Blauwkamp, Marsha N, Yu, Jingcheng, Schin, MaryLee A, Burke, Kathleen A, Berry, Marla J, Carlson, Bradley A, ...
Abstract Background Selenoproteins contain selenocysteine (Sec), commonly considered the 21 st genetically encoded amino acid. Many selenoproteins, such as the glutathione peroxidases and thioredoxin...
Xu, Xue-Ming, Carlson, Bradley A., Zhang, Yan, Mix, Heiko, Kryukov, Gregory V., Glass, Richard S., ...
We used comparative genomics and experimental analyses to show that (1) eukaryotes and archaea, which possess the selenocysteine (Sec) protein insertion machinery contain an enzyme,...
Biosynthesis of Selenocysteine on Its tRNA in Eukaryotes (2007)
Xu, Xue-Ming, Carlson, Bradley A., Mix, Heiko, Zhang, Yan, Saira, Kazima, Glass, Richard S., ...
Selenocysteine (Sec) is cotranslationally inserted into protein in response to UGA codons and is the 21st amino acid in the genetic code. However, the means by which Sec is synthesized in eukaryotes...
Biosynthesis of Selenocysteine on Its tRNA in Eukaryotes (2007)
Xue-Ming Xu, Bradley A. Carlson, Heiko Mix, Yan Zhang, Kazima Saira, Richard S. Glass, ...
Selenocysteine (Sec) is cotranslationally inserted into protein in response to UGA codons and is the 21st amino acid in the genetic code. However, the means by which Sec is synthesized in eukaryotes...
"Preface" to Selenium: Its Molecular Biology and Role in Human Health, Second Edition (2006)
Hatfield, Dolph L., Berry, Marla J., Gladyshev, Vadim N.
The purpose of the new edition book is to inform the reader of many new discoveries and to examine our present knowledge of the molecular biology of selenium, its incorporation into proteins as...
Xu, Xue-Ming, Mix, Heiko, Carlson, Bradley A., Grabowski, Paula J., Gladyshev, Vadim N., Berry, Marla J., ...
Selenocysteine (Sec) is inserted into selenoproteins co-translationally with the help of various cis- and trans-acting factors. The specific mechanisms of Sec biosynthesis and insertion into protein...
The responses of Ht22 cells to oxidative stress induced by buthionine sulfoximine (BSO) (2005)
Chen, Jun, Small-Howard, Andrea, Yin, Amy, Berry, Marla J
Abstract Background glutathione (GSH) is the most abundant thiol antioxidant in mammalian cells. It directly reacts with reactive oxygen species (ROS), functions as a cofactor of antioxidant enzymes,...
Identification and characterization of phosphoseryl-tRNA [Ser]Sec kinase (2004)
Carlson, Bradley A., Xu, Xue-Ming, Kryukov, Gregory V., Rao, Mahadev, Berry, Marla J., Gladyshev, Vadim N., ...
In 1970, a kinase activity that phosphorylated a minor species of seryl-tRNA to form phosphoseryl-tRNA was found in rooster liver [Maenpaa, P. H. & Bernfield, M. R. (1970) Proc. Natl. Acad. Sci. USA...
Moustafa, Mohamed E., Carlson, Bradley A., El-Saadani, Muhammed A., Kryukov, Gregory V., Sun, Qi-An, Harney, John W., ...
Selenocysteine (Sec) tRNA (tRNA [Ser]Sec) serves as both the site of Sec biosynthesis and the adapter molecule for donation of this amino acid to protein. The consequences on selenoprotein...
Moustafa, Mohamed E., Carlson, Bradley A., El-Saadani, Muhammad A., Kryukov, Gregory V., Sun, Qi-An, Harney, John W., ...
Selenocysteine (Sec) tRNA (tRNA[Ser]Sec) serves as both the site of Sec biosynthesis and the adapter molecule for donation of this amino acid to protein. The consequences on selenoprotein...
SECIS–SBP2 interactions dictate selenocysteine incorporation efficiency and selenoprotein hierarchy
Low, Susan C., Grundner-Culemann, Elisabeth, Harney, John W., Berry, Marla J.
Selenocysteine incorporation at UGA codons requires cis-acting mRNA secondary structures and several specialized trans-acting factors. The latter include a selenocysteine-specific tRNA, an elongation...
Identification and characterization of phosphoseryl-tRNA[Ser]Sec kinase
Carlson, Bradley A., Xu, Xue-Ming, Kryukov, Gregory V., Rao, Mahadev, Berry, Marla J., Gladyshev, Vadim N., ...
In 1970, a kinase activity that phosphorylated a minor species of seryl-tRNA to form phosphoseryl-tRNA was found in rooster liver [Maenpaa, P. H. & Bernfield, M. R. (1970) Proc. Natl. Acad. Sci. USA...
In silico identification of novel selenoproteins in the Drosophila melanogaster genome
Castellano, Sergi, Morozova, Nadya, Morey, Marta, Berry, Marla J., Serras, Florenci, Corominas, Montserrat, ...
In selenoproteins, incorporation of the amino acid selenocysteine is specified by the UGA codon, usually a stop signal. The alternative decoding of UGA is conferred by an mRNA structure, the SECIS...
Decoding apparatus for eukaryotic selenocysteine insertion
Tujebajeva, Rosa M., Copeland, Paul R., Xu, Xue-Ming, Carlson, Bradley A., Harney, John W., Driscoll, Donna M., ...
Decoding UGA as selenocysteine requires a unique tRNA, a specialized elongation factor, and specific secondary structures in the mRNA, termed SECIS elements. Eukaryotic SECIS elements are found in...
De Jesus, Lucia A., Hoffmann, Peter R., Michaud, Tanya, Forry, Erin P., Small-Howard, Andrea, Stillwell, Robert J., ...
