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  • Base Sequence  (382)
  • American Association for the Advancement of Science (AAAS)  (382)
  • American Association of Petroleum Geologists (AAPG)
  • 1995-1999  (382)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (382)
  • American Association of Petroleum Geologists (AAPG)
Years
Year
  • 1
    Publication Date: 1999-10-16
    Description: Dense genetic maps of human, mouse, and rat genomes that are based on coding genes and on microsatellite and single-nucleotide polymorphism markers have been complemented by precise gene homolog alignment with moderate-resolution maps of livestock, companion animals, and additional mammal species. Comparative genetic assessment expands the utility of these maps in gene discovery, in functional genomics, and in tracking the evolutionary forces that sculpted the genome organization of modern mammalian species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, S J -- Menotti-Raymond, M -- Murphy, W J -- Nash, W G -- Wienberg, J -- Stanyon, R -- Copeland, N G -- Jenkins, N A -- Womack, J E -- Marshall Graves, J A -- New York, N.Y. -- Science. 1999 Oct 15;286(5439):458-62, 479-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genomic Diversity, National Cancer Institute, Frederick, MD 21702-1201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10521336" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Domestic/genetics ; Base Sequence ; *Chromosome Mapping ; *Evolution, Molecular ; Genetic Markers ; *Genome ; *Genome, Human ; Humans ; Mammals/*genetics ; Mutation ; *Phylogeny ; Rodentia/genetics
    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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  • 2
    Publication Date: 1999-03-26
    Description: The carboxyl-terminal domain of colicin E5 was shown to inhibit protein synthesis of Escherichia coli. Its target, as revealed through in vivo and in vitro experiments, was not ribosomes as in the case of E3, but the transfer RNAs (tRNAs) for Tyr, His, Asn, and Asp, which contain a modified base, queuine, at the wobble position of each anticodon. The E5 carboxyl-terminal domain hydrolyzed these tRNAs just on the 3' side of this nucleotide. Tight correlation was observed between the toxicity of E5 and the cleavage of intracellular tRNAs of this group, implying that these tRNAs are the primary targets of colicin E5.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ogawa, T -- Tomita, K -- Ueda, T -- Watanabe, K -- Uozumi, T -- Masaki, H -- New York, N.Y. -- Science. 1999 Mar 26;283(5410):2097-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biotechnology, Graduate School of Agricultural and Life Sciences, University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-8657, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10092236" target="_blank"〉PubMed〈/a〉
    Keywords: Anticodon/*metabolism ; Bacterial Proteins/biosynthesis/genetics/pharmacology ; Base Sequence ; Cloning, Molecular ; Colicins/genetics/*metabolism/pharmacology ; Escherichia coli/drug effects/metabolism ; *Escherichia coli Proteins ; Guanine/analogs & derivatives/analysis ; Molecular Sequence Data ; RNA, Bacterial/chemistry/*metabolism ; RNA, Ribosomal, 16S/metabolism ; RNA, Transfer, Amino Acid-Specific/chemistry/*metabolism ; RNA, Transfer, Asn/chemistry/metabolism ; RNA, Transfer, Asp/chemistry/metabolism ; RNA, Transfer, His/chemistry/metabolism ; RNA, Transfer, Tyr/chemistry/metabolism ; Ribonucleases/genetics/*metabolism/pharmacology ; Ribosomes/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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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-04-24
    Description: Gene expression is modulated by regulatory elements that influence transcription elongation by RNA polymerase: terminators that disrupt the elongation complex and release RNA, and regulators that overcome termination signals. RNA release from Escherichia coli RNA polymerase can be induced by a complementary oligonucleotide that replaces the upstream half of the RNA hairpin stem of intrinsic terminator transcripts, implying that RNA hairpins act by extracting RNA from the transcription complex. A transcription antiterminator inhibits this activity of oligonucleotides and therefore protects the elongation complex from destabilizing attacks on the emerging transcript. These effects illuminate the structure of the complex and the mechanism of transcription termination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yarnell, W S -- Roberts, J W -- GM 21941/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Apr 23;284(5414):611-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Biochemistry, Molecular and Cell Biology, Biotechnology Building, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10213678" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Base Sequence ; DNA, Bacterial/chemistry/genetics/metabolism ; DNA-Directed RNA Polymerases/genetics/*metabolism ; Escherichia coli/*genetics/metabolism ; Models, Genetic ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry/metabolism ; RNA, Bacterial/chemistry/genetics/metabolism ; RNA, Messenger/chemistry/genetics/*metabolism ; Templates, Genetic ; *Terminator Regions, Genetic ; *Transcription, Genetic ; Viral Proteins/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-10-16
    Description: The Mammalian Gene Collection (MGC) project is a new effort by the NIH to generate full-length complementary DNA (cDNA) resources. This project will provide publicly accessible resources to the full research community. The MGC project entails the production of libraries, sequencing, and database and repository development, as well as the support of library construction, sequencing, and analytic technologies dedicated to the goal of obtaining a full set of human and other mammalian full-length (open reading frame) sequences and clones of expressed genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strausberg, R L -- Feingold, E A -- Klausner, R D -- Collins, F S -- New York, N.Y. -- Science. 1999 Oct 15;286(5439):455-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Cancer Institute, National Human Genome Research Institute, 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/10521335" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Computational Biology ; DNA, Complementary ; Databases, Factual ; Expressed Sequence Tags ; *Gene Library ; *Genome ; *Genome, Human ; Humans ; Mammals/*genetics ; Mice ; National Institutes of Health (U.S.) ; Private Sector ; Public Sector ; *Sequence Analysis, DNA ; United States
    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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  • 5
    Publication Date: 1999-11-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, S J -- Eisenberg, J F -- Miyamoto, M -- Hedges, S B -- Kumar, S -- Wilson, D E -- Menotti-Raymond, M -- Murphy, W J -- Nash, W G -- Lyons, L A -- Menninger, J C -- Stanyon, R -- Wienberg, J -- Copeland, N G -- Jenkins, N A -- Gellin, J -- Yerle, M -- Andersson, L -- Womack, J -- Broad, T -- Postlethwait, J -- Serov, O -- Bailey, E -- James, M R -- Marshall Graves, J A -- New York, N.Y. -- Science. 1999 Oct 15;286(5439):463-78.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Cancer Institute, Frederick, MD, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10577209" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Chromosome Mapping ; Chromosome Painting ; *Genome ; *Genome, Human ; Humans ; Mammals/*genetics ; Nucleic Acid Hybridization ; Phylogeny
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-10-16
    Description: Annotation of large-scale gene sequence data will benefit from comprehensive and consistent application of well-documented, standard analysis methods and from progressive and vigilant efforts to ensure quality and utility and to keep the annotation up to date. However, it is imperative to learn how to apply information derived from functional genomics and proteomics technologies to conceptualize and explain the behaviors of biological systems. Quantitative and dynamical models of systems behaviors will supersede the limited and static forms of single-gene annotation that are now the norm. Molecular biological epistemology will increasingly encompass both teleological and causal explanations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boguski, M S -- New York, N.Y. -- Science. 1999 Oct 15;286(5439):453-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, 8600 Rockville Pike, Bethesda, MD 20894, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10521334" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cloning, Molecular ; *Computational Biology ; Databases, Factual ; *Genetic Techniques ; *Genome ; Genome, Human ; Human Genome Project ; Humans ; Molecular Biology ; *Proteome ; *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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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-06-26
    Description: The photosynthetic apparatus in plant cells is associated with membranes of the thylakoids within the chloroplast and is embedded into a highly specialized lipid matrix. Diacylglycerol galactolipids are common in thylakoid membranes but are excluded from all others. Isolation of the gene DGD1, encoding a galactosyltransferase-like protein, now provides insights into assembly of the thylakoid lipid matrix and subcellular lipid trafficking in Arabidopsis thaliana.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dormann, P -- Balbo, I -- Benning, C -- New York, N.Y. -- Science. 1999 Jun 25;284(5423):2181-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Michigan State University, East Lansing, MI 48824, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10381884" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/growth & development/*metabolism ; *Arabidopsis Proteins ; Base Sequence ; Chloroplasts/metabolism ; Chromosome Mapping ; DNA, Complementary/genetics ; Endoplasmic Reticulum/metabolism ; Exons ; Galactolipids ; Galactosyltransferases/chemistry/*genetics/*metabolism ; Genes, Plant ; Glycolipids/*biosynthesis ; Intracellular Membranes/metabolism ; *Lipid Metabolism ; Molecular Sequence Data ; Mutation ; Plants, Genetically Modified ; Recombinant Proteins/metabolism
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-09-25
    Description: Cell proliferation requires cell growth; that is, cells only divide after they reach a critical size. However, the mechanisms by which cells grow and maintain their appropriate size have remained elusive. Drosophila deficient in the S6 kinase gene (dS6K) exhibited an extreme delay in development and a severe reduction in body size. These flies had smaller cells rather than fewer cells. The effect was cell-autonomous, displayed throughout larval development, and distinct from that of ribosomal protein mutants (Minutes). Thus, the dS6K gene product regulates cell size in a cell-autonomous manner without impinging on cell number.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Montagne, J -- Stewart, M J -- Stocker, H -- Hafen, E -- Kozma, S C -- Thomas, G -- F32 GM15926/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Sep 24;285(5436):2126-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher Institute, Maulbeerstrasse 66, 4058 Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10497130" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Body Constitution ; Cell Count ; Cell Division ; Cell Size ; Drosophila melanogaster/cytology/*enzymology/genetics/*growth & development ; Epithelial Cells/cytology ; Female ; Genes, Insect ; Larva/cytology/growth & development ; Male ; Metamorphosis, Biological ; Molecular Sequence Data ; Mutation ; Ribosomal Protein S6 Kinases/genetics/*metabolism ; Wings, Animal/*cytology/growth & development
