The DOI matches its Crossref record; 66 of the 66 references it cites were found in a registry or an index.
Mechanisms of AMPK in the maintenance of ATP balance during energy metabolism
Open accessAbstract
AMP‐activated protein kinase (AMPK) is a conserved sensor of cellular energy change and is activated by increased AMP/ATP and/or ADP/ATP ratios. AMPK maintains the energy balance by decreasing the ATP‐consuming processes such as transcription of synthetic fat genes and rRNA, the translation of ribosomal proteins, synthesis of cholesterol and fatty acid, while the metabolic pathways such as glucose and fatty transport, fatty acid oxidation, autophagy, mitochondrial synthesis and oxidative metabolism are increased to preserve ATP during energy deficiency. Recent advance has demonstrated that AMPK activity has a close association with the initiation and progression in various cancers. Here we review the mechanisms that AMPK controls energy metabolism through regulating ATP synthesis and consumption, and further discuss the deregulation of AMPK in cancers.
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Cites
AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint
Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., Turk, B. E., & Shaw, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.003 · Cited by 3,849
Phosphorylation of ULK1 (hATG1) by AMP-Activated Protein Kinase Connects Energy Sensing to Mitophagy
Egan, D. F., Shackelford, D. B., Mihaylova, M. M., Gelino, S., Kohnz, R. A., Mair, W., Vasquez, D. S., Joshi, A., Gwinn, D. M., Taylor, R., et al. (2011) · Science · doi:10.1126/science.1196371 · Cited by 2,600
AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α
Jäger, S., Handschin, C., St.-Pierre, J., & Spiegelman, B. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705070104 · Cited by 2,491
ULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery
Jung, C. H., Jun, C. B., Ro, S.-H., Kim, Y.-M., Otto, N. M., Cao, J., Kundu, M., & Kim, D.-H. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1249 · Cited by 2,025
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The TSC1–TSC2 complex: a molecular switchboard controlling cell growth
Huang, J., & Manning, B. D. (2008) · Biochemical Journal · doi:10.1042/bj20080281 · Cited by 1,237 · cited 1×
“Activated AMPK phosphorylates TSC2 at Ser1387 or Thr1271, results in constitutive GTPase complex of TSC2-1 to maintain the mTOR activating factor Rheb in the GDP binding status, resulting in the inactivation of mTORC1 (Huang and Manning, 2008).”
BackgroundAMPK, insulin resistance, and the metabolic syndrome
Ruderman, N. B., Carling, D., Prentki, M., & Cacicedo, J. M. (2013) · Journal of Clinical Investigation · doi:10.1172/jci67227 · Cited by 873
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Cited by
Li, Q., Tuo, X., Li, B., Deng, Z., Qiu, Y., & Xie, H. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117531 · Cited by 72
Buemann, B., & Uvnäs-Moberg, K. (2020) · Medical Hypotheses · doi:10.1016/j.mehy.2020.109597 · Cited by 66
Insulin Regulation of Hepatic Lipid Homeostasis
Uehara, K., Santoleri, D., Whitlock, A. E. G., & Titchenell, P. M. (2023) · Comprehensive Physiology · doi:10.1002/cphy.c220015 · Cited by 49
Shahini, A., Rajabian, N., Choudhury, D., Shahini, S., Vydiam, K., Nguyen, T., Kulczyk, J., Santarelli, T., Ikhapoh, I., Zhang, Y., et al. (2021) · Science Advances · doi:10.1126/sciadv.abe5671 · Cited by 38
Nucleoside diphosphate kinases 1 and 2 regulate a protective liver response to a high-fat diet
Iuso, D., Garcia-Saez, I., Couté, Y., Yamaryo-Botté, Y., Boeri Erba, E., Adrait, A., Zeaiter, N., Tokarska-Schlattner, M., Jilkova, Z. M., Boussouar, F., et al. (2023) · Science Advances · doi:10.1126/sciadv.adh0140 · Cited by 14
Metadata
- Authors
- Ke, R., Xu, Q., Li, C., Luo, L., & Huang, D.
- Venue
- Cell Biology International
- Publisher
- Wiley
- Published
- 2018-01-03
- Volume
- 42
- Issue
- 4
- Pages
- 384-392
- ISSN
- 1065-6995 (ISSN-L)
- 1095-8355
- OpenAlex
- W2775794300
- Cited by
- 414
- References
- 66
- FWCI
- 7.76
- Type
- journal article
- Language
- en
- Open access
- hybrid
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