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    An expanded eukaryotic genetic code (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-16
    Description: We describe a general and rapid route for the addition of unnatural amino acids to the genetic code of Saccharomyces cerevisiae. Five amino acids have been incorporated into proteins efficiently and with high fidelity in response to the nonsense codon TAG. The side chains of these amino acids contain a keto group, which can be uniquely modified in vitro and in vivo with a wide range of chemical probes and reagents; a heavy atom-containing amino acid for structural studies; and photocrosslinkers for cellular studies of protein interactions. This methodology not only removes the constraints imposed by the genetic code on our ability to manipulate protein structure and function in yeast, it provides a gateway to the systematic expansion of the genetic codes of multicellular eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chin, Jason W -- Cropp, T Ashton -- Anderson, J Christopher -- Mukherji, Mridul -- Zhang, Zhiwen -- Schultz, Peter G -- GM 62159/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Aug 15;301(5635):964-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Skaggs Institute for Chemical Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12920298" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/*genetics/metabolism ; Anticodon ; Azides/metabolism ; *Codon, Nonsense ; Escherichia coli/enzymology/genetics ; *Genetic Code ; Humans ; Methyltyrosines/*genetics/metabolism ; Mutation ; Phenylalanine/*analogs & derivatives/genetics/metabolism ; Protein Biosynthesis ; RNA, Transfer/genetics/metabolism ; Saccharomyces cerevisiae/*genetics/metabolism ; Superoxide Dismutase/chemistry/genetics/metabolism ; Tyrosine-tRNA Ligase/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-24
    Description: Arabidopsis thaliana De-etiolated-1 (AtDET1) is a highly conserved protein, with orthologs in vertebrate and invertebrate organisms. AtDET1 negatively regulates photomorphogenesis, but its biochemical mechanism and function in other species are unknown. We report that human DET1 (hDET1) promotes ubiquitination and degradation of the proto-oncogenic transcription factor c-Jun by assembling a multisubunit ubiquitin ligase containing DNA Damage Binding Protein-1 (DDB1), cullin 4A (CUL4A), Regulator of Cullins-1 (ROC1), and constitutively photomorphogenic-1. Ablation of any subunit by RNA interference stabilized c-Jun and increased c-Jun-activated transcription. These findings characterize a c-Jun ubiquitin ligase and define a specific function for hDET1 in mammalian cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wertz, Ingrid E -- O'Rourke, Karen M -- Zhang, Zemin -- Dornan, David -- Arnott, David -- Deshaies, Raymond J -- Dixit, Vishva M -- GM065997/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1371-4. Epub 2004 Jan 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Oncology, Genentech, Inc., South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14739464" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cloning, Molecular ; Cullin Proteins/genetics/*metabolism ; DNA-Binding Proteins/metabolism ; Genes, jun ; Humans ; Molecular Sequence Data ; Nuclear Proteins/chemistry/genetics/metabolism ; Protein Binding ; Proteomics ; Proto-Oncogene Proteins c-jun/*metabolism ; RNA, Messenger/genetics/metabolism ; RNA, Small Interfering/metabolism ; Transfection ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/chemistry/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
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