the KIS/CBM domain and assembles into SnRK1 complexes

López‐Paz, C., Vilela, B., Riera, M., Pagès, M., & Lumbreras, V. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.05.022 · Cited by 21

[AMPK as a cellular energy sensor and its function in the organism].

Miranda, N., Tovar, A. R., Palacios, B., & Torres, N. (2007) · PubMed · Cited by 21

Folic acid supplementation prevents high fructose-induced non-alcoholic fatty liver disease by activating the AMPK and LKB1 signaling pathways

Kim, H., & Min, H. (2020) · Nutrition Research and Practice · doi:10.4162/nrp.2020.14.4.309 · Cited by 20

Targeting of AMP-activated protein kinase: prospects for computer-aided drug design

Kim, J., Yang, G., & Ha, J. (2016) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2017.1255194 · Cited by 21

β-subunit myristoylation functions as an energy sensor by modulating the dynamics of AMP-activated Protein Kinase

Ali, N., Ling, N. X. Y., Krishnamurthy, S., Oakhill, J. S., Scott, J. W., Stapleton, D., Kemp, B. E., Anand, G. S., & Gooley, P. R. (2016) · Scientific Reports · doi:10.1038/srep39417 · Cited by 20

Régulation du métabolisme énergétique par l’AMPK : Une nouvelle voie thérapeutique pour le traitement des maladies métaboliques et cardiaques

Foretz, M., Taleux, N., Guigas, B., Horman, S., Beauloye, C., Andréelli, F., Bertrand, L., & Viollet, B. (2006) · Digital Access to Libraries (Université catholique de Louvain (UCL), l'Université de Namur (UNamur) and the Université Saint-Louis (USL-B)) · doi:10.7202/012810ar · 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

AMPK/SNF1 structure: a menage a trois of energy-sensing

John, W. S. (2009) · Frontiers in bioscience · doi:10.2741/3266 · Cited by 19

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

PPARβ Activation Induces Rapid Changes of Both AMPK Subunit Expression and AMPK Activation in Mouse Skeletal Muscle

Lendoye, E., Sibille, B., Rousseau, A., Murdaca, J., Grimaldi, P. A., & Lopez, P. (2011) · Molecular Endocrinology · doi:10.1210/me.2010-0504 · Cited by 18

Two structurally related starch-binding domain families CBM25 and CBM26

Majzlová, K., & Janeĉek, Ŝ. (2014) · Biologia · doi:10.2478/s11756-014-0415-3 · Cited by 18

In Vivo Assessment of Myocardial Glucose Uptake by Positron Emission Tomography in Adults With the PRKAG2 Cardiac Syndrome

Ha, A. C. T., Renaud, J. M., deKemp, R. A., Thorn, S., DaSilva, J. N., Garrard, L., Yoshinaga, K., Abraham, A., Green, M. S., Beanlands, R. S., et al. (2009) · Circulation Cardiovascular Imaging · doi:10.1161/circimaging.109.853291 · Cited by 19

Adenosine Monophosphate-Activated Protein Kinase (AMPK) as a Diverse Therapeutic Target: A Computational Perspective

Ramesh, M., Vepuri, S. B., Oosthuizen, F., & Soliman, M. E. S. (2015) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-015-1911-9 · Cited by 17

Hepatic glycogen directly regulates gluconeogenesis through an AMPK/CRTC2 axis in mice

Zhang, B., JOHNSON, M. M., Yuan, T., Nguyen, T.-N., Okada, J., Yang, F., Xiaoli, A. M., Melikian, L. H., Xu, S., Dadpey, B., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci188363 · Cited by 20

PaCS Is a Novel Cytoplasmic Structure Containing Functional Proteasome and Inducible by Cytokines/Trophic Factors

Sommi, P., Necchi, V., Vitali, A., Montagna, D., Luigi, A. D., Salmona, M., Ricci, V., & Solcia, E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0082560 · Cited by 16

Crystallization of the glycogen-binding domain of the AMP-activated protein kinase β subunit and preliminary X-ray analysis

Polekhina, G., Feil, S. C., Gupta, A., O’Donnell, P. A., Stapleton, D., & Parker, M. W. (2004) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309104025059 · Cited by 16

Dietary α-ketoglutarate alleviates glycinin and β-conglycinin induced damage in the intestine of mirror carp (Cyprinus carpio)

Luo, Q., Qian, R., Qiu, Z., Yamamoto, F. Y., Du, Y., Lin, X., Zhao, J., & Xu, Q. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1140012 · Cited by 15

