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J Huazhong Univ Sci Technolog Med Sci, 33(2), 189\u2013194. doi:https:\/\/doi.org\/10.1007\/s11596-013-1095-x.","DOI":"10.1007\/s11596-013-1095-x"},{"issue":"2","key":"10.1016\/j.lfs.2021.119252_bb0580","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1002\/hep.510290220","article-title":"Differences in the metabolism and disposition of ursodeoxycholic acid and of its taurine-conjugated species in patients with primary biliary cirrhosis","volume":"29","author":"Invernizzi","year":"1999","journal-title":"Hepatology"},{"key":"10.1016\/j.lfs.2021.119252_bb0585","doi-asserted-by":"crossref","unstructured":"Elia, A. E., Lalli, S., Monsurr\u00f2, M. R., Sagnelli, A., Taiello, A. C., Reggiori, B., . . . Albanese, A. (2016). Tauroursodeoxycholic acid in the treatment of patients with amyotrophic lateral sclerosis. Eur. J. Neurol., 23(1), 45\u201352. doi:https:\/\/doi.org\/10.1111\/ene.12664.","DOI":"10.1111\/ene.12664"},{"issue":"2","key":"10.1016\/j.lfs.2021.119252_bb0590","doi-asserted-by":"crossref","first-page":"200","DOI":"10.3346\/jkms.2012.27.2.200","article-title":"Oral solubilized ursodeoxycholic acid therapy in amyotrophic lateral sclerosis: a randomized cross-over trial","volume":"27","author":"Min","year":"2012","journal-title":"J. Korean Med. Sci."},{"key":"10.1016\/j.lfs.2021.119252_bb0595","doi-asserted-by":"crossref","unstructured":"Parry, G. J., Rodrigues, C. M., Aranha, M. M., Hilbert, S. J., Davey, C., Kelkar, P., . . . Steer, C. J. (2010). Safety, tolerability, and cerebrospinal fluid penetration of ursodeoxycholic acid in patients with amyotrophic lateral sclerosis. Clin. Neuropharmacol., 33(1), 17\u201321. doi:https:\/\/doi.org\/10.1097\/WNF.0b013e3181c47569.","DOI":"10.1097\/WNF.0b013e3181c47569"},{"key":"10.1016\/j.lfs.2021.119252_bb0600","doi-asserted-by":"crossref","unstructured":"Paganoni, S., Macklin, E. A., Hendrix, S., Berry, J. D., Elliott, M. A., Maiser, S., . . . Cudkowicz, M. E. (2020). Trial of sodium phenylbutyrate-taurursodiol for amyotrophic lateral sclerosis. N. Engl. J. 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