Abstract
1. Kryukov G V, Castellano S, Novoselov S V, Lobanov A V, Zehtab O, Guigó R, et al. Characterization of mammalian selenoproteomes. Science. 2003;300(May):1439–43.
2. Mariotti M, Ridge PG, Zhang Y, Lobanov A V., Pringle TH, Guigo R, et al. Composition and Evolution of the Vertebrate and Mammalian Selenoproteomes. PLoS One [Internet]. 2012;7(3):e33066. Available from: http://dx.plos.org/10.1371/journal.pone.003306
3. Labunskyy VM, Hatfield DL, Gladyshev VN. Selenoproteins: Molecular Pathways and Physiological Roles. Physiol Rev [Internet]. 2014;94(3):739–77. Available from: http://physrev.physiology.org/cgi/doi/10.1152/physrev.00039.201
4. Reeves MA. NIH Public Access. Cell Mol Life Sci. 2009;66(15):2457–78.
5. Bela K, Horváth E, Gallé Á, Szabados L, Tari I, Csiszár J. Plant glutathione peroxidases: Emerging role of the antioxidant enzymes in plant development and stress responses. J Plant Physiol [Internet]. Elsevier GmbH.; 2015;176:192–201. Available from: http://linkinghub.elsevier.com/retrieve/pii/S017616171500005
Informació de P.coquereli
1. Coquerel's Sifaka ( Propithecus Coquereli ) iNaturalist.org. Disponible a: http://www.inaturalist.org/taxa/74959-Propithecus-coquereli 2. Coquerel’s sifaka (Propithecus Coquereli) UK: Wildscreen. Disponible a: http://www.arkive.org/coquerels-sifaka/propithecus-coquereli/ 3. McLain AT, Meyer TJ, Faulk C, Herke SW, Oldenburg JM, Bourgeois MG, et al. An Alu-Based Phylogeny of Lemurs (Infraorder: Lemuriformes). PLoS ONE [revista a Internet]. 2012; 7(8). Disponible a: http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0044035 4. Propithecus Coquereli UK: The IUCN Red List Of Threatened Species; 2015-4. Disponible a: http://dx.doi.org/10.2305/IUCN.UK.2014-1.RLTS.T18355A16115770.en 5. Propithecus coquereli (Coquerel's sifaka) Animal Diversity Web. Disponible a: http://animaldiversity.org/accounts/Propithecus_coquereli/ 6. Sifaca de Coquerel (Viquipedia). Disponible a: https://ca.wikipedia.org/wiki/Sifaca_de_Coquerel 7. Typical coloration of each of the nine species of genus Propithecus (wikimedia commons). Disponible a: https://commons.wikimedia.org/wiki/File:Typical_coloration_of_each_of_the_nine_species_of_genus_Propithecus.svgInformació de les selenoproteïnes
1. Brown KM, Arthur JR. Selenium, selenoproteins and human health: a review. Public Health Nutr [revista a Internet]. 2001; 4(2B): 593-599. Disponible a: http://www.sbne.org.br/pdf/AC-Selenium-selenoproteins-and-human-health-a-review.pdf 2. Chumpitaz C. El selenio, un elemento poco conocido con un rol biológico importante. Revista de Química PUCP [revista a Internet]. 2001; 25: 21-33. Disponible a: http://revistas.pucp.edu.pe/index.php/quimica/article/viewFile/4780/4782 3. Lu J, Holmgren A. Selenoproteins. JBC [revista a Internet]. 2008; 284(2): 723-727. Disponible a: http://www.jbc.org/content/284/2/723.full.pdf 4. Mariotti M, Ridge PG, Zhang Y, Lobanov A, Pringle TH, Guigó R, Hatfield DL, Gladyshev VN. Composition and evolution of the vertebrate and mammalian selenoproteomes. PLoS One [revista a Internet] 2012; 7(3): e33066. Disponible a: http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0033066 5. Moghadaszadeh B, Beggs A. Selenoproteins and Their Impact on Human Health Through Diverse Physiological Pathways. APS [revista a Internet]. 2006; 21 (5): 307-315. Disponible a: http://physiologyonline.physiology.org/content/21/5/307 6. Papp LV, Lu J, Holmgren A, Khanna KK. From Selenium to Selenoproteins: Synthesis, Identitiy and Their Role in Human Health. Antioxid. Redox Signal [revista a Internet]. 2007; 9(7): 775-806. Disponible a: http://online.liebertpub.com/doi/pdf/10.1089/ars.2007.1528 7. Zwolak I, Zaporowska H. Selenium interactions and toxicity: a riview. Cell Biol Toxicol [revista a Internet]. 2012; 28: 31-36. Disponible a: http://link.springer.com/article/10.1007/s10565-011-9203-9/fulltext.htmlDiscussió
1. Romero H, Zhang Y, Gladyshev VN, Salinas G. Evolution of selenium utilization traits. Genome Biol. 2005;6(8):R66.2. Arnér ESJ. Selenoproteins—What unique properties can arise with selenocysteine in place of cysteine? Exp Cell Res [Internet]. Elsevier Inc.; 2010;316(8):1296–303. Available from: http://linkinghub.elsevier.com/retrieve/pii/S00144827100009472
3. Mariotti M, Ridge PG, Zhang Y, Lobanov A V., Pringle TH, Guigo R, et al. Composition and Evolution of the Vertebrate and Mammalian Selenoproteomes. PLoS One [Internet]. 2012;7(3):e33066. Available from: http://dx.plos.org/10.1371/journal.pone.003306>
4. Labunskyy VM, Hatfield DL, Gladyshev VN. Selenoproteins: Molecular Pathways and Physiological Roles. Physiol Rev [Internet]. 2014;94(3):739–77. Available from: http://physrev.physiology.org/cgi/doi/10.1152/physrev.00039.2013
