Muscle-generated BDNF (brain derived neurotrophic factor) maintains mitochondrial quality control in female mice
Open accessAbstract
Mitochondrial remodeling is dysregulated in metabolic diseases but the underlying mechanism is not fully understood. We report here that BDNF (brain derived neurotrophic factor) provokes mitochondrial fission and clearance in skeletal muscle via the PRKAA/AMPK-PINK1-PRKN/Parkin and PRKAA-DNM1L/DRP1-MFF pathways. Depleting Bdnf expression in myotubes reduced fatty acid-induced mitofission and mitophagy, which was associated with mitochondrial elongation and impaired lipid handling. Muscle-specific bdnf knockout (MBKO) mice displayed defective mitofission and mitophagy, and accumulation of dysfunctional mitochondria in the muscle when they were fed with a high-fat diet (HFD). These animals also have exacerbated body weight gain, increased intramyocellular lipid deposition, reduced energy expenditure, poor metabolic flexibility, and more insulin resistance. In contrast, consuming a BDNF mimetic (7,8-dihydroxyflavone) increased mitochondrial content, and enhanced mitofission and mitophagy in the skeletal muscles. Hence, BDNF is an essential myokine to maintain mitochondrial quality and function, and its repression in obesity might contribute to impaired metabolism.Abbreviations: 7,8-DHF: 7,8-dihydroxyflavone; ACACA/ACC: acetyl Coenzyme A carboxylase alpha; ACAD: acyl-Coenzyme A dehydrogenase family; ACADVL: acyl-Coenzyme A dehydrogenase, very long chain; ACOT: acyl-CoA thioesterase; CAMKK2: calcium/calmodulin-dependent protein kinase kinase 2, beta; BDNF: brain derived neurotrophic factor; BNIP3: BCL2/adenovirus E1B interacting protein 3; BNIP3L/NIX: BCL2/adenovirus E1B interacting protein 3-like; CCL2/MCP-1: chemokine (C-C motif) ligand 2; CCL5: chemokine (C-C motif) ligand 5; CNS: central nervous system; CPT1B: carnitine palmitoyltransferase 1b, muscle; Cpt2: carnitine palmitoyltransferase 2; CREB: cAMP responsive element binding protein; DNM1L/DRP1: dynamin 1-like; E2: estrogen; EHHADH: enoyl-CoenzymeA hydratase/3-hydroxyacyl CoenzymeA dehydrogenase; ESR1/ER-alpha: estrogen receptor 1 (alpha); FA: fatty acid; FAO: fatty acid oxidation; FCCP: carbonyl cyanide-4-(trifluoromethoxy)phenylhydrazone; FFA: free fatty acids; FGF21: fibroblast growth factor 21; FUNDC1: FUN14 domain containing 1; HADHA: hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha; HFD: high-fat diet; iWAT: inguinal white adipose tissues; MAP1LC3A/LC3A: microtubule-associated protein 1 light chain 3 alpha; MBKO; muscle-specific bdnf knockout; IL6/IL-6: interleukin 6; MCEE: methylmalonyl CoA epimerase; MFF: mitochondrial fission factor; NTRK2/TRKB: neurotrophic tyrosine kinase, receptor, type 2; OPTN: optineurin; PA: palmitic acid; PARL: presenilin associated, rhomboid-like; PDH: pyruvate dehydrogenase; PINK1: PTEN induced putative kinase 1; PPARGC1A/PGC-1α: peroxisome proliferative activated receptor, gamma, coactivator 1 alpha; PRKAA/AMPK: protein kinase, AMP-activated, alpha 2 catalytic subunit; ROS: reactive oxygen species; TBK1: TANK-binding kinase 1; TG: triacylglycerides; TNF/TNFα: tumor necrosis factor; TOMM20: translocase of outer mitochondrial membrane 20; ULK1: unc-51 like kinase 1
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?
Muscle-derived BDNF serves as a new regulator of mitochondrial remodeling in skeletal muscle in response to lipid overload.
“Muscle-derived BDNF serves as a new regulator of mitochondrial remodeling in skeletal muscle in response to lipid overload [108].”