Human γ2-AMPK Mutations

Yavari, A., Sarma, D., & Sternick, E. B. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7598-3_37 · Cited by 16

The function study on the interaction between Grb2 and AMPK

Pan, Z., Wang, J., Yin, X., Xie, P., Yang, J., Jiang, J., Zhang, L., & He, F. (2007) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-007-9591-6 · Cited by 14

Screening methods for AMP-activated protein kinase modulators: a patent review

Kim, J., Shin, J., & Ha, J. (2014) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2014.995626 · Cited by 13

The Role of AMP-activated Protein Kinase in Oxytosis/Ferroptosis: Protector or Potentiator?

Currais, A. J. M., Kepchia, D., Liang, Z., & Maher, P. A. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0013 · Cited by 12

AICAR and Compound C regulate food intake independently of AMP-activated protein kinase in lines of chickens selected for high or low body weight

Xu, P., Siegel, P. B., & Denbow, D. M. (2011) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2011.04.004 · Cited by 12

Role of AMPK in the Regulation of Cellular Energy Metabolism

Ha, J., & Lee, S.-H. (2010) · Journal of Korean Endocrine Society · doi:10.3803/jkes.2010.25.1.9 · Cited by 12

Yeast as a model system to study glucose-mediated signalling and response

Sanz, P. (2006) · Frontiers in bioscience · doi:10.2741/2238 · Cited by 12

AMPK associates with and causes fragmentation of the Golgi by phosphorylating the guanine nucleotide exchange factor GBF1

Freemantle, J. B., Towler, M. C., Hudson, E. R., Macartney, T., Zwirek, M., Liu, D. J. K., Pan, D. A., Ponnambalam, S., & Hardie, D. G. (2024) · Journal of Cell Science · doi:10.1242/jcs.262182 · Cited by 10

Genome-wide identification and characterization of the AMPK genes and their distinct expression patterns in response to air exposure in the Manila clam (Ruditapes philippinarum)

Wang, J., Fang, L., Wu, Q., Li, D., Huo, Z., & Yan, X. (2019) · Genes & Genomics · doi:10.1007/s13258-019-00872-0 · Cited by 11

Advances in the development of AMPK-activating compounds

Sriwijitkamol, A., & Musi, N. (2008) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.3.10.1167 · Cited by 10

Knockdown of AMP-activated protein kinase increases the insecticidal efficiency of pymetrozine to Nilaparvata lugens

Lin, Y., Ji, H., Cao, X., Cen, Y., Chen, Y., Ji, S., & Zheng, S. (2021) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2021.104856 · Cited by 9

Endocannabinoid biosynthetic enzymes regulate pain response via LKB1–AMPK signaling

Chen, M., Shin, M., Ware, T. B., Donvito, G., Muchhala, K. H., Mischel, R. A., Mustafa, M. A., Serbulea, V., Upchurch, C. M., Leitinger, N., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2304900120 · Cited by 9

Floralozone regulates MiR-7a-5p expression through AMPKα2 activation to improve cognitive dysfunction in vascular dementia

Song, Y., Li, S., Chao, C.-Y., Shuang-Guo, Chen, G.-Z., Wang, S., Zhang, M., Yin, Y.-L., & Li, P. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.114748 · Cited by 9

Branching out on AMPK Regulation

Carling, D. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2008.12.007 · Cited by 9

Polyubiquitinated proteins, proteasome, and glycogen characterize the particle-rich cytoplasmic structure (PaCS) of neoplastic and fetal cells

Necchi, V., Sommi, P., Vitali, A., Vanoli, A., Savoia, A., Ricci, V., & Solcia, E. (2014) · Histochemistry and Cell Biology · doi:10.1007/s00418-014-1202-5 · Cited by 9

The interaction between AMPKβ2 and the PP1-targeting subunit R6 is dynamically regulated by intracellular glycogen content

Oligschlaeger, Y., Miglianico, M., Dahlmans, V. E. H., Rubio-Villena, C., Chanda, D., García-Gimeno, M. A., Coumans, W. A., Liu, Y., Voncken, J. W., Luiken, J. J. F. P., et al. (2016) · Biochemical Journal · doi:10.1042/bj20151035 · Cited by 9

Does AMPK bind glycogen in skeletal muscle or is the relationship correlative?

