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  • Mutation  (595)
  • American Association for the Advancement of Science (AAAS)  (595)
  • Nature Publishing Group
  • Wiley
  • 1995-1999  (595)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (595)
  • Nature Publishing Group
  • Wiley
  • Springer  (38)
  • Wiley-Blackwell  (7)
Years
Year
  • 11
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    BSE and prions: uncertainties about the agent (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chesebro, B -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):42-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Persistent Virus Diseases, Rocky Mountain Laboratories, Hamilton, MT 59840, USA. bchesebro@nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9441410" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid/chemistry ; Amyloidosis/metabolism ; Animals ; Cattle ; Creutzfeldt-Jakob Syndrome/epidemiology/*etiology/transmission ; Disease Susceptibility ; Encephalopathy, Bovine Spongiform/epidemiology/*etiology/transmission ; Gene Expression ; Great Britain/epidemiology ; Humans ; Mice ; Mice, Transgenic ; Mutation ; Prion Diseases/*etiology/transmission ; Prions/chemistry/genetics/metabolism/*pathogenicity ; Virus Physiological Phenomena ; Viruses/pathogenicity
    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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  • 12
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    Direct phosphorylation of IkappaB by IKKalpha and IKKbeta: discrimination between free and NF-kappaB-bound substrate (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-08-28
    Description: A large protein complex mediates the phosphorylation of the inhibitor of kappaB (IkappaB), which results in the activation of nuclear factor kappaB (NF-kappaB). Two subunits of this complex, IkappaB kinase alpha (IKKalpha) and IkappaB kinase beta (IKKbeta), are required for NF-kappaB activation. Purified recombinant IKKalpha and IKKbeta expressed in insect cells were used to demonstrate that each protein can directly phosphorylate IkappaB proteins. IKKalpha and IKKbeta were found to form both homodimers and heterodimers. Both IKKalpha and IKKbeta phosphorylated IkappaB bound to NF-kappaB more efficiently than they phosphorylated free IkappaB. This result explains how free IkappaB can accumulate in cells in which IKK is still active and thus can contribute to the termination of NF-kappaB activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zandi, E -- Chen, Y -- Karin, M -- AI 43477/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Aug 28;281(5381):1360-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Gene Regulation and Signal Transduction, Department of Pharmacology, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9721103" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Dimerization ; Enzyme Activation ; HeLa Cells ; Helix-Loop-Helix Motifs ; Humans ; I-kappa B Kinase ; Leucine Zippers ; Mutation ; NF-kappa B/antagonists & inhibitors/*metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism ; Spodoptera ; Transcription Factor RelB ; *Transcription Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 13
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    Worming secrets from the C. elegans genome (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-01-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1998 Dec 11;282(5396):1972-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9874643" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/cytology/*genetics/physiology ; Cell Lineage ; Chromosome Mapping ; DNA, Helminth/chemistry/genetics ; Evolution, Molecular ; Gene Expression Regulation ; *Genes, Helminth ; Genetic Techniques ; *Genome ; Humans ; Mutation ; *Sequence Analysis, DNA
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 14
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    Yeast Ku as a regulator of chromosomal DNA end structure (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: During telomere replication in yeast, chromosome ends acquire an S-phase-specific overhang of the guanosine-rich strand. Here it is shown that in cells lacking Ku, a heterodimeric protein involved in nonhomologous DNA end joining, these overhangs are present throughout the cell cycle. In vivo cross-linking experiments demonstrated that Ku is bound to telomeric DNA. These results show that Ku plays a direct role in establishing a normal DNA end structure on yeast chromosomes, conceivably by functioning as a terminus-binding factor. Because Ku-mediated DNA end joining involving telomeres would result in chromosome instability, our data also suggest that Ku has a distinct function when bound to telomeres.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gravel, S -- Larrivee, M -- Labrecque, P -- Wellinger, R J -- New York, N.Y. -- Science. 1998 May 1;280(5364):741-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement de Microbiologie et Infectiologie, Faculte de Medecine, Universite de Sherbrooke, 3001 12th Avenue Nord, Sherbrooke, Quebec QC J1H 5N4, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9563951" target="_blank"〉PubMed〈/a〉
    Keywords: *Antigens, Nuclear ; Binding Sites ; Chromosomes, Fungal/chemistry/*metabolism ; *DNA Helicases ; DNA, Fungal/chemistry/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Fungal Proteins/*metabolism ; G2 Phase ; Genes, Fungal ; Mitosis ; Mutation ; Nuclear Proteins/genetics/*metabolism ; S Phase ; Saccharomyces cerevisiae/cytology/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Telomerase/genetics/metabolism ; Telomere/*metabolism ; Temperature ; Transformation, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 15
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    Arabidopsis NPH1: a flavoprotein with the properties of a photoreceptor for phototropism (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-30