From Exerkines and Sarcopenia: Unveiling the Mechanism Behind Exercise-Induced Mitochondrial Homeostasis (2025) · cites this paper as [108]
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
Wu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139 · see citing works
PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944 · see citing works
PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835 · 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
Koves, T. R., Ussher, J. R., Noland, R. C., Slentz, D., Mosedale, M., Ilkayeva, O., Bain, J., Stevens, R., Dyck, J. R. B., Newgard, C. B., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.013 · Cited by 1,990 · see citing works
Bhatti, J. S., Bhatti, G. K., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.010 · Cited by 1,655 · see citing works
LKB1 is the upstream kinase in the AMP-activated protein kinase cascade
Woods, A., Johnstone, S. R., Dickerson, K., Leiper, F. C., Fryer, L. G. D., Neumann, D., Schlattner, U., Wallimann, T., Carlson, M., & Carling, D. (2003) · Current Biology · doi:10.1016/j.cub.2003.10.031 · Cited by 1,650 · see citing works
Hawley, S. A., Pan, D. A., Mustard, K. J., Ross, L., Bain, J., Edelman, A. M., Frenguelli, B. G., & Hardie, D. G. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.009 · Cited by 1,589 · see citing works
Mechanisms of mitophagy in cellular homeostasis, physiology and pathology
Palikaras, K., Lionaki, E., & Tavernarakis, N. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0176-2 · Cited by 1,505 · see citing works
Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
Jin, S. M., Lazarou, M., Wang, C., Kane, L. A., Narendra, D. P., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008084 · Cited by 1,375 · see citing works
BDNF: A Key Factor with Multipotent Impact on Brain Signaling and Synaptic Plasticity
Kowiański, P., Lietzau, G., Czuba, E., Waśkow, M., Steliga, A., & Moryś, J. (2018) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-017-0510-4 · Cited by 1,359 · see citing works
OPA1 requires mitofusin 1 to promote mitochondrial fusion
Cipolat, S., de Brito, O. M., Dal Zilio, B., & Scorrano, L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407043101 · Cited by 1,300 · see citing works
PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity
Kane, L. A., Lazarou, M., Fogel, A. I., Li, Y., Yamano, K., Sarraf, S. A., Banerjee, S., & Youle, R. J. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201402104 · Cited by 1,298 · see citing works
Metabolic regulation of mitochondrial dynamics
Mishra, P., & Chan, D. C. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201511036 · Cited by 1,096 · see citing works
AMP-activated protein kinase mediates mitochondrial fission in response to energy stress
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., et al. (2016) · Science · doi:10.1126/science.aab4138 · Cited by 1,085 · see citing works
Zong, H., Ren, J. M., Young, L. H., Pypaert, M., Mu, J., Birnbaum, M. J., & Shulman, G. I. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252625599 · Cited by 1,036 · see citing works
Kondapalli, C., Kazlauskaite, A., Zhang, N., Woodroof, H. I., Campbell, D. G., Gourlay, R., Burchell, L., Walden, H., Macartney, T. J., Deak, M., et al. (2012) · Open Biology · doi:10.1098/rsob.120080 · Cited by 940 · see citing works
Chang, C., & Blackstone, C. D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700083200 · Cited by 792 · see citing works
The Interplay Between Mitochondrial Dynamics and Mitophagy
Twig, G., & Shirihai, O. S. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3779 · Cited by 778 · see citing works
Matthews, V. B., Åström, M.-B., Chan, M. H. S., Bruce, C. R., Krabbe, K. S., Prelovsek, O., Åkerström, T., Yfanti, C., Broholm, C., Mortensen, O. H., et al. (2009) · Diabetologia · doi:10.1007/s00125-009-1364-1 · Cited by 722 · see citing works
Building and decoding ubiquitin chains for mitophagy
Harper, J. W., Ordureau, A., & Heo, J. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.129 · Cited by 668 · see citing works
Mitochondrial dynamics in type 2 diabetes: Pathophysiological implications