Frankish, B. P., & Murphy, R. M. (2024) · Essays in Biochemistry · doi:10.1042/ebc20240006 · Cited by 7

Mice with Whole-Body Disruption of AMPK-Glycogen Binding Have Increased Adiposity, Reduced Fat Oxidation and Altered Tissue Glycogen Dynamics

Janzen, N. R., Whitfield, J., Murray‐Segal, L., Kemp, B. E., Hawley, J. A., & Hoffman, N. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179616 · Cited by 8

Exercise training and probiotic supplementation effects on skeletal muscle apoptosis prevention in type-Ι diabetic rats

Rezaee, N., Rahmani‐Nia, F., Delfan, M., & Ghahremani, R. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119973 · Cited by 8

Metabolomics reveals mouse plasma metabolite responses to acute exercise and effects of disrupting AMPK-glycogen interactions

Belhaj, M. R., Lawler, N. G., Hawley, J. A., Broadhurst, D., Hoffman, N. J., & Reinke, S. N. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.957549 · Cited by 7

New Regulator for Energy Signaling Pathway in Plants Highlights Conservation Among Species

Meyer, A. K., Longin, C. F. H., Klose, C. D., & Hermann, A. (2010) · Science Signaling · doi:10.1126/scisignal.3119jc5 · Cited by 8

PRKAG3 polymorphisms associated with sporadic Wolff–Parkinson–White syndrome among a Taiwanese population

Weng, K.-P., Yuh, Y., Huang, S., Hsiao, H.-C., Wu, H.-W., Chien, J., Chen, B.-H., Huang, S., Chien, K., & Ger, L. (2016) · Journal of the Chinese Medical Association · doi:10.1016/j.jcma.2016.08.008 · Cited by 8

LncRNAs are involved in regulating ageing and age-related disease through the adenosine monophosphate-activated protein kinase signalling pathway

Li, J., Xiao, F., Wang, S., Fan, X., He, Z., Yan, T., Zhang, J., Yang, M., & Yang, D. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.06.014 · Cited by 7

When phosphorylated at Thr148, the β2-subunit of AMP-activated kinase does not associate with glycogen in skeletal muscle

Xu, H., Frankenberg, N. T., Lamb, G. D., Gooley, P. R., Stapleton, D., & Murphy, R. M. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00047.2016 · Cited by 7

Starch Metabolism in Green Plants

Busi, M. V., Gomez‐Casati, D. F., Martín, M., Barchiesi, J., Grisolia, M. J., Hedín, N., & Carrillo, J. B. (2015) · Springer eBooks · doi:10.1007/978-3-319-16298-0_78 · Cited by 7

Signaling by AMP‐activated Protein Kinase

Neumann, D., Wallimann, T., Rider, M. H., Tokarska-Schlattner, M., Hardie, D. G., & Schlattner, U. (2007) · Wiley eBooks · doi:10.1002/9783527621095.ch9 · Cited by 7

Temperature, but not excess of glycogen, regulates “in vitro” AMPK activity in muscle samples of steer carcasses

Strobel, P., Galaz, A., Villarroel‐Espíndola, F., Apaoblaza, A., Slebe, J. C., Jerez-Timaure, N., Gallo, C., & Ramírez‐Reveco, A. (2021) · PLoS ONE · doi:10.1371/journal.pone.0229480 · Cited by 6

Carbon and Energy Metabolism

Thelander, M., Nilsson, A., & Ronne, H. (2009) · Wiley-Blackwell eBooks · doi:10.1002/9781444316070.ch9 · Cited by 7

Biochemical and functional studies on the regulation of the Saccharomyces cerevisiae AMPK homolog SNF1

Amodeo, G. A., Momcilovic, M., Carlson, M., & Tong, L. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.05.083 · Cited by 7

AMPK

Karabiyik, C., Vicinanza, M., & Rubinsztein, D. C. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820538-9.00004-1 · Cited by 6

Polymorphisms in the promoter region of bovine PRKAB1 gene

Zhang, Q., Chen, H., Zhao, S., Zhang, L., Zhang, L., & Wang, X. (2009) · Molecular Biology Reports · doi:10.1007/s11033-009-9612-5 · Cited by 6

Disrupting AMPK-Glycogen Binding in Mice Increases Carbohydrate Utilization and Reduces Exercise Capacity

Janzen, N. R., Whitfield, J., Murray‐Segal, L., Kemp, B. E., Hawley, J. A., & Hoffman, N. J. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.859246 · Cited by 5

Locally applied heat stress during exercise training may promote adaptations to mitochondrial enzyme activities in skeletal muscle

