{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,15]],"date-time":"2026-07-15T18:02:31Z","timestamp":1784138551152,"version":"3.55.0"},"reference-count":28,"publisher":"Japanese Society of Toxicology","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J. Toxicol. Sci."],"published-print":{"date-parts":[[2023]]},"DOI":"10.2131\/jts.48.355","type":"journal-article","created":{"date-parts":[[2023,5,31]],"date-time":"2023-05-31T22:19:00Z","timestamp":1685571540000},"page":"355-361","source":"Crossref","is-referenced-by-count":7,"title":["Proteasome and p62\/SQSTM1 are involved in methylmercury toxicity mitigation in mouse embryonic fibroblast cells"],"prefix":"10.2131","volume":"48","author":[{"given":"Yasukazu","family":"Takanezawa","sequence":"first","affiliation":[{"name":"Department of Public Health, School of Pharmacy, Kitasato University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ryosuke","family":"Nakamura","sequence":"additional","affiliation":[{"name":"Department of Public Health, School of Pharmacy, Kitasato University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuka","family":"Ohshiro","sequence":"additional","affiliation":[{"name":"Department of Public Health, School of Pharmacy, Kitasato University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shimpei","family":"Uraguchi","sequence":"additional","affiliation":[{"name":"Department of Public Health, School of Pharmacy, Kitasato University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masako","family":"Kiyono","sequence":"additional","affiliation":[{"name":"Department of Public Health, School of Pharmacy, Kitasato University"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"898","reference":[{"key":"1","doi-asserted-by":"crossref","unstructured":"Adams, J. (2003): The proteasome: structure, function, and role in the cell. Cancer Treat. Rev., <b>29<\/b> (Suppl 1), 3-9.","DOI":"10.1016\/S0305-7372(03)00081-1"},{"key":"2","doi-asserted-by":"crossref","unstructured":"Amm, I., Sommer, T. and Wolf, D.H. (2014): Protein quality control and elimination of protein waste: the role of the ubiquitin-proteasome system. Biochim. Biophys. Acta, <b>1843<\/b>, 182-196.","DOI":"10.1016\/j.bbamcr.2013.06.031"},{"key":"3","doi-asserted-by":"crossref","unstructured":"Auger, N., Kofman, O., Kosatsky, T. and Armstrong, B. (2005): Low-level methylmercury exposure as a risk factor for neurologic abnormalities in adults. Neurotoxicology, <b>26<\/b>, 149-157.","DOI":"10.1016\/j.neuro.2004.12.005"},{"key":"4","doi-asserted-by":"crossref","unstructured":"Bj\u00f8rk\u00f8y, G., Lamark, T., Brech, A., Outzen, H., Perander, M., \u00d8vervatn, A., Stenmark, H. and Johansen, T. (2005): p62\/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol., <b>171<\/b>, 603-614.","DOI":"10.1083\/jcb.200507002"},{"key":"5","doi-asserted-by":"crossref","unstructured":"Clarkson, T.W. and Magos, L. (2006): The toxicology of mercury and its chemical compounds. Crit. Rev. Toxicol., <b>36<\/b>, 609-662.","DOI":"10.1080\/10408440600845619"},{"key":"6","doi-asserted-by":"crossref","unstructured":"Cohen-Kaplan, V., Livneh, I., Avni, N., Fabre, B., Ziv, T., Kwon, Y.T. and Ciechanover, A. (2016): p62- and ubiquitin-dependent stress-induced autophagy of the mammalian 26S proteasome. Proc. Natl. Acad. Sci. USA, <b>113<\/b>, E7490-E7499.","DOI":"10.1073\/pnas.1615455113"},{"key":"7","doi-asserted-by":"crossref","unstructured":"Hiraoka, H., Nakahara, K., Kaneko, Y., Akiyama, S., Okuda, K., Iwawaki, T., Fujimura, M., Kumagai, Y., Takasugi, N. and Uehara, T. (2017): Modulation of unfolded protein response by methylmercury. Biol. Pharm. Bull., <b>40<\/b>, 1595-1598.","DOI":"10.1248\/bpb.b17-00359"},{"key":"8","doi-asserted-by":"crossref","unstructured":"Hwang, G.