Rovira-Llopis, S., Bañuls, C., Diaz-Morales, N., Hernandez-Mijares, A., Rocha, M., & Victor, V. M. (2017) · Redox Biology · doi:10.1016/j.redox.2017.01.013 · Cited by 657 · see citing works
Jheng, H.-F., Tsai, P.-J., Guo, S.-M., Kuo, L.-H., Chang, C.-S., Su, I.-J., Chang, C.-R., & Tsai, Y.-S. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.05603-11 · Cited by 650 · 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
Shiba-Fukushima, K., Imai, Y., Yoshida, S., Ishihama, Y., Kanao, T., Sato, S., & Hattori, N. (2012) · Scientific Reports · doi:10.1038/srep01002 · Cited by 577 · see citing works
Endogenous Drp1 Mediates Mitochondrial Autophagy and Protects the Heart Against Energy Stress
Ikeda, Y., Shirakabe, A., Maejima, Y., Zhai, P., Sciarretta, S., Toli, J., Nomura, M., Mihara, K., Egashira, K., Ohishi, M., et al. (2015) · Circulation Research · doi:10.1161/circresaha.116.303356 · Cited by 571 · see citing works
Monteggia, L. M., Luikart, B., Barrot, M., Theobold, D., Malkovska, I., Nef, S., Parada, L. F., & Nestler, E. J. (2007) · Biological Psychiatry · doi:10.1016/j.biopsych.2006.03.021 · Cited by 502 · see citing works
Suomalainen, A., Elo, J. M., Pietiläinen, K. H., Hakonen, A. H., Sevastianova, K., Korpela, M., Isohanni, P., Marjavaara, S. K., Tyni, T., Kiuru-Enari, S., et al. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70155-7 · Cited by 427 · see citing works
Park, H. R., Park, M.-K., Choi, J., Park, K.-Y., Chung, H. Y., & Lee, J. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.07.046 · Cited by 375 · see citing works
Nilsson, M., Vandenput, L., Tivesten, Å., Norlén, A., Lagerquist, M. K., Windahl, S. H., Börjesson, A., Farman, H. H., POUTANEN, M. H., Benrick, A., et al. (2015) · Endocrinology · doi:10.1210/en.2014-1890 · Cited by 337 · 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
Ribas, V., Drew, B. G., Zhou, Z., Phun, J., Kalajian, N. Y., Soleymani, T., Daraei, P., Widjaja, K., Wanagat, J., de Aguiar Vallim, T. Q., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aad3815 · Cited by 259 · 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
Mitochondrial quality control: An integrated network of pathways
Fischer, F., Hamann, A., & Osiewacz, H. D. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.02.004 · Cited by 248 · see citing works
High-Fat Diet Induces Hepatic Insulin Resistance and Impairment of Synaptic Plasticity
Liu, Z., Patil, I., Jiang, T., Sancheti, H., Walsh, J. P., Stiles, B. L., Yin, F., & Cadenas, E. (2015) · PLoS ONE · doi:10.1371/journal.pone.0128274 · Cited by 236 · see citing works
Quantitation of "autophagic flux" in mature skeletal muscle
Ju, J.-S., Varadhachary, A. S., Miller, S. E., & Weihl, C. C. (2010) · Autophagy · doi:10.4161/auto.6.7.12785 · Cited by 229 · see citing works
Evolving and Expanding the Roles of Mitophagy as a Homeostatic and Pathogenic Process
Gustafsson, Å. B., & Dorn, G. W. (2018) · Physiological Reviews · doi:10.1152/physrev.00005.2018 · Cited by 229 · see citing works
Hyperinsulinemic–Euglycemic Clamp to Assess Insulin Sensitivity In Vivo
Kim, J. K. (2009) · Methods in molecular biology · doi:10.1007/978-1-59745-448-3_15 · Cited by 215 · see citing works
Self-citationFan, Y., Liu, Y., Xue, K., Gu, G., Fan, W., Xu, Y., & Ding, Z. (2015) · PLoS ONE · doi:10.1371/journal.pone.0120775 · Cited by 188 · see citing works
Gibbs, R. B. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01880-6 · Cited by 186 · see citing works
Wu, W., Xu, H. Y., Wang, Z., Mao, Y. J., Yuan, L., Luo, W., Cui, Z., Cui, T., Wang, X. L., & Shen, Y. H. (2015) · PLoS ONE · doi:10.1371/journal.pone.0132499 · Cited by 181 · see citing works
Clow, C., & Jasmin, B. J. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-02-0154 · Cited by 175 · see citing works
AMPK/ULK1-mediated phosphorylation of Parkin ACT domain mediates an early step in mitophagy
Hung, C., Lombardo, P. S., Malik, N., Brun, S. N., Hellberg, K., Nostrand, J. L. V., Garcia, D., Baumgart, J. T., Diffenderfer, K. E., Asara, J. M., et al. (2021) · Science Advances · doi:10.1126/sciadv.abg4544 · Cited by 169 · see citing works
Seabright, A. P., Fine, N. H. F., Barlow, J. P., Lord, S. O., Musa, I., Gray, A., Bryant, J. A., Banzhaf, M., Lavery, G. G., Hardie, D. G., et al. (2020) · The FASEB Journal · doi:10.1096/fj.201903051r · Cited by 168 · see citing works
