Dihydromyricetin attenuates palmitic acid-induced oxidative stress by promoting autophagy via SIRT3-ATG4B signaling in hepatocytes
Open accessAbstract
Background: Oxidative stress in hepatocytes was important pathogenesis of nonalcoholic steatohepatitis (NASH). Autophagy was a cellular process that can remove damaged organelles under oxidative stress, and thus presented a potential therapeutic target against NASH. This work aimed to investigate whether autophagy was participated in the protective effects of dihydromyricetin (DHM) on palmitic acid (PA)-induced oxidative stress in hepatocytes and the underlying mechanism. Methods: HepG2 and HHL-5 cell lines were pretreated with DHM (20 μM) for 2 h, followed by PA (0.2 mM) treatment for 16 h. The oxidative stress was assessed by the quantification of intracellular reactive oxygen species (ROS), mitochondrial ROS (mtROS), mitochondrial membrane potential (MMP) and mitochondrial ultrastructural analyses. The protein expressions of SIRT3, LC3I/II, P62 and ATG4B, as well as the acetylation of AGT4B were determined by western blotting using HepG2 and HepG2/ATG4B± cells with heterozygous knockout of ATG4B. Results: Exposure to PA resulted in increased intracellular ROS and mtROS, decreased MMP and aggravated mitochondrial injury in HepG2 cells, which were notably attenuated by DHM treatment. DHM-induced inhibition of oxidative stress was associated with the induction of autophagy, characterized by upregulated ATG4B and LC3 II as well as downregulated P62 levels. Furthermore, the inhibitory effects of DHM on PA-induced autophagy arrest and oxidative stress were eliminated when pretreated with a SIRT3 inhibitor 3-TYP or conducted in HepG2/ATG4B± cells, suggesting that SIRT3 and ATG4B were involved in DHM-induced benefits. Moreover, DHM treatment increased the protein expression of SIRT3 and SIRT3-dependent deacetylation of ATG4B in HepG2 cells. Conclusion: Our results demonstrated that DHM attenuated PA-induced oxidative stress in hepatocytes through induction of autophagy, which was mediated through the increased expression of SIRT3 and SIRT3-mediated ATG4B deacetylation following DHM treatment.
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?
ROS accumulation triggers damaging cascades: a decrease in mitochondrial membrane potential, activation of caspases 3/7, apoptosis, and ER stress and inflammation via NF-κB.
“ROS accumulation triggers damaging cascades: a decrease in mitochondrial membrane potential, activation of caspases 3/7, apoptosis, and ER stress and inflammation via NF-κB [90,152,153,154,155].”
From The HepG2 Cell Line as a Model for Studying Metabolic Dysfunction-Associated Steatotic Liver Disease (2026) · cites this paper as [152]
The Introduction (page not provided) links increased ROS and oxidative stress with reduced mitochondrial membrane potential, hepatic inflammation, and hepatocyte death. It does not identify caspase-3/7 activation, apoptosis, or NF-κB as steps in that cascade. It describes ER stress as a contributor to palmitic-acid-induced oxidative stress, rather than a consequence of ROS accumulation. (LLM, conf=0.84)
Experimental — accuracy not yet measured
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
1 retracted
Zhou, H., Du, W., Li, Y., Chen, S., Hu, N., Ma, S., Wang, W., & Ren, J. T. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12450 · Cited by 290 · see citing works
RetractedSteatohepatitis: A tale of two “hits”?