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-04-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mullikin, J C -- McMurragy, A A -- New York, N.Y. -- Science. 1999 Mar 19;283(5409):1867-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sanger Centre, Wellcome Trust Genome Campus, Hinxton, Cambs, UK. jcm@sanger.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10206892" target="_blank"〉PubMed〈/a〉
    Keywords: Automation ; Base Sequence ; Fluorescence ; *Genome, Human ; Human Genome Project ; Humans ; Sequence Analysis, DNA/*instrumentation/methods ; Software
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  • 10
    Publication Date: 1999-12-22
    Description: West Nile (WN) virus, a mosquito-transmitted virus native to Africa, Asia, and Europe, was isolated from two species of mosquitoes, Culex pipiens and Aedes vexans, and from brain tissues of 28 American crows, Corvus brachyrhynchos, and one Cooper's hawk, Accipiter cooperii, in Connecticut. A portion of the genome of virus isolates from four different hosts was sequenced and analyzed by comparative phylogenetic analysis. Our isolates from Connecticut were similar to one another and most closely related to two WN isolates from Romania (2.8 and 3.6 percent difference). If established in North America, WN virus will likely have severe effects on human health and on the health of populations of birds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, J F -- Andreadis, T G -- Vossbrinck, C R -- Tirrell, S -- Wakem, E M -- French, R A -- Garmendia, A E -- Van Kruiningen, H J -- P01-AI-30548/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1999 Dec 17;286(5448):2331-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology, Department of Soil and Water, the Connecticut Agricultural Experiment Station, Post Office Box 1106, New Haven, CT 06504, USA. john.f.anderson@po.state.ct.us〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10600741" target="_blank"〉PubMed〈/a〉
    Keywords: Aedes/virology ; Animals ; Base Sequence ; Bird Diseases/epidemiology/*virology ; Brain/*virology ; Connecticut/epidemiology ; Culex/virology ; Culicidae/*virology ; Genome, Viral ; Humans ; Insect Vectors/*virology ; Phylogeny ; Raptors/virology ; Romania ; Songbirds/virology ; West Nile Fever/epidemiology/*veterinary/virology ; West Nile virus/classification/genetics/*isolation & purification
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  • 11
    Publication Date: 1999-02-19
    Description: A highly fatal hemorrhagic disease has been identified in 10 young Asian and African elephants at North American zoos. In the affected animals there was ultrastructural evidence for herpesvirus-like particles in endothelial cells of the heart, liver, and tongue. Consensus primer polymerase chain reaction combined with sequencing yielded molecular evidence that confirmed the presence of two novel but related herpesviruses associated with the disease, one in Asian elephants and another in African elephants. Otherwise healthy African elephants with external herpetic lesions yielded herpesvirus sequences identical to that found in Asian elephants with endothelial disease. This finding suggests that the Asian elephant deaths were caused by cross-species infection with a herpesvirus that is naturally latent in, but normally not lethal to, African elephants. A reciprocal relationship may exist for the African elephant disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Richman, L K -- Montali, R J -- Garber, R L -- Kennedy, M A -- Lehnhardt, J -- Hildebrandt, T -- Schmitt, D -- Hardy, D -- Alcendor, D J -- Hayward, G S -- 1 K08 AI01526-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1999 Feb 19;283(5405):1171-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Smithsonian, National Zoological Park, Washington, DC 20008, USA. lkrichma@welchlink.welch.jhu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10024244" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Amino Acid Sequence ; Animals ; Animals, Zoo/*virology ; Asia ; Base Sequence ; DNA, Viral/genetics ; DNA-Directed DNA Polymerase/chemistry/genetics ; Elephants/*virology ; Endodeoxyribonucleases/chemistry/genetics ; Endothelium, Vascular/pathology/*virology ; Female ; Genes, Viral ; Hemorrhage/pathology/veterinary/virology ; Herpesviridae/classification/genetics/*isolation & purification ; Herpesviridae Infections/pathology/transmission/*veterinary/virology ; Inclusion Bodies, Viral/ultrastructure ; Male ; Molecular Sequence Data ; Phylogeny ; Polymerase Chain Reaction ; United States ; Viral Proteins/genetics
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-01-08
    Description: The G+C nucleotide content of ribosomal RNA (rRNA) sequences is strongly correlated with the optimal growth temperature of prokaryotes. This property allows inference of the environmental temperature of the common ancestor to all life forms from knowledge of the G+C content of its rRNA sequences. A model of sequence evolution, assuming varying G+C content among lineages and unequal substitution rates among sites, was devised to estimate ancestral base compositions. This method was applied to rRNA sequences of various species representing the major lineages of life. The inferred G+C content of the common ancestor to extant life forms appears incompatible with survival at high temperature. This finding challenges a widely accepted hypothesis about the origin of life.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galtier, N -- Tourasse, N -- Gouy, M -- New York, N.Y. -- Science. 1999 Jan 8;283(5399):220-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Biometrie, Genetique et Biologie des Populations, Universite C. Bernard Lyon 1, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9880254" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Base Sequence ; Computer Simulation ; Confidence Intervals ; Cytosine/*analysis ; *Evolution, Molecular ; Guanine/*analysis ; Hot Temperature ; Likelihood Functions ; Markov Chains ; Models, Chemical ; *Origin of Life ; Phylogeny ; RNA, Archaeal/chemistry ; RNA, Bacterial/chemistry ; RNA, Ribosomal/*chemistry ; Temperature
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  • 13
    Publication Date: 1999-12-22
    Description: In late summer 1999, an outbreak of human encephalitis occurred in the northeastern United States that was concurrent with extensive mortality in crows (Corvus species) as well as the deaths of several exotic birds at a zoological park in the same area. Complete genome sequencing of a flavivirus isolated from the brain of a dead Chilean flamingo (Phoenicopterus chilensis), together with partial sequence analysis of envelope glycoprotein (E-glycoprotein) genes amplified from several other species including mosquitoes and two fatal human cases, revealed that West Nile (WN) virus circulated in natural transmission cycles and was responsible for the human disease. Antigenic mapping with E-glycoprotein-specific monoclonal antibodies and E-glycoprotein phylogenetic analysis confirmed these viruses as WN. This North American WN virus was most closely related to a WN virus isolated from a dead goose in Israel in 1998.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lanciotti, R S -- Roehrig, J T -- Deubel, V -- Smith, J -- Parker, M -- Steele, K -- Crise, B -- Volpe, K E -- Crabtree, M B -- Scherret, J H -- Hall, R A -- MacKenzie, J S -- Cropp, C B -- Panigrahy, B -- Ostlund, E -- Schmitt, B -- Malkinson, M -- Banet, C -- Weissman, J -- Komar, N -- Savage, H M -- Stone, W -- McNamara, T -- Gubler, D J -- New York, N.Y. -- Science. 1999 Dec 17;286(5448):2333-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Vector-Borne Infectious Diseases, National Center for Infectious Diseases, Centers for Disease Control and Prevention, Fort Collins, CO 80522, USA. rsl2@cdc.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10600742" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antibodies, Viral/immunology ; Base Sequence ; Bird Diseases/epidemiology/virology ; Birds/virology ; *Disease Outbreaks ; Encephalitis Viruses, Japanese/classification/genetics ; Fluorescent Antibody Technique, Indirect ; Genome, Viral ; Humans ; Molecular Sequence Data ; New England/epidemiology ; New York City/epidemiology ; Phylogeny ; Songbirds/virology ; Viral Envelope Proteins/chemistry/genetics/immunology ; West Nile Fever/*epidemiology/veterinary/*virology ; West Nile virus/*classification/*genetics/immunology/isolation & purification
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-05-15
    Description: The structure of a highly conserved complex between a 58-nucleotide domain of large subunit ribosomal RNA and the RNA-binding domain of ribosomal protein L11 has been solved at 2.8 angstrom resolution. It reveals a precisely folded RNA structure that is stabilized by extensive tertiary contacts and contains an unusually large core of stacked bases. A bulge loop base from one hairpin of the RNA is intercalated into the distorted major groove of another helix; the protein locks this tertiary interaction into place by binding to the intercalated base from the minor groove side. This direct interaction with a key ribosomal RNA tertiary interaction suggests that part of the role of L11 is to stabilize an unusual RNA fold within the ribosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Conn, G L -- Draper, D E -- Lattman, E E -- Gittis, A G -- R37 GM29048/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 May 14;284(5417):1171-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10325228" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/metabolism ; Base Pairing ; Base Sequence ; Binding Sites ; Crystallography, X-Ray ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Peptide Elongation Factor G ; Peptide Elongation Factors/metabolism ; Phylogeny ; Protein Conformation ; RNA, Bacterial/*chemistry/metabolism ; RNA, Ribosomal/*chemistry/metabolism ; Ribosomal Proteins/*chemistry/metabolism
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  • 15
    Publication Date: 1999-06-26