Li, S., Liu, C., Li, N., Hao, T., Han, T., HILL, D. E., Vidal, M., & Lin, J. D. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.06.013 · Cited by 167 · see citing works
Discrete BDNF Neurons in the Paraventricular Hypothalamus Control Feeding and Energy Expenditure
An, J. J., Liao, G., Kinney, C. E., Sahibzada, N., & Xu, B. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.008 · Cited by 164 · see citing works
BDNF is a mediator of glycolytic fiber-type specification in mouse skeletal muscle
Delezie, J., Weihrauch, M., Maier, G., Tejero, R., Ham, D. J., Gill, J. F., Karrer-Cardel, B., Rüegg, M. A., Tabares, L., & Handschin, C. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1900544116 · Cited by 141 · see citing works
Automatic Morphological Subtyping Reveals New Roles of Caspases in Mitochondrial Dynamics
Peng, J.-Y., Lin, C., Chen, Y.-J., Kao, L., Liu, Y., Chou, C.-C., Huang, Y.-H., Chang, F., Wu, Y., Tsai, Y., et al. (2011) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002212 · Cited by 127 · see citing works
Fortin, D. A., Srivastava, T., Dwarakanath, D., Pierre, P., Nygaard, S., Derkach, V. A., & Soderling, T. R. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.6034-11.2012 · Cited by 120 · see citing works
Axelrod, C. L., Fealy, C. E., Mulya, A., & Kirwan, J. P. (2018) · Acta Physiologica · doi:10.1111/apha.13216 · Cited by 120 · see citing works
Sebori, R., Kuno, A., Hosoda, R., Hayashi, T., & Horio, Y. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/9179270 · Cited by 113 · see citing works
Novel metabolic role for BDNF in pancreatic β-cell insulin secretion
Fulgenzi, G., Hong, Z., Tomassoni‐Ardori, F., Barella, L. F., Becker, J., Barrick, C. A., Swing, D. A., Yanpallewar, S. U., Croix, B. S., Wess, J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15833-5 · Cited by 111 · see citing works
Miwa, S., Lawless, C., & von Zglinicki, T. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2008.00426.x · Cited by 109 · see citing works
Melatonin prevents mitochondrial dysfunction and insulin resistance in rat skeletal muscle
Teodoro, B. G., Baraldi, F. G., Sampaio, I. H., Bomfim, L. H. M., Queiroz, A. L., Passos, M. A., Carneiro, E. M., Alberici, L. C., Gomis, R., Amaral, F. G., et al. (2014) · Journal of Pineal Research · doi:10.1111/jpi.12157 · Cited by 106 · see citing works
Su, B., Ji, Y.-S., Sun, X., Liu, X., & Chen, Z.-Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.526129 · Cited by 99 · see citing works
Muscle-generated BDNF is a sexually dimorphic myokine that controls metabolic flexibility
Yang, X., Brobst, D., Chan, W. S., Tse, M. C. L., Herlea-Pana, O., Ahuja, P., Bi, X., Zaw, A. M., Kwong, Z. S. W., Jia, W.-H., et al. (2019) · Science Signaling · doi:10.1126/scisignal.aau1468 · Cited by 99 · see citing works
Self-citationIuso, A., Repp, B. M., Biagosch, C., Terrile, C., & Prokisch, H. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6824-4_13 · Cited by 94 · see citing works
Yamaguchi, O., Murakawa, T., Nishida, K., & Otsu, K. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.03.010 · Cited by 84 · see citing works
McCoy, C. E., Carpenter, S., Pålsson-McDermott, E. M., Gearing, L. J., & O'Neill, L. A. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709731200 · Cited by 82 · see citing works
Gabhann, J. N., Higgs, R., Brennan, K., Thomas, W., Damen, J. E., Ben Larbi, N., Krystal, G., & Jefferies, C. A. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0902589 · Cited by 81 · see citing works
Blood BDNF Level Is Gender Specific in Severe Depression
Kreinin, A., Lisson, S., Nesher, E., Schneider, J., Bergman, J., Farhat, K., Farah, J., Lejbkowicz, F., Yadid, G., Raskin, L., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0127643 · Cited by 76 · see citing works
Jeanblanc, J., Logrip, M. L., Janak, P. H., & Dorit Ron, A. (2012) · European Journal of Neuroscience · doi:10.1111/ejn.12067 · Cited by 72 · see citing works
TBK1 (TANK-binding kinase 1)-mediated regulation of autophagy in health and disease
Herhaus, L. (2021) · Matrix Biology · doi:10.1016/j.matbio.2021.01.004 · Cited by 72 · see citing works
Bdnf expression in rat skeletal muscle after acute or repeated exercise.
