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  • DNA/genetics
  • 1990-1994  (101)
  • 1985-1989  (156)
  • 1970-1974
  • 1950-1954
  • 1945-1949
  • 1
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    Naturally occurring variation in bristle number and DNA polymorphisms at the scabrous locus of Drosophila melanogaster (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-09
    Description: The association between quantitative genetic variation in bristle number and molecular variation at a candidate neurogenic locus, scabrous, was examined in Drosophila melanogaster. Approximately 32 percent of the genetic variation in abdominal bristle number (21 percent for sternopleural bristle number) among 47 second chromosomes from a natural population was correlated with DNA sequence polymorphisms at this locus. Several polymorphic sites associated with large phenotypic effects occurred at intermediate frequency. Quantitative genetic variation in natural populations caused by alleles that have large effects at a few loci and that segregate at intermediate frequencies conflicts with the classical infinitesimal model of the genetic basis of quantitative variation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lai, C -- Lyman, R F -- Long, A D -- Langley, C H -- Mackay, T F -- GM45146/GM/NIGMS NIH HHS/ -- GM45344/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1697-702.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Population Biology, University of California at Davis 95616.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7992053" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; DNA/genetics ; *Drosophila Proteins ; Drosophila melanogaster/anatomy & histology/*genetics ; Female ; *Genes, Insect ; *Genetic Variation ; *Glycoproteins ; Haplotypes ; Linkage Disequilibrium ; Male ; Molecular Sequence Data ; Phenotype ; *Polymorphism, Genetic ; Proteins/*genetics ; Restriction Mapping ; Sense Organs/anatomy & histology
    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
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    Vaccine technologies: view to the future (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-02
    Description: The development of vaccines to prevent infectious diseases has been one of the most important contributions of biomedical science. Recent advances in the basic sciences are now fueling the development of a new generation of vaccines that will be based on rational design approaches. Two factors are making this possible: an improved understanding of the microbial factors required for virulence and the nature of the immune response to infection. The status of new vaccine technologies is summarized here.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rabinovich, N R -- McInnes, P -- Klein, D L -- Hall, B F -- New York, N.Y. -- Science. 1994 Sep 2;265(5177):1401-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Microbiology and Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20982-9902.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7521064" target="_blank"〉PubMed〈/a〉
    Keywords: Adjuvants, Immunologic ; Animals ; Antigens/genetics/immunology ; Cytokines/immunology ; DNA/genetics ; Epitopes/immunology ; Humans ; ISCOMs/immunology ; Vaccination ; *Vaccines, Combined/immunology ; *Vaccines, Conjugate/immunology ; *Vaccines, Synthetic/immunology
    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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    An adenovirus vector for gene transfer into neurons and glia in the brain (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-12
    Description: The efficient introduction of genetic material into quiescent nerve cells is important in the study of brain function and for gene therapy of neurological disorders. A replication-deficient adenoviral vector that contained a reporter gene encoding beta-galactosidase infected rat nerve cells in vitro and in vivo. beta-Galactosidase was expressed in almost all sympathetic neurons and astrocytes in culture. After stereotactic inoculations into the rat hippocampus and the substantia nigra, beta-galactosidase activity was detected for 2 months. Infected cells were identified as microglial cells, astrocytes, or neurons with anatomical, morphological, and immunohistochemical criteria. No obvious cytopathic effect was observed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Le Gal La Salle, G -- Robert, J J -- Berrard, S -- Ridoux, V -- Stratford-Perricaudet, L D -- Perricaudet, M -- Mallet, J -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):988-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut Alfred Fessard, Unite Propre de Recherche 2212, Centre National de la Recherche Scientifique (CNRS), Gif sur Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8382374" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/*genetics ; Animals ; Astrocytes/metabolism/microbiology ; Avian Sarcoma Viruses/genetics ; Brain/*cytology ; DNA/genetics ; Gene Expression ; *Genetic Vectors ; Hippocampus/cytology/metabolism ; Neuroglia/*metabolism/microbiology ; Neurons/*metabolism/microbiology ; Promoter Regions, Genetic/genetics ; Rats ; Substantia Nigra/cytology/metabolism ; *Transfection ; beta-Galactosidase/genetics
    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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  • 4
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    Primers for mitochondrial DNA replication generated by endonuclease G (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-06
    Description: Endonuclease G (Endo G) is widely distributed among animals and cleaves DNA at double-stranded (dG)n.(dC)n and at single-stranded (dC)n tracts. Endo G is synthesized as a propeptide with an amino-terminal presequence that targets the nuclease to mitochondria. Endo G can also be detected in extranucleolar chromatin. In addition to deoxyribonuclease activities, Endo G also has ribonuclease (RNase) and RNase H activities and specifically cleaves mouse mitochondrial RNA and DNA-RNA substrates containing the origin of heavy-strand DNA replication (OH). The cleavage sites match those found in vivo, indicating that Endo G is capable of generating the RNA primers required by DNA polymerase gamma to initiate replication of mitochondrial DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cote, J -- Ruiz-Carrillo, A -- New York, N.Y. -- Science. 1993 Aug 6;261(5122):765-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research Center, Medical School of Laval University, L'Hotel-Dieu de Quebec, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7688144" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cell Nucleus/enzymology ; DNA/genetics ; *DNA Replication ; DNA, Mitochondrial/*metabolism ; Endodeoxyribonucleases/chemistry/genetics/*metabolism ; Genetic Vectors ; Mitochondria/enzymology ; Molecular Sequence Data ; RNA/*metabolism ; Ribonuclease H/metabolism ; Ribonucleases/metabolism ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Presentation of a viral T cell epitope expressed in the CDR3 region of a self immunoglobulin molecule (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-08
    Description: Synthetic peptides corresponding to microbial epitopes stimulate T cell immunity but their immunogenicity is poor and their half-lives are short. A viral epitope inserted into the complementarity-determining region 3 (CDR3) loop of the heavy chain of a self immunoglobulin (Ig) molecule was generated from the Ig context and was presented by I-Ed class II molecules to virus-specific, CD4+ T cells. Chimeric Ig-peptide was presented 100 to 1000 times more efficiently than free synthetic peptide and was able to prime virus-specific T cells in vivo. These features suggest that antigenized Ig can provide an improved and safe vaccine for the presentation of microbial and other peptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zaghouani, H -- Steinman, R -- Nonacs, R -- Shah, H -- Gerhard, W -- Bona, C -- AI13013/AI/NIAID NIH HHS/ -- AI18316/AI/NIAID NIH HHS/ -- AI24460/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Jan 8;259(5092):224-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Mount Sinai School of Medicine, New York, NY 10029.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7678469" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigen-Presenting Cells/*immunology ; Antigens, Viral/*immunology ; Arsenic/immunology ; *Arsenicals ; Base Sequence ; CD4-Positive T-Lymphocytes/immunology ; DNA/genetics ; Epitopes/*immunology ; Hemagglutinin Glycoproteins, Influenza Virus ; Hemagglutinins, Viral/genetics/immunology ; Histocompatibility Antigens Class II/immunology ; Immunoglobulin Heavy Chains/genetics/immunology ; Immunoglobulin Variable Region/genetics/immunology ; Immunoglobulins/genetics/*immunology ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Mutagenesis ; Receptors, Fc/immunology ; Recombinant Fusion Proteins/immunology ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Sequencing the human genome (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-04-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, R W -- New York, N.Y. -- Science. 1993 Apr 30;260(5108):606-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8480170" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/genetics ; *Human Genome Project ; Humans
    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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  • 7
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    Identification of a whitefly species by genomic and behavioral studies (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-01
    Description: An introduced whitefly species, responsible for over a half billion dollars in damage to U.S. agricultural production in 1991, is morphologically indistinguishable from Bemisia tabaci (Gennadius). However, with the use of polymerase chain reaction-based DNA differentiation tests, allozymic frequency analyses, crossing experiments, and mating behavior studies, the introduced whitefly is found to be a distinct species. Recognition of this new species, the silverleaf whitefly, is critical in the search for management options.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perring, T M -- Cooper, A D -- Rodriguez, R J -- Farrar, C A -- Bellows, T S Jr -- New York, N.Y. -- Science. 1993 Jan 1;259(5091):74-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology, University of California, Riverside 92521.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8418497" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; Crosses, Genetic ; DNA/genetics ; Diptera/*classification/genetics/*physiology ; Enzymes/genetics ; Female ; Genetic Linkage ; Male ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Sexual Behavior, Animal ; United States