    Description: Motilin is a 22-amino acid peptide hormone expressed throughout the gastrointestinal (GI) tract of humans and other species. It affects gastric motility by stimulating interdigestive antrum and duodenal contractions. A heterotrimeric guanosine triphosphate-binding protein (G protein)-coupled receptor for motilin was isolated from human stomach, and its amino acid sequence was found to be 52 percent identical to the human receptor for growth hormone secretagogues. The macrolide antibiotic erythromycin also interacted with the cloned motilin receptor, providing a molecular basis for its effects on the human GI tract. The motilin receptor is expressed in enteric neurons of the human duodenum and colon. Development of motilin receptor agonists and antagonists may be useful in the treatment of multiple disorders of GI motility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feighner, S D -- Tan, C P -- McKee, K K -- Palyha, O C -- Hreniuk, D L -- Pong, S S -- Austin, C P -- Figueroa, D -- MacNeil, D -- Cascieri, M A -- Nargund, R -- Bakshi, R -- Abramovitz, M -- Stocco, R -- Kargman, S -- O'Neill, G -- Van Der Ploeg, L H -- Evans, J -- Patchett, A A -- Smith, R G -- Howard, A D -- New York, N.Y. -- Science. 1999 Jun 25;284(5423):2184-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Metabolic Disorders, Department of Medicinal Chemistry, Merck Research Laboratories, Building RY-80Y-265, 126 East Lincoln Avenue, Rahway, NJ 07065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10381885" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; Calcium/metabolism ; Cell Line ; Chromosome Mapping ; Chromosomes, Human, Pair 13 ; Cloning, Molecular ; Colon/*metabolism ; Erythromycin/metabolism ; GTP-Binding Proteins/metabolism ; Humans ; In Situ Hybridization ; Intestine, Small/*metabolism ; Ligands ; Molecular Sequence Data ; Motilin/analogs & derivatives/*metabolism ; Receptors, Gastrointestinal Hormone/*chemistry/*genetics/metabolism ; Receptors, Neuropeptide/*chemistry/*genetics/metabolism ; Stomach/*metabolism ; Thyroid Gland/metabolism ; Transfection
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-11-05
    Description: Although data on nucleotide sequence variation in the human nuclear genome have begun to accumulate, little is known about genomic diversity in chimpanzees (Pan troglodytes) and bonobos (Pan paniscus). A 10,154-base pair sequence on the chimpanzee X chromosome is reported, representing all major subspecies and bonobos. Comparison to humans shows the diversity of the chimpanzee sequences to be almost four times as high and the age of the most recent common ancestor three times as great as the corresponding values of humans. Phylogenetic analyses show the sequences from the different chimpanzee subspecies to be intermixed and the distance between some chimpanzee sequences to be greater than the distance between them and the bonobo sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaessmann, H -- Wiebe, V -- Paabo, S -- New York, N.Y. -- Science. 1999 Nov 5;286(5442):1159-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institute for Evolutionary Anthropology, Inselstrasse 22, D-04103 Leipzig, Germany. kaessmann@eva.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10550054" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA/*genetics ; *Genetic Variation ; *Genome ; Gorilla gorilla/genetics ; Humans ; Molecular Sequence Data ; Mutation ; Pan paniscus/classification/*genetics ; Pan troglodytes/classification/*genetics ; Phylogeny ; Recombination, Genetic ; Species Specificity ; X Chromosome/*genetics
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  • 17
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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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  • 18
    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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  • 19
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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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  • 20
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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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  • 21
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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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  • 22
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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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  • 23
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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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  • 24
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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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  • 25
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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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  • 26
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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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  • 27
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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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  • 28
    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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  • 29
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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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  • 30
    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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  • 31
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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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  • 32
    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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  • 33
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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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  • 34
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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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  • 35
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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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  • 36
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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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  • 37
    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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  • 38
    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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  • 39
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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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  • 40
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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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  • 41
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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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  • 42
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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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  • 43
    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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  • 44
    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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  • 45
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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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  • 46
    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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  • 47
    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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  • 48
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 49
    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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  • 50
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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
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  • 51
    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
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  • 52
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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
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  • 53
    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
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  • 54
    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
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  • 55
    Publication Date: 1997-03-21
    Description: The "Spanish" influenza pandemic killed at least 20 million people in 1918-1919, making it the worst infectious pandemic in history. Understanding the origins of the 1918 virus and the basis for its exceptional virulence may aid in the prediction of future influenza pandemics. RNA from a victim of the 1918 pandemic was isolated from a formalin-fixed, paraffin-embedded, lung tissue sample. Nine fragments of viral RNA were sequenced from the coding regions of hemagglutinin, neuraminidase, nucleoprotein, matrix protein 1, and matrix protein 2. The sequences are consistent with a novel H1N1 influenza A virus that belongs to the subgroup of strains that infect humans and swine, not the avian subgroup.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taubenberger, J K -- Reid, A H -- Krafft, A E -- Bijwaard, K E -- Fanning, T G -- New York, N.Y. -- Science. 1997 Mar 21;275(5307):1793-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Pathology, Department of Cellular Pathology, Armed Forces Institute of Pathology, Washington DC 20306-6000, USA. taubenbe@email.afip.osd.mil〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9065404" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Base Sequence ; *Genes, Viral ; Hemagglutinin Glycoproteins, Influenza Virus/genetics ; History, 20th Century ; Humans ; Influenza A virus/classification/*genetics/pathogenicity ; Influenza, Human/history/*virology ; Lung/virology ; Molecular Sequence Data ; Neuraminidase/genetics ; Nucleoproteins/genetics ; Phylogeny ; Polymerase Chain Reaction ; RNA, Viral/*genetics ; *RNA-Binding Proteins ; Viral Core Proteins/genetics ; Viral Matrix Proteins/genetics ; Virulence
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  • 56
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-05-23
    Description: During translation errors of aminoacylation are corrected in editing reactions which ensure that an amino acid is stably attached to its corresponding transfer RNA (tRNA). Previous studies have not shown whether the tRNA nucleotides needed for effecting translational editing are the same as or distinct from those required for aminoacylation, but several considerations have suggested that they are the same. Here, designed tRNAs that are highly active for aminoacylation but are not active in translational editing are presented. The editing reaction can be controlled by manipulation of nucleotides at the corner of the L-shaped tRNA. In contrast, these manipulations do not affect aminoacylation. These results demonstrate the segregation of nucleotide determinants for the editing and aminoacylation functions of tRNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hale, S P -- Auld, D S -- Schmidt, E -- Schimmel, P -- GM15539/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 May 23;276(5316):1250-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9157882" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Base Sequence ; Binding Sites ; Cloning, Molecular ; Escherichia coli ; Molecular Sequence Data ; Nucleic Acid Conformation ; *RNA Editing ; RNA, Transfer/*metabolism ; RNA, Transfer, Ile/chemistry/metabolism ; RNA, Transfer, Val/chemistry/metabolism
