The DOI matches its Crossref record; 185 of the 185 references it cites were found in a registry or an index.
AMP-activated protein kinase: new regulation, new roles?
Abstract
The hydrolysis of ATP drives virtually all of the energy-requiring processes in living cells. A prerequisite of living cells is that the concentration of ATP needs to be maintained at sufficiently high levels to sustain essential cellular functions. In eukaryotic cells, the AMPK (AMP-activated protein kinase) cascade is one of the systems that have evolved to ensure that energy homoeostasis is maintained. AMPK is activated in response to a fall in ATP, and recent studies have suggested that ADP plays an important role in regulating AMPK. Once activated, AMPK phosphorylates a broad range of downstream targets, resulting in the overall effect of increasing ATP-producing pathways whilst decreasing ATP-utilizing pathways. Disturbances in energy homoeostasis underlie a number of disease states in humans, e.g. Type 2 diabetes, obesity and cancer. Reflecting its key role in energy metabolism, AMPK has emerged as a potential therapeutic target. In the present review we examine the recent progress aimed at understanding the regulation of AMPK and discuss some of the latest developments that have emerged in key areas of human physiology where AMPK is thought to play an important role.
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Citations
Cites
3 retracted
Functional dissection of lysine deacetylases reveals that HDAC1 and p300 regulate AMPK
Lin, Y.-Y., Kiihl, S. F., Suhail, Y., Liu, S., Chou, Y., Kuang, Z., Lu, J., Khor, C. N., Lin, C.-L., Bader, J. S., et al. (2012) · Nature · doi:10.1038/nature10804 · Cited by 100
RetractedDevelopment of Novel Adenosine Monophosphate-Activated Protein Kinase Activators
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RetractedAdipose Expression of Tumor Necrosis Factor-α: Direct Role in Obesity-Linked Insulin Resistance
Hotamisligil, G. S., Shargill, N. S., & Spiegelman, B. M. (1993) · Science · doi:10.1126/science.7678183 · Cited by 7,518
AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227
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
mTOR: from growth signal integration to cancer, diabetes and ageing
Zoncu, R., Efeyan, A., & Sabatini, D. M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3025 · Cited by 3,941
TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914
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
Autophagy and the Integrated Stress Response
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Cited by
AMPK: An Energy-Sensing Pathway with Multiple Inputs and Outputs
Hardie, D. G., Schaffer, B. E., & Brunet, A. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.10.013 · Cited by 859
AMPK, 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
Self-citationAMPK signalling in health and disease
Carling, D. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.01.005 · Cited by 797
Self-citationZhang, C.-S., Jiang, B., Li, M., Zhu, M., Peng, Y., Zhang, Y.-L., Wu, Y.-Q., Li, T. Y., Liang, Y., Lu, Z., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.06.014 · Cited by 555
Structural basis of AMPK regulation by small molecule activators
Xiao, B., Sanders, M. J., Carmena, D., Bright, N. J., Haire, L. F., Underwood, E., Patel, B. R., Heath, R. B., Walker, P. A., Hallen, S., et al. (2013) · Nature Communications · doi:10.1038/ncomms4017 · Cited by 543
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Metadata
- Authors
- Carling, D., Thornton, C., Woods, A., & Sanders, M. J.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2012-06-15
- Volume
- 445
- Issue
- 1
- Pages
- 11-27
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W2035651268
- Cited by
- 379
- References
- 185
- FWCI
- 15.10
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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