    Print ISSN: 0036-8075
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  • 8
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    mSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-09
    Description: Complementary DNAs (cDNAs) from mSlo, a gene encoding calcium-activated potassium channels, were isolated from mouse brain and skeletal muscle, sequenced, and expressed in Xenopus oocytes. The mSlo-encoded channel resembled "maxi" or BK (high conductance) channel types; single channel conductance was 272 picosiemens with symmetrical potassium concentrations. Whole cell and single channel currents were blocked by charybdotoxin, iberiotoxin, and tetraethylammonium ion. A large number of variant mSlo cDNAs were isolated, indicating that several diverse mammalian BK channel types are produced by a single gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Butler, A -- Tsunoda, S -- McCobb, D P -- Wei, A -- Salkoff, L -- R01 NS24785-01/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 9;261(5118):221-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7687074" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Animals ; Calcium/metabolism/*pharmacology ; Charybdotoxin ; DNA/genetics ; Drosophila ; Electric Conductivity ; Large-Conductance Calcium-Activated Potassium Channels ; Membrane Proteins/chemistry/*genetics ; Mice ; Molecular Sequence Data ; Oocytes/metabolism ; Peptides/pharmacology ; Potassium/metabolism ; Potassium Channels/chemistry/drug effects/*genetics/metabolism ; *Potassium Channels, Calcium-Activated ; RNA/genetics ; RNA, Complementary ; Scorpion Venoms/pharmacology ; Sodium/metabolism ; Tetraethylammonium ; Tetraethylammonium Compounds/pharmacology ; Transcription, Genetic ; Xenopus
    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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  • 9
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    Translocation of TCR alpha chains into the lumen of the endoplasmic reticulum and their degradation (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-26
    Description: After synthesis, the alpha chain of the T cell antigen receptor (TCR alpha) can form a complex with other TCR chains and move to the cell surface, or TCR alpha can undergo degradation in the endoplasmic reticulum (ER) if it remains unassembled. The mechanism of translocation and degradation in the ER is unclear. It was found that the putative transmembrane region of TCR alpha (alpha tm) was incompetent on its own to act as a transmembrane region. Molecules that contained alpha tm were translocated into the ER lumen and then underwent either rapid degradation or secretion, depending on the sequence of the cytoplasmic domain. A specific signal for ER degradation within alpha tm does not appear to be present.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shin, J -- Lee, S -- Strominger, J L -- AI20182/AI/NIAID NIH HHS/ -- CA47554/CA/NCI NIH HHS/ -- GM48961/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 26;259(5103):1901-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Tumor Virology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456316" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD4/chemistry/genetics/metabolism ; Cytoplasm/metabolism ; DNA/genetics ; Endoplasmic Reticulum/*metabolism ; Glycosylation ; HeLa Cells/metabolism ; Humans ; Immunosorbent Techniques ; Lipid Bilayers/metabolism ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; Mutagenesis ; Protein Structure, Secondary ; Receptors, Antigen, T-Cell/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Toxicology goes molecular (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1993 Mar 5;259(5100):1394-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8451635" target="_blank"〉PubMed〈/a〉
    Keywords: Aflatoxins/analysis ; Animals ; Base Sequence ; Cytochrome P-450 Enzyme System/analysis ; DNA/genetics ; Dioxins/toxicity ; Humans ; Liver Neoplasms/diagnosis ; Molecular Biology/*methods ; Toxicology/*methods
    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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  • 11
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    Zeroing in on a breast cancer susceptibility gene (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1993 Jan 29;259(5095):622-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430309" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Breast Neoplasms/*genetics ; Chromosome Mapping ; *Chromosomes, Human, Pair 17 ; DNA/genetics ; Female ; Genetic Counseling ; Genetic Markers ; *Genetic Predisposition to Disease ; Humans ; Polymerase Chain Reaction/methods ; Repetitive Sequences, Nucleic Acid
    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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  • 12
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    The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-26
    Description: The glycosylphosphatidylinositol (GPI) anchor is a membrane attachment structure of many proteins and occurs in a wide variety of eukaryotes from yeasts to mammals. The structure of the core of the GPI anchor is conserved in protozoa and mammals and so is its biosynthetic pathway. A complementary DNA encoding a human protein termed PIG-A (phosphatidylinositol glycan-class A) was cloned. PIG-A was necessary for synthesis of N-acetylglucosaminyl-phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miyata, T -- Takeda, J -- Iida, Y -- Yamada, N -- Inoue, N -- Takahashi, M -- Maeda, K -- Kitani, T -- Kinoshita, T -- New York, N.Y. -- Science. 1993 Feb 26;259(5099):1318-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunoregulation, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7680492" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD/metabolism ; Antigens, CD55 ; Antigens, CD59 ; Antigens, Surface/metabolism ; Antigens, Thy-1 ; Cloning, Molecular ; DNA/genetics ; Genetic Complementation Test ; Glycosylphosphatidylinositols/*biosynthesis ; HeLa Cells ; Humans ; In Vitro Techniques ; Membrane Glycoproteins/metabolism ; Membrane Proteins/*genetics/metabolism ; Mice ; Molecular Sequence Data ; Solubility ; Species Specificity
    Print ISSN: 0036-8075
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  • 13
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    Why did they die? (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Black, F L -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1739-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Epidemiology and Public Health, Yale University, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1465610" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/genetics ; *Disease Susceptibility ; Europe ; Genes, MHC Class I ; Genetic Variation ; Humans ; *Indians, North American ; *Mortality ; North America
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 14
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    Regulation of plasma membrane recycling by CFTR (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-24
    Description: The gene that encodes the cystic fibrosis transmembrane conductance regulator (CFTR) is defective in patients with cystic fibrosis. Although the protein product of the CFTR gene has been proposed to function as a chloride ion channel, certain aspects of its function remain unclear. The role of CFTR in the adenosine 3',5'-monophosphate (cAMP)-dependent regulation of plasma membrane recycling was examined. Adenosine 3',5'-monophosphate is known to regulate endocytosis and exocytosis in chloride-secreting epithelial cells that express CFTR. However, mutant epithelial cells derived from a patient with cystic fibrosis exhibited no cAMP-dependent regulation of endocytosis and exocytosis until they were transfected with complementary DNA encoding wild-type CFTR. Thus, CFTR is critical for cAMP-dependent regulation of membrane recycling in epithelial tissues, and this function of CFTR could explain in part the pleiotropic nature of cystic fibrosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bradbury, N A -- Jilling, T -- Berta, G -- Sorscher, E J -- Bridges, R J -- Kirk, K L -- New York, N.Y. -- Science. 1992 Apr 24;256(5056):530-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Alabama, Birmingham 35294.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373908" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Membrane/*physiology ; Chlorides/metabolism ; Colforsin/pharmacology ; Cyclic AMP/pharmacology ; Cystic Fibrosis/*physiopathology ; Cystic Fibrosis Transmembrane Conductance Regulator ; DNA/genetics ; Endocytosis/drug effects/physiology ; Epithelium/secretion ; Exocytosis/drug effects/physiology ; Gene Expression ; Horseradish Peroxidase/metabolism ; Humans ; Membrane Proteins/genetics/*physiology ; Molecular Sequence Data ; Pancreatic Neoplasms ; Transfection ; Tumor Cells, Cultured ; Wheat Germ Agglutinins/metabolism
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  • 15
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    Cloning and expression in yeast of a plant potassium ion transport system (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-01
    Description: A membrane polypeptide involved in K+ transport in a higher plant was cloned by complementation of a yeast mutant defective in K+ uptake with a complementary DNA library from Arabidopsis thaliana. A 2.65-kilobase complementary DNA conferred ability to grow on media with K+ concentration in the micromolar range and to absorb K+ (or 86Rb+) at rates similar to those in wild-type yeast. The predicted amino acid sequence (838 amino acids) has three domains: a channel-forming region homologous to animal K+ channels, a cyclic nucleotide-binding site, and an ankyrin-like region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sentenac, H -- Bonneaud, N -- Minet, M -- Lacroute, F -- Salmon, J M -- Gaymard, F -- Grignon, C -- New York, N.Y. -- Science. 1992 May 1;256(5057):663-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochimie et Physiologie Vegetales, ENSA-M/INRA/CNRS URA 573, Montpellier, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1585180" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Arabidopsis Proteins ; Biological Transport ; Blotting, Southern ; Carrier Proteins/chemistry/genetics ; *Cloning, Molecular ; DNA/genetics ; Deoxyribonuclease EcoRI ; Gene Expression ; Kinetics ; Molecular Sequence Data ; Plant Proteins/chemistry/*genetics ; Plants/*genetics ; Potassium/*metabolism ; Potassium Channels/chemistry/*genetics ; Saccharomyces cerevisiae/*genetics ; Sequence Homology, Nucleic Acid