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-01-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lorimer, B G -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):601-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9019811" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes ; Base Sequence ; DNA, Complementary/*genetics ; Databases, Factual ; *Genome, Human ; Humans ; Intellectual Property ; Publishing ; Research Support as Topic ; Sequence Analysis, DNA ; United States
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  • 58
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-08-22
    Description: Mutations in the SUPERMAN gene affect flower development in Arabidopsis. Seven heritable but unstable sup epi-alleles (the clark kent alleles) are associated with nearly identical patterns of excess cytosine methylation within the SUP gene and a decreased level of SUP RNA. Revertants of these alleles are largely demethylated at the SUP locus and have restored levels of SUP RNA. A transgenic Arabidopsis line carrying an antisense methyltransferase gene, which shows an overall decrease in genomic cytosine methylation, also contains a hypermethylated sup allele. Thus, disruption of methylation systems may yield more complex outcomes than expected and can result in methylation defects at known genes. The clark kent alleles differ from the antisense line because they do not show a general decrease in genomic methylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobsen, S E -- Meyerowitz, E M -- New York, N.Y. -- Science. 1997 Aug 22;277(5329):1100-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology 156-29, 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/9262479" target="_blank"〉PubMed〈/a〉
    Keywords: *Alleles ; Arabidopsis/*genetics/growth & development/metabolism ; *Arabidopsis Proteins ; Base Sequence ; Crosses, Genetic ; Cytosine/metabolism ; DNA (Cytosine-5-)-Methyltransferase/genetics ; *DNA Methylation ; DNA, Antisense ; DNA, Plant/metabolism ; Gene Expression Regulation, Plant ; *Genes, Plant ; Genetic Complementation Test ; Molecular Sequence Data ; Mutation ; Phenotype ; Plants, Genetically Modified ; RNA, Messenger/metabolism ; RNA, Plant/metabolism ; Transcription Factors/*genetics
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  • 59
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-11-14
    Description: Pathogenic Yersinia species have a specialized secretion system (type III) to target cytotoxic Yop proteins during infection. The signals of YopE and YopN sufficient for the secretion of translational reporter fusions were mapped to the first 15 codons. No common amino acid or peptide sequence could be identified among the secretion signals. Systematic mutagenesis of the secretion signal yielded mutants defective in Yop translation; however, no point mutants could be identified that specifically abolished secretion. Frameshift mutations that completely altered the peptide sequences of these signals also failed to prevent secretion. Thus, the signal that leads to the type III secretion of Yop proteins appears to be encoded in their messenger RNA rather than the peptide sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, D M -- Schneewind, O -- AI 07323/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 7;278(5340):1140-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Molecular Biology Institute, University of California, Los Angeles, School of Medicine, 10833 Le Conte Avenue, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9353199" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Outer Membrane Proteins/chemistry/genetics/*secretion ; Bacterial Proteins/chemistry/genetics/*secretion ; Base Sequence ; Codon ; Frameshift Mutation ; *Membrane Proteins ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Point Mutation ; Protein Biosynthesis ; RNA, Bacterial/chemistry/*genetics/metabolism ; RNA, Messenger/chemistry/*genetics/metabolism ; Recombinant Fusion Proteins/biosynthesis/secretion ; Yersinia enterocolitica/*metabolism/pathogenicity
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  • 60
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-04-11
    Description: The use of molecular phylogenies to examine evolutionary questions has become commonplace with the automation of DNA sequencing and the availability of efficient computer programs to perform phylogenetic analyses. The application of computer simulation and likelihood ratio tests to evolutionary hypotheses represents a recent methodological development in this field. Likelihood ratio tests have enabled biologists to address many questions in evolutionary biology that have been difficult to resolve in the past, such as whether host-parasite systems are cospeciating and whether models of DNA substitution adequately explain observed sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huelsenbeck, J P -- Rannala, B -- GM40282/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Apr 11;276(5310):227-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Integrative Biology, University of California, Berkeley, CA 94720, USA. john@mws4.biol.berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9092465" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Biological Evolution ; Computer Simulation ; *DNA/genetics ; Electron Transport Complex IV/genetics ; *Evolution, Molecular ; Hantavirus/genetics ; Likelihood Functions ; Mutation ; Phthiraptera/genetics ; *Phylogeny ; RNA, Viral/genetics ; Rodentia/genetics
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  • 61
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-05-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1997 May 23;276(5316):1189-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9182326" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Computer Communication Networks ; *Dna ; Europe ; Germany ; Humans ; *Information Dissemination ; Intellectual Property ; *Internationality ; *Patents as Topic ; Time Factors ; United States
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  • 62
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-01-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Warren, S T -- New York, N.Y. -- Science. 1997 Jan 17;275(5298):408-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9005557" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Base Sequence ; *Crossing Over, Genetic ; Homeodomain Proteins/chemistry/*genetics ; Humans ; Molecular Sequence Data ; Mutation ; Peptides/analysis/*genetics ; Polydactyly/*genetics ; Syndactyly/*genetics ; *Transcription Factors ; Trinucleotide Repeats
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  • 63
    Publication Date: 1997-06-27
    Description: Individual plastids of vascular plants have generally been considered to be discrete autonomous entities that do not directly communicate with each other. However, in transgenic plants in which the plastid stroma was labeled with green fluorescent protein (GFP), thin tubular projections emanated from individual plastids and sometimes connected to other plastids. Flow of GFP between interconnected plastids could be observed when a single plastid or an interconnecting plastid tubule was photobleached and the loss of green fluorescence by both plastids was seen. These tubules allow the exchange of molecules within an interplastid communication system, which may facilitate the coordination of plastid activities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kohler, R H -- Cao, J -- Zipfel, W R -- Webb, W W -- Hanson, M R -- R07719/PHS HHS/ -- RR04224/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 27;276(5321):2039-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Genetics and Development, Cornell University, Biotechnology Building, Ithaca, NY 14853-2703, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9197266" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chloroplasts/*metabolism/*ultrastructure ; Cytoplasm/metabolism ; Green Fluorescent Proteins ; Luminescent Proteins/*metabolism ; Microscopy/methods ; Microscopy, Fluorescence ; Molecular Sequence Data ; Plant Leaves/*ultrastructure ; Plants, Genetically Modified ; Plants, Toxic ; Recombinant Fusion Proteins/metabolism ; Tobacco
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  • 64
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-08-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ehrenstein, D -- New York, N.Y. -- Science. 1997 Aug 8;277(5327):762.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9273696" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Mapping ; *Computer Communication Networks ; *Databases, Factual ; *Genes ; Genome, Human ; Humans ; National Institutes of Health (U.S.) ; National Library of Medicine (U.S.) ; Neoplasms/*genetics ; United States
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  • 65
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-05-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1997 May 2;276(5313):699-702.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9157549" target="_blank"〉PubMed〈/a〉
    Keywords: Archaea/*classification/genetics/physiology ; Bacteria/*classification/genetics ; Base Sequence ; Biological Evolution ; History, 20th Century ; Origin of Life ; *Phylogeny ; RNA, Bacterial/genetics ; RNA, Ribosomal/genetics ; Sequence Analysis, RNA ; Temperature ; United States
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  • 66
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-04-25
    Description: A population of RNA molecules that catalyze the template-directed ligation of RNA substrates was made to evolve in a continuous manner in the test tube. A simple serial transfer procedure was used to achieve approximately 300 successive rounds of catalysis and selective amplification in 52 hours. During this time, the population size was maintained against an overall dilution of 3 x 10(298). Both the catalytic rate and amplification rate of the RNAs improved substantially as a consequence of mutations that accumulated during the evolution process. Continuous in vitro evolution makes it possible to maintain laboratory "cultures" of catalytic molecules that can be perpetuated indefinitely.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wright, M C -- Joyce, G F -- New York, N.Y. -- Science. 1997 Apr 25;276(5312):614-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, The Skaggs Institute for Chemical Biology, The 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/9110984" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Catalysis ; DNA-Directed RNA Polymerases/genetics/metabolism ; *Directed Molecular Evolution ; Evolution, Molecular ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Promoter Regions, Genetic ; *RNA, Catalytic/chemistry/genetics/metabolism ; Saccharomyces cerevisiae/chemistry ; Templates, Genetic ; Transcription, Genetic ; Viral Proteins
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  • 67
    Publication Date: 1997-07-11
