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  • 1
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    Intellectual property. Patents, secrecy, and DNA (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-07-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cook-Deegan, R M -- McCormack, S J -- New York, N.Y. -- Science. 2001 Jul 13;293(5528):217.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Kennedy Institute of Ethics, Georgetown University, Washington, DC 20057-1212, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11452101" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Biotechnology/legislation & jurisprudence ; *Dna ; Databases, Factual ; Genomics/legislation & jurisprudence ; Humans ; *Intellectual Property ; *Patents as Topic ; Truth Disclosure
    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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    Coupled transcription and translation within nuclei of mammalian cells (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-06-26
    Description: It is widely assumed that the vital processes of transcription and translation are spatially separated in eukaryotes and that no translation occurs in nuclei. We localized translation sites by incubating permeabilized mammalian cells with [3H]lysine or lysyl-transfer RNA tagged with biotin or BODIPY; although most nascent polypeptides were cytoplasmic, some were found in discrete nuclear sites known as transcription "factories." Some of this nuclear translation also depends on concurrent transcription by RNA polymerase II. This coupling is simply explained if nuclear ribosomes translate nascent transcripts as those transcripts emerge from still-engaged RNA polymerases, much as they do in bacteria.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Iborra, F J -- Jackson, D A -- Cook, P R -- New York, N.Y. -- Science. 2001 Aug 10;293(5532):1139-42. Epub 2001 Jun 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11423616" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoradiography ; Biotin/metabolism ; Boron Compounds/metabolism ; COS Cells ; Cell Fractionation ; Cell Membrane Permeability ; Cell Nucleus/*genetics/metabolism ; Cycloheximide/pharmacology ; Cytoplasm/metabolism ; Fluorescence ; HeLa Cells ; Humans ; Immunohistochemistry ; Mitochondria/metabolism ; *Protein Biosynthesis ; Protein Synthesis Inhibitors/pharmacology ; Protein Transport ; Proteins/metabolism ; RNA Polymerase II/metabolism ; RNA, Transfer, Amino Acyl/metabolism ; Ribosomes/metabolism ; *Transcription, Genetic ; Tumor Cells, Cultured
    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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  • 3
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    Human PAD4 regulates histone arginine methylation levels via demethylimination (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-04
    Description: Methylation of arginine (Arg) and lysine residues in histones has been correlated with epigenetic forms of gene regulation. Although histone methyltransferases are known, enzymes that demethylate histones have not been identified. Here, we demonstrate that human peptidylarginine deiminase 4 (PAD4) regulates histone Arg methylation by converting methyl-Arg to citrulline and releasing methylamine. PAD4 targets multiple sites in histones H3 and H4, including those sites methylated by coactivators CARM1 (H3 Arg17) and PRMT1 (H4 Arg3). A decrease of histone Arg methylation, with a concomitant increase of citrullination, requires PAD4 activity in human HL-60 granulocytes. Moreover, PAD4 activity is linked with the transcriptional regulation of estrogen-responsive genes in MCF-7 cells. These data suggest that PAD4 mediates gene expression by regulating Arg methylation and citrullination in histones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Yanming -- Wysocka, Joanna -- Sayegh, Joyce -- Lee, Young-Ho -- Perlin, Julie R -- Leonelli, Lauriebeth -- Sonbuchner, Lakshmi S -- McDonald, Charles H -- Cook, Richard G -- Dou, Yali -- Roeder, Robert G -- Clarke, Steven -- Stallcup, Michael R -- Allis, C David -- Coonrod, Scott A -- DK55274/DK/NIDDK NIH HHS/ -- GM R01 26020/GM/NIGMS NIH HHS/ -- GM R01 50659/GM/NIGMS NIH HHS/ -- HD R01 38353/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 8;306(5694):279-83. Epub 2004 Sep 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetic Medicine, Weill Medical College of Cornell University, 1300 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15345777" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arginine/*metabolism ; Blotting, Western ; Calcimycin/pharmacology ; Cell Line, Tumor ; Citrulline/metabolism ; Gene Expression Regulation ; Genes, Reporter ; HL-60 Cells ; Histones/*metabolism ; Humans ; Hydrolases/*metabolism ; Ionophores/pharmacology ; Membrane Proteins/genetics ; Methylamines/metabolism ; Methylation ; Molecular Sequence Data ; Presenilin-2 ; Promoter Regions, Genetic ; Protein-Arginine N-Methyltransferases/metabolism ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/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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  • 4
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    Human amygdala responsivity to masked fearful eye whites (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-18
    Description: The amygdala was more responsive to fearful (larger) eye whites than to happy (smaller) eye whites presented in a masking paradigm that mitigated subjects' awareness of their presence and aberrant nature. These data demonstrate that the amygdala is responsive to elements of.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whalen, Paul J -- Kagan, Jerome -- Cook, Robert G -- Davis, F Caroline -- Kim, Hackjin -- Polis, Sara -- McLaren, Donald G -- Somerville, Leah H -- McLean, Ashly A -- Maxwell, Jeffrey S -- Johnstone, Tom -- 01866/PHS HHS/ -- 069315/PHS HHS/ -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2061.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, W. M. Keck Laboratory for Brain Imaging and Behavior, University of Wisconsin, Madison, WI, USA. pwhalen@wisc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604401" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amygdala/*physiology ; *Facial Expression ; *Fear ; Female ; Happiness ; Humans ; Magnetic Resonance Imaging ; Male ; Pattern Recognition, Visual ; Perceptual Masking ; *Sclera
    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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