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  • 16
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    Functional transcription elongation complexes from synthetic RNA-DNA bubble duplexes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-20
    Description: A synthetic RNA-DNA bubble duplex construct intended to mimic the nucleic acid framework of a functional transcription elongation complex was designed and assembled. The construct consisted of a double-stranded DNA duplex of variable length (the template and nontemplate strands) containing an internal noncomplementary DNA "bubble" sequence. The 3' end of an RNA oligonucleotide that is partially complementary to the template DNA strand was hybridized within the DNA bubble to form an RNA-DNA duplex with a non-complementary 5'-terminal RNA tail. The addition of either Escherichia coli or T7 RNA polymerase to this construct formed a complex that synthesized RNA with good efficiency from the hybridized RNA primer in a template-directed and processive manner, and displayed other features of a normal promoter-initiated transcription elongation complex. Other such constructs can be designed to examine many of the functional and regulatory properties of transcription systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Daube, S S -- von Hippel, P H -- GM-15792/GM/NIGMS NIH HHS/ -- GM-29158/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 20;258(5086):1320-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1280856" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/genetics ; DNA-Directed RNA Polymerases/*metabolism ; Escherichia coli/enzymology/genetics ; In Vitro Techniques ; Molecular Sequence Data ; Nucleic Acid Hybridization ; *Promoter Regions, Genetic ; RNA/genetics ; Structure-Activity Relationship ; Templates, Genetic ; *Transcription, Genetic
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  • 17
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    NF-kappa B subunit regulation in nontransformed CD4+ T lymphocytes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-06-05
    Description: Regulation of interleukin-2 (IL-2) gene expression by the p50 and p65 subunits of the DNA binding protein NF-kappa B was studied in nontransformed CD4+ T lymphocyte clones. A homodimeric complex of the NF-kappa B p50 subunit was found in resting T cells. The amount of p50-p50 complex decreased after full antigenic stimulation, whereas the amount of the NF-kappa B p50-p65 heterodimer was increased. Increased expression of the IL-2 gene and activity of the IL-2 kappa B DNA binding site correlated with a decrease in the p50-p50 complex. Overexpression of p50 repressed IL-2 promoter expression. The switch from p50-p50 to p50-p65 complexes depended on a protein that caused sequestration of the p50-p50 complex in the nucleus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kang, S M -- Tran, A C -- Grilli, M -- Lenardo, M J -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1452-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunology, National Institute for Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1604322" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/*immunology ; Base Sequence ; Binding Sites ; Cell Line ; Cell Nucleus/physiology ; Chloramphenicol O-Acetyltransferase/genetics/metabolism ; Clone Cells ; Columbidae ; DNA/genetics ; *Gene Expression Regulation ; Interleukin-2/*genetics ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; NF-kappa B/*metabolism ; Oligonucleotide Probes ; Promoter Regions, Genetic ; RNA, Messenger/metabolism ; Recombinant Fusion Proteins/metabolism ; T-Lymphocyte Subsets/*immunology ; Transfection ; Tumor Necrosis Factor-alpha/pharmacology
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  • 18
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    Balancing selection at allozyme loci in oysters: implications from nuclear RFLPs (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-03
    Description: Population genetic analyses that depend on the assumption of neutrality for allozyme markers are used widely. Restriction fragment length polymorphisms in nuclear DNA of the American oyster evidence a pronounced population subdivision concordant with mitochondrial DNA. This finding contrasts with a geographic uniformity in allozyme frequencies previously thought to reflect high gene flow mediated by the pelagic gametes and larvae. The discordance likely is due to selection on protein electrophoretic characters that balances allozyme frequencies in the face of severe constraints to gene flow. These results raise a cautionary note for studies that rely on assumptions of neutrality for allozyme markers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karl, S A -- Avise, J C -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):100-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1348870" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; Cell Nucleus/*physiology ; DNA/genetics ; Gene Frequency ; Geography ; Isoenzymes/*genetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Ostreidae/enzymology/*genetics ; *Polymorphism, Restriction Fragment Length ; United States
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  • 19
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    An amino acid mutation in a potassium channel that prevents inhibition by protein kinase C (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-27
    Description: A slowly activating, voltage-dependent potassium channel protein cloned from rat kidney was expressed in Xenopus oocytes. Two activators of protein kinase C, 1-oleoyl-2-acetyl-rac-glycerol and phorbol 12,13-didecanoate, inhibited the current. This inhibition was blocked by the kinase inhibitor staurosporine. Inhibition of the current was not seen in channels in which Ser103 was replaced by Ala, although other properties of the current were unchanged. These results indicate that inhibition of the potassium current results from direct phosphorylation of the channel subunit protein at Ser103.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Busch, A E -- Varnum, M D -- North, R A -- Adelman, J P -- DA03160/DA/NIDA NIH HHS/ -- NS28504/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 Mar 27;255(5052):1705-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, Portland 97201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553557" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; DNA/genetics ; Diglycerides/pharmacology ; Ion Channel Gating ; Membrane Potentials ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phorbol Esters/pharmacology ; Phosphorylation ; Potassium Channels/*physiology ; Protein Kinase C/*metabolism ; Rats ; Structure-Activity Relationship
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
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    Cloning of a second type of activin receptor and functional characterization in Xenopus embryos (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-03-27
    Description: A complementary DNA coding for a second type of activin receptor (ActRIIB) has been cloned from Xenopus laevis that fulfills the structural criteria of a transmembrane protein serine kinase. Ectodermal explants from embryos injected with activin receptor RNA show increased sensitivity to activin, as measured by the induction of muscle actin RNA. In addition, injected embryos display developmental defects characterized by inappropriate formation of dorsal mesodermal tissue. These results demonstrate that this receptor is involved in signal transduction and are consistent with the proposed role of activin in the induction and patterning of mesoderm in Xenopus embryos.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mathews, L S -- Vale, W W -- Kintner, C R -- DK-26741/DK/NIDDK NIH HHS/ -- HD-07343/HD/NICHD NIH HHS/ -- HD-13275/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1992 Mar 27;255(5052):1702-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Clayton Foundation Laboratories for Peptide Biology, Salk Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1313188" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors ; Activins ; Amino Acid Sequence ; Animals ; Cloning, Molecular ; DNA/genetics ; Inhibins/*physiology ; Membrane Proteins/genetics ; Molecular Sequence Data ; Protein Kinases/genetics ; Protein-Serine-Threonine Kinases ; Receptors, Cell Surface/*genetics ; Signal Transduction ; Xenopus laevis/embryology/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 21
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    Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-09-18
    Description: The double-stranded RNA-dependent protein kinase (dsRNA-PK) is thought to be a key mediator of the antiviral and antiproliferative effects of interferons (IFNs). Studies examining the physiological function of the kinase suggest that it participates in cell growth and differentiation by regulating protein synthesis. Autophosphorylation and consequent activation of dsRNA-PK in vitro and in vivo result in phosphorylation of the alpha subunit of eukaryotic initiation factor-2 (eIF-2) and inhibition of protein synthesis. Expression of a functionally defective mutant of human dsRNA-PK in NIH 3T3 cells resulted in malignant transformation, suggesting that dsRNA-PK may function as a suppressor of cell proliferation and tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koromilas, A E -- Roy, S -- Barber, G N -- Katze, M G -- Sonenberg, N -- AI22646/AI/NIAID NIH HHS/ -- RR00166/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1992 Sep 18;257(5077):1685-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Faculty of Medicine, McGill University, Montreal, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1382315" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Cell Division ; Cell Line ; *Cell Transformation, Neoplastic ; Cloning, Molecular ; DNA/genetics ; Enzyme Induction ; Gene Expression ; Humans ; Immunoblotting ; Interferons/*pharmacology ; Mice ; Molecular Sequence Data ; *Mutation ; Phosphorylation ; Protein Kinases/chemistry/*genetics/physiology ; Transfection ; eIF-2 Kinase
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  • 22
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    Fatty acid biosynthesis redirected to medium chains in transgenic oilseed plants (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-03
