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  • Base Sequence
  • American Association for the Advancement of Science (AAAS)  (38)
  • American Meteorological Society
  • PANGAEA
  • 1995-1999  (38)
  • 1998  (38)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (38)
  • American Meteorological Society
  • PANGAEA
Years
  • 1995-1999  (38)
Year
  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-03-21
    Description: Mice homozygous for a disrupted allele of the mismatch repair gene Pms2 have a mutator phenotype. When this allele is crossed into quasi-monoclonal (QM) mice, which have a very limited B cell repertoire, homozygotes have fewer somatic mutations at the immunoglobulin heavy chain and lambda chain loci than do heterozygotes or wild-type QM mice. That is, mismatch repair seems to contribute to somatic hypermutation rather than stifling it. It is suggested that at immunoglobulin loci in hypermutable B cells, mismatched base pairs are "corrected" according to the newly synthesized DNA strand, thereby fixing incipient mutations instead of eliminating them.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cascalho, M -- Wong, J -- Steinberg, C -- Wabl, M -- 1R01 GM37699/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1207-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California, San Francisco, CA 94143-0670, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9469811" target="_blank"〉PubMed〈/a〉
    Keywords: *Adenosine Triphosphatases ; Alleles ; Amino Acid Sequence ; Animals ; B-Lymphocytes/immunology ; Base Composition ; Base Sequence ; Cloning, Molecular ; Crosses, Genetic ; *DNA Repair ; *DNA Repair Enzymes ; *DNA-Binding Proteins ; Female ; Gene Rearrangement ; *Genes, Immunoglobulin ; Heterozygote ; Immunoglobulin Heavy Chains/chemistry/genetics ; Immunoglobulin Variable Region/chemistry/*genetics ; Immunoglobulin lambda-Chains/chemistry/genetics ; Male ; Mice ; Mice, Knockout ; Molecular Sequence Data ; *Mutation ; Proteins/*genetics/physiology
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  • 2
    Publication Date: 1998-12-05
    Description: Group I introns possess a single active site that catalyzes the two sequential reactions of self-splicing. An RNA comprising the two domains of the Tetrahymena thermophila group I intron catalytic core retains activity, and the 5.0 angstrom crystal structure of this 247-nucleotide ribozyme is now described. Close packing of the two domains forms a shallow cleft capable of binding the short helix that contains the 5' splice site. The helix that provides the binding site for the guanosine substrate deviates significantly from A-form geometry, providing a tight binding pocket. The binding pockets for both the 5' splice site helix and guanosine are formed and oriented in the absence of these substrates. Thus, this large ribozyme is largely preorganized for catalysis, much like a globular protein enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Golden, B L -- Gooding, A R -- Podell, E R -- Cech, T R -- New York, N.Y. -- Science. 1998 Oct 9;282(5387):259-64.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309-0215, USA. bgolden@petunia.colorado.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9841391" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Pairing ; Base Sequence ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; Guanosine/metabolism ; Introns ; Magnesium/metabolism ; Manganese/metabolism ; *Models, Molecular ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Phosphates/metabolism ; RNA Splicing ; RNA, Catalytic/*chemistry/metabolism ; Tetrahymena thermophila/*genetics
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-09-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kyrpides, N C -- Ouzounis, C A -- New York, N.Y. -- Science. 1998 Sep 4;281(5382):1457.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9750114" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Genes, Archaeal ; Open Reading Frames ; Publishing/*standards ; *Review Literature as Topic ; Sequence Analysis, DNA/*standards
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-08-07
    Description: The red clover necrotic mosaic virus genome is composed of two single-stranded RNA components, RNA-1 and RNA-2. The viral capsid protein is translated from a subgenomic RNA (sgRNA) that is transcribed from genomic RNA-1. Here, a 34-nucleotide sequence in RNA-2 is shown to be required for transcription of sgRNA. Mutations that prevent base-pairing between the RNA-1 subgenomic promoter and the 34-nucleotide trans-activator prevent expression of a reporter gene. A model is proposed in which direct binding of RNA-2 to RNA-1 trans-activates sgRNA synthesis. This RNA-mediated regulation of transcription is unusual among RNA viruses, which typically rely on protein regulators.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sit, T L -- Vaewhongs, A A -- Lommel, S A -- New York, N.Y. -- Science. 1998 Aug 7;281(5378):829-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Pathology, North Carolina State University, Raleigh, NC 27695-7616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9694655" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; DNA, Complementary ; Gene Expression ; Genes, Reporter ; Green Fluorescent Proteins ; Luminescent Proteins/genetics ; Models, Genetic ; Molecular Sequence Data ; Mosaic Viruses/*genetics ; Mutation ; Nucleic Acid Conformation ; Promoter Regions, Genetic ; RNA, Double-Stranded/genetics/metabolism ; RNA, Messenger/biosynthesis/genetics ; RNA, Viral/biosynthesis/chemistry/*genetics ; Sequence Alignment ; *Transcriptional Activation
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-10-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1998 Sep 18;281(5384):1787-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9776677" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Ethnic Groups/genetics ; *Genetic Markers ; Genetic Predisposition to Disease ; *Genetic Techniques ; Genetic Variation ; *Genetics, Medical ; *Genome, Human ; Humans ; Point Mutation ; *Polymorphism, Genetic ; Recombination, Genetic