Day, C. P., & James, O. F. W. (1998) · Gastroenterology · doi:10.1016/s0016-5085(98)70599-2 · Cited by 4,285 · see citing works
Autophagy: process and functionPreprint
Mizushima, N. (2007) · Genes & Development · doi:10.1101/gad.1599207 · Cited by 3,967 · see citing works
Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
Scherz‐Shouval, R., Shvets, E., Fass, E., Shorer, H., Gil, L., & Elazar, Z. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601623 · Cited by 2,101 · see citing works
Estes, C., Anstee, Q. M., Arias, M., Bantel, H., Bellentani, S., Caballería, J., Colombo, M., Craxı̀, A., Crespo, J., Day, C. P., et al. (2018) · Journal of Hepatology · doi:10.1016/j.jhep.2018.05.036 · Cited by 1,986 · see citing works
Global epidemiology of NAFLD-related HCC: trends, predictions, risk factors and prevention
Huang, D. Q., El-Serag, H. B., & Loomba, R. (2021) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-020-00381-6 · Cited by 1,855 · see citing works
Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey
Kim, S. C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., Cheng, T., Kho, Y., Xiao, H., Xiao, L., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.026 · Cited by 1,487 · see citing works
A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
Ahn, B.-H., Kim, H.-S., Song, S., Lee, I. H., Liu, J., Vassilopoulos, A., Deng, C.-X., & Finkel, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803790105 · Cited by 1,291 · see citing works
Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
Hallows, W. C., Lee, S., & Denu, J. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604392103 · Cited by 792 · see citing works
Hirschey, M. D., Shimazu, T., Jing, E., Grueter, C. A., Collins, A. M., Aouizerat, B., Stančáková, A., Goetzman, E., Lam, M. M., Schwer, B., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.019 · Cited by 787 · 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
González‐Rodríguez, Á., Mayoral, R., Agra, N., Valdecantos, M. P., Pardo, V., Miquilena-Colina, M. E., Vargas‐Castrillón, J., Iacono, O. L., Corazzari, M., Fimia, G. M., et al. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.162 · Cited by 611 · see citing works
Arroyave-Ospina, J. C., Wu, Z., Geng, Y., & Moshage, H. J. (2021) · Antioxidants · doi:10.3390/antiox10020174 · Cited by 531 · see citing works
Yu, W., Dittenhafer‐Reed, K. E., & Denu, J. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.355206 · Cited by 445 · see citing works
Free Radicals in Cross Talk Between Autophagy and Apoptosis
Kaminskyy, V. O., & Zhivotovsky, B. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5746 · Cited by 409 · see citing works
Oxidative Stress as a Critical Factor in Nonalcoholic Fatty Liver Disease Pathogenesis
Spahis, S., DELVIN, E. E., Borys, J.-M., & Levy, E. H. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6776 · Cited by 386 · see citing works
Oxidative stress and calcium dysregulation by palmitate in type 2 diabetes
Ly, L. D., Xu, S., Choi, S.-K., Ha, C.-M., Thoudam, T., Cha, S.-K., Wiederkehr, A., Wollheim, C. B., Lee, I.-K., & Park, K.-S. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.157 · Cited by 378 · see citing works
Li, R., Xin, T., Li, D., Wang, C., Zhu, H., & Zhou, H. (2018) · Redox Biology · doi:10.1016/j.redox.2018.07.011 · Cited by 353 · see citing works
Self-citationHale, A. N., Ledbetter, D., Gawriluk, T. R., & Rucker, E. B. (2013) · Autophagy · doi:10.4161/auto.24273 · Cited by 336 · see citing works
Sirt3 Impairment and SOD2 Hyperacetylation in Vascular Oxidative Stress and Hypertension
Dikalova, A., Itani, H. A., Nazarewicz, R. R., McMaster, W. G., Flynn, C. R., Uzhachenko, R. V., Fessel, J. P., Gamboa, J. L., Harrison, D. G., & Dikalov, S. (2017) · Circulation Research · doi:10.1161/circresaha.117.310933 · Cited by 317 · see citing works
Sirt3 deficiency exacerbates diabetic cardiac dysfunction: Role of Foxo3A-Parkin-mediated mitophagy
Yu, W., Gao, B., Li, N., Wang, J., Qiu, C., Zhang, G., Liu, M., Zhang, R., Li, C., Ji, G., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.10.021 · Cited by 275 · see citing works
