Zobrazeno 1 - 10
of 75
pro vyhledávání: '"Paul R, Copeland"'
Publikováno v:
PLoS ONE, Vol 17, Iss 7, p e0271453 (2022)
Selenoproteins contain the 21st amino acid, selenocysteine (Sec), which is incorporated at select UGA codons when a specialized hairpin sequence, the Sec insertion sequence (SECIS) element, is present in the 3' UTR. Aside from the SECIS, selenoprotei
Externí odkaz:
https://doaj.org/article/86a551bf86584cd4adc10d9c6ba77498
Autor:
Paul R. Copeland, Michael T. Howard
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 24, p 13204 (2021)
Decoding of genetic information into polypeptides occurs during translation, generally following the codon assignment rules of the organism’s genetic code. However, recoding signals in certain mRNAs can overwrite the normal rules of translation. An
Externí odkaz:
https://doaj.org/article/d670704c8f7445b69cc005b1c6a8d510
Many of the proteins that contain the amino acid selenocysteine (Sec) are required for optimal defense against cellular stress. As such, one might expect selenoprotein synthesis to persist or be induced upon cellular insult. Because Sec is incorporat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2c673c67ded11b004693b3ac20da4a8b
https://doi.org/10.1101/2023.05.12.540527
https://doi.org/10.1101/2023.05.12.540527
Autor:
Malgorzata Dobosz-Bartoszek, Mark H. Pinkerton, Zbyszek Otwinowski, Srinivas Chakravarthy, Dieter Söll, Paul R. Copeland, Miljan Simonović
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Specialized translation elongation factors (eEFSec and SelB) promote selenocysteine incorporation into proteins. Here, the authors report the structure of human eEFSec, examine its interactions with guanine nucleotides, and propose a non-canonical me
Externí odkaz:
https://doaj.org/article/1bc117eaac2c4b32ae01b3db056620d1
Autor:
Aditi Dubey, Paul R Copeland
Publikováno v:
PLoS ONE, Vol 11, Iss 11, p e0165642 (2016)
Selenocysteine (Sec) is a critical residue in at least 25 human proteins that are essential for antioxidant defense and redox signaling in cells. Sec is inserted into proteins cotranslationally by the recoding of an in-frame UGA termination codon to
Externí odkaz:
https://doaj.org/article/842dc742f11946649f1960cf0ba16e02
Autor:
Belinda Willard, Eric M. Cockman, Donna M. Driscoll, Sumangala P. Shetty, Vivek Narayan, Paul R. Copeland
Publikováno v:
RNA Biology
Selenoproteins are a unique class of proteins that contain the 21st amino acid, selenocysteine (Sec). Addition of Sec into a protein is achieved by recoding of the UGA stop codon. All 25 mammalian selenoprotein mRNAs possess a 3′ UTR stem-loop stru
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:
Sumangala P. Shetty, Paul R. Copeland
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1862:2506-2510
Background Selenoprotein synthesis requires the reinterpretation of a UGA stop codon as one that encodes selenocysteine (Sec), a process that requires a set of dedicated translation factors. Among the mammalian selenoproteins, Selenoprotein P (SELENO
Autor:
Mark H. Pinkerton, Paul R. Copeland
Publikováno v:
Encyclopedia of Biological Chemistry III ISBN: 9780128220405
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5a5309c6942c054b5eb9906cb972e22b
https://doi.org/10.1016/b978-0-12-809633-8.21357-5
https://doi.org/10.1016/b978-0-12-809633-8.21357-5
Selenoproteins contain the 21st amino acid, selenocysteine (Sec), which is incorporated at select UGA codons when a specialized hairpin sequence, the Sec insertion sequence (SECIS) element, is present in the 3’ UTR. Aside from the SECIS, selenoprot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b11fbe20c7f909aac4275d6bbce2b0e9
https://doi.org/10.1101/2020.11.23.394817
https://doi.org/10.1101/2020.11.23.394817