    Description: Medium-chain fatty acids (FAs), found in storage lipids of certain plants, are an important renewable resource. Seeds of undomesticated California bay accumulate laurate (12:0), and a 12:0-acyl-carrier protein thioesterase (BTE) has been purified from this tissue. Sequencing of BTE enabled the cloning of a complementary DNA coding for a plastid-targeted preprotein. Expression of the complementary DNA in the seeds of Arabidopsis thaliana resulted in BTE activity, and medium chains accumulated at the expense of long-chain (greater than or equal to 16) FAs. Laurate became the most abundant FA species and was deposited in the storage triacylglycerols. These results demonstrate a mechanism for medium-chain FA synthesis in plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Voelker, T A -- Worrell, A C -- Anderson, L -- Bleibaum, J -- Fan, C -- Hawkins, D J -- Radke, S E -- Davies, H M -- New York, N.Y. -- Science. 1992 Jul 3;257(5066):72-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Calgene, Inc., Davis, CA 95616.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1621095" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/genetics/*metabolism ; Acyl-Carrier Protein S-Acetyltransferase ; Amino Acid Sequence ; DNA/genetics ; Fatty Acids/*biosynthesis/isolation & purification ; Genetic Engineering ; Lauric Acids/*metabolism ; Molecular Sequence Data ; Plants/genetics/*metabolism ; Plants, Genetically Modified ; Plasmids ; Seeds/metabolism
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  • 23
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    The skeletal muscle chloride channel in dominant and recessive human myotonia (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-07
    Description: Autosomal recessive generalized myotonia (Becker's disease) (GM) and autosomal dominant myotonia congenita (Thomsen's disease) (MC) are characterized by skeletal muscle stiffness that is a result of muscle membrane hyperexcitability. For both diseases, alterations in muscle chloride or sodium currents or both have been observed. A complementary DNA for a human skeletal muscle chloride channel (CLC-1) was cloned, physically localized on chromosome 7, and linked to the T cell receptor beta (TCRB) locus. Tight linkage of these two loci to GM and MC was found in German families. An unusual restriction site in the CLC-1 locus in two GM families identified a mutation associated with that disease, a phenylalanine-to-cysteine substitution in putative transmembrane domain D8. This suggests that different mutations in CLC-1 may cause dominant or recessive myotonia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koch, M C -- Steinmeyer, K -- Lorenz, C -- Ricker, K -- Wolf, F -- Otto, M -- Zoll, B -- Lehmann-Horn, F -- Grzeschik, K H -- Jentsch, T J -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):797-800.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Center for Human Genetics, Marburg University, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1379744" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Southern ; Chloride Channels ; *Chromosomes, Human, Pair 7 ; Cloning, Molecular ; DNA/genetics ; Female ; *Genes, Dominant ; *Genes, Recessive ; Genetic Linkage ; Humans ; Ion Channels/*genetics ; Lod Score ; Male ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Muscular Dystrophies/*genetics ; Myotonia Congenita/*genetics ; Pedigree ; Polymorphism, Restriction Fragment Length ; Receptors, Antigen, T-Cell/genetics ; Recombination, Genetic ; Sequence Homology, Nucleic Acid
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  • 24
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    Finding RNA makes proteins gives 'RNA world' a big boost (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-06-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Waldrop, M M -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1396-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1376495" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Biological Evolution ; DNA/genetics ; Molecular Sequence Data ; *Protein Biosynthesis ; Proteins/genetics ; RNA/*genetics
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  • 25
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    Heteromeric NMDA receptors: molecular and functional distinction of subtypes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-22
    Description: The N-methyl D-aspartate (NMDA) receptor subtype of glutamate-gated ion channels possesses high calcium permeability and unique voltage-dependent sensitivity to magnesium and is modulated by glycine. Molecular cloning identified three complementary DNA species of rat brain, encoding NMDA receptor subunits NMDAR2A (NR2A), NR2B, and NR2C, which are 55 to 70% identical in sequence. These are structurally related, with less than 20% sequence identity, to other excitatory amino acid receptor subunits, including the NMDA receptor subunit NMDAR1 (NR1). Upon expression in cultured cells, the new subunits yielded prominent, typical glutamate- and NMDA-activated currents only when they were in heteromeric configurations with NR1. NR1-NR2A and NR1-NR2C channels differed in gating behavior and magnesium sensitivity. Such heteromeric NMDA receptor subtypes may exist in neurons, since NR1 messenger RNA is synthesized throughout the mature rat brain, while NR2 messenger RNA show a differential distribution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Monyer, H -- Sprengel, R -- Schoepfer, R -- Herb, A -- Higuchi, M -- Lomeli, H -- Burnashev, N -- Sakmann, B -- Seeburg, P H -- New York, N.Y. -- Science. 1992 May 22;256(5060):1217-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Biology, University of Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1350383" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/*physiology ; Cell Line ; Cloning, Molecular ; DNA/genetics ; Glutamates/pharmacology ; Glutamic Acid ; Glycine/pharmacology ; Macromolecular Substances ; Magnesium/pharmacology ; Membrane Potentials/drug effects ; Molecular Sequence Data ; Multigene Family ; N-Methylaspartate/pharmacology ; Oligonucleotide Probes ; Organ Specificity ; Peptides ; RNA, Messenger/genetics/metabolism ; Rats ; Receptors, N-Methyl-D-Aspartate/*genetics/*metabolism ; Recombinant Proteins/drug effects/metabolism ; Sequence Homology, Nucleic Acid ; Transfection
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  • 26
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    New evidence found for a nuclear matrix (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-01-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, M -- New York, N.Y. -- Science. 1992 Jan 3;255(5040):34.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1372752" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/genetics ; Nuclear Matrix/physiology/*ultrastructure ; RNA/analysis/genetics ; RNA Splicing ; Ribonucleoproteins/analysis ; Ribonucleoproteins, Small Nuclear ; Transcription, Genetic
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  • 27
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    The mouse pink-eyed dilution gene: association with human Prader-Willi and Angelman syndromes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-21
    Description: Complementary DNA clones from the pink-eyed dilution (p) locus of mouse chromosome 7 were isolated from murine melanoma and melanocyte libraries. The transcript from this gene is missing or altered in six independent mutant alleles of the p locus, suggesting that disruption of this gene results in the hypopigmentation phenotype that defines mutant p alleles. Characterization of the human homolog revealed that it is localized to human chromosome 15 at q11.2-q12, a region associated with Prader-Willi and Angelman syndromes, suggesting that altered expression of this gene may be responsible for the hypopigmentation phenotype exhibited by certain individuals with these disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gardner, J M -- Nakatsu, Y -- Gondo, Y -- Lee, S -- Lyon, M F -- King, R A -- Brilliant, M H -- CA06927/CA/NCI NIH HHS/ -- GM22167/GM/NIGMS NIH HHS/ -- GM43840/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Aug 21;257(5073):1121-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, PA 19111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1509264" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Carrier Proteins ; Chromosomes, Human, Pair 15 ; Cloning, Molecular ; DNA/genetics ; Humans ; Melanocytes/chemistry ; Melanoma, Experimental/chemistry ; *Membrane Proteins ; *Membrane Transport Proteins ; Mice ; Mice, Mutant Strains ; Molecular Sequence Data ; Mutation ; Nucleic Acid Hybridization ; Phenotype ; Pigmentation Disorders/*genetics ; Prader-Willi Syndrome/*genetics ; Proteins/chemistry ; Sequence Homology, Nucleic Acid
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 28
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    Malignant hyperthermia (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Larach, M G -- New York, N.Y. -- Science. 1992 Jul 3;257(5066):11-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1621085" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/genetics ; Disease Susceptibility ; Humans ; Malignant Hyperthermia/*diagnosis/epidemiology/mortality ; Morbidity
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  • 29
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    Differential display of eukaryotic messenger RNA by means of the polymerase chain reaction (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-14
    Description: Effective methods are needed to identify and isolate those genes that are differentially expressed in various cells or under altered conditions. This report describes a method to separate and clone individual messenger RNAs (mRNAs) by means of the polymerase chain reaction. The key element is to use a set of oligonucleotide primers, one being anchored to the polyadenylate tail of a subset of mRNAs, the other being short and arbitrary in sequence so that it anneals at different positions relative to the first primer. The mRNA subpopulations defined by these primer pairs were amplified after reverse transcription and resolved on a DNA sequencing gel. When multiple primer sets were used, reproducible patterns of amplified complementary DNA fragments were obtained that showed strong dependence on sequence specificity of either primer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liang, P -- Pardee, A B -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):967-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1354393" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Breast Neoplasms/genetics ; Cloning, Molecular/methods ; DNA/genetics ; Humans ; Molecular Sequence Data ; Neoplasm Metastasis ; Nucleoside-Phosphate Kinase/genetics ; Oligodeoxyribonucleotides ; Poly A/genetics ; Polymerase Chain Reaction/*methods ; RNA, Messenger/biosynthesis/*genetics ; Templates, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Evolutionary biology. Is "flying primate" hypothesis headed for a crash landing? (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):34.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1314419" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Chiroptera/*genetics ; DNA/genetics ; DNA, Mitochondrial/genetics ; Electron Transport Complex IV/genetics ; *Models, Genetic ; Primates/*genetics