Borrelli, A., Bonelli, P., Tuccillo, F. M., Goldfine, I. D., Evans, J. L., Buonaguro, F. M., & Mancini, A. (2018) · Redox Biology · doi:10.1016/j.redox.2018.01.009 · Cited by 269 · see citing works
Li, M., Hou, Y., Wang, J., Chen, X., Shao, Z.-M., & Yin, X. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.199059 · Cited by 246 · see citing works
Redundancy of human ATG4 protease isoforms in autophagy and LC3/GABARAP processing revealed in cells
Agrotis, A., Pengo, N., Burden, J. J., & Ketteler, R. (2019) · Autophagy · doi:10.1080/15548627.2019.1569925 · Cited by 239 · see citing works
Chen, S., Zhao, X., Wan, J., Ran, L., Qin, Y., Wang, X., Gao, Y., Shu, F., Zhang, Y., Liu, P., et al. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.05.009 · Cited by 235 · see citing works
Self-citationMitochondria in non-alcoholic fatty liver disease
Simões, I. C. M., Fontes, A., Pinton, P., Zischka, H., & Wieckowski, M. R. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.12.019 · Cited by 234 · see citing works
SIRT3 deregulation is linked to mitochondrial dysfunction in Alzheimer's disease
Lee, J., Kim, Y., Liu, T., Hwang, Y. J., Hyeon, S. J., Im, H., Lee, K., Alvarez, V. E., McKee, A. C., Um, S., et al. (2018) · Aging Cell · doi:10.1111/acel.12679 · Cited by 213 · see citing works
Zhou, X., Chen, M., Zeng, X., Yang, J., Deng, H., Yi, L., & Mt, M. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.530 · Cited by 208 · see citing works
Self-citationSirt3 promotes antimycobacterial defenses by coordinating mitochondrial and autophagic functions
Kim, T. S., Jin, Y. B., Kim, Y. S., Kim, S., Kim, J. K., Lee, H.-M., Suh, H.-W., Choe, J. H., Kim, Y. J., Koo, B.-S., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1582743 · Cited by 172 · see citing works
Zeng, X., Yang, J., Hu, O., Huang, J., Li, R., Chen, M., Zhang, Y., Zhou, X., Zhu, J., Zhang, Q., et al. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7172 · Cited by 163 · see citing works
Self-citationDai, S., Chen, T., Li, X., Yue, K., Luo, P., Yang, L., Zhu, J., Wang, Y., Fei, Z., & Jiang, X. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.04.005 · Cited by 157 · see citing works
Dietary Polyphenols and Non-Alcoholic Fatty Liver Disease
Abenavoli, L., Larussa, T., Corea, A., Procopio, A. C., Boccuto, L., Dallio, M., Federico, A., & Luzza, F. (2021) · Nutrients · doi:10.3390/nu13020494 · Cited by 133 · see citing works
Li, S., Dou, X., Ning, H., Song, Q., Wei, W., Zhang, X., Shen, C., Li, J., Sun, C., & Song, Z. (2017) · Hepatology · doi:10.1002/hep.29229 · Cited by 130 · see citing works
Role of autophagy in the pathophysiology of nonalcoholic fatty liver disease: A controversial issue
Kwanten, W. J. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i23.7325 · Cited by 113 · see citing works
The novel relationship between Sirt3 and autophagy in myocardial ischemia–reperfusion
Zheng, Y., Shi, B., Ma, M., Wu, X., & Lin, X. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27329 · Cited by 107 · see citing works
Shi, L., Zhang, T., Zhou, Y. G., Zeng, X., Ran, L., Zhang, Q., Zhu, J., & Mi, M. (2015) · Endocrine · doi:10.1007/s12020-015-0599-5 · Cited by 105 · see citing works
Self-citationQiu, P., Dong, Y. H., Li, B., Kang, X., Gu, C., Zhu, T., Luo, Y., Pang, M.-X., Du, W., & Ge, W. (2017) · Toxicology Letters · doi:10.1016/j.toxlet.2017.04.009 · Cited by 105 · see citing works
Self-citationAutophagy in non-alcoholic fatty liver disease and alcoholic liver disease
Khambu, B., Yan, S., Huda, N., Liu, G., & Yin, X. (2018) · Liver Research · doi:10.1016/j.livres.2018.09.004 · Cited by 105 · see citing works
Gao, J., Liu, B., NING, Z., Zhao, R., Zhang, A., & Wu, Q. (2009) · Journal of Food Biochemistry · doi:10.1111/j.1745-4514.2009.00253.x · Cited by 94 · see citing works
Upadhyay, K. K., Jadeja, R. N., Vyas, H., Pandya, B. A., Joshi, A., Vohra, A., Thounaojam, M. C., Martin, P. M., Bartoli, M., & Devkar, R. V. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101314 · Cited by 91 · see citing works