    Description: An integrated human-mouse positional candidate approach was used to identify the gene responsible for the phenotypes observed in a mouse model of Niemann-Pick type C (NP-C) disease. The predicted murine NPC1 protein has sequence homology to the putative transmembrane domains of the Hedgehog signaling molecule Patched, to the cholesterol-sensing regions of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase and SREBP cleavage-activating protein (SCAP), and to the NPC1 orthologs identified in human, the nematode Caenorhabditis elegans, and the yeast Saccharomyces cerevisiae. The mouse model may provide an important resource for studying the role of NPC1 in cholesterol homeostasis and neurodegeneration and for assessing the efficacy of new drugs for NP-C disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Loftus, S K -- Morris, J A -- Carstea, E D -- Gu, J Z -- Cummings, C -- Brown, A -- Ellison, J -- Ohno, K -- Rosenfeld, M A -- Tagle, D A -- Pentchev, P G -- Pavan, W J -- New York, N.Y. -- Science. 1997 Jul 11;277(5323):232-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetic Disease Research, National Human Genome Research Institute, National Institutes of Health (NIH), Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9211850" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cholesterol/*metabolism ; *Disease Models, Animal ; Homeostasis ; Humans ; Hydroxymethylglutaryl CoA Reductases/chemistry ; Intracellular Signaling Peptides and Proteins ; Lysosomes/metabolism ; Membrane Proteins/chemistry ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mice, Mutant Strains ; Molecular Sequence Data ; Mutation ; Niemann-Pick Diseases/*genetics/metabolism ; Phenotype ; Protein Sorting Signals/chemistry ; Proteins/chemistry/*genetics/physiology ; Sequence Homology, Amino Acid
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  • 68
    Publication Date: 1997-11-21
    Description: The gene responsible for autosomal dominant, fully penetrant, nonsyndromic sensorineural progressive hearing loss in a large Costa Rican kindred was previously localized to chromosome 5q31 and named DFNA1. Deafness in the family is associated with a protein-truncating mutation in a human homolog of the Drosophila gene diaphanous. The truncation is caused by a single nucleotide substitution in a splice donor, leading to a four-base pair insertion in messenger RNA and a frameshift. The diaphanous protein is a profilin ligand and target of Rho that regulates polymerization of actin, the major component of the cytoskeleton of hair cells of the inner ear.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lynch, E D -- Lee, M K -- Morrow, J E -- Welcsh, P L -- Leon, P E -- King, M C -- R01-DC01076/DC/NIDCD NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1315-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Washington, Seattle, WA 98195, USA. eric@lynch.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9360932" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/chemistry/*genetics/physiology ; Chromosome Mapping ; Chromosomes, Human, Pair 5 ; Cochlea/metabolism ; *Contractile Proteins ; Deafness/*genetics/metabolism/pathology ; Drosophila/genetics ; *Drosophila Proteins ; Female ; Frameshift Mutation ; GTP-Binding Proteins/metabolism ; Gene Expression ; Hair Cells, Auditory/*metabolism/ultrastructure ; Humans ; Male ; Microfilament Proteins/metabolism ; Molecular Sequence Data ; Pedigree ; Profilins ; RNA Splicing ; RNA, Messenger/genetics/metabolism ; X Chromosome
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  • 69
    Publication Date: 1997-02-14
    Description: Cancers of the microsatellite mutator phenotype (MMP) show exaggerated genomic instability at simple repeat sequences. More than 50 percent (21 out of 41) of human MMP+ colon adenocarcinomas examined were found to have frameshift mutations in a tract of eight deoxyguanosines [(G)8] within BAX, a gene that promotes apoptosis. These mutations were absent in MMP- tumors and were significantly less frequent in (G)8 repeats from other genes. Frameshift mutations were present in both BAX alleles in some MMP+ colon tumor cell lines and in primary tumors. These results suggest that inactivating BAX mutations are selected for during the progression of colorectal MMP+ tumors and that the wild-type BAX gene plays a suppressor role in a p53-independent pathway for colorectal carcinogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rampino, N -- Yamamoto, H -- Ionov, Y -- Li, Y -- Sawai, H -- Reed, J C -- Perucho, M -- CA38579/CA/NCI NIH HHS/ -- CA63585/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Feb 14;275(5302):967-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Burnham Institute, La Jolla Cancer Research Center, 10901 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/9020077" target="_blank"〉PubMed〈/a〉
    Keywords: Adenocarcinoma/*genetics ; Alleles ; Apoptosis ; Base Sequence ; Colonic Neoplasms/*genetics ; *Frameshift Mutation ; Gene Expression ; *Genes, Tumor Suppressor ; Humans ; Microsatellite Repeats/*genetics ; Molecular Sequence Data ; Mutation ; Phenotype ; Polymerase Chain Reaction ; Proto-Oncogene Proteins/*genetics ; *Proto-Oncogene Proteins c-bcl-2 ; Sequence Deletion ; Tumor Cells, Cultured ; bcl-2-Associated X Protein
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  • 70
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-08-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1997 Aug 22;277(5329):1028-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9289846" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; California ; *Cloning, Molecular ; DNA, Recombinant ; Drug Industry ; *Genetic Research ; *Genetic Vectors ; Guideline Adherence/legislation & jurisprudence ; Humans ; Insulin/*genetics ; National Institutes of Health (U.S.) ; *Patents as Topic ; *Plasmids ; Rats ; Recombinant Proteins ; Scientific Misconduct/*legislation & jurisprudence ; United States ; Universities
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  • 71
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-06-13
    Description: Intron excision is an essential step in eukaryotic gene expression, but the molecular mechanisms by which the spliceosome accurately identifies splice sites in nuclear precursors to messenger RNAs (pre-mRNAs) are not well understood. A bimolecular assay for the second step of splicing has now revealed that exon ligation by the human spliceosome does not require covalent attachment of a 3' splice site to the branch site. Furthermore, accurate definition of the 3' splice site in this system is independent of either a covalently attached polypyrimidine tract or specific 3' exon sequences. Rather, in this system 3' splice site selection apparently occurs with a 5' --〉 3' directionality.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, K -- Moore, M J -- GM53007/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 13;276(5319):1712-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉W. M. Keck Institute for Cellular Visualization, Department of Biochemistry, Brandeis University, Waltham, MA 02254, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9180084" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/genetics ; Base Sequence ; Binding Sites ; *Exons ; Humans ; Introns ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA Precursors/genetics/*metabolism ; *RNA Splicing ; Spliceosomes/*metabolism
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  • 72
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-05-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, M -- New York, N.Y. -- Science. 1997 May 16;276(5315):1032-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9173539" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amphibians/*classification/genetics ; Animals ; Base Sequence ; Biological Evolution ; DNA, Mitochondrial/genetics ; Humans ; Mammals/*classification/genetics ; *Phylogeny
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  • 73
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-07-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, N -- New York, N.Y. -- Science. 1997 Jul 25;277(5325):478.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9254420" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/*genetics ; Base Sequence ; DNA, Bacterial/genetics ; DNA, Circular/genetics ; European Union ; *Genome, Bacterial ; International Cooperation ; Japan ; *Sequence Analysis, DNA
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  • 74
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-02-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1997 Feb 21;275(5303):1068.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9054008" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Base Sequence ; *Biological Evolution ; *Birds/genetics ; DNA, Mitochondrial/genetics ; Evolution, Molecular ; *Fossils ; *Genes ; Mutation ; Phylogeny
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  • 75
    Publication Date: 1997-11-21
    Description: The Janus family of tyrosine kinases (JAK) plays an essential role in development and in coupling cytokine receptors to downstream intracellular signaling events. A t(9;12)(p24;p13) chromosomal translocation in a T cell childhood acute lymphoblastic leukemia patient was characterized and shown to fuse the 3' portion of JAK2 to the 5' region of TEL, a gene encoding a member of the ETS transcription factor family. The TEL-JAK2 fusion protein includes the catalytic domain of JAK2 and the TEL-specific oligomerization domain. TEL-induced oligomerization of TEL-JAK2 resulted in the constitutive activation of its tyrosine kinase activity and conferred cytokine-independent proliferation to the interleukin-3-dependent Ba/F3 hematopoietic cell line.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lacronique, V -- Boureux, A -- Valle, V D -- Poirel, H -- Quang, C T -- Mauchauffe, M -- Berthou, C -- Lessard, M -- Berger, R -- Ghysdael, J -- Bernard, O A -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1309-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉U 301 de l'Institut National de la Sante et de la Recherche Medicale and SD 401 No. 301 CNRS, Institut de Genetique Moleculaire, 27 rue Juliette Dodu, 75010 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9360930" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biopolymers ; Cell Division ; Cell Line ; Child, Preschool ; DNA-Binding Proteins/chemistry/genetics/metabolism ; Enzyme Activation ; Humans ; Interleukin-3/physiology ; Janus Kinase 2 ; Leukemia-Lymphoma, Adult T-Cell/genetics/*metabolism ; Male ; Mice ; *Milk Proteins ; Molecular Sequence Data ; Oncogene Proteins, Fusion/chemistry/genetics/*metabolism ; Phosphorylation ; Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; *Proto-Oncogene Proteins ; Proto-Oncogene Proteins c-ets ; *Repressor Proteins ; STAT5 Transcription Factor ; Signal Transduction ; Trans-Activators/metabolism ; Transcription Factors/chemistry/genetics/metabolism ; Transfection ; Translocation, Genetic
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  • 76
    Publication Date: 1997-01-31