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-03-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Graves, B J -- New York, N.Y. -- Science. 1998 Feb 13;279(5353):1000-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Huntsman Cancer Institute, Department of Oncological Sciences, University of Utah, Salt Lake City, UT 84132, USA. graves@bioscience.utah.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9490475" target="_blank"〉PubMed〈/a〉
    Keywords: Ankyrins/chemistry ; Base Sequence ; Binding Sites ; DNA/chemistry/*metabolism ; DNA-Binding Proteins/*chemistry/*metabolism ; Dimerization ; GA-Binding Protein Transcription Factor ; Hydrogen Bonding ; Leucine Zippers ; Models, Molecular ; Protein Conformation ; Protein Structure, Secondary ; Transcription Factors/*chemistry/*metabolism ; Transcriptional Activation
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-03-28
    Description: The OxyR transcription factor is sensitive to oxidation and activates the expression of antioxidant genes in response to hydrogen peroxide in Escherichia coli. Genetic and biochemical studies revealed that OxyR is activated through the formation of a disulfide bond and is deactivated by enzymatic reduction with glutaredoxin 1 (Grx1). The gene encoding Grx1 is regulated by OxyR, thus providing a mechanism for autoregulation. The redox potential of OxyR was determined to be -185 millivolts, ensuring that OxyR is reduced in the absence of stress. These results represent an example of redox signaling through disulfide bond formation and reduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zheng, M -- Aslund, F -- Storz, G -- New York, N.Y. -- Science. 1998 Mar 13;279(5357):1718-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9497290" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Bacterial Proteins/genetics/metabolism ; Base Sequence ; Cysteine/metabolism ; *DNA-Binding Proteins ; Disulfides/*metabolism ; Escherichia coli/genetics/*metabolism ; Escherichia coli Proteins ; Gene Expression Regulation, Bacterial ; Glutaredoxins ; Glutathione/metabolism ; Glutathione Disulfide/metabolism ; Glutathione Reductase/metabolism ; Hydrogen Peroxide/*metabolism/pharmacology ; Molecular Sequence Data ; Oxidation-Reduction ; Oxidative Stress ; *Oxidoreductases ; Proteins/genetics/metabolism ; Repressor Proteins/genetics/*metabolism ; Signal Transduction ; Thioredoxins/metabolism ; Transcription Factors/genetics/*metabolism
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-10-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garber, K -- New York, N.Y. -- Science. 1998 Sep 18;281(5384):1788.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9776678" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromatography, High Pressure Liquid ; Databases, Factual ; *Genetic Markers ; Genetic Predisposition to Disease ; *Genetic Techniques ; *Genome, Human ; Humans ; National Institutes of Health (U.S.) ; Neoplasms/*genetics ; Point Mutation ; *Polymorphism, Genetic ; United States
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-08-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Normilw, D -- New York, N.Y. -- Science. 1998 Aug 7;281(5378):774-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9714680" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Artiodactyla/anatomy & histology/classification ; Base Sequence ; *Biological Evolution ; DNA/genetics ; Evolution, Molecular ; *Fossils ; *Mammals/anatomy & histology/classification/genetics ; Paleodontology ; Phylogeny ; Whales/anatomy & histology/classification
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-10-30
    Description: Many filamentous cyanobacteria grow as multicellular organisms that show a developmental pattern of single nitrogen-fixing heterocysts separated by approximately 10 vegetative cells. Overexpression of a 54-base-pair gene, patS, blocked heterocyst differentiation in Anabaena sp. strain PCC 7120. A patS null mutant showed an increased frequency of heterocysts and an abnormal pattern. Expression of a patS-gfp reporter was localized in developing proheterocysts. The addition of a synthetic peptide corresponding to the last five amino acids of PatS inhibited heterocyst development. PatS appears to control heterocyst pattern formation through intercellular signaling mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoon, H S -- Golden, J W -- GM36890/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 30;282(5390):935-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Texas A&M University, College Station, TX 77843-3258, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9794762" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anabaena/cytology/genetics/*growth & development/metabolism ; Bacterial Proteins/chemistry/genetics/*physiology ; Base Sequence ; Cosmids ; Culture Media ; Diffusion ; Genes, Bacterial ; Genes, Reporter ; Genetic Complementation Test ; Molecular Sequence Data ; Mutation, Missense ; Nitrates/metabolism ; Nitrogen Fixation ; Oligopeptides/pharmacology ; Peptide Fragments/pharmacology ; Phenotype ; Promoter Regions, Genetic ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transcription, Genetic
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-12-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amitai, M -- New York, N.Y. -- Science. 1998 Nov 20;282(5393):1436-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Compugen Ltd., Tel Aviv, Israel. mor@compugen.co.il〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9867651" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Databases, Factual ; *Markov Chains ; Molecular Sequence Data ; Platelet-Derived Growth Factor/chemistry/genetics ; Probability ; Proteins/*chemistry/genetics ; *Sequence Alignment ; Software
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  • 12
    Publication Date: 1998-08-14