-W., Furuchi, T. and Naganuma, A. (2002): A ubiquitin-proteasome system is responsible for the protection of yeast and human cells against methylmercury. FASEB J., <b>16<\/b>, 709-711.","DOI":"10.1096\/fj.01-0899fje"},{"key":"9","doi-asserted-by":"crossref","unstructured":"Hwang, G.-W., Sasaki, D. and Naganuma, A. (2005): Overexpression of Rad23 confers resistance to methylmercury in saccharomyces cerevisiae via inhibition of the degradation of ubiquitinated proteins. Mol. Pharmacol., <b>68<\/b>, 1074-1078.","DOI":"10.1124\/mol.105.013516"},{"key":"10","doi-asserted-by":"crossref","unstructured":"Karagas, M.R., Choi, A.L., Oken, E., Horvat, M., Schoeny, R., Kamai, E., Cowell, W., Grandjean, P. and Korrick, S. (2012): Evidence on the human health effects of low-level methylmercury exposure. Environ. Health Perspect., <b>120<\/b>, 799-806.","DOI":"10.1289\/ehp.1104494"},{"key":"11","doi-asserted-by":"crossref","unstructured":"Ke, T., Gon\u00e7alves, F.M., Gon\u00e7alves, C.L., Dos Santos, A.A., Rocha, J.B., Farina, M., Skalny, A., Tsatsakis, A., Bowman, A.B. and Aschner, M. (2019): Post-translational modifications in MeHg-induced neurotoxicity. Biochim. Biophys. Acta Mol. Basis Dis., <b>1865<\/b>, 2068-2081.","DOI":"10.1016\/j.bbadis.2018.10.024"},{"key":"12","doi-asserted-by":"crossref","unstructured":"Komatsu, M., Kurokawa, H., Waguri, S., Taguchi, K., Kobayashi, A., Ichimura, Y., Sou, Y.S., Ueno, I., Sakamoto, A., Tong, K.I., Kim, M., Nishito, Y., Iemura, S., Natsume, T., Ueno, T., Kominami, E., Motohashi, H., Tanaka, K. and Yamamoto, M. (2010): The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1. Nat. Cell Biol., <b>12<\/b>, 213-223.","DOI":"10.1038\/ncb2021"},{"key":"13","doi-asserted-by":"crossref","unstructured":"Korolchuk, V.I., Mansilla, A., Menzies, F.M. and Rubinsztein, D.C. (2009): Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates. Mol. Cell, <b>33<\/b>, 517-527.","DOI":"10.1016\/j.molcel.2009.01.021"},{"key":"14","doi-asserted-by":"crossref","unstructured":"Kumagai, Y., Kanda, H., Shinkai, Y. and Toyama, T. (2013): The role of the Keap1\/Nrf2 pathway in the cellular response to methylmercury. Oxid. Med. Cell. Longev., <b>2013<\/b>, 848279.","DOI":"10.1155\/2013\/848279"},{"key":"15","doi-asserted-by":"crossref","unstructured":"Liu, W.J., Ye, L., Huang, W.F., Guo, L.J., Xu, Z.G., Wu, H.L., Yang, C. and Liu, H.F. (2016): p62 links the autophagy pathway and the ubiqutin-proteasome system upon ubiquitinated protein degradation. Cell. Mol. Biol. Lett., <b>21<\/b>, 29.","DOI":"10.1186\/s11658-016-0031-z"},{"key":"16","doi-asserted-by":"crossref","unstructured":"Salminen, A., Kaarniranta, K., Haapasalo, A., Hiltunen, M., Soininen, H. and Alafuzoff, I. (2012): Emerging role of p62\/sequestosome-1 in the pathogenesis of Alzheimer\u2019s disease. Prog. Neurobiol., <b>96<\/b>, 87-95.","DOI":"10.1016\/j.pneurobio.2011.11.005"},{"key":"17","doi-asserted-by":"crossref","unstructured":"Seibenhener, M.L., Babu, J.R., Geetha, T., Wong, H.C., Krishna, N.R. and Wooten, M.W. (2004): Sequestosome 1\/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol. Cell. Biol., <b>24<\/b>, 8055-8068.","DOI":"10.1128\/MCB.24.18.8055-8068.2004"},{"key":"18","doi-asserted-by":"crossref","unstructured":"Shin, W.H., Park, J.H. and Chung, K.C. (2020): The central regulator p62 between ubiquitin proteasome system and autophagy and its role in the mitophagy and Parkinson\u2019s disease. BMB Rep., <b>53<\/b>, 56-63.","DOI":"10.5483\/BMBRep.2020.53.1.283"},{"key":"19","doi-asserted-by":"crossref","unstructured":"Takanezawa, Y., Nakamura, R., Harada, R., Sone, Y., Uraguchi, S. and Kiyono, M. (2017): Sequestosome1\/p62 protects mouse embryonic fibroblasts against low-dose methylercury-induced cytotoxicity