Cuppini, R., Sartini, S., Agostini, D., Guescini, M., Ambrogini, P., Betti, M., Bertini, L., Vallasciani, M., & Stocchi, V. (2007) · PubMed · doi:10.4449/aib.v145i2.868 · Cited by 63 · see citing works
Wood, J., Tse, M. C. L., Yang, X., Brobst, D. E., Liu, Z., Pang, B. P. S., Chan, W. S., Zaw, A. M., Chow, B., Ye, K., et al. (2018) · Metabolism · doi:10.1016/j.metabol.2018.06.007 · Cited by 58 · see citing works
Self-citationBoutagy, N. E., Rogers, G. W., Pyne, E. S., Ali, M. M., Hulver, M. W., & Frisard, M. I. (2015) · Journal of Visualized Experiments · doi:10.3791/53216 · Cited by 53 · see citing works
Wang, S., Kandadi, M. R., & Ren, J. T. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.08.011 · Cited by 52 · see citing works
Wang, T., Zhu, Q., Cao, B., Yuan, Y., Wen, S., & Liu, Z. (2020) · Cell Proliferation · doi:10.1111/cpr.12817 · Cited by 46 · see citing works
Teillon, S., Calderon, G. A., & Rios, M. (2010) · Journal of Endocrinology · doi:10.1677/joe-09-0405 · Cited by 43 · see citing works
Kumar, D., Dwivedi, D. K., Lahkar, M., & Jangra, A. (2019) · Pharmacological Reports · doi:10.1016/j.pharep.2019.07.002 · Cited by 41 · see citing works
Huang, Y., Huang, C., Zhang, Q., Wu, W., & Sun, J. (2020) · Journal of Neurology · doi:10.1007/s00415-020-10299-3 · Cited by 41 · see citing works
Effect of brain-derived neurotrophic factor (BDNF) on hepatocyte metabolism
Genzer, Y., Chapnik, N., & Froy, O. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.05.008 · Cited by 40 · see citing works
Overweight in the Elderly Induces a Switch in Energy Metabolism that Undermines Muscle Integrity
Potes, Y., Pérez-Martínez, Z., Bermejo-Millo, J. C., Rubio‐González, A., Fernández, M. F., Bermúdez, M., Arche-Coto, J. M., Solano, J. J., Boga, J. A., Oliván, M., et al. (2018) · Aging and Disease · doi:10.14336/ad.2018.0430 · Cited by 39 · see citing works
Pandey, S. N., Kwatra, M., Dwivedi, D. K., Choubey, P., Lahkar, M., & Jangra, A. (2020) · Psychopharmacology · doi:10.1007/s00213-020-05502-2 · Cited by 37 · see citing works
Camerino, C., Conte, E., Cannone, M., Caloiero, R., Fonzino, A., & Tricarico, D. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00456 · Cited by 36 · see citing works
Gundersen, A. E., Kugler, B. A., McDonald, P. M., Veraksa, A. N., Houmard, J. A., & Zou, K. (2019) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2019-0208 · Cited by 34 · see citing works
Zhao, Z., Fan, X., Gu, Y., Han, J., Jia, Y., Ye, K., & Zhang, Y. Q. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101149 · Cited by 27 · see citing works
Self-citationEXPRESSION OF CONCERN: Mitophagy protects against statin‐mediated skeletal muscle toxicity
Ramesh, I., Campos, J. C., Lee, P., Song, Y., Hernandez, G., Sin, J., Tucker, K. C., Saadaeijahromi, H., Gurney, M., Ferreira, J. C. B., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201900807rr · Cited by 17 · see citing works
Hogan, N. L., Jaehne, E. J., Bak, S., Djouma, E., & van den Buuse, M. (2020) · Behavioural Brain Research · doi:10.1016/j.bbr.2020.113090 · Cited by 14 · see citing works
Wahwah, N., Kras, K. A., Roust, L. R., & Katsanos, C. S. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00463.2019 · Cited by 13 · see citing works
Zhang, Y., Zhang, S.-W., Khandekar, N., Shi-fei, T., Yang, H.-Q., Wang, W., Huang, X., Song, Z.-Y., & Lin, S. (2016) · Endocrine · doi:10.1007/s12020-016-1197-x · Cited by 11 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- Ramesh M, Campos JC, Lee P, et al. Mitophagy protects against statin-mediated skeletal muscle toxicity. FASEB J. 2019;33 (11):11857-11869.
