AMP-activated protein kinase mediates mitochondrial fission in response to energy stress
Open accessAbstract
How to shape mitochondrial networks: Mitochondria undergo fragmentation or fusion in response to changes in cellular metabolism. Toyama et al. report that adenosine monophosphate-activated protein kinase (AMPK) is both necessary and sufficient to control mitochondrial fragmentation. AMPK functions as a sensor to monitor the energy status of the cell by phosphorylating mitochondrial fission factor (MFF), a protein of the mitochondrial outer membrane. MFF then acts to recruit a cytoplasmic guanosine triphosphatase that promotes mitochondrial fission. Science , this issue p. 275
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
Under mitochondrial stress, fission is activated by AMPK-mediated phosphorylation of mitochondrial fission factor, facilitating removal of damaged mitochondria.
“Under mitochondrial stress, fission is activated by AMPK-mediated phosphorylation of mitochondrial fission factor, facilitating the removal of damaged mitochondria43.”
From Mitochondrial and metabolic dysfunction in ageing and age-related diseases (2022) · cites this paper as [43]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351 · see citing works
Genome engineering using the CRISPR-Cas9 system
Ran, F. A., Hsu, P. D., Wright, J., Agarwala, V., Scott, D. A., & Zhang, F. (2013) · Nature Protocols · doi:10.1038/nprot.2013.143 · Cited by 11,133 · see citing works
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 · see citing works
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 · see citing works
Self-citationMitochondrial Fission, Fusion, and Stress
Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674 · see citing works
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082 · see citing works
The AMPK signalling pathway coordinates cell growth, autophagy and metabolism
Mihaylova, M. M., & Shaw, R. J. (2011) · Nature Cell Biology · doi:10.1038/ncb2329 · Cited by 2,923 · see citing works
Self-citationKahn, B. B., Alquier, T., Carling, D., & Hardie, D. G. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2004.12.003 · Cited by 2,799 · see citing works
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 · see citing works
Self-citationLi, Y., Xu, S., Mihaylova, M. M., Zheng, B., Hou, X., Jiang, B., Park, O., Luo, Z., Lefai, É., Shyy, J. Y.-J., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.009 · Cited by 1,788 · see citing works
Self-citationDuring autophagy mitochondria elongate, are spared from degradation and sustain cell viability
Gomes, L. C., Benedetto, G. D., & Scorrano, L. (2011) · Nature Cell Biology · doi:10.1038/ncb2220 · Cited by 1,735 · see citing works
Mitochondrial Dynamics in the Regulation of Nutrient Utilization and Energy Expenditure
Liesa, M., & Shirihai, O. S. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.03.002 · Cited by 1,341 · see citing works
Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission
Losón, O. C., Song, Z., Chen, H., & Chan, D. C. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0721 · Cited by 1,235 · see citing works
Self-citationRambold, A. S., Kostelecky, B., Elia, N., & Lippincott‐Schwartz, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107402108 · Cited by 1,144 · see citing works
Otera, H., Wang, C., Cleland, M. M., Setoguchi, K., Yokota, S., Youle, R. J., & Mihara, K. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007152 · Cited by 1,110 · see citing works
Rambold, A. S., Cohen, S., & Lippincott-Schwartz, J. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.01.029 · Cited by 1,038 · see citing works
Mitochondrial dynamics and inheritance during cell division, development and disease
Mishra, P., & Chan, D. C. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3877 · Cited by 1,038 · see citing works
Self-citationCool, B. L., Zinker, B. A., Chiou, W. J. H., Kifle, L., Cao, N., Perham, M., Dickinson, R., Adler, A. L., Gagné, G. D., Iyengar, R., et al. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.05.005 · Cited by 932 · see citing works
Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
Ishihara, N., Fujita, Y., Oka, T., & Mihara, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601184 · Cited by 899 · see citing works