Autophagy in chronic liver diseases: the two faces of Janus
Gual, P., Gilgenkrantz, H., & Lotersztajn, S. (2017) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00295.2016 · Cited by 91 · see citing works
Unraveling the roles of Atg4 proteases from autophagy modulation to targeted cancer therapy
Zhang, L., Li, J., Ouyang, L., Liu, B., & Cheng, Y. (2016) · Cancer Letters · doi:10.1016/j.canlet.2016.01.022 · Cited by 89 · see citing works
Regulation of ATG8 membrane association by ATG4 in the parasitic protistToxoplasma gondii
Kong-Hap, M., Mouammine, A., Daher, W., Berry, L., Lebrun, M., Dubremetz, J., & Besteiro, S. (2013) · Autophagy · doi:10.4161/auto.25189 · Cited by 69 · see citing works
Tanida, I., Sou, Y., Minematsu‐Ikeguchi, N., Ueno, T., & Kominami, E. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05260.x · Cited by 68 · see citing works
Mehmood, A., Zhao, L., Wang, Y., Pan, F., Hao, S., Zhang, H., Iftikhar, A., & Usman, M. A. (2021) · Food Research International · doi:10.1016/j.foodres.2021.110180 · Cited by 67 · see citing works
Zeng, Y., Hua, Y. Q., Wang, W., Zhang, H., & Xu, X. L. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.113927 · Cited by 63 · see citing works
Xia, J., Guo, S., Fang, T., Feng, D., Zhang, X., Zhang, Q., Liu, J., Liu, B., Li, M., & Zhu, R. (2014) · Food and Chemical Toxicology · doi:10.1016/j.fct.2014.01.014 · Cited by 60 · see citing works
Zhang, N., Wu, Y., Lyu, X., Li, B., Yan, X., Xiong, H., Li, X., Huang, G., Zeng, Y., Zhang, Y., et al. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.08.039 · Cited by 59 · see citing works
Self-citationBetin, V. M. S., MacVicar, T., Parsons, S. F., Anstee, D. J., & Lane, J. D. (2012) · Autophagy · doi:10.4161/auto.19227 · Cited by 58 · see citing works
HIF‐1α Expression as a Protective Strategy of HepG2 Cells Against Fatty Acid‐Induced Toxicity
Yoo, W., Noh, K. H., Ahn, J. H., Yu, J. H., Seo, J. A., Kim, S. G., Choi, K. M., Baik, S. H., Choi, D. S., Kim, T. W., et al. (2014) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24757 · Cited by 47 · see citing works
Yang, J., Zhou, X., Zeng, X., Hu, O., Yi, L., & Mi, M. (2019) · Nutrition & Metabolism · doi:10.1186/s12986-019-0338-7 · Cited by 27 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Oxidative stress: A common pathological state in a high-risk population for osteoporosis
Zhang, C., Li, H., Li, J., Hu, J., Yang, K., & Tao, L. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114834 · Cited by 219 · see citing works
Xie, J., Zhang, T., Li, P., Wang, D., Liu, T., & Xu, S. (2022) · Drug Design Development and Therapy · doi:10.2147/dddt.s378786 · Cited by 88 · see citing works
Effect of Fluoride on Cytotoxicity Involved in Mitochondrial Dysfunction: A Review of Mechanism
Wei, M., Ye, Y., Ali, M. M., Chamba, Y., Tang, J., & Shang, P. (2022) · Frontiers in Veterinary Science · doi:10.3389/fvets.2022.850771 · Cited by 56 · see citing works
Sirtuins and their influence on autophagy
Baeken, M. W. (2023) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30377 · Cited by 52 · see citing works
Moliterni, C., Vari, F., Schifano, E., Tacconi, S., Stanca, E., Friuli, M., Longo, S., Conte, M., Salvioli, S., Gnocchi, D., et al. (2024) · Journal of Lipid Research · doi:10.1016/j.jlr.2024.100692 · Cited by 35 · see citing works
Dihydromyricetin supplementation improves ethanol-induced lipid accumulation and inflammation
Janilkarn-Urena, I., Idrissova, A., Zhang, M., VanDreal, M., Sanghavi, N., Skinner, S. G., Cheng, S., Zhang, Z., Watanabe, J., Asatryan, L., et al. (2023) · Frontiers in Nutrition · doi:10.3389/fnut.2023.1201007 · Cited by 29 · see citing works
Wang, C., Li, X., Zhang, W., Liu, W., Lv, Z., Gui, R., Li, M., Li, Y., Sun, X., Liu, P., et al. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.02.017 · Cited by 27 · see citing works
Self-citationLiu, Y., Wei, H., & Li, J. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.176155 · Cited by 22 · see citing works
