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Bradley A. Carlson
Researcher at National Institutes of Health
Publications - 167
Citations - 10795
Bradley A. Carlson is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Selenoprotein & Selenocysteine. The author has an hindex of 54, co-authored 163 publications receiving 9665 citations. Previous affiliations of Bradley A. Carlson include University of Nebraska–Lincoln.
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Journal Article
Flavopiridol Induces G1 Arrest with Inhibition of Cyclin-dependent Kinase (CDK) 2 and CDK4 in Human Breast Carcinoma Cells
TL;DR: Inhibition of the CDK4 and/or CDK2 kinase activity by Flavopiridol can account for the G1 arrest observed after exposure to FlavopIRidol.
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Selenium and selenocysteine: roles in cancer, health, and development
TL;DR: By the mid-1990s selenium emerged as one of the most promising cancer chemopreventive agents, but subsequent human clinical trials yielded contradictory results, however, basic research on Selenium continued to move at a rapid pace, elucidating its many roles in health, development, and in cancer prevention and promotion.
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A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs
TL;DR: It is established that SBP2 is essential for the co‐translational insertion of Sec into selenoproteins and hypothesize that the binding activity of SBp2 may be involved in preventing termination at the UGA/Sec codon.
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Potent Inhibition of Cdc2 Kinase Activity by the Flavonoid L86-8275
TL;DR: L86-8275 directly inhibits immunoprecipitated Cdc2 kinase activity from G2/M synchronized MDA-MB-468 breast carcinoma cells and is at least 250-fold more potent than either quercetin or genistein.
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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.