Karbowski, M., Lee, Y.-J., Gaume, B., Jeong, S.-Y., Frank, S., Nechushtan, A., Santel, A., Fuller, M., Smith, C. L., & Youle, R. J. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200209124 · Cited by 846 · see citing works
Mitochondrial fission in apoptosis
Youle, R. J., & Karbowski, M. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1697 · Cited by 773 · see citing works
Gandre-Babbe, S., & van der Bliek, A. M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1287 · Cited by 769 · see citing works
Metabolic control of cell death
Green, D. R., Galluzzi, L., & Kroemer, G. (2014) · Science · doi:10.1126/science.1250256 · Cited by 661 · see citing works
Mitochondrial bioenergetics and structural network organization
Benard, G., Bellance, N., James, D., Parrone, P., Fernandez, H., Letellier, T., & Rossignol, R. (2007) · Journal of Cell Science · doi:10.1242/jcs.03381 · Cited by 618 · see citing works
Regulation of OPA1 processing and mitochondrial fusion by m -AAA protease isoenzymes and OMA1
Ehses, S., Lauria, I., Mancuso, G., Bernacchia, A., Geimer, S., Tondera, D., Martinou, J., Westermann, B., Rugarli, E. I., & Langer, T. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200906084 · Cited by 570 · see citing works
Mihaylova, M. M., Vasquez, D. S., Ravnskjær, K., Denechaud, P., Yu, R. T., Alvarez, J. G. A., Downes, M., Evans, R. M., Montminy, M., & Shaw, R. J. (2011) · Cell · doi:10.1016/j.cell.2011.03.043 · Cited by 554 · see citing works
Self-citationStructural 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., Hallén, S., et al. (2013) · Nature Communications · doi:10.1038/ncomms4017 · Cited by 547 · see citing works
Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells
Head, B., Griparic, L., Amiri, M., Gandre-Babbe, S., & van der Bliek, A. M. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200906083 · Cited by 515 · see citing works
Mishra, P., Carelli, V., Manfredi, G., & Chan, D. C. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.011 · Cited by 473 · see citing works
Self-citationLaderoute, K. R., Amin, K., Calaoagan, J. M., Knapp, M., Le, T., Orduna, J. M., Foretz, M., & Viollet, B. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00166-06 · Cited by 443 · see citing works
Novel Drp1 inhibitor diminishes aberrant mitochondrial fission and neurotoxicity
Qi, X., Qvit, N., Su, Y.-C., & Mochly‐Rosen, D. (2012) · Journal of Cell Science · doi:10.1242/jcs.114439 · Cited by 441 · see citing works
Duvezin‐Caubet, S., Jagasia, R., Wagener, J., Hofmann, S., Trifunović, A., Hansson, A., Chomyn, A., Bauer, M. F., Attardi, G. M., Larsson, N., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606059200 · Cited by 431 · see citing works
Membrane Remodeling Induced by the Dynamin-Related Protein Drp1 Stimulates Bax Oligomerization
Montessuit, S., Somasekharan, S. P., Terrones, O., Lucken‐Ardjomande, S., Herzig, S., Schwarzenbacher, R., Manstein, D. J., Bossy‐Wetzel, E., Basáñez, G., Meda, P., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.017 · Cited by 422 · see citing works
Self-citationCourchet, J., Lewis, T. L., Lee, S., Courchet, V., Liou, D.-Y., Aizawa, S., & Polleux, F. (2013) · Cell · doi:10.1016/j.cell.2013.05.021 · Cited by 351 · see citing works
Self-citationMairet-Coello, G., Courchet, J., Pieraut, S., Courchet, V., Maximov, A., & Polleux, F. (2013) · Neuron · doi:10.1016/j.neuron.2013.02.003 · Cited by 351 · see citing works
Self-citationA novel direct activator of AMPK inhibits prostate cancer growth by blocking lipogenesis
Zadra, G., Photopoulos, C., Tyekucheva, S., Heidari, P., Weng, Q. P., Fedele, G., Liu, H., Scaglia, N., Priolo, C., Sicińska, E., et al. (2014) · EMBO Molecular Medicine · doi:10.1002/emmm.201302734 · Cited by 210 · see citing works
Mutations in Fis1 disrupt orderly disposal of defective mitochondria
Shen, Q., Yamano, K., Head, B. P., Kawajiri, S., Cheung, J. T. M., Wang, C., Cho, J.-H., Hattori, N., Youle, R. J., & van der Bliek, A. M. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-09-0525 · Cited by 209 · see citing works