    Description: Glaucoma is a major cause of blindness and is characterized by progressive degeneration of the optic nerve and is usually associated with elevated intraocular pressure. Analyses of sequence tagged site (STS) content and haplotype sharing between families affected with chromosome 1q-linked open angle glaucoma (GLC1A) were used to prioritize candidate genes for mutation screening. A gene encoding a trabecular meshwork protein (TIGR) mapped to the narrowest disease interval by STS content and radiation hybrid mapping. Thirteen glaucoma patients were found to have one of three mutations in this gene (3.9 percent of the population studied). One of these mutations was also found in a control individual (0.2 percent). Identification of these mutations will aid in early diagnosis, which is essential for optimal application of existing therapies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, E M -- Fingert, J H -- Alward, W L -- Nguyen, T D -- Polansky, J R -- Sunden, S L -- Nishimura, D -- Clark, A F -- Nystuen, A -- Nichols, B E -- Mackey, D A -- Ritch, R -- Kalenak, J W -- Craven, E R -- Sheffield, V C -- EY02477/EY/NEI NIH HHS/ -- EY08905/EY/NEI NIH HHS/ -- EY10564/EY/NEI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):668-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ophthalmology, University of Iowa College of Medicine, Iowa City, IA 52242, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9005853" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Mapping ; Chromosomes, Artificial, Yeast ; *Chromosomes, Human, Pair 1 ; Cytoskeletal Proteins ; Eye Proteins/*genetics ; Female ; Genetic Linkage ; Glaucoma, Open-Angle/*genetics ; *Glycoproteins ; Haplotypes ; Humans ; Male ; Molecular Sequence Data ; Mutation ; Pedigree ; Polymerase Chain Reaction ; Polymorphism, Single-Stranded Conformational ; Sequence Tagged Sites ; Trabecular Meshwork/*metabolism
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  • 77
    Publication Date: 1997-01-31
    Description: A method is described for selecting DNA-binding proteins that recognize desired sequences. The protocol involves gradually extending a new zinc finger protein across the desired 9- or 10-base pair target site, adding and optimizing one finger at a time. This procedure was tested with a TATA box, a p53 binding site, and a nuclear receptor element, and proteins were obtained that bind with nanomolar dissociation constants and discriminate effectively (greater than 20,000-fold) against nonspecific DNA. This strategy may provide important information about protein-DNA recognition as well as powerful tools for biomedical research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greisman, H A -- Pabo, C O -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):657-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9005850" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Composition ; Base Sequence ; Binding Sites ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Genes, p53 ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Peptide Library ; Protein Conformation ; *Protein Engineering ; Protein Structure, Secondary ; Receptors, Cytoplasmic and Nuclear/genetics ; TATA Box ; Transcription Factors/chemistry/metabolism ; *Zinc Fingers
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  • 78
    Publication Date: 1997-11-21
    Description: The wild-type Caenorhabditis elegans nematode ages rapidly, undergoing development, senescence, and death in less than 3 weeks. In contrast, mutants with reduced activity of the gene daf-2, a homolog of the insulin and insulin-like growth factor receptors, age more slowly than normal and live more than twice as long. These mutants are active and fully fertile and have normal metabolic rates. The life-span extension caused by daf-2 mutations requires the activity of the gene daf-16. daf-16 appears to play a unique role in life-span regulation and encodes a member of the hepatocyte nuclear factor 3 (HNF-3)/forkhead family of transcriptional regulators. In humans, insulin down-regulates the expression of certain genes by antagonizing the activity of HNF-3, raising the possibility that aspects of this regulatory system have been conserved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, K -- Dorman, J B -- Rodan, A -- Kenyon, C -- AG11816/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1319-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143-0554, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9360933" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/genetics ; Amino Acid Sequence ; Animals ; Base Sequence ; Caenorhabditis elegans/*genetics/physiology ; *Caenorhabditis elegans Proteins ; Cloning, Molecular ; DNA, Complementary ; Forkhead Transcription Factors ; Genes, Helminth ; Humans ; Insulin/physiology ; Longevity/genetics ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/genetics ; Phenotype ; Receptor, Insulin/genetics/physiology ; Sequence Alignment ; Somatomedins/physiology ; Transcription Factors/chemistry/*genetics/*physiology
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  • 79
    Publication Date: 1997-06-27
    Description: Parkinson's disease (PD) is a common neurodegenerative disorder with a lifetime incidence of approximately 2 percent. A pattern of familial aggregation has been documented for the disorder, and it was recently reported that a PD susceptibility gene in a large Italian kindred is located on the long arm of human chromosome 4. A mutation was identified in the alpha-synuclein gene, which codes for a presynaptic protein thought to be involved in neuronal plasticity, in the Italian kindred and in three unrelated families of Greek origin with autosomal dominant inheritance for the PD phenotype. This finding of a specific molecular alteration associated with PD will facilitate the detailed understanding of the pathophysiology of the disorder.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Polymeropoulos, M H -- Lavedan, C -- Leroy, E -- Ide, S E -- Dehejia, A -- Dutra, A -- Pike, B -- Root, H -- Rubenstein, J -- Boyer, R -- Stenroos, E S -- Chandrasekharappa, S -- Athanassiadou, A -- Papapetropoulos, T -- Johnson, W G -- Lazzarini, A M -- Duvoisin, R C -- Di Iorio, G -- Golbe, L I -- Nussbaum, R L -- New York, N.Y. -- Science. 1997 Jun 27;276(5321):2045-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetic Disease Research, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD 20892-1430, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9197268" target="_blank"〉PubMed〈/a〉
    Keywords: Age of Onset ; Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human, Pair 4 ; Female ; Genes, Dominant ; Genetic Markers ; Greece ; Humans ; Italy ; Male ; Molecular Sequence Data ; Nerve Tissue Proteins/chemistry/*genetics/physiology ; Parkinson Disease/*genetics ; Pedigree ; Phenotype ; *Point Mutation ; Polymerase Chain Reaction ; Protein Structure, Secondary ; Synucleins ; alpha-Synuclein
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  • 80
    Publication Date: 1997-07-04
    Description: The steady state of histone acetylation is established and maintained by multiple histone acetyltransferases and deacetylases, and this steady state affects chromatin structure and function. The identification of a maize complementary DNA encoding the chromatin-bound deacetylase HD2 is reported. This protein was not homologous to the yeast RPD3 transcriptional regulator. It was expressed throughout embryo germination in correlation with the proliferative activity of cells. Antibodies against recombinant HD2-p39 immunoprecipitated the native enzyme complex, which was composed of phosphorylated p39 subunits. Immunofluorescence microscopy and sequence homologies suggested nucleolar localization. HD2 is an acidic nucleolar phosphoprotein that might regulate ribosomal chromatin structure and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lusser, A -- Brosch, G -- Loidl, A -- Haas, H -- Loidl, P -- New York, N.Y. -- Science. 1997 Jul 4;277(5322):88-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Innsbruck Medical School, Fritz-Pregl-Str. 3, A-6020 Innsbruck, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9204905" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Amino Acid Sequence ; Base Sequence ; Cell Nucleolus/*enzymology ; Chromatin/metabolism ; Cloning, Molecular ; DNA, Complementary ; Germination ; Histone Deacetylases/*chemistry/genetics/isolation & purification/*metabolism ; Histones/metabolism ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Phosphoproteins/*chemistry/metabolism ; Phosphorylation ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Seeds/enzymology ; Zea mays/embryology/*enzymology
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  • 81
    Publication Date: 1997-10-24
    Description: Ancient duplications and rearrangements of protein-coding segments have resulted in complex gene family relationships. Duplications can be tandem or dispersed and can involve entire coding regions or modules that correspond to folded protein domains. As a result, gene products may acquire new specificities, altered recognition properties, or modified functions. Extreme proliferation of some families within an organism, perhaps at the expense of other families, may correspond to functional innovations during evolution. The underlying processes are still at work, and the large fraction of human and other genomes consisting of transposable elements may be a manifestation of the evolutionary benefits of genomic flexibility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Henikoff, S -- Greene, E A -- Pietrokovski, S -- Bork, P -- Attwood, T K -- Hood, L -- GM29009/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 24;278(5338):609-14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fred Hutchinson Cancer Research Center and Howard Hughes Medical Institute, Seattle, WA 98109-1024, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381171" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Computer Communication Networks ; Databases as Topic ; Evolution, Molecular ; Genetic Variation ; Humans ; *Multigene Family ; Phylogeny ; Proteins/chemistry/classification/*genetics/physiology ; Repetitive Sequences, Nucleic Acid
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  • 82
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-02-21
    Description: The extent of terrestrial vertebrate extinctions at the end of the Cretaceous is poorly understood, and estimates have ranged from a mass extinction to limited extinctions of specific groups. Molecular and paleontological data demonstrate that modern bird orders started diverging in the Early Cretaceous; at least 22 avian lineages of modern birds cross the Cretaceous-Tertiary boundary. Data for several other terrestrial vertebrate groups indicate a similar pattern of survival and, taken together, favor incremental changes during a Cretaceous diversification of birds and mammals rather than an explosive radiation in the Early Tertiary.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cooper, A -- Penny, D -- New York, N.Y. -- Science. 1997 Feb 21;275(5303):1109-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biological Sciences, Victoria University of Wellington, Wellington, New Zealand. alan.cooper@bioanth.ox.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9027308" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Biological Evolution ; *Birds/genetics ; Evolution, Molecular ; *Fossils ; *Genes ; Genes, mos ; Mammals/genetics ; Mitochondria/genetics ; Molecular Sequence Data ; Phylogeny ; RNA, Ribosomal/genetics
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  • 83
    Publication Date: 1997-06-13