5. Reeves MA. NIH Public Access. Cell Mol Life Sci. 2009;66(15):2457–78.
6. Pastorini J, Forstner MRJ, Martin RD. Phylogenetic History of Sifakas (Propithecus: Lemuriformes) Derived from mtDNA Sequences. Am J Primatol J Primatol. 2001;53(53):1–171.
7. Kryukov G V, Castellano S, Novoselov S V, Lobanov A V, Zehtab O, Guigó R, et al. Characterization of mammalian selenoproteomes. Science. 2003;300(May):1439–43.
8. Callebaut I, Curcio-Morelli C, Mornon J-P, Gereben B, Buettner C, Huang S, et al. The Iodothyronine Selenodeiodinases Are Thioredoxin-fold Family Proteins Containing a Glycoside Hydrolase Clan GH-A-like Structure. J Biol Chem [Internet]. 2003;278(38):36887–96. Available from: http://www.jbc.org/cgi/doi/10.1074/jbc.M305725200
9. Berry MJ, Kieffer JD, Harney JW, Larsen PR. Selenocysteine confers the biochemical properties characteristic of the type I iodothyronine deiodinase. J Biol Chem [Internet]. 1991;266(22):14155–8. Available from: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=183058
10. Sambasivarao S V. NIH Public Access. 2013;18(9):1199–216.
11. Sagar GDV, Gereben B, Callebaut I, Mornon J-P, Zeöld A, Curcio-Morelli C, et al. The thyroid hormone-inactivating deiodinase functions as a homodimer. Mol Endocrinol [Internet]. 2008;22(6):1382–93. Available from: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2422829&tool=pmcentrez&rendertype=abstrac
12. Wright DT, Cohn L a, Li H, Fischer B, Li CM, Adler KB. Interactions of oxygen radicals with airway epithelium. Environ Health Perspect [Internet]. 1994;102 Suppl (14):85–90. Available from: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1566982&tool=pmcentrez&rendertype=abstrac
13. Bela K, Horváth E, Gallé Á, Szabados L, Tari I, Csiszár J. Plant glutathione peroxidases: Emerging role of the antioxidant enzymes in plant development and stress responses. J Plant Physiol [Internet]. Elsevier GmbH.; 2015;176:192–201. Available from: http://linkinghub.elsevier.com/retrieve/pii/S017616171500005
14. Xia X, Zheng J, Shao G, Wang J, Liu X, Wang Y. Cloning and functional analysis of glutathione peroxidase gene in red swamp cray fi sh Procambarus clarkii. Fish Shellfish Immunol [Internet]. Elsevier Ltd; 2013;34(6):1587–95. Available from: http://dx.doi.org/10.1016/j.fsi.2013.03.375
15. Brigelius-Flohé R, Maiorino M. Glutathione peroxidases. Biochim Biophys Acta - Gen Subj [Internet]. Elsevier B.V.; 2013;1830(5):3289–303. Available from: http://linkinghub.elsevier.com/retrieve/pii/S030441651200340
16. Herbette S, Roeckel-Drevet P, Drevet JR. Seleno-independent glutathione peroxidases. FEBS J [Internet]. 2007;274(9):2163–80. Available from: http://doi.wiley.com/10.1111/j.1742-4658.2007.05774.
17. Margis R, Dunand C, Teixeira FK, Margis-Pinheiro M. Glutathione peroxidase family - An evolutionary overview. FEBS J. 2008;275(15):3959–70.
18. Sen K, Podder S, Ghosh TC. Insights into the genomic features and evolutionary impact of the genes configuring duplicated pseudogenes in human. FEBS Lett [Internet]. Federation of European Biochemical Societies; 2010;584(18):4015–8. Available from: http://www.ncbi.nlm.nih.gov/pubmed/2070861
19. Chen SM, Ma KY, Zeng J. Pseudogene: Lessons from PCR bias, identification and resurrection. Mol Biol Rep. 2011;38:3709–15. 20. Li W, Yang W, Wang X-J. Pseudogenes: Pseudo or Real Functional Elements? J Genet Genomics [Internet]. Elsevier Limited and Science Press; 2013;40(4):171–7. Available from: http://www.sciencedirect.com/science/article/pii/S167385271300056