Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Michael B. Vetick"'
Publikováno v:
Life Science Alliance. 5:e202101291
The dietary requirement for selenium is based on its incorporation into selenoproteins, which contain the amino acid selenocysteine (Sec). The Sec insertion sequence (SECIS) is an RNA structure found in the 3′ UTR of all selenoprotein mRNAs, and it
Publikováno v:
Journal of Biological Chemistry. 293:19377-19386
RNA stem loop structures have been frequently shown to regulate essential cellular processes. The selenocysteine insertion sequence (SECIS) element, found in the 3′ UTRs of all selenoprotein mRNAs, is an example of such a structure, as it is requir
Autor:
Didac Santesmasses, Janinah Baclaocos, Rob McAllen, Paul R. Copeland, Marco Mariotti, Michael B. Vetick, Sharon A. Lynch, John J. Mackrill, John F. Atkins, Gary Loughran, Katarzyna Bierla, Roderic Guigó, Joanna Szpunar, Vadim N. Gladyshev
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2019, 431, pp.4381-4407. ⟨10.1016/j.jmb.2019.08.007⟩
Recercat. Dipósit de la Recerca de Catalunya
instname
J Mol Biol
Journal of Molecular Biology, Elsevier, 2019, 431, pp.4381-4407. ⟨10.1016/j.jmb.2019.08.007⟩
Recercat. Dipósit de la Recerca de Catalunya
instname
J Mol Biol
Selenoproteins typically contain a single selenocysteine, the 21st amino acid, encoded by a context-redefined UGA. However, human selenoprotein P (SelenoP) has a redox-functioning selenocysteine in its N-terminal domain and nine selenium transporter-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e7588cfce6c657b22da0fc45af7865b
https://hal-univ-pau.archives-ouvertes.fr/hal-02282676
https://hal-univ-pau.archives-ouvertes.fr/hal-02282676
Autor:
Paul R. Copeland, Michael B. Vetick
Publikováno v:
Current Developments in Nutrition. 3:nzz044.OR11-01
OBJECTIVES: We have established a zebrafish model system that will allow unprecedented access to the role of selenoprotein function during development. The work described here focuses on a poorly characterized RNA binding protein that is similar to S