    Description: Mitochondrial DNA control region sequences were analyzed from 162 wolves at 27 localities worldwide and from 140 domestic dogs representing 67 breeds. Sequences from both dogs and wolves showed considerable diversity and supported the hypothesis that wolves were the ancestors of dogs. Most dog sequences belonged to a divergent monophyletic clade sharing no sequences with wolves. The sequence divergence within this clade suggested that dogs originated more than 100,000 years before the present. Associations of dog haplotypes with other wolf lineages indicated episodes of admixture between wolves and dogs. Repeated genetic exchange between dog and wolf populations may have been an important source of variation for artificial selection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vila, C -- Savolainen, P -- Maldonado, J E -- Amorim, I R -- Rice, J E -- Honeycutt, R L -- Crandall, K A -- Lundeberg, J -- Wayne, R K -- New York, N.Y. -- Science. 1997 Jun 13;276(5319):1687-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, Los Angeles, CA 90095-1606, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9180076" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Biological Evolution ; Breeding ; Carnivora/*genetics ; Crosses, Genetic ; DNA, Mitochondrial/*genetics ; Dogs/classification/*genetics ; Female ; Haplotypes ; Male ; Molecular Sequence Data ; Phylogeny ; Sequence Homology, Nucleic Acid
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  • 84
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-02-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1997 Feb 28;275(5304):1263.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9064781" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/genetics ; *Genes ; HIV Infections/virology ; Humans ; Membrane Proteins/genetics ; *Patents as Topic ; Receptors, CCR5 ; Receptors, CXCR4 ; Receptors, Cytokine/*genetics ; Receptors, HIV/*genetics ; United States
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  • 85
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-06-20
    Description: The plant hormone auxin regulates plant physiology by modulating the interaction of transcription factors with auxin response elements (AuxREs) of the affected genes. A transcription factor, Auxin Response Factor 1 (ARF1), that binds to the sequence TGTCTC in AuxREs was cloned from Arabidopsis by using a yeast one-hybrid system. ARF1 has an amino-terminal DNA-binding domain related to the carboxyl terminus of the maize transactivator Viviparous-1. Sequence requirements for ARF1 binding in vitro are identical to those that confer auxin responsiveness in vivo. The carboxyl terminus of ARF1 contains two motifs found in the Aux/IAA class of proteins and appears to mediate protein-protein interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ulmasov, T -- Hagen, G -- Guilfoyle, T J -- New York, N.Y. -- Science. 1997 Jun 20;276(5320):1865-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Missouri, 117 Schweitzer Hall, Columbia, MO 65211, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9188533" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/genetics ; Arabidopsis Proteins ; Base Sequence ; Binding Sites ; Cloning, Molecular ; DNA, Plant/genetics/*metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Genes, Plant ; Indoleacetic Acids/*pharmacology ; Molecular Sequence Data ; Mutation ; Plant Proteins ; *Promoter Regions, Genetic ; *Repetitive Sequences, Nucleic Acid ; Transcription Factors/chemistry/genetics/*metabolism
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  • 86
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-09-20
    Description: To adhere to solid surfaces, marine mussels produce byssal threads, each of which is a stiff tether at one end and a shock absorber with 160 percent extensibility at the other end. The elastic extensibility of proximal byssus is extraordinary given its construction of collagen and the limited extension (less than 10 percent) of most collagenous materials. From the complementary DNA, we deduced that the primary structure of a collagenous protein (preCol-P) predominating in the extensible proximal portion of the threads encodes an unprecedented natural block copolymer with three major domain types: a central collagen domain, flanking elastic domains, and histidine-rich terminal domains. The elastic domains have sequence motifs that strongly resemble those of elastin and the amorphous glycine-rich regions of spider silk fibroins. Byssal thread extensibility may be imparted by the elastic domains of preCol-P.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coyne, K J -- Qin, X X -- Waite, J H -- New York, N.Y. -- Science. 1997 Sep 19;277(5333):1830-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉College of Marine Studies and Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9295275" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/chemistry ; Amino Acid Sequence ; Animals ; Base Sequence ; Biopolymers/chemistry ; Bivalvia/*chemistry/genetics ; Collagen/*chemistry/genetics ; DNA, Complementary ; Elasticity ; Elastin/chemistry/genetics ; Fibroins/chemistry ; Glycine/chemistry ; Histidine/chemistry ; Molecular Sequence Data ; Proline/chemistry ; Protein Conformation ; Protein Precursors/*chemistry/genetics ; Protein Structure, Secondary ; Sequence Alignment ; Serine/chemistry
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  • 87
    Publication Date: 1997-05-16
    Description: In many organisms, pattern formation in the embryo develops from the polarized distributions of messenger RNAs (mRNAs) in the egg. In Xenopus, the mRNA encoding Vg1, a growth factor involved in mesoderm induction, is localized to the vegetal cortex of oocytes. A protein named Vera was shown to be involved in Vg1 mRNA localization. Vera cofractionates with endoplasmic reticulum (ER) membranes, and endogenous Vg1 mRNA is associated with a subcompartment of the ER. Vera may promote mRNA localization in Xenopus oocytes by mediating an interaction between the Vg1 3' untranslated region and the ER subcompartment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deshler, J O -- Highett, M I -- Schnapp, B J -- GM16114-03/GM/NIGMS NIH HHS/ -- NS-26846/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1997 May 16;276(5315):1128-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9148809" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Transport ; Endoplasmic Reticulum/*metabolism ; Glycoproteins/*genetics ; Molecular Sequence Data ; Mutation ; Oocytes/*metabolism ; Oogenesis ; Protein Binding ; Proteins/*metabolism ; RNA, Messenger/genetics/*metabolism ; Repetitive Sequences, Nucleic Acid ; Transforming Growth Factor beta/*genetics ; Xenopus Proteins ; Xenopus laevis
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  • 88
    Publication Date: 1997-02-28
    Description: The molecular mechanisms that link cell-cycle controls to the mitotic apparatus are poorly understood. A component of the Saccharomyces cerevisiae spindle, Ase1, was observed to undergo cell cycle-specific degradation mediated by the cyclosome, or anaphase promoting complex (APC). Ase1 was degraded when cells exited from mitosis and entered G1. Inappropriate expression of stable Ase1 during G1 produced a spindle defect that is sensed by the spindle assembly checkpoint. In addition, loss of ASE1 function destabilized telophase spindles, and expression of a nondegradable Ase1 mutant delayed spindle disassembly. APC-mediated proteolysis therefore appears to regulate both spindle assembly and disassembly.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Juang, Y L -- Huang, J -- Peters, J M -- McLaughlin, M E -- Tai, C Y -- Pellman, D -- New York, N.Y. -- Science. 1997 Feb 28;275(5304):1311-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatric Oncology, The Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9036857" target="_blank"〉PubMed〈/a〉
    Keywords: *Anaphase ; Base Sequence ; Cell Cycle Proteins/*metabolism ; G1 Phase ; Microtubule-Associated Proteins/*metabolism ; Mitosis ; Molecular Sequence Data ; Morphogenesis ; Mutagenesis, Site-Directed ; Saccharomyces cerevisiae/*cytology/metabolism ; Spindle Apparatus/*metabolism/ultrastructure ; Telophase
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  • 89
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-11-14
    Description: The structure of ribosomal RNA (rRNA) in the ribosome was probed with hydroxyl radicals generated locally from iron(II) tethered to the 5' ends of anticodon stem-loop analogs (ASLs) of transfer RNA. The ASLs, ranging in length from 4 to 33 base pairs, bound to the ribosome in a messenger RNA-dependent manner and directed cleavage to specific regions of the 16S, 23S, and 5S rRNA chains. The positions and intensities of cleavage depended on whether the ASLs were bound to the ribosomal A or P site, and on the lengths of their stems. These data predict the three-dimensional locations of the rRNA targets relative to the positions of A- and P- site transfer RNAs inside the ribosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joseph, S -- Weiser, B -- Noller, H F -- GM-17129/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 7;278(5340):1093-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Biology of RNA, Sinsheimer Laboratories, University of California, Santa Cruz, CA 95064, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9353184" target="_blank"〉PubMed〈/a〉
    Keywords: Anticodon ; Base Composition ; Base Sequence ; Edetic Acid/analogs & derivatives/metabolism ; Ferrous Compounds/metabolism ; Hydroxyl Radical ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Organometallic Compounds/metabolism ; RNA Probes ; RNA, Ribosomal/*chemistry/metabolism ; RNA, Ribosomal, 16S/chemistry/metabolism ; RNA, Ribosomal, 23S/chemistry/metabolism ; RNA, Ribosomal, 5S/chemistry/metabolism ; RNA, Transfer/chemistry/*metabolism ; RNA, Transfer, Phe/chemistry/metabolism ; Ribosomes/*chemistry/metabolism
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  • 90
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-07-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kahn, P -- Gibbons, A -- New York, N.Y. -- Science. 1997 Jul 11;277(5323):176-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9235628" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Animals ; Base Sequence ; *Biological Evolution ; DNA, Mitochondrial/*genetics/isolation & purification ; Hominidae/*genetics ; Humans ; Mutation ; Polymerase Chain Reaction ; Sequence Analysis, DNA ; Sequence Homology, Nucleic Acid
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  • 91
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-06-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mindell, D P -- New York, N.Y. -- Science. 1997 Jun 13;276(5319):1629.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9206819" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Evolution, Molecular ; *Phylogeny
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  • 92
    Publication Date: 1997-03-07
    Description: Telomeres are essential for chromosome stability, but their functions at specific cell-cycle stages are unknown. Telomeres are now shown to have a role in chromosome separation during mitosis. In telomeric DNA mutants of Tetrahymena thermophila, created by expression of a telomerase RNA with an altered template sequence, division of the germline nucleus was severely delayed or blocked in anaphase. The mutant chromatids failed to separate completely at the midzone, becoming stretched to up to twice their normal length. These results suggest a physical block in mutant telomere separation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kirk, K E -- Harmon, B P -- Reichardt, I K -- Sedat, J W -- Blackburn, E H -- GM26259/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 7;275(5305):1478-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California, San Francisco, San Francisco, CA 94143-0414, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9045613" target="_blank"〉PubMed〈/a〉