Calabrese, M. F., Rajamohan, F., Harris, M. S., Caspers, N. L., Magyar, R. A., Withka, J. M., Wang, H., Borzilleri, K. A., Sahasrabudhe, P. V., Hoth, L. R., et al. (2014) · Structure · doi:10.1016/j.str.2014.06.009 · Cited by 182 · see citing works
Scott, J. W., Norman, D., Hawley, S. A., Kontogiannis, L., & Hardie, D. G. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5316 · Cited by 179 · see citing works
Ducommun, S., Deak, M., Sumpton, D., Ford, R. J., Núñez Galindo, A., Kussmann, M., Viollet, B., Steinberg, G. R., Foretz, M., Dayon, L., et al. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.02.008 · Cited by 167 · see citing works
The mitochondrial respiratory chain is a modulator of apoptosis
Kwong, J. Q., Henning, M. S., Starkov, A. A., & Manfredi, G. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704059 · Cited by 145 · see citing works
Flagged first, then by citations
Research works printed but not linked: 2
- [21]Duvezin-Caubet S J. Biol. Chem 2006 281 37972 37979 17003040
- [37]Mairet-Coello G Neuron 2013 78 94 108 23583109 PMC3784324
Cited by
Sorted by citations
Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance
Pickles, S., Vigié, P., & Youle, R. J. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.004 · Cited by 2,081 · see citing works
Fang, E. F., Hou, Y., Palikaras, K., Adriaanse, B. A., Kerr, J. S., Yang, B., Lautrup, S., Hasan-Olive, M. M., Caponio, D., Dan, X., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0332-9 · Cited by 1,740 · see citing works
Vyas, S., Zaganjor, E., & Haigis, M. C. (2016) · Cell · doi:10.1016/j.cell.2016.07.002 · Cited by 1,735 · see citing works
The cell biology of mitochondrial membrane dynamics
Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550 · see citing works
Mitochondrial Dynamics and Its Involvement in Disease
Chan, D. C. (2020) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-012419-032711 · Cited by 1,416 · see citing works
Self-citationMitochondrial dynamics in health and disease: mechanisms and potential targets
Chen, W., Zhao, H., & Li, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01547-9 · Cited by 1,306 · see citing works
Mitochondrial dysfunction in cell senescence and aging
Miwa, S., Kashyap, S., Chini, E., & von Zglinicki, T. (2022) · Journal of Clinical Investigation · doi:10.1172/jci158447 · Cited by 1,061 · see citing works
Mitochondrial and metabolic dysfunction in ageing and age-related diseases
Amorim, J. A., Coppotelli, G., Rolo, A. P., Palmeira, C. M., Ross, J. M., & Sinclair, D. A. (2022) · Nature Reviews Endocrinology · doi:10.1038/s41574-021-00626-7 · Cited by 990 · see citing works
AMPK and TOR: The Yin and Yang of Cellular Nutrient Sensing and Growth Control
González, A., Hall, M. N., Lin, S.-C., & Hardie, D. G. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.01.015 · Cited by 797 · see citing works
Mitochondrial dynamics in adaptive and maladaptive cellular stress responses
Eisner, V., Picard, M., & Hajnóczky, G. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0133-0 · Cited by 622 · see citing works
Maintenance of Skeletal Muscle Mitochondria in Health, Exercise, and Aging
Hood, D. A., Memme, J. M., Oliveira, A. N., & Triolo, M. (2019) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020518-114310 · Cited by 567 · see citing works
Zhou, H., Wang, S., Zhu, P., Hu, S., Chen, Y., & Ren, J. (2018) · Redox Biology · doi:10.1016/j.redox.2017.12.019 · Cited by 550 · see citing works
Rabinovitch, R. C., Samborska, B., Faubert, B., Ma, E. H., Gravel, S.-P., Andrzejewski, S., Raissi, T. C., Pause, A., St.-Pierre, J., & Jones, R. G. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.09.026 · Cited by 543 · see citing works
Laker, R. C., Drake, J. C., Wilson, R. J., Lira, V. A., Lewellen, B. M., Ryall, K. A., Fisher, C. C., Zhang, M., Saucerman, J. J., Goodyear, L. J., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00520-9 · Cited by 529 · see citing works
Exercise Promotes Healthy Aging of Skeletal Muscle
Cartee, G. D., Hepple, R. T., Bamman, M. M., & Zierath, J. R. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.007 · Cited by 483 · see citing works
Li, Y., & Chen, Y. (2019) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-15-0602-4_4 · Cited by 431 · see citing works
Metformin Improves Mitochondrial Respiratory Activity through Activation of AMPK