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    Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-03
    Description: A family of highly polymorphic neuronal cell surface proteins, the neurexins, has been identified. At least two genes for neurexins exist. Each gene uses alternative promoters and multiple variably spliced exons to potentially generate more than a 100 different neurexin transcripts. The neurexins were discovered by the identification of one member of the family as the receptor for alpha-latrotoxin. This toxin is a component of the venom from black widow spiders; it binds to presynaptic nerve terminals and triggers massive neurotransmitter release. Neurexins contain single transmembrane regions and extracellular domains with repeated sequences similar to sequences in laminin A, slit, and agrin, proteins that have been implicated in axon guidance and synaptogenesis. An antibody to neurexin I showed highly concentrated immunoreactivity at the synapse. The polymorphic structure of the neurexins, their neural localization, and their sequence similarity to proteins associated with neurogenesis suggest a function as cell recognition molecules in the nerve terminal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ushkaryov, Y A -- Petrenko, A G -- Geppert, M -- Sudhof, T C -- New York, N.Y. -- Science. 1992 Jul 3;257(5066):50-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1621094" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Isomerases/genetics ; Amino Acid Sequence ; Animals ; Antibodies ; Carrier Proteins/genetics ; Cloning, Molecular ; Cyclosporins/metabolism ; DNA/genetics ; Exons ; Laminin/*genetics ; Molecular Sequence Data ; Nerve Tissue Proteins/chemistry/*genetics ; Organ Specificity ; PC12 Cells ; Peptidylprolyl Isomerase ; Polymerase Chain Reaction ; RNA, Messenger/genetics/metabolism ; Rats ; Receptors, Cholinergic/*genetics ; *Receptors, Peptide ; Sequence Homology, Nucleic Acid ; Spider Venoms/metabolism ; Synapses/*physiology
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    Peptide processing and targeting in the neuronal secretory pathway (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-15
    Description: The abdominal ganglion of the marine mollusk Aplysia contains a pair of identified neuronal clusters, the bag cells, which control egg laying by means of a number of unique regulatory mechanisms. Each neuron in the bag cell clusters synthesizes several peptides derived from a single prohormone and packages them into separate vesicles. These vesicles are then differentially localized in specific neuronal processes, thus segregating peptides destined for autocrine and hormonal release sites. Therefore in this system, protein trafficking through the secretory pathway organizes multiple peptide neurochemical messengers to efficiently regulate simple behaviors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jung, L J -- Scheller, R H -- New York, N.Y. -- Science. 1991 Mar 15;251(4999):1330-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Beckman Center, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2003219" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aplysia/genetics/*physiology ; Cell Compartmentation ; Cloning, Molecular ; DNA/genetics ; Invertebrate Hormones/genetics/*metabolism ; Neuropeptides/*physiology ; Neurosecretory Systems/*physiology ; Protein Precursors/metabolism ; Protein Processing, Post-Translational ; Sexual Behavior, Animal/physiology ; Transfection
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    Fight erupts over DNA fingerprinting (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1721-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1763321" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; *Crime ; DNA/genetics ; *DNA Fingerprinting ; Genetic Variation ; Humans ; United States
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    MRC denies blocking access to genome data (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1583.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1749932" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/genetics ; Databases, Factual ; Federal Government ; Great Britain ; *Human Genome Project ; Humans ; *Information Dissemination ; Internationality
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    Genome patent fight erupts (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1991 Oct 11;254(5029):184-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925568" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/genetics ; Federal Government ; *Genome, Human ; Human Genome Project ; Humans ; Internationality ; *National Institutes of Health (U.S.) ; *Patents as Topic ; United States
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    An RNA first: it's part of the gene-copying machinery (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-04-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, M -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):506-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1708525" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bombyx/*genetics ; DNA/genetics ; RNA/*genetics ; Transcription Factors/*metabolism
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    Isolation of a rel-related human cDNA that potentially encodes the 65-kD subunit of NF-kappa B (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-22
    Description: A DNA probe that spanned a domain conserved among the proto-oncogene c-rel, the Drosophila morphogen dorsal, and the p50 DNA binding subunit of NF-kappa B was generated from Jurkat T cell complementary DNA with the polymerase chain reaction (PCR) and degenerate oligonucleotides. This probe was used to identify a rel-related complementary DNA that hybridized to a 2.6-kilobase messenger RNA present in human T and B lymphocytes. In vitro transcription and translation of the complementary DNA resulted in the synthesis of a protein with an apparent molecular size of 65 kilodaltons (kD). The translated protein showed weak DNA binding with a specificity for the kappa B binding motif. This protein-DNA complex comigrated with the complex obtained with the purified human p65 NF-kappa B subunit and binding was inhibited by I kappa B-alpha and -beta proteins. In addition, the 65-kD protein associated with the p50 subunit of NF-kappa B and the kappa B probe to form a complex with the same electrophoretic mobility as the NF-kappa B-DNA complex. Therefore the rel-related 65-kD protein may represent the p65 subunit of the active NF-kappa B transcription factor complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ruben, S M -- Dillon, P J -- Schreck, R -- Henkel, T -- Chen, C H -- Maher, M -- Baeuerle, P A -- Rosen, C A -- New York, N.Y. -- Science. 1991 Mar 22;251(5000):1490-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Oncology and Virology, Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110-1199.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006423" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Blotting, Northern ; Cloning, Molecular ; DNA/genetics ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; NF-kappa B/*genetics ; Polymerase Chain Reaction ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins c-rel ; T-Lymphocytes
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    Expression cloning of an adenylate cyclase-coupled calcitonin receptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-25
    Description: A calcitonin receptor complementary DNA (cDNA) was cloned by expression of a cDNA library from a porcine kidney epithelial cell line in COS cells. The 482-amino acid receptor has high affinity for salmon calcitonin (dissociation constant Kd approximately 6 nM) and is functionally coupled to increases in intracellular cyclic adenosine monophosphate (cAMP). The receptor shows no sequence similarity to other reported G protein-coupled receptors but is homologous to the parathyroid hormone-parathyroid hormone-related peptide (PTH-PTHrP) receptor, indicating that the receptors for these hormones, which regulate calcium homeostasis, represent a new family of G protein-coupled receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, H Y -- Harris, T L -- Flannery, M S -- Aruffo, A -- Kaji, E H -- Gorn, A -- Kolakowski, L F Jr -- Lodish, H F -- Goldring, S R -- AM 03564/AM/NIADDK NIH HHS/ -- HL-41484/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 15;254(5034):1022-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658940" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/physiology ; Amino Acid Sequence ; Animals ; Blotting, Northern ; Calcitonin/*metabolism ; Cloning, Molecular ; Cyclic AMP/physiology ; DNA/genetics ; Gene Expression ; Kidney/physiology ; Molecular Sequence Data ; RNA, Messenger/genetics ; Receptors, Calcitonin ; Receptors, Cell Surface/*genetics ; Swine
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    Cloning of complementary DNA encoding a functional human interleukin-8 receptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-13
    Description: Interleukin-8 (IL-8) is an inflammatory cytokine that activates neutrophil chemotaxis, degranulation, and the respiratory burst. Neutrophils express receptors for IL-8 that are coupled to guanine nucleotide-binding proteins (G proteins); binding of IL-8 to its receptor induces the mobilization of intracellular calcium stores. A cDNA clone from HL-60 neutrophils, designated p2, has now been isolated that encodes a human IL-8 receptor. When p2 is expressed in oocytes from Xenopus laevis, the oocytes bind 125I-labeled IL-8 specifically and respond to IL-8 by mobilizing calcium stores with an EC50 of 20 nM. This IL-8 receptor has 77% amino acid identity with a second human neutrophil receptor isotype that binds IL-8 with higher affinity. It also exhibits 69% amino acid identity with a protein reported to be an N-formyl peptide receptor from rabbit neutrophils, but less than 30% identity with all other known G protein-coupled receptors, including the human N-formyl peptide receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murphy, P M -- Tiffany, H L -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1280-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1891716" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; Cloning, Molecular/methods ; DNA/genetics ; Gene Library ; Humans ; Interleukin-8/*metabolism/pharmacology ; Kinetics ; Molecular Sequence Data ; Neutrophils/immunology ; Oocytes/drug effects/physiology ; Protein Biosynthesis ; Rabbits ; Receptors, Immunologic/drug effects/*genetics/physiology ; Receptors, Interleukin-8A ; Recombinant Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Signal Transduction ; Transcription, Genetic ; Xenopus
