{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T04:54:34Z","timestamp":1791003274800,"version":"4.1.0"},"reference-count":16,"publisher":"Japanese Society of Toxicology","issue":"10","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J. Toxicol. Sci."],"published-print":{"date-parts":[[2026]]},"DOI":"10.2131\/jts.51.557","type":"journal-article","created":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T22:15:20Z","timestamp":1790806520000},"page":"557-563","source":"Crossref","is-referenced-by-count":0,"title":["Aged black garlic-derived S-allyl-L-cysteine serves as a dietary precursor for supersulfide production by cystathionine \u03b3-lyase"],"prefix":"10.2131","volume":"51","author":[{"given":"Shoma","family":"Araki","sequence":"first","affiliation":[{"name":"Department of Pharmacology, Showa Pharmaceutical University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takahisa","family":"Nakane","sequence":"additional","affiliation":[{"name":"Department of Pharmacognosy and Natural Products Chemistry, Showa Pharmaceutical University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yasuo","family":"Watanabe","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Showa Pharmaceutical University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yukihiro","family":"Tsuchiya","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Showa Pharmaceutical University"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"898","reference":[{"key":"1","doi-asserted-by":"crossref","unstructured":"Akaike, T., Ida, T., Wei, F.Y., Nishida, M., Kumagai, Y., Alam, M.M., Ihara, H., Sawa, T., Matsunaga, T., Kasamatsu, S., Nishimura, A., Morita, M., Tomizawa, K., Nishimura, A., Watanabe, S., Inaba, K., Shima, H., Tanuma, N., Jung, M., Fujii, S., Watanabe, Y., Ohmuraya, M., Nagy, P., Feelisch, M., Fukuto, J.M. and Motohashi, H. (2017): Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics. Nat. Commun., <b>8<\/b>, 1177.","DOI":"10.1038\/s41467-017-01311-y"},{"key":"2","doi-asserted-by":"crossref","unstructured":"Akaike, T., Morita, M., Ogata, S., Yoshitake, J., Jung, M., Sekine, H., Motohashi, H., Barayeu, U. and Matsunaga, T. (2024): New aspects of redox signaling mediated by supersulfides in health and disease. Free Radic. Biol. Med., <b>222<\/b>, 539-551.","DOI":"10.1016\/j.freeradbiomed.2024.07.007"},{"key":"3","doi-asserted-by":"crossref","unstructured":"Amagase, H. (2006): Clarifying the real bioactive constituents of garlic. J. Nutr., <b>136<\/b> (Suppl), 716S-725S.","DOI":"10.1093\/jn\/136.3.716S"},{"key":"4","doi-asserted-by":"crossref","unstructured":"Araki, S., Takata, T., Ono, K., Sawa, T., Kasamatsu, S., Ihara, H., Kumagai, Y., Akaike, T., Watanabe, Y. and Tsuchiya, Y. (2023): Cystathionine \u03b3-lyase self-inactivates by polysulfidation during cystine metabolism. Int. J. Mol. Sci., <b>24<\/b>, 9982.","DOI":"10.3390\/ijms24129982"},{"key":"5","doi-asserted-by":"publisher","unstructured":"Araki, S., Takata, T., Yoon, S., Kasamatsu, S., Ihara, H., Nakagawa, H., Akaike, T., Tsuchiya, Y. and Watanabe, Y. (2025): The supersulfide-producing activity of rat cystathionine \u03b3-lyase is irreversibly inactivated by L-CysNO but not by L-GSNO. Antioxidants, <b>14<\/b>, 1113.","DOI":"10.3390\/antiox14091113"},{"key":"6","doi-asserted-by":"crossref","unstructured":"Barayeu, U., Sawa, T., Nishida, M., Wei, F.Y., Motohashi, H. and Akaike, T. (2026): Supersulfide biology and translational medicine for disease control. Br. J. Pharmacol., <b>183<\/b>, 115-130.","DOI":"10.1111\/bph.16271"},{"key":"7","doi-asserted-by":"crossref","unstructured":"Bradford, M.M. (1976): A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., <b>72<\/b>, 