Asai, H., Hirata, J., & Watanabe-Akanuma, M. (2018). Indoxyl glucuronide, a protein-bound uremic toxin, inhibits hypoxia-inducible factor‒dependent erythropoietin expression through activation of aryl hydrocarbon receptor. Biochemical and biophysical research communications, 504(2), 538-544.

Gryp, T., De Paepe, K., Vanholder, R., Kerckhof, F. M., Van Biesen, W., Van de Wiele, T., ... & Glorieux, G. (2020). Gut microbiota generation of protein-bound uremic toxins and related metabolites is not altered at different stages of chronic kidney disease. Kidney international, 97(6), 1230-1242.

Zelante, T., Iannitti, R. G., Cunha, C., De Luca, A., Giovannini, G., Pieraccini, G., ... & Romani, L. (2013). Tryptophan catabolites from microbiota engage aryl hydrocarbon receptor and balance mucosal reactivity via interleukin-22. Immunity, 39(2), 372-385.

Tsavkelova, E., Oeser, B., Oren-Young, L., Israeli, M., Sasson, Y., Tudzynski, B., & Sharon, A. (2012). Identification and functional characterization of indole-3-acetamide-mediated IAA biosynthesis in plant-associated Fusarium species. Fungal Genetics and Biology, 49(1), 48-57.

Graboski, A. L., & Redinbo, M. R. (2020). Gut-derived protein-bound uremic toxins. Toxins, 12(9), 590.

Lim, Y. J., Sidor, N. A., Tonial, N. C., Che, A., & Urquhart, B. L. (2021). Uremic Toxins in the Progression of Chronic Kidney Disease and Cardiovascular Disease: Mechanisms and Therapeutic Targets. Toxins, 13(2), 142.

Deeley MC, Yanofsky C: Nucleotide sequence of the structural gene for tryptophanase of Escherichia coli K-12. J Bacteriol. 1981 Sep;147(3):787-96.

Tokushige M, Tsujimoto N, Oda T, Honda T, Yumoto N, Ito S, Yamamoto M, Kim EH, Hiragi Y: Role of cysteine residues in tryptophanase for monovalent cation-induced activation. Biochimie. 1989 Jun;71(6):711-20. doi: 10.1016/0300-9084(89)90087-4.

Burland V, Plunkett G 3rd, Daniels DL, Blattner FR: DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication. Genomics. 1993 Jun;16(3):551-61. doi: 10.1006/geno.1993.1230.

Hu Y, Oscarson M, Johansson I, Yue QY, Dahl ML, Tabone M, Arinco S, Albano E, Ingelman-Sundberg M: Genetic polymorphism of human CYP2E1: characterization of two variant alleles. Mol Pharmacol. 1997 Mar;51(3):370-6.

Fairbrother KS, Grove J, de Waziers I, Steimel DT, Day CP, Crespi CL, Daly AK: Detection and characterization of novel polymorphisms in the CYP2E1 gene. Pharmacogenetics. 1998 Dec;8(6):543-52.

Song BJ, Gelboin HV, Park SS, Yang CS, Gonzalez FJ: Complementary DNA and protein sequences of ethanol-inducible rat and human cytochrome P-450s. Transcriptional and post-transcriptional regulation of the rat enzyme. J Biol Chem. 1986 Dec 15;261(35):16689-97.

Gamage NU, Duggleby RG, Barnett AC, Tresillian M, Latham CF, Liyou NE, McManus ME, Martin JL: Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition. J Biol Chem. 2003 Feb 28;278(9):7655-62. doi: 10.1074/jbc.M207246200. Epub 2002 Dec 5.

Lu J, Li H, Zhang J, Li M, Liu MY, An X, Liu MC, Chang W: Crystal structures of SULT1A2 and SULT1A1 *3: insights into the substrate inhibition and the role of Tyr149 in SULT1A2. Biochem Biophys Res Commun. 2010 May 28;396(2):429-34. doi: 10.1016/j.bbrc.2010.04.109. Epub 2010 Apr 22.

Zhu X, Veronese ME, Bernard CC, Sansom LN, McManus ME: Identification of two human brain aryl sulfotransferase cDNAs. Biochem Biophys Res Commun. 1993 Aug 31;195(1):120-7. doi: 10.1006/bbrc.1993.2018.

Sarsero JP, Wookey PJ, Gollnick P, Yanofsky C, Pittard AJ: A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli. J Bacteriol. 1991 May;173(10):3231-4. doi: 10.1128/jb.173.10.3231-3234.1991.

Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. doi: 10.1126/science.277.5331.1453.