    Description: Tumor necrosis factor-alpha (TNF-alpha) is a major mediator of both acute and chronic inflammatory responses in many diseases. Tristetraprolin (TTP), the prototype of a class of Cys-Cys-Cys-His (CCCH) zinc finger proteins, inhibited TNF-alpha production from macrophages by destabilizing its messenger RNA. This effect appeared to result from direct TTP binding to the AU-rich element of the TNF-alpha messenger RNA. TTP is a cytosolic protein in these cells, and its biosynthesis was induced by the same agents that stimulate TNF-alpha production, including TNF-alpha itself. These findings identify TTP as a component of a negative feedback loop that interferes with TNF-alpha production by destabilizing its messenger RNA. This pathway represents a potential target for anti-TNF-alpha therapies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carballo, E -- Lai, W S -- Blackshear, P J -- New York, N.Y. -- Science. 1998 Aug 14;281(5379):1001-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Office of Clinical Research and Laboratory of Signal Transduction, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9703499" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Base Sequence ; Biological Transport ; Cell Line ; Cell Nucleus/metabolism ; Chick Embryo ; Cytosol/metabolism ; *DNA-Binding Proteins ; Feedback ; Gene Expression Regulation ; Humans ; *Immediate-Early Proteins ; Lipopolysaccharides/pharmacology ; Macrophages/*physiology ; Mice ; Mice, Knockout ; Proteins/*physiology ; RNA Probes ; RNA, Messenger/chemistry/genetics/metabolism ; Transfection ; Tristetraprolin ; Tumor Necrosis Factor-alpha/antagonists & inhibitors/*biosynthesis/genetics ; *Zinc Fingers
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-06-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gavaghan, H -- New York, N.Y. -- Science. 1998 May 22;280(5367):1188.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9634397" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Biotechnology/*legislation & jurisprudence ; *European Union ; Genetic Engineering/*legislation & jurisprudence ; *Genome, Human ; Humans ; Internationality ; *Patents as Topic ; *Plants, Genetically Modified
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  • 14
    Publication Date: 1998-06-11
    Description: A human member of the immunoglobulin superfamily was shown to mediate entry of several alphaherpesviruses, including herpes simplex viruses (HSV) 1 and 2, porcine pseudorabies virus (PRV), and bovine herpesvirus 1 (BHV-1). This membrane glycoprotein is poliovirus receptor-related protein 1 (Prr1), designated here as HveC. Incubation of HSV-1 with a secreted form of HveC inhibited subsequent infection of a variety of cell lines, suggesting that HveC interacts directly with the virus. Poliovirus receptor (Pvr) itself mediated entry of PRV and BHV-1 but not of the HSV strains tested. HveC was expressed in human cells of epithelial and neuronal origin; it is the prime candidate for the coreceptor that allows both HSV-1 and HSV-2 to infect epithelial cells on mucosal surfaces and spread to cells of the nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geraghty, R J -- Krummenacher, C -- Cohen, G H -- Eisenberg, R J -- Spear, P G -- NS-30606/NS/NINDS NIH HHS/ -- NS-36731/NS/NINDS NIH HHS/ -- R01 AI 36293/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1618-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology-Immunology, Northwestern University Medical School, Chicago, IL 60611, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9616127" target="_blank"〉PubMed〈/a〉
    Keywords: Alphaherpesvirinae/*physiology ; Animals ; Base Sequence ; CHO Cells ; Cell Adhesion Molecules/genetics/*physiology ; Cells, Cultured ; Cricetinae ; Epithelial Cells/virology ; Gene Expression ; Herpesvirus 1, Bovine/physiology ; Herpesvirus 1, Human/*physiology ; Herpesvirus 1, Suid/physiology ; Herpesvirus 2, Human/*physiology ; Humans ; *Membrane Proteins ; Molecular Sequence Data ; Neurons/virology ; Polymerase Chain Reaction ; *Receptors, Virus ; Transfection ; Tumor Cells, Cultured ; Viral Envelope Proteins/metabolism
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-10-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wuethrich, B -- New York, N.Y. -- Science. 1998 Sep 25;281(5385):1980-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9767049" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Biological Evolution ; Female ; Genome, Human ; Humans ; Male ; *Mutation ; Recombination, Genetic ; Reproduction, Asexual ; Rotifera/genetics/physiology ; Selection, Genetic ; *Sex
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  • 16
    Publication Date: 1998-04-16
    Description: The genomic regulatory network that controls gene expression ultimately determines form and function in each species. The operational nature of the regulatory programming specified in cis-regulatory DNA sequence was determined from a detailed functional analysis of a sea urchin control element that directs the expression of a gene in the endoderm during development. Spatial expression and repression, and the changing rate of transcription of this gene, are mediated by a complex and extended cis-regulatory system. The system may be typical of developmental cis-regulatory apparatus. All of its activities are integrated in the proximal element, which contains seven target sites for DNA binding proteins. A quantitative computational model of this regulatory element was constructed that explicitly reveals the logical interrelations hard-wired into the DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuh, C H -- Bolouri, H -- Davidson, E H -- New York, N.Y. -- Science. 1998 Mar 20;279(5358):1896-902.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9506933" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cell Adhesion Molecules/*genetics/physiology ; Computer Simulation ; DNA-Binding Proteins/metabolism ; Embryo, Nonmammalian/metabolism ; Endoderm/metabolism ; Gastrula/metabolism ; *Gene Expression Regulation, Developmental ; Lithium Chloride/pharmacology ; Models, Genetic ; Molecular Sequence Data ; Mutagenesis ; Promoter Regions, Genetic/genetics/*physiology ; Proteins/*genetics/physiology ; Sea Urchins/embryology/*genetics/metabolism ; *Transcription, Genetic/drug effects
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  • 17
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-10-30
