about
Making sense of nonsense: the evolution of selenocysteine usage in proteins.Characterization of the SECIS binding protein 2 complex required for the co-translational insertion of selenocysteine in mammalsThe molecular biology of selenocysteineSelenocysteine incorporation: A trump card in the game of mRNA decayThe selenocysteine-specific elongation factor contains a novel and multi-functional domainCrystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation.Efficiency of mammalian selenocysteine incorporation.Threading the needle: getting selenocysteine into proteinsMechanism and regulation of selenoprotein synthesis.The efficiency of selenocysteine incorporation is regulated by translation initiation factors.Regulation of selenocysteine incorporation into the selenium transport protein, selenoprotein P.Selenocysteine insertion sequence binding protein 2L is implicated as a novel post-transcriptional regulator of selenoprotein expression.Structural asymmetry of the terminal catalytic complex in selenocysteine synthesisRegulation of gene expression by stop codon recoding: selenocysteine.Selenocysteine insertion sequence (SECIS)-binding protein 2 alters conformational dynamics of residues involved in tRNA accommodation in 80 S ribosomes.The L7Ae RNA binding motif is a multifunctional domain required for the ribosome-dependent Sec incorporation activity of Sec insertion sequence binding protein 2.The Selenocysteine-Specific Elongation Factor Contains Unique Sequences That Are Required for Both Nuclear Export and Selenocysteine Incorporation.Genome-wide screen of Saccharomyces cerevisiae null allele strains identifies genes involved in selenomethionine resistance.Selenoprotein expression is regulated at multiple levels in prostate cells.Reconstitution of selenocysteine incorporation reveals intrinsic regulation by SECIS elements.Functional analysis of the interplay between translation termination, selenocysteine codon context, and selenocysteine insertion sequence-binding protein 2.Evolutionary history of selenocysteine incorporation from the perspective of SECIS binding proteinsA novel protein domain induces high affinity selenocysteine insertion sequence binding and elongation factor recruitment.Eukaryotic polyribosome profile analysis.Analysis of Saccharomyces cerevisiae null allele strains identifies a larger role for DNA damage versus oxidative stress pathways in growth inhibition by selenium.Purification and analysis of selenocysteine insertion sequence-binding protein 2.Selenoprotein Gene Nomenclature.Uptake and Utilization of Selenium from Selenoprotein P.The utilization of selenocysteine-tRNA[Ser]Sec isoforms is regulated in part at the level of translation in vitro.The Selenium Transport Protein, Selenoprotein P, Requires Coding Sequence Determinants to Promote Efficient Selenocysteine IncorporationEukaryotic Mechanisms of Selenocysteine Incorporation and Its Reconstitution In VitroA Ribosomal Perspective on the Mechanism of Selenocysteine IncorporationMolecular Mechanism of Eukaryotic Selenocysteine IncorporationA birth-to-death view of mRNA from the RNA recognition motif perspectiveErratum: Selenoprotein expression is regulated at multiple levels in prostate cellsSECIS binding proteins and eukaryotic selenoprotein synthesisSECIS binding proteinsPurification, Redox Sensitivity, and RNA Binding Properties of SECIS-binding Protein 2, a Protein Involved in Selenoprotein BiosynthesisProcessive incorporation of multiple selenocysteine residues is driven by a novel feature of the selenocysteine insertion sequenceGained in translation: The power of digging deep into disease models
P50
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P50
description
hulumtues
@sq
onderzoeker
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researcher
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հետազոտող
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name
Paul R. Copeland
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Paul R. Copeland
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Paul R. Copeland
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Paul R. Copeland
@nl
Paul R. Copeland
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type
label
Paul R. Copeland
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Paul R. Copeland
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Paul R. Copeland
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Paul R. Copeland
@nl
Paul R. Copeland
@sl
prefLabel
Paul R. Copeland
@ast
Paul R. Copeland
@en
Paul R. Copeland
@es
Paul R. Copeland
@nl
Paul R. Copeland
@sl
P106
P108
P1153
7006303199
P21
P31
P496
0000-0003-3343-0587