M
Marla J. Berry
Researcher at University of Hawaii at Manoa
Publications - 145
Citations - 12166
Marla J. Berry is an academic researcher from University of Hawaii at Manoa. The author has contributed to research in topics: Selenoprotein & Selenocysteine. The author has an hindex of 52, co-authored 140 publications receiving 11062 citations. Previous affiliations of Marla J. Berry include University of Hawaii & Harvard University.
Papers
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Journal ArticleDOI
Selenium and selenoproteins in the brain and brain diseases
Jun Chen,Marla J. Berry +1 more
TL;DR: Recent studies in cell culture and gene knockout models support a function for selenoprotein P in delivery of selenium to the brain, reported to possess antioxidant activities and the ability to promote neuronal cell survival.
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Regulation and function of selenoproteins in human disease
TL;DR: Selenoproteins are proteins containing selenium in the form of the 21st amino acid, selenocysteine, which has roles in a variety of cell processes and diseases.
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Decoding apparatus for eukaryotic selenocysteine insertion
Rosa M. Tujebajeva,Paul R. Copeland,Xue Ming Xu,Bradley A. Carlson,John W. Harney,Donna M. Driscoll,Dolph L. Hatfield,Marla J. Berry +7 more
TL;DR: expression of the two functional domains of the bacterial elongation factor–SECIS binding protein as two separate proteins in eukaryotes suggests a mechanism for rapid exchange of charged for uncharged selenocysteyl‐tRNA–elongation factor complex, allowing a single SECIS element to serve multiple UGA codons.
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Biosynthesis of selenocysteine on its tRNA in eukaryotes.
Xue-Ming Xu,Bradley A. Carlson,Heiko Mix,Yan Zhang,Kazima Saira,Richard S. Glass,Marla J. Berry,Vadim N. Gladyshev,Dolph L. Hatfield +8 more
TL;DR: Comparative genomics and experimental analyses revealed that the mammalian Sec synthase (SecS) is the previously identified pyridoxal phosphate-containing protein known as the soluble liver antigen.
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Translational termination efficiency in mammals is influenced by the base following the stop codon
TL;DR: Data suggest that the base following the stop codon influences translational termination efficiency as part of a larger termination signal in the expression of mammalian genes.