    Description: Toward a genetic dissection of the processes involved in aging, a screen for gene mutations that extend life-span in Drosophila melanogaster was performed. The mutant line methuselah (mth) displayed approximately 35 percent increase in average life-span and enhanced resistance to various forms of stress, including starvation, high temperature, and dietary paraquat, a free-radical generator. The mth gene predicted a protein with homology to several guanosine triphosphate-binding protein-coupled seven-transmembrane domain receptors. Thus, the organism may use signal transduction pathways to modulate stress response and life-span.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, Y J -- Seroude, L -- Benzer, S -- AG12289/AG/NIA NIH HHS/ -- EY09278/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 30;282(5390):943-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9794765" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Base Sequence ; Cloning, Molecular ; DNA Transposable Elements ; *Drosophila Proteins ; Drosophila melanogaster/*genetics/*physiology ; Female ; Food Deprivation ; GTP-Binding Proteins/chemistry/*genetics/metabolism/physiology ; *Genes, Insect ; Hot Temperature ; Insecticide Resistance ; Longevity/genetics ; Male ; Molecular Sequence Data ; Mutation ; Oxidative Stress ; Paraquat/pharmacology ; Receptors, Cell Surface/chemistry/*genetics/metabolism/physiology ; *Receptors, G-Protein-Coupled ; Signal Transduction
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-07-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1998 Jun 12;280(5370):1692-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9660707" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; Base Sequence ; Chromosome Inversion ; DNA/*genetics ; Evolution, Molecular ; *Genome, Human ; Humans ; *Multigene Family ; Nucleic Acid Hybridization ; *Polymorphism, Genetic ; RNA, Fungal/genetics ; RNA, Small Nuclear/*genetics ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-02-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maley, L E -- Marshall, C R -- New York, N.Y. -- Science. 1998 Jan 23;279(5350):505-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth and Space Sciences, University of California, Los Angeles, CA 90095-1567, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9454349" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA, Ribosomal/*genetics ; *Evolution, Molecular ; *Phylogeny ; Proteins/chemistry ; RNA, Ribosomal, 18S/*genetics
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-01-24
    Description: Sites of DNA synthesis initiation have been detected at the nucleotide level in a yeast origin of bidirectional replication with the use of replication initiation point mapping. The ARS1 origin of Saccharomyces cerevisiae showed a transition from discontinuous to continuous DNA synthesis in an 18-base pair region (nucleotides 828 to 845) from within element B1 toward B2, adjacent to the binding site for the origin recognition complex, the putative initiator protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bielinsky, A K -- Gerbi, S A -- GM 35929/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):95-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Cell Biology and Biochemistry, Division of Biology and Medicine, Brown University, Providence, RI 02912, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417033" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Binding Sites ; DNA Helicases/metabolism ; DNA Primers ; *DNA Replication ; DNA, Fungal/*biosynthesis ; *DNA-Binding Proteins ; Molecular Sequence Data ; *Replication Origin ; Saccharomyces cerevisiae/*metabolism ; Trans-Activators/metabolism
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  • 21
    Publication Date: 1998-08-26
    Description: Nitrogen-fixing bacteroids in legume root nodules are surrounded by the plant-derived peribacteroid membrane, which controls nutrient transfer between the symbionts. A nodule complementary DNA (GmSAT1) encoding an ammonium transporter has been isolated from soybean. GmSAT1 is preferentially transcribed in nodules and immunoblotting indicates that GmSAT1 is located on the peribacteroid membrane. [14C]methylammonium uptake and patch-clamp analysis of yeast expressing GmSAT1 demonstrated that it shares properties with a soybean peribacteroid membrane NH4〈SUP ARRANGE="STAGGER"〉+ channel described elsewhere. GmSAT1 is likely to be involved in the transfer of fixed nitrogen from the bacteroid to the host.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, B N -- Finnegan, P M -- Tyerman, S D -- Whitehead, L F -- Bergersen, F J -- Day, D A -- Udvardi, M K -- New York, N.Y. -- Science. 1998 Aug 21;281(5380):1202-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biochemistry and Molecular Biology, The Australian National University, Canberra ACT 0200, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9712587" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Biological Transport ; Carrier Proteins/chemistry/*genetics/*metabolism/*secretion ; *Cation Transport Proteins ; Cell Membrane/metabolism ; DNA, Complementary ; Ion Channels/metabolism ; Kinetics ; Methylamines/metabolism ; Molecular Sequence Data ; Organelles/metabolism ; Patch-Clamp Techniques ; Plant Roots/genetics/metabolism/microbiology ; Potassium/metabolism ; Quaternary Ammonium Compounds/*metabolism ; Saccharomyces cerevisiae/genetics/metabolism ; *Soybean Proteins ; Soybeans/chemistry/*genetics/metabolism/microbiology ; Spheroplasts/metabolism ; Symbiosis ; Transformation, Genetic
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  • 22
    Publication Date: 1998-05-02
    Description: Accuracy in transfer RNA (tRNA) splicing is essential for the formation of functional tRNAs, and hence for gene expression, in both Eukaryotes and Archaea. The specificity for recognition of the tRNA precursor (pre-tRNA) resides in the endonuclease, which removes the intron by making two independent endonucleolytic cleavages. Although the eukaryal and archaeal enzymes appear to use different features of pre-tRNAs to determine the sites of cleavage, analysis of hybrid pre-tRNA substrates containing eukaryal and archaeal sequences, described here, reveals that the eukaryal enzyme retains the ability to use the archaeal recognition signals. This result indicates that there may be a common ancestral mechanism for recognition of pre-tRNA by proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fabbri, S -- Fruscoloni, P -- Bufardeci, E -- Di Nicola Negri, E -- Baldi, M I -- Attardi, D G -- Mattoccia, E -- Tocchini-Valentini, G P -- New York, N.Y. -- Science. 1998 Apr 10;280(5361):284-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉EniChem, Istituto Guido Donegani SpA, Laboratori di Biotecnologie, 00015 Monterotondo, Rome, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9535657" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anticodon ; Base Composition ; Base Sequence ; Endoribonucleases/chemistry/*metabolism ; Introns ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA Precursors/*chemistry/*metabolism ; *RNA Splicing ; RNA, Archaeal/*chemistry/*metabolism ; RNA, Transfer, Phe/chemistry/metabolism ; Saccharomyces cerevisiae/enzymology ; Substrate Specificity ; Xenopus
