1. Kubo M, Purevdorj M (2004) The future of rice production and consumption. Journal of Food Distribution Research. 35(1): 128–142.
2. Moffett JR, Namboodiri MA (2003) Tryptophan and the immune response. Immunol Cell Biol. 81(4): 247–65. 12848846
3. Ishihara A, Matsuda F, Miyagawa H, Wakasa K (2007) Metabolomics for metabolically manipulated plants: effects of tryptophan overproduction. Metabolomics. 3: 319–334.
4. Ishikawa Y, Park J, Kisaka H, Lee H, Kanno A, Kameya T (2003) A 5-methyltryptophan resistant mutant of rice has an altered regulation of anthranilate synthase gene expression. Plant Science. 164(6): 1037–1045.
5. Ranch JP, Rick S, Brotherton JE, Widholm JM (1983) Expression of 5-Methyltryptophan resistance in plants regenerated from resistant cell lines of Datura innoxia. Plant Physiol. 71: 136–140. 16662772
6. Niyogi KK, Fink GR (1992) Two anthranilate synthase genes in Arabidopsis: defense-related regulation of the tryptophan pathway. Plant Cell. 4: 721–733. doi: 10.1105/tpc.4.6.721 1392592
7. Kang KK, Kameya T (1993) Selection and characterization of a 5-methyltryptophan resistant mutant in Zea mays L. Euphytica. 69: 95.
8. Tam YY, Slovin JP, Cohen JD (1995) Selection and characterization of α-methyltryptophan-resistant lines of Lemna gibba showing a rapid rate of Indole-3-acetic acid turnover. Plant Physiol. 107: 77–85. 12228344
9. Cho HJ, Brotherton JE, Song HS, Widholm JM (2000) Increasing tryptophan synthesis in a forage legume Astragalus sinicus by expressing the tobacco feedback-insensitive anthranilate synthase (ASA2) Gene. Plant Physiol. 123: 1069–1076. 10889256
10. Zhang XH, Brotherton JE, Widholm JM, Portis AR Jr. (2001) Targeting a nuclear anthranilate synthase α-subunit gene to the tobacco plastid genome results in enhanced tryptophan biosynthesis. Return of a gene to its pre-endosymbiotic origin. Plant Physiol. 127: 131–141. 11553741
11. Hanafy MS, Rahman SM, Khalafalla M, El-Shemy HA, Nakamoto Y, Ishimoto M, et al. (2006) Accumulation of free tryptophan in Azuki bean (Vigna angularis) induced by expression of a gene (OASA1D) for a modified α-subunit of rice anthranilate synthase. Plant Science. 171: 670–676.
12. Lee HY and Kameya T (1991) Selection and characterization of a rice mutant resistant to 5-methyltryptophan. Theor Appl Genet. 82: 405–408. doi: 10.1007/BF00588590 24213253
13. Tozawa Y, Hasegawa H, Terakawa T, Wakasa K (2001) Characterization of rice anthranilate synthase alpha-subunit genes OASA1 and OASA2. Plant Physiology. 126(4): 1493–1506. 11500548
14. Kim D, Le I, Jang C, Kang S, Park I, Song H, et al. (2005) High amino acid accumulating 5-methyltryptophan-resistant rice mutants may include an increased antioxidative response system. Physiologia Plantarum. 123(3): 302–313.
15. Kanno T, Kasai K, Ikejiri-Kanno Y, Wakasa K, Tozawa Y (2004) In vitro reconstitution of rice anthranilate synthase: distinct functional properties of the α subunits OASA1 and OASA2. Plant Molecular Biology. 54(1): 11–22. 15159631
16. Yamada T, Tozawa Y, Hasegawa H, Terakawa T, Ohkawa Y, Wakasa K (2004) Use of a feedback-insensitive subunit of anthranilate synthase as a selectable marker for transformation of rice and potato. Molecular Breeding. 14: 363–373.
17. Kim DS, Kim JB, Lee GJ, Kang SY, Jang CS, Lee SY, et al. (2007) Identification of expressed sequence tags from a cDNA library of 5-Methyltryptophan resistant rice mutants. Journal of Radiation Industry. 1(1): 1–13.
18. Cho YG, Lee HJ, Nogoy FM, Nino MC. (2014) Development of high quality rice variety producing high content tryptophan by gene targeting technology. Agriculture, Forestry and Livestock 11-1543000-000753-01.
19. Corpet F (1988) Multiple sequence alignment with hierarchical clustering. Nucl. Acids Res. 16(22): 10881–10890. doi: 10.1093/nar/16.22.10881 2849754
20. Juliano BO (1971) A simplified assay for milled rice amylose. Cereal Science Today. 16: 334–338.
21. Kambhampati S, Li J, Evans BS, Allen DK (2019) Accurate and efficient amino acid analysis for protein quantification using hydrophilic interaction chromatography coupled tandem mass spectrometry. Plant Methods. 15:46. doi: 10.1186/s13007-019-0430-z 31110556
22. Lee HJ, Jee MG, Kim JK, Nogoy FMC, Niño MC, Yu DA, et al. (2014) Modification of starch composition using RNAi targeting soluble starch synthase I in Japonica rice. Plant Breed. Biotech. 2: 301–312.
23. Nogoy FM, Jung YJ, Kang KK, Cho YG (2018) Characterization of ‘GolSam’ lines developed from the cross between Samgwang and 5MT resistant lines in rice. Plant Breed. Biotech. 6: 233–244.
24. Mi H, Thomas P (2009) Protein networks and pathway analysis. Methods in Molecular Biology. 563(2): 123–140.
25. Mi H, Muruganujan A, Casagrande JT, Thomas PD (2013) Large-scale gene function analysis with the PANTHER classification system. Nature Protocols. 8: 1551–1566. doi: 10.1038/nprot.2013.092 23868073
26. Mi H, Huang X, Muruganujan A, Tang H, Mills C, Kang D, et al. (2016) PANTHER version 11: expanded annotation data from gene ontology and reactome pathways, and data analysis tool enhancements. Nucl. Acids Res. 45(D1): D183–D189. doi: 10.1093/nar/gkw1138 27899595
27. Gene Ontology Consortium (2016) Expansion of the gene ontology knowledgebase and resources. Nucleic Acids Res. 45(D1): D331–D338. doi: 10.1093/nar/gkw1108 27899567
28. Lester G (1968) In vivo regulation of intermediate reactions in the pathway of tryptophan biosynthesis in Neurospora crassa. Journal of Bacteriology. 96: 1768–1773. 5726311
29. Marmorstein RQ, Sigler PB (1989) Stereochemical effects of L-Tryptophan and its analogues on trp repressor’s affinity for operator-DNA. Journal of Biological Chemistry. 264(16): 9149–9154. 2656696
30. Hyde EI, Ramesh V, Frederick R, Roberts GCK (1991) NMR studies of the activation of the Escherichia coli trp repressor. FEBS Journal. 201(3): 569–579.
31. Wakasa K, Hasegawa H, Nemoto H, Matsuda F, Miyazawa H, Tozawa Y, et al. (2006) High-level tryptophan accumulation in seeds of transgenic rice and its limited effects on agronomic traits and seed metabolite profile. Journal of Experimental Botany. 57: 3069–3078. 16908506