Manis javanica

References

[1] Aachmann F, Sal L, Kim H, Marino S, Gladyshev V, Dikly A. Insights into function, catalytic mechanism, and fold evolution of Selenoprotein Methionine Sulfoxide Reductase B1 through structural analysis. J Biol Chem. 2010;285(43);33315-23.

[2] Allmang C, Wurth L, Krol A. The selenium to selenoprotein pathway in eukaryotes: more particular partners than anticipated. BBA. 2009;1970:1415-23.

[3] Böck A. Biosynthesis of selenoproteins - an overview. BioFactors. 2000;11:77-8.

[4] Brown KM, Arthur JR. Selenium, selenoproteins and human health: a review. Pub Health Nutr. 2016;4(2B):593-99.

[5] Brozmanová J, Mániková D, Vlčková V, Chovanec M. Selenium: a double-edged sword for defence and offence in cancer. Arch Toxicol. 2010;84(12):919-38.

[6] Budiman ME, Bubenik JL, Driscoll DM. Identification of a signature motif for the eIF4a3-SECIS interaction. Nucleic Acids Res. 2011;39(17):7730–9.

[7] Collins R, Johansson AL, Karlberg T, Markova N, van den Berg S, Olesen K, et al. Biochemical discrimination beetween selenium and sulfur 1: a single residue provides selenium specificity to human selenocysteine lyase. PLoS One. 2012;7(1):e30581.

[8] Challender D, Nguyen Van T, Shepherd C, Krishnasamy K, Wang A, Lee B, et al. Manis javanica, Sunda pangolin. IUCN Red list.2014.

[9] Chavatte L, Brown BA, Driscoll DM. Ribosomal protein L30 is a component of the UGA-selenocysteine recoding machinery in eukaryotes. Nat Struct Mol Biol. 2005;12:408–16.

[10] Copeland P, Stepanik V, Driscoll D. Insight into mammalian selenocysteine insertion: domain structure and ribosome binding properties of Sec insertion Sequence Binding Protein 2. Mol Cel Biol. 2001;21(5):1491-8.

[11] Driscoll DM, Copelan PR. Mechanism and regulation of selenoprotein synthesis. Annu Rev Nutr. 2003;23(1):17-40.

[12] Fixsen S, Howard M. Processive Selenocysteine incorporation during synthesis of eukaryotic selenoproteins. J Mol Biol. 2010;399(3):385-96.

[13] Hatfield DL, Schweizer U, Tsuji PA, Gladyshev VN. Selenium: its molecular biology and role in human health. 4th ed. New York, USA:Springer;2016.

[14] Khalifa O, Al-Sahlawi Z, Imtiaz F, Ramzan K, Allam R, Al-Mostafa A, Abdel-Fattah M, Abuharb G, Nester M, Verloes A, Al-Zaidan H. Variable expression pattern in Donnai-Barrow syndrome: report of two novel LRP2 mutations and review of the literature. Eur J Med Genet. 2015;58(5):293–9.

[15] Kryukov G, Castellano S, Novoselov S, Lobanov A, Zehtab O, Guigó R, et al. Characterization of Mammalian Selenoproteomes. Science. 2003;300:1439-43.

[16] Kumaraswamy E, Malykh A, Korotkov K, Kozyavkin S, Hu Y, Kwon SY, et al. Structure-expression relationships of the 15-kDA Selenoprotein gene: possible role of the protein in cancer etiology. J Biol Chem. 2000;275:35540-47.

[17] Labunskyy V, Hatfield D, Gladyshev V. Selenoproteins: molecular pathways and physiological roles. Physiol Rev. 2014;94(3):739-77.

[18] Lobanov A, Hatfield D, Gladyshev V. Eukaryotic selenoproteins and selenoproteomes. BBA. 2009;1970:1424-28.

[19] Lu J, Holmgren A. Selenoproteins. J Biol Chem. 2009;284(2):723-27.

[20] Mariotti M, Ridge PG, Zhang Y, et al. Composition and evolution of the vertebrate and mammalian selenoproteomes. PLoS ONE. 2012;7(3):e33066.

[21] Mariotti M, Santesmasses D, Capella-Gutierrez S, Mateo A, Arnan C, Johnson R, et al. Evolution of selenophosphate synthetases: emergence and relocation of function through independent duplications and recurrent subfunctionalization. Genome Research. 2015;25:1256-67.

[22] Masella R, Mazza G. Glutathione and sulfur amino acids in human health and disease. 1st ed. USA:Wiley;2009.

[23] Paap L, Lu J, Holmgren A, Khanna K. From Selenium to Selenoproteins: Synthesis, identity and their role in human health. Redox Signal. 2007;9(7):775-806.

[24] Palioura S, Sherrer RL, Steitz TA, Söll D, Simonovic M. The human SepSecS-tRNASec complex reveals the mechanism of selenocsteine formation. Science. 2009;325(5938):321-25.

[25] Qichang S, Chu F, Newburger P. Sequences in the 3’-untranslated region of the human cellular Glutathione Peroxidase gene are necessary and sufficient for Selenocysteine incorporation at the UGA codon. J Biol Chem. 1993;268(15);11463-69.

[26] Roman M, Jitaru P, Barbante C. Selenium biochemistry and its role for human health. Metallomics. 2014;6(1):25-54.

[27] Schilitter D. Subgenus Paramanis. A: Wilson D. Mammal species of the world: A taxonomic and geographic reference. 3rd ed. Johns Hopkins University Press;2005.

[28] Shepherd C, Shepherd L. A naturalist’s guide to the mammals of Southeast Asia. Wiltshire, UK:John Beuafoy Publishing;2012.

[29] Shetty S, Shah R, Copeland P. Regulation of Selenocysteine incorporation into the Selenium transport protein, Selenoprotein P. J Biol Chem. 2014;289(36):25317-26.

[30] Stade K, Ford CS, Guthrie C, Weis K. Exportin 1 (Crm1p) is an essential nuclear export factor. Cell. 1997;90(6):1041-50.

[31] Tujebajeva R, Copeland P, Xu X, Carlson B, Harney J, Driscoll D. Decoding apparatus for eukaryotic selenocysteine insertion. EMBO reports. 2000;1(2):158-63.

[32] Whanger PD. Selenium and its relationship to cancer: an update. Brit Journ Nutr. 2004;91:11-28.

[33] Xu X, Mix H, Carlson B, Grabowski P, Gladyshev V, Berry M, et al. Evidence for diet roles of two additional factors, Secp43 and soluble liver antigen, in the Selenoprotein synthesis machinery. J Biol Chem. 2005;280(50):41568-75.

[34] Xu X, Carlson B, Mix H, Zhang Y, Saira K, Glass R, et al. Biosynthesis of selenocysteine on its tRNA in eukaryotes. PLoS Biol. 2007;5(1):e4.

[35] Zhao HD, Zhang WG, Sun MN, Duan QF, Li FL, Li H. The role of Sep (O-phosphoserine) tRNA: Sec (selenocysteine) synthase (SEPSECS) in prolifeation, apoptosis and hormone secretion of trophoblast cells. Placenta. 2013;34(11):967-72.