THUNNUS ORIENTALIS

REFERENCES

ARTICLES

[1] Labunskyy VM, Hatfield DL, Gladyshev VN. Selenoproteins: molecular pathways and physiological roles. Physiol Rev. 2014; 94 (3): 739-77

[2] World Health Organization, Food and Agriculture Organization of the United Nations. Vitamin and Mineral Requirements in Human Nutrition. 2004

[3] Rayman MP. Selenium and human health. Lancet. 2012; 379 (9822): 1256-68

[4] Papp LV, Lu J, Holmgren A, Khanna KK. From selenium to selenoproteins: synthesis, identity, and their role in human health. Antioxid Redox Signal. 2007; 9 (7): 775-806

[5] Squires JE and Berry MJ. Eukaryotic Selenoprotein Synthesis: Mechanistic Insight Incorporating New Factors and New Functions for Old Factors. IUBMB Life. 2008; 60 (4): 232-5

[6] Mariotti M, Ridge PG, Zhang Y, Lobanov AV, Pringle TH, Guigo R, Hatfield DL, Gladyshev VN. Composition and evolution of the vertebrate and mammalian selenoproteomes. PloS One. 2012; 7 (3): e33066

[7] Allmang C, Wurth L, Krol A. The selenium to selenoprotein pathway in eukaryotes: more molecular partners than anticipated. Biochim Biophys Acta. 2009; 11 : 1415-23

[8] Lu J, Holmgren A. Selenoproteins. J Biol Chem. 2009; 284 (2):723-7

[9] Hoffmann PR, Berry MJ. Selenoprotein synthesis: a unique translational mechanism used by a diverse family of proteins. Thyroid. 2005; 15: 769–775

[10] Allmang C, Krol A. Selenoprotein synthesis: UGA does not end the story. Biochimie, 2006; 88(11):1561-71

[11] Lobanov AV, Hatfield DL, Gladyshev VN. Eukaryotic selenoproteins and selenoproteomes. Biochim Biophys Acta. 1790(11):1424-8

[12] Castellano S, Andrés AM, Bosch E, Bayes M, Guigó R, Clark AG. Low exchangeability of selenocysteine, the 21st amino acid, in vertebrate proteins. Mol Biol Evol, 2009; 26(9):2031-40

[13] Reeves MA, Hoffmann PR. The human selenoproteome: recent insights into functions and regulation. Cell Mol Life Sci. 2009; 66 (15): 2457-78

[14] Gladyshev VN et al. Structure–Function Relations, Physiological Roles, and Evolution of Mammalian ER-Resident Selenoproteins. Antioxid. Redox Signaling. 2010; 12: 7.

[15] Flohé L and Brigelius-Flohé R. Selenoproteins of the Gluthione Peroxidase Family. Springer. 2012; 167-180.

[16] Novoselov SV, Hua D, Lobanov AV, Gladyshev VN. Identification and characterization of Fep15, a new selenocysteine-containing member of the Sep15 protein family. Biochem J. 2006; 394: 575–579.

[17] Lee BC, Dikiy A, Kim HY, Gladyshev VN. Functions and evolution of selenoprotein methionine sulfoxide reductases. Elsevier. 2009; 94.

[18] Castellano S1, Lobanov AV, Chapple C, Novoselov SV, Albrecht M, Hua D, Lescure A, Lengauer T, Krol A, Gladyshev VN, Guigó R. Diversity and functional plasticity of eukaryotic selenoproteins: Identification and characterization of the SelJ family. Proc Natl Acad Sci U S A. Nov 8, 2005; 102(45): 16188–16193.

[19] Gladyshev VN et al. Structure–Function Relations, Physiological Roles, and Evolution of Mammalian ER-Resident Selenoproteins. Antioxid. Redox Signaling. 2010; 12: 7.

[20] Shchedrina VA, Novoselov SV, Malinouski MY, Gladyshev VN. Identification and characterization of a selenoprotein family containing a diselenide bond in a redox motif. Proc Natl Acad Sci U S A. Aug 28, 2007; 104(35): 13919–13924.

[21] Kryukov GV, Kryukov VM, Gladyshev VN. New mammalian selenocysteine-containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elements.J Biol Chem. 1999 Nov 26;274(48):33888-97.

[22] Guigó R, et al. Reconsidering the evolution of eukaryotic selenoproteins: a novel nonmammalian family with scattered phylogenetic distribution. EMBO reports. 2004; 71-77.