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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-03-28
    Description: The transfer RNA (tRNA) multigene family comprises 20 amino acid-accepting groups, many of which contain isoacceptors. The addition of isoacceptors to the tRNA repertoire was critical to establishing the genetic code, yet the origin of isoacceptors remains largely unexplored. A model of tRNA evolution, termed "tRNA gene recruitment," was formulated. It proposes that a tRNA gene can be recruited from one isoaccepting group to another by a point mutation that concurrently changes tRNA amino acid identity and messenger RNA coupling capacity. A test of the model showed that an Escherichia coli strain, in which the essential tRNAUGUThr gene was inactivated, was rendered viable when a tRNAArg with a point mutation that changed its anticodon from UCU to UGU (threonine) was expressed. Insertion of threonine at threonine codons by the "recruited" tRNAArg was corroborated by in vitro aminoacylation assays showing that its specificity had been changed from arginine to threonine. Therefore, the recruitment model may account for the evolution of some tRNA genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saks, M E -- Sampson, J R -- Abelson, J -- GM 48560/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Mar 13;279(5357):1665-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology 147-75, California Institute of Technology, Pasadena, CA 91125, USA. peggy@seqaxp.bio.caltech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9497276" target="_blank"〉PubMed〈/a〉
    Keywords: Anticodon/*genetics ; Arginine/metabolism ; Base Composition ; Base Sequence ; Escherichia coli/*genetics ; *Evolution, Molecular ; Genes, Bacterial ; Haemophilus influenzae/genetics ; Models, Genetic ; Molecular Sequence Data ; Multigene Family ; Nucleic Acid Conformation ; *Point Mutation ; Polymerase Chain Reaction ; RNA, Bacterial/chemistry/genetics/metabolism ; RNA, Transfer, Arg/chemistry/*genetics/metabolism ; RNA, Transfer, Thr/chemistry/*genetics/metabolism ; Recombination, Genetic ; Temperature ; Threonine/metabolism ; Transformation, Bacterial
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  • 24
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-10-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferber, D -- New York, N.Y. -- Science. 1998 Sep 11;281(5383):1581-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9767017" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cells, Cultured ; DNA, Complementary ; Databases, Factual ; Gene Expression ; Humans ; Mass Spectrometry ; Proteins/*chemistry/genetics/isolation & purification ; *RNA Splicing ; Spliceosomes/*chemistry
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  • 25
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-10-09
    Description: Short RNA aptamers that specifically bind to a wide variety of ligands in vitro can be isolated from randomized pools of RNA. Here it is shown that small molecule aptamers also bound their ligand in vivo, enabling development of a method for controlling gene expression in living cells. Insertion of a small molecule aptamer into the 5' untranslated region of a messenger RNA allowed its translation to be repressible by ligand addition in vitro as well as in mammalian cells. The ability of small molecules to control expression of specific genes could facilitate studies in many areas of biology and medicine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Werstuck, G -- Green, M R -- New York, N.Y. -- Science. 1998 Oct 9;282(5387):296-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Program in Molecular Medicine, University of Massachusetts Medical Center, 373 Plantation Street, Suite 309, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9765156" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Bacterial Agents/*metabolism/pharmacology ; Base Sequence ; Benzimidazoles/pharmacology ; Bisbenzimidazole/*metabolism/pharmacology ; CHO Cells ; Cricetinae ; Drug Resistance, Microbial ; Escherichia coli/genetics ; *Gene Expression Regulation/drug effects ; Kanamycin/metabolism/pharmacology ; Ligands ; Molecular Sequence Data ; Protein Biosynthesis/drug effects ; RNA/*metabolism ; RNA, Messenger/genetics ; Tobramycin/metabolism/pharmacology ; Transfection
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  • 26
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-05-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doll, J J -- New York, N.Y. -- Science. 1998 May 1;280(5364):689-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biotechnology Examination, U.S. Patent and Trademark Office, Washington, DC 20231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9599146" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Biotechnology/*legislation & jurisprudence ; *Dna ; DNA, Complementary ; Databases, Factual ; Federal Government ; Genetic Research ; Genetic Techniques ; Human Genome Project ; *Patents as Topic ; Polymorphism, Genetic ; United States
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  • 27
    Publication Date: 1998-01-07
    Description: Nucleosomes, the nucleohistone subunits of chromatin, are present on transcribed eukaryotic genes but do not prevent transcription. It is shown here that the large yeast RNA polymerase III transcribes through a single nucleosome. This takes place through a direct internal nucleosome transfer in which histones never leave the DNA template. During this process, the polymerase pauses with a pronounced periodicity of 10 to 11 base pairs, which is consistent with restricted rotation in the DNA loop formed during transfer. Transcription through nucleosomes by the eukaryotic enzyme and by much smaller prokaryotic RNA polymerases thus shares many features, reflecting an important property of nucleosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Studitsky, V M -- Kassavetis, G A -- Geiduschek, E P -- Felsenfeld, G -- New York, N.Y. -- Science. 1997 Dec 12;278(5345):1960-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9395401" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA/chemistry/metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Histones/metabolism ; Models, Genetic ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleosomes/genetics/*metabolism ; Promoter Regions, Genetic ; RNA Polymerase III/*metabolism ; Templates, Genetic ; *Transcription, Genetic