    Description: The NPH1 gene of Arabidopsis thaliana encodes a 120-kilodalton serine-threonine protein kinase hypothesized to function as a photoreceptor for phototropism. When expressed in insect cells, the NPH1 protein is phosphorylated in response to blue light irradiation. The biochemical and photochemical properties of the photosensitive protein reflect those of the native protein in microsomal membranes. Recombinant NPH1 noncovalently binds flavin mononucleotide, a likely chromophore for light-dependent autophosphorylation. The fluorescence excitation spectrum of the recombinant protein is similar to the action spectrum for phototropism, consistent with the conclusion that NPH1 is an autophosphorylating flavoprotein photoreceptor mediating phototropic responses in higher plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Christie, J M -- Reymond, P -- Powell, G K -- Bernasconi, P -- Raibekas, A A -- Liscum, E -- Briggs, W R -- New York, N.Y. -- Science. 1998 Nov 27;282(5394):1698-701.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Biology, Carnegie Institution of Washington, 260 Panama Street, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9831559" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arabidopsis/genetics/*physiology ; *Arabidopsis Proteins ; Cell Line ; Cryptochromes ; *Drosophila Proteins ; *Eye Proteins ; Flavin Mononucleotide/metabolism ; Flavoproteins/physiology ; Genes, Plant ; Light ; Mutation ; Phosphoproteins/genetics/*metabolism ; Phosphorylation ; *Photoreceptor Cells, Invertebrate ; *Phototropism ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Receptors, G-Protein-Coupled ; Recombinant Proteins/metabolism ; Spectrometry, Fluorescence ; Spodoptera ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 16
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    More deafness genes (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steel, K P -- Brown, S D -- New York, N.Y. -- Science. 1998 May 29;280(5368):1403.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council, Institute of Hearing Research, University Park, Nottingham NG7 2RD, UK. karen@ihr.mrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9634418" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/physiology ; Animals ; Cilia/physiology ; Deafness/*genetics ; Dyneins ; Extracellular Matrix Proteins/*genetics/physiology ; GPI-Linked Proteins ; Hair Cells, Auditory/physiology/ultrastructure ; Hearing ; Humans ; Membrane Glycoproteins/*genetics/physiology ; Mice ; Mice, Mutant Strains ; Mutation ; Myosin Heavy Chains/genetics/physiology ; Myosins/*genetics/physiology ; Tectorial Membrane/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
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    How the genome readies itself for evolution (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1998 Aug 21;281(5380):1131,1133-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9735027" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA Repair ; DNA Transposable Elements ; *Evolution, Molecular ; Exons ; Gene Rearrangement ; *Genome ; Humans ; Micronuclei, Chromosome-Defective/genetics ; Multigene Family ; Mutation ; Plants/genetics ; Repetitive Sequences, Nucleic Acid
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 18
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    RNAi in C. elegans: soaking in the genome sequence (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tabara, H -- Grishok, A -- Mello, C C -- DK32520-15/DK/NIDDK NIH HHS/ -- R01 HD33769-01/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 16;282(5388):430-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9841401" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*genetics ; *Gene Expression Regulation ; *Genes, Helminth ; Mutation ; Phenotype ; RNA, Antisense/*genetics ; RNA, Double-Stranded/genetics ; RNA, Helminth/*genetics ; RNA, Messenger/genetics ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
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    An essential role for ectodomain shedding in mammalian development (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-13
    Description: The ectodomains of numerous proteins are released from cells by proteolysis to yield soluble intercellular regulators. The responsible protease, tumor necrosis factor-alpha converting enzyme (TACE), has been identified only in the case when tumor necrosis factor-alpha (TNFalpha) is released. Analyses of cells lacking this metalloproteinase-disintegrin revealed an expanded role for TACE in the processing of other cell surface proteins, including a TNF receptor, the L-selectin adhesion molecule, and transforming growth factor-alpha (TGFalpha). The phenotype of mice lacking TACE suggests an essential role for soluble TGFalpha in normal development and emphasizes the importance of protein ectodomain shedding in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peschon, J J -- Slack, J L -- Reddy, P -- Stocking, K L -- Sunnarborg, S W -- Lee, D C -- Russell, W E -- Castner, B J -- Johnson, R S -- Fitzner, J N -- Boyce, R W -- Nelson, N -- Kozlosky, C J -- Wolfson, M F -- Rauch, C T -- Cerretti, D P -- Paxton, R J -- March, C J -- Black, R A -- CA43793/CA/NCI NIH HHS/ -- DK53804/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 13;282(5392):1281-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Corporation, Seattle, WA 98101, USA. peschon@immunex.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9812885" target="_blank"〉PubMed〈/a〉
    Keywords: ADAM Proteins ; Amino Acid Sequence ; Animals ; Catalytic Domain ; Cell Membrane/*metabolism ; Cells, Cultured ; Crosses, Genetic ; *Embryonic and Fetal Development ; L-Selectin/metabolism ; Ligands ; Membrane Proteins/*metabolism ; Metalloendopeptidases/chemistry/genetics/*metabolism ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; Phenotype ; Protein Processing, Post-Translational ; Receptors, Tumor Necrosis Factor/metabolism ; Transforming Growth Factor alpha/metabolism ; Tumor Necrosis Factor-alpha/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
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    Shifting RNA polymerase into overdrive (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-05-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Landick, R -- New York, N.Y. -- Science. 1999 Apr 23;284(5414):598-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bacteriology, University of Wisconsin-Madison, Madison, WI 53706, USA. landick@macc.wisc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10328742" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Binding Sites ; DNA/chemistry/*metabolism ; DNA-Directed RNA Polymerases/genetics/*metabolism ; Escherichia coli/enzymology/genetics ; Gene Expression Regulation ; Humans ; Models, Genetic ; Mutation ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides, Antisense/chemistry/metabolism ; RNA, Messenger/chemistry/*metabolism ; *Terminator Regions, Genetic ; *Transcription, Genetic ; Viral 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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