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    Spatial control of gut-specific gene expression during Caenorhabditis elegans development (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-04-26
    Description: The nematode Caenorhabditis elegans was transformed with constructs containing upstream deletions of the gut-specific ges-1 carboxylesterase gene. With particular deletions, ges-1 was expressed, not as normally in the gut, but rather in muscle cells of the pharynx (which belong to a sister lineage of the gut) or in body wall muscle and hypodermal cells (which belong to a cousin lineage of the gut). These observations suggest that gut-specific gene expression in C. elegans involves not only gut-specific activators but also multiple repressors that are present in particular nongut lineages.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aamodt, E J -- Chung, M A -- McGhee, J D -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):579-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Biochemistry, University of Calgary, Alberta, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2020855" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis/embryology/enzymology/*genetics ; Carboxylesterase ; Carboxylic Ester Hydrolases/*genetics ; Chromosome Deletion ; DNA/genetics ; Digestive System/embryology/enzymology ; Embryo, Nonmammalian/physiology ; *Gene Expression Regulation, Enzymologic ; Models, Biological ; Organ Specificity
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    Electronic data publishing and GenBank (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-31
    Description: GenBank, the national repository for nucleotide sequence data, has implemented a new model of scientific data management, which we term electronic data publishing. In traditional publishing, both scientific conclusions and supporting data are communicated via the printed page, and in electronic journal publishing, both types of information are communicated via electronic media. In electronic data publishing, by contrast, conclusions are published in a journal while data are published via a network-accessible, electronic database.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cinkosky, M J -- Fickett, J W -- Gilna, P -- Burks, C -- GM-7-2110/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1273-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, NM 87545.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925538" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/genetics ; Data Collection/methods ; *Databases, Factual ; *Electronics ; Human Genome Project ; Humans ; *Publishing ; Software
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    Role of nucleosomal cores and histone H1 in regulation of transcription by RNA polymerase II (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-11
    Description: The relation between chromatin structure and transcriptional activity was examined by in vitro transcription analysis of chromatin reconstituted in the absence or presence of histone H1. To maintain well-defined template DNA, purified components were used in the reconstitution of chromatin. Reconstitution of nucleosomal cores to an average density of 1 nucleosome per 200 base pairs of DNA resulted in a mild reduction of basal RNA polymerase II transcription to 25 to 50 percent of that obtained with naked DNA templates. This nucleosome-mediated repression was due to nucleosomal cores located at the RNA start site and could not be counteracted by the sequence-specific transcription activators Sp1 and GAL4-VP16. When H1 was incorporated into the chromatin at 0.5 to 1.0 molecule per nucleosome (200 base pairs of DNA), RNA synthesis was reduced to 1 to 4 percent of that observed with chromatin containing only nucleosomal cores, and this H1-mediated repression could be counteracted by the addition of Sp1 or GAL4-VP16 (antirepression). With naked DNA templates, transcription was increased by a factor of 3 and 8 by Sp1 and GAL4-VP-16, respectively (true activation). With H1-repressed chromatin templates, however, the magnitude of transcriptional activation mediated by Sp1 and GAL4-VP16 was 90 and more than 200 times higher, respectively, because of the combined effects of true activation and antirepression. The data provide direct biochemical evidence that support and clarify previously proposed models in which there is depletion or reconfiguration of nucleosomal cores and histone H1 at the promoter regions of active genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Laybourn, P J -- Kadonaga, J T -- New York, N.Y. -- Science. 1991 Oct 11;254(5029):238-45.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1718039" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromatin/physiology ; DNA/genetics ; Gene Expression Regulation ; Histones/*physiology ; Nucleosomes/*physiology ; RNA/genetics ; RNA Polymerase II/*metabolism ; *Transcription, Genetic
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    Identification of a competitive HGF antagonist encoded by an alternative transcript (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-29
    Description: We identified a naturally occurring hepatocyte growth factor (HGF) variant, whose predicted sequence extends only through the second kringle domain of this plasminogen-related molecule. This smaller molecule, derived from an alternative HGF transcript, lacked mitogenic activity but specifically inhibited HGF-induced mitogenesis. Cross-linking studies demonstrated that the truncated molecule competes with HGF for binding to the HGF receptor, which has been identified as the c-met protooncogene product. Thus, the same gene encodes both a growth factor and its direct antagonist.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, A M -- Rubin, J S -- Bottaro, D P -- Hirschfield, D W -- Chedid, M -- Aaronson, S A -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1382-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1720571" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blotting, Northern ; Cell Line ; Culture Media ; DNA/genetics ; DNA Replication/drug effects ; Epidermal Growth Factor/pharmacology ; Growth Substances/*genetics/isolation & purification/pharmacology ; Hepatocyte Growth Factor ; Humans ; Kinetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Plasmids ; Poly A/genetics/isolation & purification ; Polymerase Chain Reaction/methods ; RNA/genetics/isolation & purification ; RNA, Messenger ; Thymidine/metabolism ; *Transcription, Genetic ; Transfection
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    Presence of an SH2 domain in the actin-binding protein tensin (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-03
    Description: The molecular cloning of the complementary DNA coding for a 90-kilodalton fragment of tensin, an actin-binding component of focal contacts and other submembraneous cytoskeletal structures, is reported. The derived amino acid sequence revealed the presence of a Src homology 2 (SH2) domain. This domain is shared by a number of signal transduction proteins including nonreceptor tyrosine kinases such as Abl, Fps, Src, and Src family members, the transforming protein Crk, phospholipase C-gamma 1, PI-3 (phosphatidylinositol) kinase, and guanosine triphosphatase-activating protein (GAP). Like the SH2 domain found in Src, Crk, and Abl, the SH2 domain of tensin bound specifically to a number of phosphotyrosine-containing proteins from v-src-transformed cells. Tensin was also found to be phosphorylated on tyrosine residues. These findings suggest that by possessing both actin-binding and phosphotyrosine-binding activities and being itself a target for tyrosine kinases, tensin may link signal transduction pathways with the cytoskeleton.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Lu, M L -- Lo, S H -- Lin, S -- Butler, J A -- Druker, B J -- Roberts, T M -- An, Q -- Chen, L B -- GM 22289/GM/NIGMS NIH HHS/ -- GM 38318/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):712-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cellular and Molecular Biology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1708917" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Chick Embryo ; Cloning, Molecular ; Cytoskeletal Proteins/*chemistry/genetics/metabolism ; DNA/genetics ; Fluorescent Antibody Technique ; Immunoblotting ; *Microfilament Proteins ; Molecular Sequence Data ; Peptide Fragments/genetics ; Phosphotyrosine ; Protein-Tyrosine Kinases/genetics ; Sequence Homology, Nucleic Acid ; Signal Transduction ; Tyrosine/analogs & derivatives/metabolism
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  • 45
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    A distinct potassium channel polypeptide encoded by the Drosophila eag locus (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-14
    Description: Many of the signaling properties of neurons and other electrically excitable cells are determined by a diverse family of potassium channels. A number of genes that encode potassium channel polypeptides have been cloned from various organisms on the basis of their sequence similarity to the Drosophila Shaker (Sh) locus. As an alternative strategy, a molecular analysis of other Drosophila genes that were defined by mutations that perturb potassium channel function was undertaken. Sequence analysis of complementary DNA from the ether a go-go (eag) locus revealed that it encodes a structural component of potassium channels that is related to but is distinct from all identified potassium channel polypeptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Warmke, J -- Drysdale, R -- Ganetzky, B -- NS15390/NS/NINDS NIH HHS/ -- T32GM07131/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 14;252(5012):1560-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Cambridge, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840699" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; DNA/genetics ; Drosophila/*genetics ; Molecular Sequence Data ; Potassium Channels/*genetics ; Protein Conformation ; Sequence Homology, Nucleic Acid