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  • 28
    Publication Date: 1998-01-31
    Description: The cerebral cortex of Alzheimer's and Down syndrome patients is characterized by the presence of protein deposits in neurofibrillary tangles, neuritic plaques, and neuropil threads. These structures were shown to contain forms of beta amyloid precursor protein and ubiquitin-B that are aberrant (+1 proteins) in the carboxyl terminus. The +1 proteins were not found in young control patients, whereas the presence of ubiquitin-B+1 in elderly control patients may indicate early stages of neurodegeneration. The two species of +1 proteins displayed cellular colocalization, suggesting a common origin, operating at the transcriptional level or by posttranscriptional editing of RNA. This type of transcript mutation is likely an important factor in the widely occurring nonfamilial early- and late-onset forms of Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van Leeuwen, F W -- de Kleijn, D P -- van den Hurk, H H -- Neubauer, A -- Sonnemans, M A -- Sluijs, J A -- Koycu, S -- Ramdjielal, R D -- Salehi, A -- Martens, G J -- Grosveld, F G -- Peter, J -- Burbach, H -- Hol, E M -- New York, N.Y. -- Science. 1998 Jan 9;279(5348):242-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate School for Neurosciences Amsterdam, Netherlands Institute for Brain Research, 1105 AZ Amsterdam, The Netherlands. f.van.leeuwen@nih.knaw.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9422699" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Aging/genetics ; Alzheimer Disease/*genetics/metabolism/pathology ; Amino Acid Sequence ; Amyloid beta-Protein Precursor/analysis/chemistry/*genetics ; Base Sequence ; *Brain Chemistry ; Cerebral Cortex/chemistry/pathology ; Cloning, Molecular ; Down Syndrome/*genetics/metabolism/pathology ; Female ; *Frameshift Mutation ; Hippocampus/chemistry/pathology ; Humans ; Male ; Molecular Sequence Data ; Neurites/chemistry ; Neurofibrillary Tangles/chemistry ; Neuropil/chemistry ; Polymerase Chain Reaction ; RNA Editing ; Repetitive Sequences, Nucleic Acid ; Sequence Deletion ; Transcription, Genetic ; Ubiquitins/analysis/chemistry/*genetics/metabolism
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  • 29
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bemis, W E -- Simons, A M -- New York, N.Y. -- Science. 1997 Oct 17;278(5337):370.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381130" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA, Mitochondrial/genetics ; Fishes/classification/*genetics ; Phylogeny
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  • 30
    Publication Date: 1998-06-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Venter, J C -- Adams, M D -- Sutton, G G -- Kerlavage, A R -- Smith, H O -- Hunkapiller, M -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1540-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genomic Research, Rockville, MD 20850, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9644018" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; Base Sequence ; Cloning, Molecular ; DNA, Complementary ; Databases, Factual ; Drosophila melanogaster/genetics ; Genetic Markers ; *Genome, Human ; *Human Genome Project ; Humans ; Patents as Topic ; Polymorphism, Genetic ; Sequence Analysis, DNA/instrumentation/*methods ; Sequence Tagged Sites
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  • 31
    Publication Date: 1998-02-07
    Description: The bacterium Helicobacter pylori is the causative agent for peptic ulcer disease. Bacterial adherence to the human gastric epithelial lining is mediated by the fucosylated Lewis b (Leb) histo-blood group antigen. The Leb-binding adhesin, BabA, was purified by receptor activity-directed affinity tagging. The bacterial Leb-binding phenotype was associated with the presence of the cag pathogenicity island among clinical isolates of H. pylori. A vaccine strategy based on the BabA adhesin might serve as a means to target the virulent type I strains of H. pylori.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ilver, D -- Arnqvist, A -- Ogren, J -- Frick, I M -- Kersulyte, D -- Incecik, E T -- Berg, D E -- Covacci, A -- Engstrand, L -- Boren, T -- New York, N.Y. -- Science. 1998 Jan 16;279(5349):373-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Umea University, SE-901 87 Umea, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9430586" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/chemistry/genetics/*isolation & purification/metabolism ; Amino Acid Sequence ; *Antigens, Bacterial ; Bacterial Adhesion ; Bacterial Proteins/genetics/physiology ; Base Composition ; Base Sequence ; Biotinylation ; Cell Membrane/chemistry ; Cloning, Molecular ; Codon, Initiator ; Fucose ; Gastric Mucosa/microbiology ; Genes, Bacterial ; Glycoconjugates/metabolism ; Helicobacter pylori/isolation & purification/*metabolism/pathogenicity ; Humans ; Lewis Blood-Group System/*metabolism ; Ligands ; Molecular Sequence Data ; Virulence
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  • 32
    Publication Date: 1998-06-20