Cited by
Sorted by citations
TrkB/BDNF signaling pathway and its small molecular agonists in CNS injury
Wang, Y., Liang, J., Xu, B., Yang, J., Wu, Z., & Cheng, L. (2024) · Life Sciences · doi:10.1016/j.lfs.2023.122282 · Cited by 152 · see citing works
Myokines: Metabolic regulation in obesity and type 2 diabetes
Chen, Z.-T., Weng, Z.-X., Lin, J. D., & Meng, Z.-X. (2024) · Life Metabolism · doi:10.1093/lifemeta/loae006 · Cited by 58 · see citing works
Exerkines and Sarcopenia: Unveiling the Mechanism Behind Exercise-Induced Mitochondrial Homeostasis
Wang, J., Jia, D., Zhang, Z., & Wang, D. (2025) · Metabolites · doi:10.3390/metabo15010059 · Cited by 23 · see citing works
Study on the comorbid mechanisms of sarcopenia and late-life depression
Wu, J., Tang, J., Huang, D., Wang, Y., Zhou, E., Ru, Q., Xu, G., Chen, L., & Wu, Y. (2025) · Behavioural Brain Research · doi:10.1016/j.bbr.2025.115538 · Cited by 12 · see citing works
- Authors
- 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., Du, G., Saengnipanthkul, S., Noh, H. L., Jiao, B., Kim, J. K., Lee, C. W., Ye, K., & Chan, C. B.
- Affiliations
- University of Hong Kong (HK)
- University of Oklahoma Health Sciences Center (US)
- Department of Physiology, The University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA
- Chinese Academy of Medical Sciences & Peking Union Medical College (CN)
- University of Massachusetts Chan Medical School (US)
- Kunming Institute of Zoology (CN)
- Emory University (US)
- Corresponding author
- Chan, Chi Bun
- ORCID
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2021-10-25
- Volume
- 18
- Issue
- 6
- Pages
- 1367-1384
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- PMC
- PMC9225428
- OpenAlex
- W3208384640
- Cited by
- 116
- References
- 81
- Citations by year
- 2026: 25 · 2025: 34 · 2024: 30 · 2023: 15 · 2022: 10 · 2021: 2
- FWCI
- 4.47
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Autophagy (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Hong Kong Government Research Grant Council to CBC (GRF17113817)
- Hong Kong Medical Research Fund (HMRF6171836)
- CAMS Initiative for Innovative Medicine (CAMS-I2M 2016-I2M-3007)
- National Major Science and Technology Projects of China (2018ZX09711001012, 2018ZX09711001003-005)
- NIH grant (5U2C-DK093000)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- brain-derived neurotrophic factor, mitochondrial quality control, mitophagy, mitochondrial fission, skeletal muscle, myokines, AMPK, PINK1, Parkin, Drp1, high-fat diet, obesity, insulin resistance, 7,8-dihydroxyflavone, lipid metabolism, energy expenditure, metabolic flexibility
- MeSH terms
- Animals, Autophagy, Fatty Acids, Female, Mitochondria, Muscle, Muscle, Skeletal, Brain-Derived Neurotrophic Factor, Mice, 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