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  • 46
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    Primary structure and functional activity of a phosphatidylinositol-glycan-specific phospholipase D (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-04-19
    Description: A phosphatidylinositol-glycan-specific phospholipase D (PI-G PLD) that specifically hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol-glycans (PI-Gs) has recently been purified from human and bovine sera. The primary structure of bovine PI-G PLD has now been determined and the functional activity of the enzyme has been studied. Expression of PI-G PLD complementary DNA in COS cells produced a protein that specifically hydrolyzed the inositol phosphate linkage of the PI-G anchor. Cotransfection of PI-G PLD with a PI-G-anchored protein resulted in the secretion of the PI-G-anchored protein. The results suggest that the expression of PI-G PLD may influence the expression and location of PI-G-anchored proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scallon, B J -- Fung, W J -- Tsang, T C -- Li, S -- Kado-Fong, H -- Huang, K S -- Kochan, J P -- New York, N.Y. -- Science. 1991 Apr 19;252(5004):446-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular/Cellular Biology and Biochemistry, Hoffmann-La Roche, Inc., Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2017684" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cattle ; Cell Line ; Cloning, Molecular ; DNA/genetics ; Gene Expression ; Glycosylphosphatidylinositols ; Humans ; Hydrolysis ; Molecular Sequence Data ; Peptide Fragments/chemistry ; Phosphatidylinositols/metabolism ; Phospholipase D/*chemistry/genetics/metabolism ; Polysaccharides/metabolism ; Sequence Homology, Nucleic Acid ; Transfection ; Trypsin
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  • 47
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    Targeting of the master receptor MOM19 to mitochondria (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-13
    Description: The targeting of proteins to mitochondria involves the recognition of the precursor proteins by receptors on the mitochondrial surface followed by insertion of the precursors into the outer membrane at the general insertion site GIP. Most mitochondrial proteins analyzed so far use a mitochondrial outer membrane protein of 19 kilodaltons (MOM19) as an import receptor. The gene encoding MOM19 has now been isolated. The deduced amino acid sequence predicts that MOM19 is anchored in the outer membrane by an NH2-terminal hydrophobic sequence, while the rest of the protein forms a hydrophilic domain exposed to the cytosol. MOM19 was targeted to the mitochondria via a pathway that is independent of protease-accessible surface receptors and controlled by direct assembly of the MOM19 precursor with GIP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schneider, H -- Sollner, T -- Dietmeier, K -- Eckerskorn, C -- Lottspeich, F -- Trulzsch, B -- Neupert, W -- Pfanner, N -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1659-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Physiologische Chemie, Universitat Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1661031" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Compartmentation ; DNA/genetics ; Fungal Proteins/chemistry/genetics ; Genes, Fungal ; Intracellular Membranes/metabolism ; Macromolecular Substances ; Membrane Proteins/*metabolism ; Mitochondria/*metabolism ; Molecular Sequence Data ; Protein Precursors/metabolism ; Receptors, Cell Surface/*genetics/*metabolism ; *Receptors, Cytoplasmic and Nuclear ; Recombinant Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 48
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    Organizer-specific homeobox genes in Xenopus laevis embryos (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-12
    Description: The dorsal blastopore lip of the early Xenopus laevis gastrula can organize a complete secondary body axis when transplanted to another embryo. A search for potential gene regulatory components specifically expressed in the organizer was undertaken that resulted in the identification of four types of complementary DNAs from homeobox-containing genes that fulfill this criterion. The most abundant of these encodes a DNA-binding specificity similar to that of the Drosophila melanogaster anterior morphogen bicoid. The other three are also homologous to developmentally significant Drosophila genes. These four genes may participate in the regulation of the developmental potential of the organizer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blumberg, B -- Wright, C V -- De Robertis, E M -- Cho, K W -- HD-07273/HD/NICHD NIH HHS/ -- HD-21502/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):194-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1677215" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; DNA/genetics ; DNA-Binding Proteins/*physiology ; Embryonic Induction ; Gene Expression ; Gene Library ; *Genes, Homeobox ; Molecular Sequence Data ; Morphogenesis ; Oligonucleotides/chemistry ; RNA, Messenger/genetics ; Xenopus laevis/*embryology/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 49
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    Deposits of amyloid beta protein in the central nervous system of transgenic mice (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-19
    Description: Alzheimer's disease is characterized by widespread deposition of amyloid in the central nervous system. The 4-kilodalton amyloid beta protein is derived from a larger amyloid precursor protein and forms amyloid deposits in the brain by an unknown pathological mechanism. Except for aged nonhuman primates, there is no animal model for Alzheimer's disease. Transgenic mice expressing amyloid beta protein in the brain could provide such a model. To investigate this possibility, the 4-kilodalton human amyloid beta protein was expressed under the control of the promoter of the human amyloid precursor protein in two lines of transgenic mice. Amyloid beta protein accumulated in the dendrites of some but not all hippocampal neurons in 1-year-old transgenic mice. Aggregates of the amyloid beta protein formed amyloid-like fibrils that are similar in appearance to those in the brains of patients with Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wirak, D O -- Bayney, R -- Ramabhadran, T V -- Fracasso, R P -- Hart, J T -- Hauer, P E -- Hsiau, P -- Pekar, S K -- Scangos, G A -- Trapp, B D -- New York, N.Y. -- Science. 1991 Jul 19;253(5017):323-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Therapeutics Inc., Miles Research Center, West Haven, CT 06516.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857970" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics/pathology ; Amyloid beta-Peptides/analysis/*genetics ; Animals ; Base Sequence ; Brain/*metabolism/pathology ; DNA/genetics ; Hippocampus/ultrastructure ; Humans ; Mice ; Mice, Transgenic ; Microscopy, Electron ; Molecular Sequence Data ; Neurofibrils/ultrastructure ; Oligonucleotide Probes ; Restriction Mapping
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  • 50
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    In vivo footprinting of MHC class II genes: bare promoters in the bare lymphocyte syndrome (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-05-03
    Description: Major histocompatibility complex (MHC) class II genes are coordinately regulated and show tissue-specific expression. With the use of in vivo footprinting, common promoter sites in these genes were found to be occupied only in cells that expressed the genes, in spite of the presence of the promoter binding proteins. In vivo analysis of mutant cell lines that exhibited coordinate loss of class II MHC expression, including several from individuals with bare lymphocyte syndrome, revealed two in vivo phenotypes. One suggests a defect in gene activation, whereas the other suggests a defect in promoter accessibility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kara, C J -- Glimcher, L H -- AI21163/AI/NIAID NIH HHS/ -- GM36864/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):709-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Harvard School of Public Health, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1902592" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*immunology ; Base Sequence ; Cell Line ; DNA/genetics ; *Gene Expression ; Genes, MHC Class II/*genetics ; Humans ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; *Mutation ; Polymerase Chain Reaction ; *Promoter Regions, Genetic ; Regulatory Sequences, Nucleic Acid ; Syndrome
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    Cloning and expression of the cDNA for human gamma-glutamyl carboxylase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-13
    Description: The cDNA for human gamma-glutamyl carboxylase, which accomplishes the post-translational modification required for the activity of all of the vitamin K-dependent proteins, was cloned. The enzyme is a 758-residue integral membrane protein and appears to have three transmembrane domains near its amino terminus. The hydrophilic COOH-terminal half of the carboxylase has 19.3 percent identity with soybean seed lipoxygenase. Expression of the cloned cDNA resulted in an increase in carboxylase activity in microsomes of transfected cells compared to mock-transfected cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, S M -- Cheung, W F -- Frazier, D -- Stafford, D W -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1634-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of North Carolina, Chapel Hill 27599-3280.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1749935" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; *Carbon-Carbon Ligases ; Cattle ; Cloning, Molecular ; DNA/genetics ; Humans ; Ligases/*genetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; Polymerase Chain Reaction ; Recombinant Proteins ; Sequence Alignment
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    Molecular cloning of an invertebrate glutamate receptor subunit expressed in Drosophila muscle (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-04