    Description: The apical ectodermal ridge (AER) is an essential structure for vertebrate limb development. Wnt3a is expressed during the induction of the chick AER, and misexpression of Wnt3a induces ectopic expression of AER-specific genes in the limb ectoderm. The genes beta-catenin and Lef1 can mimic the effect of Wnt3a, and blocking the intrinsic Lef1 activity disrupts AER formation. Hence, Wnt3a functions in AER formation through the beta-catenin/LEF1 pathway. In contrast, neither beta-catenin nor Lef1 affects the Wnt7a-regulated dorsoventral polarity of the limb. Thus, two related Wnt genes elicit distinct responses in the same tissues by using different intracellular pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kengaku, M -- Capdevila, J -- Rodriguez-Esteban, C -- De La Pena, J -- Johnson, R L -- Izpisua Belmonte, J C -- Tabin, C J -- New York, N.Y. -- Science. 1998 May 22;280(5367):1274-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9596583" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Avian Proteins ; Base Sequence ; *Body Patterning ; Chick Embryo ; Cloning, Molecular ; Cytoskeletal Proteins/genetics/metabolism ; DNA-Binding Proteins/genetics/metabolism ; Ectoderm/*metabolism ; Fibroblast Growth Factor 4 ; Fibroblast Growth Factor 8 ; Fibroblast Growth Factors/biosynthesis/genetics ; *Gene Expression Regulation, Developmental ; Glucosyltransferases ; Growth Substances/biosynthesis/genetics ; Homeodomain Proteins/genetics ; Intercellular Signaling Peptides and Proteins ; Limb Buds/embryology/*metabolism ; Lymphoid Enhancer-Binding Factor 1 ; Mesoderm/metabolism ; Molecular Sequence Data ; Morphogenesis ; Protein Biosynthesis ; Proteins/*genetics/physiology ; Proto-Oncogene Proteins/biosynthesis/*genetics/physiology ; Signal Transduction ; *Trans-Activators ; Transcription Factors/genetics/metabolism ; Up-Regulation ; Wnt Proteins ; Wnt3 Protein ; Wnt3A Protein ; beta Catenin
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  • 33
    Publication Date: 1998-01-24
    Description: Selenium, an essential trace element, is a component of prokaryotic and eukaryotic antioxidant proteins. A candidate selenoprotein homologous to glutathione peroxidase was deduced from the sequence of molluscum contagiosum, a poxvirus that causes persistent skin neoplasms in children and acquired immunodeficiency syndrome (AIDS) patients. Selenium was incorporated into this protein during biosynthesis, and a characteristic stem-loop structure near the end of the messenger RNA was required for alternative selenocysteine decoding of a potential UGA stop codon within the open reading frame. The selenoprotein protected human keratinocytes against cytotoxic effects of ultraviolet irradiation and hydrogen peroxide, providing a mechanism for a virus to defend itself against environmental stress.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shisler, J L -- Senkevich, T G -- Berry, M J -- Moss, B -- DK47320/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):102-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 4 Center Drive, MSC 0445, Bethesda, MD 20892-0445, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417017" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Base Sequence ; Cell Line ; Codon ; Glutathione Peroxidase/genetics/*metabolism ; HeLa Cells ; Humans ; Hydrogen Peroxide/pharmacology ; Keratinocytes/*cytology/drug effects ; Molecular Sequence Data ; Molluscum contagiosum virus/genetics/*physiology ; Open Reading Frames ; Point Mutation ; Proteins/genetics/*metabolism ; Selenium/metabolism ; Selenocysteine/genetics ; Selenoproteins ; Transfection ; Ultraviolet Rays ; Viral Proteins/genetics/*metabolism
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  • 34
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-01-31
    Description: The transduction of many cellular stimuli results in oscillations in the intracellular concentration of calcium ions (Ca2+). Although information is thought to be encoded in the frequency of such oscillations, no frequency decoder has been identified. Rapid superfusion of immobilized Ca2+- and calmodulin-dependent protein kinase II (CaM kinase II) in vitro showed that the enzyme can decode the frequency of Ca2+ spikes into distinct amounts of kinase activity. The frequency response of CaM kinase II was modulated by several factors, including the amplitude and duration of individual spikes as well as the subunit composition and previous state of activation of the kinase. These features should provide specificity in the activation of this multifunctional enzyme by distinct cellular stimuli and may underlie its pivotal role in activity-dependent forms of synaptic plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉De Koninck, P -- Schulman, H -- GM30179/GM/NIGMS NIH HHS/ -- GM40600/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 9;279(5348):227-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Stanford University School of Medicine, Stanford, CA 94305-5401, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9422695" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; COS Cells ; Calcium/*metabolism/pharmacology ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Calmodulin/metabolism/pharmacology ; Cercopithecus aethiops ; Enzyme Activation ; Enzymes, Immobilized ; Molecular Sequence Data ; Neuronal Plasticity ; Phosphorylation ; Phosphothreonine/metabolism ; Polyvinyl Chloride ; Recombinant Proteins/metabolism ; *Signal Transduction
    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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  • 35
    Publication Date: 1998-07-17
    Description: DNA from excrements can be amplified by means of the polymerase chain reaction. However, this has not been possible with ancient feces. Cross-links between reducing sugars and amino groups were shown to exist in a Pleistocene coprolite from Gypsum Cave, Nevada. A chemical agent, N-phenacylthiazolium bromide, that cleaves such cross-links made it possible to amplify DNA sequences. Analyses of these DNA sequences showed that the coprolite is derived from an extinct sloth, presumably the Shasta ground sloth Nothrotheriops shastensis. Plant DNA sequences from seven groups of plants were identified in the coprolite. The plant assemblage that formed part of the sloth's diet exists today at elevations about 800 meters higher than the cave.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Poinar, H N -- Hofreiter, M -- Spaulding, W G -- Martin, P S -- Stankiewicz, B A -- Bland, H -- Evershed, R P -- Possnert, G -- Paabo, S -- New York, N.Y. -- Science. 1998 Jul 17;281(5375):402-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institute for Evolutionary Anthropology and Zoological Institute, University of Munich, Luisenstrasse 14, D-80333 Munich, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9665881" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cloning, Molecular ; DNA, Mitochondrial/chemistry/*isolation & purification ; DNA, Plant/chemistry/*isolation & purification ; DNA, Ribosomal/chemistry/*isolation & purification ; *Diet ; Feces/*chemistry ; *Fossils ; Maillard Reaction ; Molecular Sequence Data ; Plants/classification/genetics ; Polymerase Chain Reaction ; RNA, Ribosomal/genetics ; Ribulose-Bisphosphate Carboxylase/genetics ; *Sloths/genetics ; Thiazoles