Maunder, E., King, A., Rothschild, J. A., Brick, M. J., Leigh, W. B., Hedges, C. P., Merry, T. L., & Kilding, A. E. (2024) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-024-02939-8 · Cited by 4

Comparative transcriptome analysis reveals a strategy involving dietary manipulation for reducing the mortality of Litopenaeus vannamei exposed to sublethal ammonia through the energy metabolism pathway

Wang, T., Gao, L., Li, W., Li, Y., & Shan, H. (2022) · Aquaculture International · doi:10.1007/s10499-022-00855-1 · Cited by 5

Opinion: alternative views of AMP-activated protein kinase

Brenman, J. E., & Temple, B. R. S. (2007) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-007-0005-x · Cited by 5

Structural Heterogeneity of Proteoform-Ligand Complexes in Adenosine Monophosphate-Activated Protein Kinase Uncovered by Integrated Top-Down Mass Spectrometry

Chan, H., Krichel, B., Bandura, L. J., Chapman, E. A., Rogers, H. T., Fischer, M. S., Roberts, D. S., Gao, Z., Wang, M., Wu, J., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c06950 · Cited by 7

Single Nucleotide Polymorphisms and Haplotypic Diversity in the Bovine PRKAB1 Gene

Zhang, Q., Chen, H., Zhao, S., Zhang, L., Zhang, L., Li, F., & Wang, X. (2009) · Molecular Biotechnology · doi:10.1007/s12033-009-9194-4 · Cited by 4

Birt–Hogg–Dubé Syndrome

Patel, T. M., Beal, M. A., Schroeder, G., & Shifren, A. (2025) · Clinics in Chest Medicine · doi:10.1016/j.ccm.2025.07.004 · Cited by 3

Starch Metabolism in Green Plants

Busi, M. V., Gomez‐Casati, D. F., Martín, M., Barchiesi, J., Grisolia, M. J., Hedín, N., & Carrillo, J. B. (2014) · Springer eBooks · doi:10.1007/978-3-319-03751-6_78-1 · Cited by 3

Diagnosis and Management of Horses with Equine Metabolic Syndrome (EMS)

Chameroy, K. A. (2010) · Cited by 3

AMP-activated protein kinase Activating Agent and Its Implication

Choi, H. C. (2012) · Endocrinology and Metabolism · doi:10.3803/enm.2012.27.2.109 · Cited by 3

Amp-activated protein kinase (Ampk) in skeletal muscle during physical exercise

Pagliara, V., Nasso, R., Liguori, L., Crescenzo, F. D., Masullo, M., Arcone, R., & Di Palma, D. (2020) · Journal of Physical Education and Sport · doi:10.7752/jpes.2020.s4323 · Cited by 3

AMPK-Orchestrated Metabolic Reprogramming in Some Flavivirus Infections: Mechanisms and Therapeutic Opportunities

Craft, K., Muhammad, I., Pei, S., & Tang, Q. (2026) · Viruses · doi:10.3390/v18080910 · Cited by 2

Seasonal Changes in White Adipose Tissue in American Black Bears (Ursus americanus)

Hill, E. (2013) · Cited by 2

Maintaining Energy Balance in Health and Disease: Role of the AMP-Activated Protein Kinase

Scott, J. W. (2010) · Springer eBooks · doi:10.1007/978-1-4419-6382-6_9 · Cited by 2

Effects of AMP-activated Protein Kinase Activating Compounds and Its Mechanism

Choi, H. C. (2012) · Journal of Yeungnam Medical Science · doi:10.12701/yujm.2012.29.2.77 · Cited by 2

The α subunit of AMP ‐activated protein kinase is critical for the metabolic success and tachyzoite proliferation of Toxoplasma gondii

Yang, X., Yang, J., Lyu, M., Li, Y., Liu, A., & Shen, B. (2024) · Microbial Biotechnology · doi:10.1111/1751-7915.14455 · Cited by 4

Adaptation to endurance training

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Harach, T. (2010) · edoc (University of Basel) · doi:10.5451/unibas-005405424

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The Impact of Reduced-Exertion High-Intensity Interval Training on Insulin Sensitivity and Aerobic Capacity

Metcalfe, R. S. (2015) · The University of Bath Online Publications Store (The University of Bath) · doi:10.13140/rg.2.1.4944.0088

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AMPK β Subunit Targets Metabolic Stress Sensing to Glycogen

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Aberrant activation of AMP-activated protein kinase remodels metabolic network in favor of cardiac glycogen storage

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