    Keywords: *Anaphase ; Animals ; Base Sequence ; Chromatids/physiology ; Chromosomes/*physiology/ultrastructure ; DNA, Protozoan/genetics ; Micronucleus, Germline/ultrastructure ; Microscopy, Fluorescence ; Mitotic Index ; Mutation ; Phenotype ; RNA, Protozoan/genetics ; Repetitive Sequences, Nucleic Acid ; Telomerase/genetics/*metabolism ; Telomere/genetics/*physiology ; Templates, Genetic ; Tetrahymena thermophila/*cytology/genetics ; Transformation, Genetic
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  • 93
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-10-23
    Description: The fate of ventral epidermal cells differs among nematode species. Nonvulval cells fuse with the epidermis in Caenorhabditis elegans, whereas the homologous cells undergo apoptosis in Pristionchus pacificus. The homeotic gene lin-39 is involved in the regulation of these epidermal cell fates. In Caenorhabditis, lin-39 prevents cell fusion of potential vulval cells and specifies the vulva equivalence group. Pristionchus vulvaless mutants that displayed apoptosis of the vulval precursor cells were isolated, and point mutations in lin-39 were identified. Thus, the evolution of these epidermal cell fates is driven by different intrinsic properties of homologous cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eizinger, A -- Sommer, R J -- New York, N.Y. -- Science. 1997 Oct 17;278(5337):452-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck Institut fur Entwicklungsbiologie, Abteilung Zellbiologie, Spemannstrasse 35, 72076 Tubingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9334302" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Apoptosis ; Base Sequence ; *Biological Evolution ; Caenorhabditis elegans/cytology/genetics/growth & development ; Cell Fusion ; Cell Lineage ; Epidermis/cytology ; Exons ; Female ; *Genes, Helminth ; *Genes, Homeobox ; Molecular Sequence Data ; Mutation ; Phenotype ; Rhabditida/*cytology/*genetics ; Stem Cells/cytology ; Vulva/cytology
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  • 94
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-10-23
    Description: The maximal clique problem has been solved by means of molecular biology techniques. A pool of DNA molecules corresponding to the total ensemble of six-vertex cliques was built, followed by a series of selection processes. The algorithm is highly parallel and has satisfactory fidelity. This work represents further evidence for the ability of DNA computing to solve NP-complete search problems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ouyang, Q -- Kaplan, P D -- Liu, S -- Libchaber, A -- New York, N.Y. -- Science. 1997 Oct 17;278(5337):446-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉NEC Research Institute, 4 Independence Way, Princeton, NJ 08540, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9334300" target="_blank"〉PubMed〈/a〉
    Keywords: *Algorithms ; Base Sequence ; *Computing Methodologies ; *DNA/metabolism ; DNA Restriction Enzymes/metabolism ; Escherichia coli/genetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction
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  • 95
    Publication Date: 1997-06-13
    Description: Transposable elements of the mariner/Tc1 family are postulated to have spread by horizontal transfer and be relatively independent of host-specific factors. This was tested by introducing the Drosophila mauritiana element mariner into the human parasite Leishmania major, a trypanosomatid protozoan belonging to one of the most ancient eukaryotic lineages. Transposition in Leishmania was efficient, occurring in more than 20 percent of random transfectants, and proceeded by the same mechanism as in Drosophila. Insertional inactivation of a specific gene was obtained, and a modified mariner element was used to select for gene fusions, establishing mariner as a powerful genetic tool for Leishmania and other organisms. These experiments demonstrate the evolutionary range of mariner transposition in vivo and underscore the ability of this ubiquitous DNA to parasitize the eukaryotic genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gueiros-Filho, F J -- Beverley, S M -- AI2964/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 13;276(5319):1716-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9180085" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biological Evolution ; *Cinnamates ; DNA Nucleotidyltransferases/chemistry/*genetics ; *DNA Transposable Elements ; Drosophila/*genetics ; Drug Resistance ; Genes, Protozoan ; Genome, Protozoan ; Hygromycin B/analogs & derivatives/pharmacology ; Leishmania major/drug effects/*genetics ; Mutagenesis, Insertional ; RNA, Messenger/genetics/metabolism ; RNA, Protozoan/genetics/metabolism ; Species Specificity ; Transfection ; Transposases
    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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  • 96
    Publication Date: 1996-07-26
    Description: The SWI/SNF complex participates in the restructuring of chromatin for transcription. The function of the yeast SWI/SNF complex in the remodeling of a nucleosome array has now been analyzed in vitro. Binding of the purified SWI/SNF complex to a nucleosome array disrupted multiple nucleosomes in an adenosine triphosphate-dependent reaction. However, removal of SWI/SNF left a deoxyribonuclease I-hypersensitive site specifically at a nucleosome that was bound by derivatives of the transcription factor Gal4p. Analysis of individual nucleosomes revealed that the SWI/SNF complex catalyzed eviction of histones from the Gal4-bound nucleosomes. Thus, the transient action of the SWI/SNF complex facilitated irreversible disruption of transcription factor-bound nucleosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Owen-Hughes, T -- Utley, R T -- Cote, J -- Peterson, C L -- Workman, J L -- GM47867/GM/NIGMS NIH HHS/ -- R01 GM049650/GM/NIGMS NIH HHS/ -- R37 GM049650/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 26;273(5274):513-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology and Center for Gene Regulation, Pennsylvania State University, University Park, PA 16802-4500, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662543" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases ; Adenosine Triphosphate/metabolism ; Base Sequence ; Binding Sites ; DNA, Fungal/metabolism ; DNA-Binding Proteins/*metabolism ; Deoxyribonuclease I/metabolism ; Fungal Proteins/*metabolism ; Histones/metabolism ; Molecular Sequence Data ; *Nuclear Proteins ; Nucleosomes/*metabolism/ultrastructure ; Saccharomyces cerevisiae ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/*metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 97
    Publication Date: 1996-07-19
    Description: Signaling molecules are essential for vertebrate embryonic development. Here, two Xenopus homologs of the Drosophila gene fringe, lunatic Fringe (lFng) and radical Fringe (rFng), were identified and the protein product of lFng further characterized. The messenger RNA of lFng is supplied as a maternal message. Its product is a precursor protein consisting of pre-, pro-, and mature regions. The mature lunatic Fringe protein is secreted extracellularly, and it induced mesodermal tissue formation in animal cap assays. These results indicate that secreted lunatic Fringe can induce mesoderm and reveal that the Fringe proteins are a family of vertebrate signaling molecules.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2080353/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2080353/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, J Y -- Wen, L -- Zhang, W J -- Rao, Y -- R01 CA114197/CA/NCI NIH HHS/ -- R01 CA114197-01A2/CA/NCI NIH HHS/ -- R01 EY014576/EY/NEI NIH HHS/ -- R01 EY014576-03/EY/NEI NIH HHS/ -- R01 GM070967/GM/NIGMS NIH HHS/ -- R01 GM070967-02/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):355-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Washington University School of Medicine, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662522" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blastocyst/metabolism ; Cell Line ; Culture Media, Conditioned ; Culture Techniques ; Drosophila Proteins ; Embryo, Nonmammalian/metabolism ; Embryonic Development ; *Embryonic Induction ; *Glycosyltransferases ; Mesoderm/*metabolism ; Molecular Sequence Data ; *N-Acetylglucosaminyltransferases ; Polymerase Chain Reaction ; Protein Processing, Post-Translational ; Proteins/chemistry/genetics/*physiology/secretion ; RNA, Messenger/genetics/metabolism ; *Signal Transduction ; Xenopus/*embryology/genetics ; *Xenopus Proteins
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perros, M -- Steitz, T A -- New York, N.Y. -- Science. 1996 Dec 13;274(5294):1929-30; author reply 1931-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8984647" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Crystallography, X-Ray ; Cyclic AMP Receptor Protein/*metabolism ; DNA, Bacterial/chemistry/*metabolism ; Escherichia coli/genetics ; *Lac Operon ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Operator Regions, Genetic ; *Promoter Regions, Genetic ; Protein Binding ; Protein Conformation ; Repressor Proteins/chemistry/*metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-06-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1730-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650562" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Biotechnology/manpower ; DNA/genetics ; Databases, Factual ; Drug Industry/*manpower ; Humans ; Information Science/education/*manpower ; Molecular Biology/*manpower ; Universities
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
    Publication Date: 1996-03-08
    Description: Friedreich's ataxia (FRDA) is an autosomal recessive, degenerative disease that involves the central and peripheral nervous systems and the heart. A gene, X25, was identified in the critical region for the FRDA locus on chromosome 9q13. This gene encodes a 210-amino acid protein, frataxin, that has homologs in distant species such as Caenorhabditis elegans and yeast. A few FRDA patients were found to have point mutations in X25, but the majority were homozygous for an unstable GAA trinucleotide expansion in the first X25 intron.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Campuzano, V -- Montermini, L -- Molto, M D -- Pianese, L -- Cossee, M -- Cavalcanti, F -- Monros, E -- Rodius, F -- Duclos, F -- Monticelli, A -- Zara, F -- Canizares, J -- Koutnikova, H -- Bidichandani, S I -- Gellera, C -- Brice, A -- Trouillas, P -- De Michele, G -- Filla, A -- De Frutos, R -- Palau, F -- Patel, P I -- Di Donato, S -- Mandel, J L -- Cocozza, S -- Koenig, M -- Pandolfo, M -- 722/Telethon/Italy -- NS34192/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1423-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department de Genetica, University of Valencia, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596916" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Base Sequence ; Chromosomes, Human, Pair 9/*genetics ; DNA Primers ; Female ; Friedreich Ataxia/*genetics ; Genes, Recessive ; Heterozygote ; Humans ; *Introns ; *Iron-Binding Proteins ; Male ; Molecular Sequence Data ; Pedigree ; Point Mutation ; Polymerase Chain Reaction ; Proteins/chemistry/*genetics ; Sequence Alignment ; *Trinucleotide Repeats
    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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