    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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  • 36
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-06-20
    Description: To distinguish continuous from discontinuous evolutionary change, a relation of nearness between phenotypes is needed. Such a relation is based on the probability of one phenotype being accessible from another through changes in the genotype. This nearness relation is exemplified by calculating the shape neighborhood of a transfer RNA secondary structure and provides a characterization of discontinuous shape transformations in RNA. The simulation of replicating and mutating RNA populations under selection shows that sudden adaptive progress coincides mostly, but not always, with discontinuous shape transformations. The nature of these transformations illuminates the key role of neutral genetic drift in their realization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fontana, W -- Schuster, P -- New York, N.Y. -- Science. 1998 May 29;280(5368):1451-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Theoretische Chemie, Universitat Wien, Wahringerstrasse 17, A-1090 Wien, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9603737" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Computer Simulation ; *Evolution, Molecular ; Gene Frequency ; Genotype ; Mutation ; *Nucleic Acid Conformation ; Phenotype ; RNA/*chemistry/genetics/metabolism ; RNA, Transfer/chemistry ; Stochastic Processes ; Thermodynamics
    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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  • 37
    Publication Date: 1998-07-17
    Description: The complete genome sequence of Treponema pallidum was determined and shown to be 1,138,006 base pairs containing 1041 predicted coding sequences (open reading frames). Systems for DNA replication, transcription, translation, and repair are intact, but catabolic and biosynthetic activities are minimized. The number of identifiable transporters is small, and no phosphoenolpyruvate:phosphotransferase carbohydrate transporters were found. Potential virulence factors include a family of 12 potential membrane proteins and several putative hemolysins. Comparison of the T. pallidum genome sequence with that of another pathogenic spirochete, Borrelia burgdorferi, the agent of Lyme disease, identified unique and common genes and substantiates the considerable diversity observed among pathogenic spirochetes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fraser, C M -- Norris, S J -- Weinstock, G M -- White, O -- Sutton, G G -- Dodson, R -- Gwinn, M -- Hickey, E K -- Clayton, R -- Ketchum, K A -- Sodergren, E -- Hardham, J M -- McLeod, M P -- Salzberg, S -- Peterson, J -- Khalak, H -- Richardson, D -- Howell, J K -- Chidambaram, M -- Utterback, T -- McDonald, L -- Artiach, P -- Bowman, C -- Cotton, M D -- Fujii, C -- Garland, S -- Hatch, B -- Horst, K -- Roberts, K -- Sandusky, M -- Weidman, J -- Smith, H O -- Venter, J C -- AI31068/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Jul 17;281(5375):375-88.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genomic Research, Rockville, MD 20850, USA. tpdb@tigr.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9665876" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics/metabolism ; Base Sequence ; Borrelia burgdorferi Group/genetics ; Carrier Proteins/genetics/metabolism ; DNA Repair/genetics ; DNA Replication/genetics ; DNA Restriction Enzymes/genetics ; Energy Metabolism/genetics ; Genes, Bacterial ; Genes, Regulator ; *Genome, Bacterial ; Heat-Shock Response/genetics ; Lipoproteins/genetics ; Membrane Proteins/genetics ; Molecular Sequence Data ; Movement ; Open Reading Frames ; Oxygen Consumption/genetics ; Protein Biosynthesis ; Recombination, Genetic ; Replication Origin ; *Sequence Analysis, DNA ; Transcription, Genetic ; Treponema pallidum/*genetics/metabolism/pathogenicity
    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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  • 38
    Publication Date: 1998-02-07
    Description: The three-dimensional structure of the human immunodeficiency virus-type 1 (HIV-1) nucleocapsid protein (NC) bound to the SL3 stem-loop recognition element of the genomic Psi RNA packaging signal has been determined by heteronuclear magnetic resonance spectroscopy. Tight binding (dissociation constant, approximately 100 nM) is mediated by specific interactions between the amino- and carboxyl-terminal CCHC-type zinc knuckles of the NC protein and the G7 and G9 nucleotide bases, respectively, of the G6-G7-A8-G9 RNA tetraloop. A8 packs against the amino-terminal knuckle and forms a hydrogen bond with conserved Arg32, and residues Lys3 to Arg10 of NC form a 310 helix that binds to the major groove of the RNA stem and also packs against the amino-terminal zinc knuckle. The structure provides insights into the mechanism of viral genome recognition, explains extensive amino acid conservation within NC, and serves as a basis for the development of inhibitors designed to interfere with genome encapsidation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉De Guzman, R N -- Wu, Z R -- Stalling, C C -- Pappalardo, L -- Borer, P N -- Summers, M F -- GM32691/GM/NIGMS NIH HHS/ -- GM42561/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 16;279(5349):384-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of Maryland-Baltimore County (UMBC), 1000 Hilltop Circle, Baltimore, MD 21250, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9430589" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Gene Products, gag/*chemistry/metabolism ; Genome, Viral ; HIV-1/*chemistry/genetics ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleocapsid/*chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; RNA, Viral/*chemistry/genetics/metabolism ; Zinc/chemistry/metabolism ; Zinc Fingers
    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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