and is involved in clearance of ubiquitinated proteins. Sci. Rep., <b>7<\/b>, 16735.","DOI":"10.1038\/s41598-017-17112-8"},{"key":"20","doi-asserted-by":"crossref","unstructured":"Takanezawa, Y., Nakamura, R., Matsuda, H., Yagi, T., Egawa, Z., Sone, Y., Uraguchi, S., Adachi, T. and Kiyono, M. (2019a): Intracellular demethylation of methylmercury to inorganic mercury by organomercurial lyase (MerB) strengthens cytotoxicity. Toxicol. Sci., <b>170<\/b>, 438-451.","DOI":"10.1093\/toxsci\/kfz094"},{"key":"21","doi-asserted-by":"crossref","unstructured":"Takanezawa, Y., Nakamura, R., Sone, Y., Uraguchi, S. and Kiyono, M. (2019b): An autophagy deficiency promotes methylmercury-induced multinuclear cell formation. Biochem. Biophys. Res. Commun., <b>511<\/b>, 460-467.","DOI":"10.1016\/j.bbrc.2019.02.084"},{"key":"22","doi-asserted-by":"crossref","unstructured":"Takanezawa, Y., Nakamura, R., Sone, Y., Uraguchi, S. and Kiyono, M. (2016): Atg5-dependent autophagy plays a protective role against methylmercury-induced cytotoxicity. Toxicol. Lett., <b>262<\/b>, 135-141.","DOI":"10.1016\/j.toxlet.2016.09.007"},{"key":"23","doi-asserted-by":"crossref","unstructured":"Takanezawa, Y., Nakamura, R., Sugimoto, T., Ohshiro, Y., Uraguchi, S. and Kiyono, M. (2021): p62\/sequestosome 1 attenuates methylmercury-induced endoplasmic reticulum stress in mouse embryonic fibroblasts. Toxicol. Lett., <b>353<\/b>, 93-99.","DOI":"10.1016\/j.toxlet.2021.10.008"},{"key":"24","doi-asserted-by":"crossref","unstructured":"Tominaga, T., Goto, M., Onoue, T., Mizoguchi, A., Sugiyama, M., Tsunekawa, T., Hagiwara, D., Morishita, Y., Ito, Y., Iwama, S., Suga, H., Banno, R. and Arima, H. (2017): Sequestosome 1 (SQSTM1\/p62) maintains protein folding capacity under endoplasmic reticulum stress in mouse hypothalamic organotypic culture. Neurosci. Lett., <b>656<\/b>, 103-107.","DOI":"10.1016\/j.neulet.2017.06.014"},{"key":"25","doi-asserted-by":"crossref","unstructured":"Unoki, T., Akiyama, M., Kumagai, Y., Gon\u00e7alves, F.M., Farina, M., da Rocha, J.B. and Aschner, M. (2018): Molecular pathways associated with methylmercury-induced Nrf2 modulation. Front. Genet., <b>9<\/b>, 373.","DOI":"10.3389\/fgene.2018.00373"},{"key":"26","doi-asserted-by":"crossref","unstructured":"Usuki, F., Fujimura, M. and Yamashita, A. (2017): Endoplasmic reticulum stress preconditioning modifies intracellular mercury content by upregulating membrane transporters. Sci. Rep., <b>7<\/b>, 12390.","DOI":"10.1038\/s41598-017-09435-3"},{"key":"27","doi-asserted-by":"crossref","unstructured":"Wang, L., Jiang, H., Yin, Z., Aschner, M. and Cai, J. (2009): Methylmercury toxicity and Nrf2-dependent detoxification in astrocytes. Toxicol. Sci., <b>107<\/b>, 135-143.","DOI":"10.1093\/toxsci\/kfn201"},{"key":"28","doi-asserted-by":"crossref","unstructured":"Yokoo, E.M., Valente, J.G., Grattan, L., Schmidt, S.L., Platt, I. and Silbergeld, E.K. (2003): Low level methylmercury exposure affects neuropsychological function in adults. Environ. Health, <b>2<\/b>, 8.","DOI":"10.1186\/1476-069X-2-8"}],"container-title":["The Journal of Toxicological Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/jts\/48\/6\/48_355\/_pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,6,3]],"date-time":"2023-06-03T04:37:11Z","timestamp":1685767031000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/jts\/48\/6\/48_355\/_article"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023]]},"references-count":28,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2023]]}},"URL":"https:\/\/doi.org\/10.2131\/jts.48.355","relation":{},"ISSN":["0388-1350","1880-3989"],"issn-type":[{"value":"0388-1350","type":"print"},{"value":"1880-3989","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023]]}}}