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...
The Western Europe union :--Europe's security and defense identity /--by John W. Harney. (1994)
Typescript (photocopy)
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...
Curcio-Morelli, Cyntia, Zavacki, Ann Marie, Christofollete, Marcelo, Gereben, Balazs, De Freitas, Beatriz C.G., Harney, John W., ...
The type 2 iodothyronine deiodinase (D2) is an integral membrane ER-resident selenoenzyme that activates the pro-hormone thyroxine (T4) and supplies most of the 3,5,3′-triiodothyronine (T3) that is...
The type 2 iodothyronine deiodinase is essential for adaptive thermogenesis in brown adipose tissue
De Jesus, Lucia A., Carvalho, Suzy D., Ribeiro, Mirian O., Schneider, Mark, Kim, Sung-Woo, Harney, John W., ...
Type 2 iodothyronine deiodinase (D2) is a selenoenzyme, the product of the recently cloned cAMP-dependent Dio2 gene, which increases 10- to 50-fold during cold stress only in brown adipose tissue...
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...
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...
Type 2 iodothyronine deiodinase is the major source of plasma T3 in euthyroid humans
Maia, Ana Luiza, Kim, Brian W., Huang, Stephen A., Harney, John W., Larsen, P. Reed
The relative roles of the types 1 and 2 iodothyronine deiodinases (D1 and D2) in extrathyroidal 3,5,3′-triiodothyronine (T3) production in humans are unknown. We calculated the rate of thyroxine...
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...
Curcio-Morelli, Cyntia, Zavacki, Ann Marie, Christofollete, Marcelo, Gereben, Balazs, De Freitas, Beatriz C.G., Harney, John W., ...
The type 2 iodothyronine deiodinase (D2) is an integral membrane ER-resident selenoenzyme that activates the pro-hormone thyroxine (T4) and supplies most of the 3,5,3′-triiodothyronine (T3) that is...
The type 2 iodothyronine deiodinase is essential for adaptive thermogenesis in brown adipose tissue
De Jesus, Lucia A., Carvalho, Suzy D., Ribeiro, Mirian O., Schneider, Mark, Kim, Sung-Woo, Harney, John W., ...
Type 2 iodothyronine deiodinase (D2) is a selenoenzyme, the product of the recently cloned cAMP-dependent Dio2 gene, which increases 10- to 50-fold during cold stress only in brown adipose tissue...
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...
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...
Type 2 iodothyronine deiodinase is the major source of plasma T3 in euthyroid humans
Maia, Ana Luiza, Kim, Brian W., Huang, Stephen A., Harney, John W., Larsen, P. Reed
The relative roles of the types 1 and 2 iodothyronine deiodinases (D1 and D2) in extrathyroidal 3,5,3′-triiodothyronine (T3) production in humans are unknown. We calculated the rate of thyroxine...
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...
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,...
Sagar, G. D. Vivek, Gereben, Balázs, Callebaut, Isabelle, Mornon, Jean-Paul, Zeöld, Anikó, Da Silva, Wagner S., ...
Ubiquitination is a critical posttranslational regulator of protein stability and/or subcellular localization. Here we show that ubiquitination can also regulate proteins by transiently inactivating...