Recoding of UGA from a stop codon to selenocysteine poses a dilemma for the protein translation machinery. In eukaryotes, two factors that are crucial to this recoding process are the mRNA binding...
Supramolecular Complexes Mediate Selenocysteine Incorporation In Vivo
Small-Howard, Andrea, Morozova, Nadya, Stoytcheva, Zoia, Forry, Erin P., Mansell, John B., Harney, John W., ...
Selenocysteine incorporation in eukaryotes occurs cotranslationally at UGA codons via the interactions of RNA-protein complexes, one comprised of selenocysteyl (Sec)-tRNA[Ser]Sec and its specific...
Moustafa, Mohamed E., Carlson, Bradley A., El-Saadani, Muhammad A., Kryukov, Gregory V., Sun, Qi-An, Harney, John W., ...
Selenocysteine (Sec) tRNA (tRNA[Ser]Sec) serves as both the site of Sec biosynthesis and the adapter molecule for donation of this amino acid to protein. The consequences on selenoprotein...
SECIS–SBP2 interactions dictate selenocysteine incorporation efficiency and selenoprotein hierarchy
Low, Susan C., Grundner-Culemann, Elisabeth, Harney, John W., Berry, Marla J.
Selenocysteine incorporation at UGA codons requires cis-acting mRNA secondary structures and several specialized trans-acting factors. The latter include a selenocysteine-specific tRNA, an elongation...
Identification and characterization of phosphoseryl-tRNA[Ser]Sec kinase
Carlson, Bradley A., Xu, Xue-Ming, Kryukov, Gregory V., Rao, Mahadev, Berry, Marla J., Gladyshev, Vadim N., ...
In 1970, a kinase activity that phosphorylated a minor species of seryl-tRNA to form phosphoseryl-tRNA was found in rooster liver [Maenpaa, P. H. & Bernfield, M. R. (1970) Proc. Natl. Acad. Sci. USA...
In silico identification of novel selenoproteins in the Drosophila melanogaster genome
Castellano, Sergi, Morozova, Nadya, Morey, Marta, Berry, Marla J., Serras, Florenci, Corominas, Montserrat, ...
In selenoproteins, incorporation of the amino acid selenocysteine is specified by the UGA codon, usually a stop signal. The alternative decoding of UGA is conferred by an mRNA structure, the SECIS...
Decoding apparatus for eukaryotic selenocysteine insertion
Tujebajeva, Rosa M., Copeland, Paul R., Xu, Xue-Ming, Carlson, Bradley A., Harney, John W., Driscoll, Donna M., ...
Decoding UGA as selenocysteine requires a unique tRNA, a specialized elongation factor, and specific secondary structures in the mRNA, termed SECIS elements. Eukaryotic SECIS elements are found in...
De Jesus, Lucia A., Hoffmann, Peter R., Michaud, Tanya, Forry, Erin P., Small-Howard, Andrea, Stillwell, Robert J., ...
Recoding of UGA from a stop codon to selenocysteine poses a dilemma for the protein translation machinery. In eukaryotes, two factors that are crucial to this recoding process are the mRNA binding...
Supramolecular Complexes Mediate Selenocysteine Incorporation In Vivo
Small-Howard, Andrea, Morozova, Nadya, Stoytcheva, Zoia, Forry, Erin P., Mansell, John B., Harney, John W., ...
Selenocysteine incorporation in eukaryotes occurs cotranslationally at UGA codons via the interactions of RNA-protein complexes, one comprised of selenocysteyl (Sec)-tRNA[Ser]Sec and its specific...
Biosynthesis of Selenocysteine on Its tRNA in Eukaryotes
Xu, Xue-Ming, Carlson, Bradley A, Mix, Heiko, Zhang, Yan, Saira, Kazima, Glass, Richard S, ...
Selenocysteine (Sec) is cotranslationally inserted into protein in response to UGA codons and is the 21st amino acid in the genetic code. However, the means by which Sec is synthesized in eukaryotes...
Ben Jilani, Kamel E., Panee, Jun, He, Qingping, Berry, Marla J., Li, Ping-An
Selenoproteins have been shown to exhibit a variety of biological functions, including antioxidant functions, maintaining cellular redox balance, and heavy metal detoxification. UV...
Stoytcheva, Zoia, Tujebajeva, Rosa M., Harney, John W., Berry, Marla J.
Selenocysteine is incorporated into proteins via “recoding” of UGA from a stop codon to a sense codon, a process that requires specific secondary structures in the 3′ untranslated region,...
Hoffmann, Peter R., Höge, Simone C., Li, Ping-An, Hoffmann, Fukun W., Hashimoto, Ann C., Berry, Marla J.
Selenoprotein P (Sel P) is a selenium-rich glycoprotein believed to play a key role in selenium (Se) transport throughout the body. Development of a Sel P knockout mouse model has supported this...
Panee, Jun, Liu, Wanyu, Nakamura, Kyoko, Berry, Marla J.
Mitochondria are the major reactive oxygen species (ROS) – generating sites in mammalian cells. Blockade of complexes in the electron transport chain (ETC) increases the leakage of single electrons...
SelenoDB 1.0 : a database of selenoprotein genes, proteins and SECIS elements
Castellano, Sergi, Gladyshev, Vadim N., Guigó, Roderic, Berry, Marla J.
Selenoproteins are a diverse group of proteins usually misidentified and misannotated in sequence databases. The presence of an in-frame UGA (stop) codon in the coding sequence of selenoprotein genes...
Squires, Jeffrey E., Stoytchev, Ilko, Forry, Erin P., Berry, Marla J.
Selenoprotein mRNAs are potential targets for degradation via nonsense-mediated decay due to the presence of in-frame UGA codons that can be decoded as either selenocysteine or termination codons....