Wang, Y., An, H., Liu, T., Qin, C., Sesaki, H., Guo, S., Radovick, S., Hussain, M., Maheshwari, A., Wondisford, F. E., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.09.070 · Cited by 432 · see citing works
Wang, Q., Zhang, M., Torres, G., Wu, S., Ouyang, C., Xie, Z., & Zou, M.-H. (2017) · Diabetes · doi:10.2337/db16-0915 · Cited by 370 · see citing works
Dietary Restriction and AMPK Increase Lifespan via Mitochondrial Network and Peroxisome Remodeling
Weir, H. J., Yao, P., Huynh, F. K., Escoubas, C. C., Goncalves, R. L., Burkewitz, K., Laboy, R., Hirschey, M. D., & Mair, W. B. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.09.024 · Cited by 372 · see citing works
Exercise and mitochondrial health
Memme, J. M., Erlich, A. T., Phukan, G., & Hood, D. A. (2021) · The Journal of Physiology · doi:10.1113/jp278853 · Cited by 343 · see citing works
Cooperative and independent roles of the Drp1 adaptors Mff, MiD49 and MiD51 in mitochondrial fission
Osellame, L. D., Singh, A. P., Stroud, D. A., Palmer, C. S., Stojanovski, D., Ramachandran, R., & Ryan, M. T. (2016) · Journal of Cell Science · doi:10.1242/jcs.185165 · Cited by 336 · see citing works
Wang, B., Nie, J., Wu, L., Hu, Y., Wen, Z., Dong, L., Zou, M.-H., Chen, C., & Wang, D. W. (2018) · Circulation Research · doi:10.1161/circresaha.117.312317 · Cited by 334 · see citing works
Exercise Metabolism and Adaptation in Skeletal Muscle
Smith, J. A. B., Murach, K. A., Dyar, K. A., & Zierath, J. R. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00606-x · Cited by 342 · see citing works
AMPK, Mitochondrial Function, and Cardiovascular Disease
Wu, S., & Zou, M.-H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144987 · Cited by 286 · see citing works
Marin, T. L., Gongol, B., Zhang, F., Martin, M., Johnson, D. A., Xiao, H., Wang, Y., Subramaniam, S., Chien, S., & Shyy, J. Y.-J. (2017) · Science Signaling · doi:10.1126/scisignal.aaf7478 · Cited by 257 · see citing works
The constriction and scission machineries involved in mitochondrial fission
Kraus, F., & Ryan, M. T. (2017) · Journal of Cell Science · doi:10.1242/jcs.199562 · Cited by 244 · see citing works
Emerging Role of cAMP/AMPK Signaling
Aslam, M., & Ladilov, Y. (2022) · Cells · doi:10.3390/cells11020308 · Cited by 241 · see citing works
Grassi, D., Howard, S., Zhou, M., Diaz-Perez, N., Urban, N. T., Guerrero-Given, D., Kamasawa, N., Volpicelli-Daley, L. A., LoGrasso, P., & Lasmézas, C. I. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1713849115 · Cited by 228 · see citing works
Hong, X., Isern, J., Campanario, S., Perdiguero, E., Ramírez-Pardo, I., Segalés, J., Hernansanz-Agustín, P., Curtabbi, A., Deryagin, O., Pollán, A., et al. (2022) · Cell stem cell · doi:10.1016/j.stem.2022.07.009 · Cited by 213 · see citing works
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works
Li, A., Zhang, S., Li, J., Liu, K., Huang, F., & Liu, B. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.06.008 · Cited by 197 · see citing works
The RNA-Binding Protein PUM2 Impairs Mitochondrial Dynamics and Mitophagy During Aging
D’Amico, D., Mottis, A., Potenza, F., Sorrentino, V., Li, H., Romani, M., Lemos, V., Schoonjans, K., Zamboni, N., Knott, G., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.11.034 · Cited by 159 · see citing works
Unravelling the mechanisms regulating muscle mitochondrial biogenesis
Hood, D. A., Tryon, L. D., Carter, H. N., Kim, Y., & Chen, C. C. W. (2016) · Biochemical Journal · doi:10.1042/bcj20160009 · Cited by 159 · see citing works
Exercise and mitochondrial dynamics: keeping in shape with ROS and AMPK
Trewin, A., Berry, B., & Wojtovich, A. (2018) · Antioxidants · doi:10.3390/antiox7010007 · Cited by 129 · see citing works
Qureshi, R., Picon-Ruiz, M., Aurrekoetxea-Rodriguez, I., Nunes de Paiva, V., D’Amico, M., Yoon, H., Radhakrishnan, R., Morata-Tarifa, C., Ince, T., Lippman, M. E., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.05.008 · Cited by 127 · see citing works
Zhang, Y., Recouvreux, M. V., Jung, M., Galenkamp, K. M. O., Li, Y., Zagnitko, O., Scott, D. A., Lowy, A. M., & Commisso, C. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-0119 · Cited by 116 · see citing works