Zhao, X. Q., Zhang, W., Jiang, F., Chen, X., Chen, C., Wang, M., Chen, B., Cannon, R. D., Saffery, R., Han, T.-L., et al. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.06.029 · Cited by 20 · see citing works
McGinnis, C. D., Jennings, E. Q., Harris, P. S., Galligan, J. J., & Fritz, K. S. (2022) · Cells · doi:10.3390/cells11132045 · Cited by 18 · see citing works
Molecular mechanisms and promising role of dihydromyricetin in cardiovascular diseases
Nie, H., Ji, T., Fu, Y., Chen, D., Tang, Z., & Zhang, C. (2022) · Physiological Research · doi:10.33549/physiolres.934915 · Cited by 13 · see citing works
Importance of Autophagy in Mediating Cellular Responses to Iron Overload in Cardiomyocytes
Tam, E., Reno, C., Nguyen, K. D., Cho, S., & Sweeney, G. (2022) · Reviews in Cardiovascular Medicine · doi:10.31083/j.rcm2305167 · Cited by 11 · see citing works
Zhang, K., Li, T., Li, Q., Nie, C., Sun, Y., Xue, L., Wang, Y., Fan, M., Qian, H., Li, Y., et al. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c07073 · Cited by 7 · see citing works
The HepG2 Cell Line as a Model for Studying Metabolic Dysfunction-Associated Steatotic Liver Disease
Kotlyarova, A., Iskrina, A., & Kotlyarov, S. (2026) · International journal of molecular sciences · doi:10.3390/ijms27083399 · Cited by 5 · see citing works
Yang, Y., & Huang, Y. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.178107 · Cited by 5 · see citing works
Mishra, Y., & Kumar, A. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.12.035 · Cited by 5 · see citing works
Zhang, K., Jiang, L., Xue, L., Wang, Y., Sun, Y., Fan, M., Qian, H., Wang, L., & Li, Y. (2024) · Nutrients · doi:10.3390/nu16070978 · Cited by 3 · see citing works
SIRT3, a New Hope in Liver Diseases from Pathogenic Mechanisms to Therapeutic Strategies
Tan, S.-Y., Chen, X., Zhang, R., Liu, P., Wang, J.-P., Wang, T. T., & Xiong, Z.-E. (2024) · Current Pharmaceutical Biotechnology · doi:10.2174/0113892010340592241011052133 · Cited by 2 · see citing works
Salas, S. S., Damba, T., Buist‐Homan, M., & Moshage, H. J. (2025) · Cell Biochemistry and Function · doi:10.1002/cbf.70057 · Cited by 1 · see citing works
Autophagy in age-related liver disease
Palacios, R., Francés, D. E., & Motiño, O. (2025) · Geromedicine · doi:10.70401/geromedicine.2025.0005 · Cited by 2 · see citing works
SIRT3 ameliorates hepatic inflammation, oxidative stress, and fibrosis in HFD- or MCD diet-fed mice
Lv, H., Sun, W., Tian, C., Bian, C., Lu, Z., & Guo, X. (2026) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2026.110276 · Cited by 1 · see citing works
Liao, X., Hao, Y., Wu, M., Liu, H., Jiang, L., Ye, Z.-N., Liao, W., & Deng, H. (2022) · PubMed Central · doi:10.12122/j.issn.1673-4254.2022.04.07
The role of antioxidant supplementation in neuronal disorders
ShamsEldeen, A. M., Ammar, H. I., Al-Hashem, F. H., Alrefaie, Z. A., Aly, M. H., & Hanna, M. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-27333-9.00004-x
- Authors
- Huang, L., Zeng, X., Li, B., Wang, C., Zhou, M., Lang, H., Yi, L., & Mi, M.
- Affiliations
- Army Medical University (CN)
- Chinese People's Liberation Army (CN)
- Corresponding author
- Yi, Long
- Mi, Mantian
- Venue
- Nutrition & Metabolism
- Published
- 2021-09-09
- Volume
- 18
- Issue
- 1
- Pages
- 83-83
- ISSN
- 1743-7075 (ISSN-L)
- PMC
- PMC8428134
- OpenAlex
- W3157872931
- Cited by
- 23
- References
- 51
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 4 · 2023: 5 · 2022: 7
- FWCI
- 2.88
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nutrition & Metabolism (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Natural Science Foundation of China (81903317)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Complementary and alternative medicine › Medicinal plant effects and applications
- Health Sciences › Medicine › Epidemiology › Liver Disease Diagnosis and Treatment
- Keywords
- dihydromyricetin, palmitic acid, oxidative stress, autophagy, SIRT3, ATG4B, hepatocytes, nonalcoholic steatohepatitis, mitochondrial dysfunction, reactive oxygen species, LC3, p62, mitochondrial membrane potential
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