248-254.","DOI":"10.1016\/0003-2697(76)90527-3"},{"key":"8","doi-asserted-by":"crossref","unstructured":"Imai, T., Kosuge, Y., Saito, H., Uchiyama, T., Wada, T., Shimba, S., Ishige, K., Miyairi, S., Makishima, M. and Ito, Y. (2016): Neuroprotective effect of S-allyl-l-cysteine derivatives against endoplasmic reticulum stress-induced cytotoxicity is independent of calpain inhibition. J. Pharmacol. Sci., <b>130<\/b>, 185-188.","DOI":"10.1016\/j.jphs.2016.03.004"},{"key":"9","doi-asserted-by":"crossref","unstructured":"Kasamatsu, S., Kinno, A., Hishiyama, J.I., Akaike, T. and Ihara, H. (2023): Development of methods for quantitative determination of the total and reactive polysulfides: reactive polysulfide profiling in vegetables. Food Chem., <b>413<\/b>, 135610.","DOI":"10.1016\/j.foodchem.2023.135610"},{"key":"10","doi-asserted-by":"crossref","unstructured":"Kasamatsu, S., Kinno, A., Miura, C., Hishiyama, J.I., Fukui, K., Kure, S., Tsumura, K., Ida, T., Matsunaga, T., Akaike, T. and Ihara, H. (2024): Quantitative profiling of supersulfides naturally occurring in dietary meats and beans. Anal. Biochem., <b>685<\/b>, 115392.","DOI":"10.1016\/j.ab.2023.115392"},{"key":"11","doi-asserted-by":"crossref","unstructured":"Khajevand-Khazaei, M.R., Azimi, S., Sedighnejad, L., Salari, S., Ghorbanpour, A., Baluchnejadmojarad, T., Mohseni-Moghaddam, P., Khamse, S. and Roghani, M. (2019): S-allyl cysteine protects against lipopolysaccharide-induced acute kidney injury in the C57BL\/6 mouse strain: involvement of oxidative stress and inflammation. Int. Immunopharmacol., <b>69<\/b>, 19-26.","DOI":"10.1016\/j.intimp.2019.01.026"},{"key":"12","doi-asserted-by":"crossref","unstructured":"Liu, L. and Yeh, Y.Y. (2002): S-alk(en)yl cysteines of garlic inhibit cholesterol synthesis by deactivating HMG-CoA reductase in cultured rat hepatocytes. J. Nutr., <b>132<\/b>, 1129-1134.","DOI":"10.1093\/jn\/132.6.1129"},{"key":"13","doi-asserted-by":"crossref","unstructured":"Nishi, N., Tanabe, H., Oya, H., Urushihara, M., Miyanaka, H. and Wada, F. (1994): Identification of probasin-related antigen as cystathionine \u03b3-lyase by molecular cloning. J. Biol. Chem., <b>269<\/b>, 1015-1019.","DOI":"10.1016\/S0021-9258(17)42213-7"},{"key":"14","doi-asserted-by":"crossref","unstructured":"Sbodio, J.I., Snyder, S.H. and Paul, B.D. (2019): Regulators of the transsulfuration pathway. Br. J. Pharmacol., <b>176<\/b>, 583-593.","DOI":"10.1111\/bph.14446"},{"key":"15","doi-asserted-by":"crossref","unstructured":"Steegborn, C., Clausen, T., Sondermann, P., Jacob, U., Worbs, M., Marinkovic, S., Huber, R. and Wahl, M.C. (1999): Kinetics and inhibition of recombinant human cystathionine \u03b3-lyase. Toward the rational control of transsulfuration. J. Biol. Chem., <b>274<\/b>, 12675-12684.","DOI":"10.1074\/jbc.274.18.12675"},{"key":"16","doi-asserted-by":"crossref","unstructured":"Tsai, S.J., Chiu, C.P., Yang, H.T. and Yin, M.C. (2011): s-Allyl cysteine, s-ethyl cysteine, and s-propyl cysteine alleviate \u03b2-amyloid, glycative, and oxidative injury in brain of mice treated by D-galactose. J. Agric. Food Chem., <b>59<\/b>, 6319-6326.","DOI":"10.1021\/jf201160a"}],"container-title":["The Journal of Toxicological Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/jts\/51\/10\/51_557\/_pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T04:43:33Z","timestamp":1791002613000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/jts\/51\/10\/51_557\/_article"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026]]},"references-count":16,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2026]]}},"URL":"https:\/\/doi.org\/10.2131\/jts.51.557","relation":{},"ISSN":["0388-1350","1880-3989"],"issn-type":[{"value":"0388-1350","type":"print"},{"value":"1880-3989","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026]]}}}