Circadian Rhythms and Mitochondria: Connecting the Dots
Sardon Puig, L., Valera-Alberni, M., Cantó, C., & Pillon, N. J. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00452 · Cited by 113 · see citing works
Ahuja, P., Ng, C. F., Pang, B. P. S., Chan, W. S., Tse, M. C. L., Bi, X., Kwan, H.-L. R., Brobst, D., Herlea-Pana, O., Yang, X., et al. (2022) · Autophagy · doi:10.1080/15548627.2021.1985257 · Cited by 116 · see citing works
The mitochondrial permeability transition: Nexus of aging, disease and longevity
Rottenberg, H., & Hoek, J. B. (2021) · Cells · doi:10.3390/cells10010079 · Cited by 94 · see citing works
Little, A. C., Kovalenko, I., Goo, L. E., Hong, H. S., Kerk, S. A., Yates, J. A., Purohit, V., Lombard, D. B., Merajver, S. D., & Lyssiotis, C. A. (2020) · Communications Biology · doi:10.1038/s42003-020-0988-z · Cited by 88 · see citing works
Novel Insights into the Anti-Aging Role of Mitophagy
(2018) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2018.05.005 · Cited by 56 · see citing works
Shah, S. Z. A., Zhao, D., Hussain, T., & Yang, L. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.09.004 · Cited by 55 · see citing works
Liu, H., Xiang, H., Zhao, S., Sang, H., Lv, F., Chen, R., Shu, Z., Chen, A. F., Chen, S., & Lu, H. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13975 · Cited by 52 · see citing works
Kalita, B., Utkin, Y. N., & Mukherjee, A. K. (2022) · Toxins · doi:10.3390/toxins14120839 · Cited by 50 · see citing works
Acylated Ghrelin as a Multi-Targeted Therapy for Alzheimer's and Parkinson's Disease
Reich, N., & Hölscher, C. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.614828 · Cited by 48 · see citing works
“This is in line with the Mfn2-upregulating and Drp1-impeding function of PGC-1α (Peng et al., 2017), suggesting that AG stimulates the AMPK/PGC-1α axis to ameliorate mitochondrial fragmentation in response to cellular stress (Sirago et al., 2017).”
BackgroundInfluentialWang, Q., Wu, S., Zhu, H., Ding, Y., Dai, X., Ouyang, C., Han, Y.-M., Xie, Z., & Zou, M.-H. (2017) · Autophagy · doi:10.1080/15548627.2016.1263776 · Cited by 45 · see citing works
The link between Mitochondria and Sarcopenia
Kamarulzaman, N. T., & Makpol, S. (2025) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-024-01062-7 · Cited by 33 · see citing works
- Authors
- Toyama, E. Q., Herzig, S., Courchet, J., Lewis, T. L., Losón, O. C., Hellberg, K., Young, N. P., Chen, H., Polleux, F., Chan, D. C., & Shaw, R. J.
- Affiliations
- Salk Institute for Biological Studies (US)
- Mortimer B. Zuckerman Mind Brain Behavior Institute (US)
- California Institute of Technology (US)
- Corresponding author
- Toyama, Erin Quan
- Herzig, Sébastien
- Shaw, Reuben J.
- ORCID
- Venue
- Science
- Published
- 2016-01-15
- Volume
- 351
- Issue
- 6270
- Pages
- 275-281
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC4852862
- OpenAlex
- W2269336718
- Cited by
- 1,085
- References
- 41
- Citations by year
- 2026: 87 · 2025: 98 · 2024: 113 · 2023: 93 · 2022: 110 · 2021: 141 · 2020: 120 · 2019: 98 · 2018: 96 · 2017: 82 · 2016: 46
- FWCI
- 55.97
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- HAL (submittedVersion)
- Funders
- NIH (R01DK080425, R01CA172229, P01 CA120964, R01GM062967, R01GM110039, R01NS089456, K99NS091526)
- Leona M. and Harry B. Helmsley Charitable Trust (2012-PG-MED002)
- American Cancer Society (122123-PF-12-029-01-TBE, 123016-PF-PF-12-191-01-TBE)
- European Molecular Biology Organization (EMBO) (ALTF 1101-2013)
- George E. Hewitt Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- AMPK, mitochondrial fission, mitochondrial fragmentation, mitochondrial fusion, energy stress, electron transport chain inhibitors, mitochondrial DNA mutations, mitochondrial fission factor, Drp1, phosphorylation, energy sensing
- MeSH terms
- Adenosine Monophosphate, Cytoplasm, Dactinomycin, Energy Metabolism, Enzyme Activation, Humans, Microtubule-Associated Proteins, Mitochondria, Molecular Sequence Data, Rotenone, Stress, Physiological, GTP Phosphohydrolases, Amino Acid Motifs, Mitochondrial Proteins, Dynamins, Cell Line, Tumor, AMP-Activated Protein Kinases, Mitochondrial Dynamics
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