    Description: Insects and other invertebrates use glutamate as a neurotransmitter in the central nervous system and at the neuromuscular junction. A complementary DNA from Drosophila melanogaster, designated DGluR-II, has been isolated that encodes a distant homolog of the cloned mammalian ionotropic glutamate receptor family and is expressed in somatic muscle tissue of Drosophila embryos. Electrophysiological recordings made in Xenopus oocytes that express DGluR-II revealed depolarizing responses to L-glutamate and L-aspartate but low sensitivity to quisqualate, alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA), and kainate. The DGluR-II protein may represent a distinct glutamate receptor subtype, which shares its structural design with other members of the ionotropic glutamate receptor family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schuster, C M -- Ultsch, A -- Schloss, P -- Cox, J A -- Schmitt, B -- Betz, H -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):112-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zentrum fur Molekulare Biologie, Universitat Heidelberg, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1681587" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Drosophila melanogaster/*genetics/physiology ; Gene Expression ; Glutamates/pharmacology ; Glutamic Acid ; Molecular Sequence Data ; Muscles/*physiology ; Oligonucleotides/chemistry ; Receptors, Glutamate ; Receptors, Neurotransmitter/*genetics/physiology ; Sequence Alignment
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    Transcriptional repression mediated by the WT1 Wilms tumor gene product (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-07
    Description: The wt1 gene, a putative tumor suppressor gene located at the Wilms tumor (WT) locus on chromosome 11p13, encodes a zinc finger-containing protein that binds to the same DNA sequence as EGR-1, a mitogen-inducible immediate-early gene product that activates transcription. The transcriptional regulatory potential of WT1 has not been demonstrated. In transient transfection assays, the WT1 protein functioned as a repressor of transcription when bound to the EGR-1 site. The repression function was mapped to the glutamine- and proline-rich NH2-terminus of WT1; fusion of this domain to the zinc finger region of EGR-1 converted EGR-1 into a transcriptional repressor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Madden, S L -- Cook, D M -- Morris, J F -- Gashler, A -- Sukhatme, V P -- Rauscher, F J 3rd -- CA-0917-15/CA/NCI NIH HHS/ -- CA-23413/CA/NCI NIH HHS/ -- CA-52009/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Sep 27;253(5027):1550-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wistar Institute of Anatomy and Biology, Philadelphia, PA 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1654597" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; Chromosomes, Human, Pair 11 ; DNA/genetics ; DNA-Binding Proteins/*genetics ; Gene Expression Regulation ; *Genes, Tumor Suppressor ; Humans ; Kidney Neoplasms/*genetics ; Molecular Sequence Data ; Repressor Proteins/*genetics ; *Transcription, Genetic ; Wilms Tumor/*genetics ; Zinc Fingers/*genetics
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    Recent advances in the polymerase chain reaction (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-06-21
    Description: The polymerase chain reaction (PCR) has dramatically altered how molecular studies are conducted as well as what questions can be asked. In addition to simplifying molecular tasks typically carried out with the use of recombinant DNA technology, PCR has allowed a spectrum of advances ranging from the identification of novel genes and pathogens to the quantitation of characterized nucleotide sequences. PCR can provide insights into the intricacies of single cells as well as the evolution of species. Some recent developments in instrumentation, methodology, and applications of the PCR are presented in this review.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erlich, H A -- Gelfand, D -- Sninsky, J J -- New York, N.Y. -- Science. 1991 Jun 21;252(5013):1643-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics, Core Technology, Cetus Corporation, Emeryville, CA 94608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047872" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Biological Evolution ; DNA/genetics ; DNA Fingerprinting ; Forensic Medicine/methods ; Gene Expression ; Genetic Diseases, Inborn/genetics ; Human Genome Project ; Humans ; Multigene Family ; Mutation ; Oligonucleotides/chemistry ; *Polymerase Chain Reaction
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    The Human Genome Project and patents (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1991 Dec 20;254(5039):1710, 1712.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1763316" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/genetics ; Federal Government ; Genetics, Medical ; *Human Genome Project ; Humans ; Information Dissemination ; Internationality ; National Institutes of Health (U.S.) ; *Patents as Topic ; Risk Assessment ; Societies, Scientific ; United States
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  • 56
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    A homolog of the armadillo protein in Drosophila (plakoglobin) associated with E-cadherin (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-29
    Description: Three cytoplasmic proteins, called catenins, bind to the cytoplasmic tail of the epithelial cell-cell adhesion molecule E-cadherin. The complementary DNA sequence was determined for the 92-kilodalton beta catenin of Xenopus laevis. The sequence is homologous to mammalian plakoglobin, a protein of desmosomal and zonula adherens cell junctions, and to the plakoglobin homolog in Drosophila melanogaster, the product of the segment polarity gene armadillo. A monoclonal antibody to bovine plakoglobin recognizes the analogous beta catenin in the Madin-Darby canine kidney (MDCK) cell line. Armadillo plakoglobin may link E-cadherin to the underlying actin cytoskeleton at cell-cell junctions; the E-cadherin-catenin protein complex may also participate in the transmission of developmental information.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCrea, P D -- Turck, C W -- Gumbiner, B -- 5-F32-GM-13060/GM/NIGMS NIH HHS/ -- GM37432/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1359-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962194" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cadherins/*genetics ; Cell Line ; Cytoskeletal Proteins/*genetics ; DNA/genetics ; Desmoplakins ; Drosophila melanogaster/*genetics ; Molecular Sequence Data ; Sequence Homology, Nucleic Acid ; *Trans-Activators ; Xenopus Proteins ; Xenopus laevis ; beta Catenin ; gamma Catenin
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  • 57
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    A gene encoding an antigen recognized by cytolytic T lymphocytes on a human melanoma (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-13
    Description: Many human melanoma tumors express antigens that are recognized in vitro by cytolytic T lymphocytes (CTLs) derived from the tumor-bearing patient. A gene was identified that directed the expression of antigen MZ2-E on a human melanoma cell line. This gene shows no similarity to known sequences and belongs to a family of at least three genes. It is expressed by the original melanoma cells, other melanoma cell lines, and by some tumor cells of other histological types. No expression was observed in a panel of normal tissues. Antigen MZ2-E appears to be presented by HLA-A1; anti-MZ2-E CTLs of the original patient recognized two melanoma cell lines of other HLA-A1 patients that expressed the gene. Thus, precisely targeted immunotherapy directed against antigen MZ2-E could be provided to individuals identified by HLA typing and analysis of the RNA of a small tumor sample.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van der Bruggen, P -- Traversari, C -- Chomez, P -- Lurquin, C -- De Plaen, E -- Van den Eynde, B -- Knuth, A -- Boon, T -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1643-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research, Brussels, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840703" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Neoplasm/*genetics ; Base Sequence ; Blotting, Northern ; Cloning, Molecular ; DNA/genetics ; Gene Expression ; Genes, Neoplasm ; Humans ; Melanoma/*immunology ; Melanoma-Specific Antigens ; Molecular Sequence Data ; *Neoplasm Proteins ; Polymerase Chain Reaction ; RNA, Messenger/genetics ; RNA, Neoplasm/genetics ; T-Lymphocytes, Cytotoxic/*immunology ; Tumor Cells, Cultured
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    Fibroblast growth factor receptors from liver vary in three structural domains (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-02-08
    Description: Changes in heparin-binding fibroblast growth factor gene expression and receptor phenotype occur during liver regeneration and in hepatoma cells. The nucleotide sequence of complementary DNA predicts that three amino-terminal domain motifs, two juxtamembrane motifs, and two intracellular carboxyl-terminal domain motifs combine to form a minimum of 6 and potentially 12 homologous polypeptides that constitute the growth factor receptor family in a single human liver cell population. Amino-terminal variants consisted of two transmembrane molecules that contained three and two immunoglobulin-like disulfide loops, as well as a potential intracellular form of the receptor. The two intracellular juxtamembrane motifs differed in a potential serine-threonine kinase phosphorylation site. One carboxyl-terminal motif was a putative tyrosine kinase that contained potential tyrosine phosphorylation sites. The second carboxyl-terminal motif was probably not a tyrosine kinase and did not exhibit the same candidate carboxyl-terminal tyrosine phosphorylation sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hou, J Z -- Kan, M K -- McKeehan, K -- McBride, G -- Adams, P -- McKeehan, W L -- New York, N.Y. -- Science. 1991 Feb 8;251(4994):665-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉W. Alton Jones Cell Science Center, Inc., Lake Placid, NY 12946.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1846977" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Humans ; Liver/*physiology ; Membrane Glycoproteins/*genetics ; Molecular Sequence Data ; Multigene Family ; Protein-Tyrosine Kinases/*genetics ; Receptors, Cell Surface/*physiology ; Receptors, Fibroblast Growth Factor ; Receptors, Mitogen/*physiology ; Receptors, Vascular Endothelial Growth Factor ; Tumor Cells, Cultured
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    Cloning, expression, and gene structure of a G protein-coupled glutamate receptor from rat brain (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-31
    Description: A complementary DNA encoding a G protein-coupled glutamate receptor from rat brain, GluGR, was cloned by functional expression in Xenopus oocytes. The complementary DNA encodes a protein of 1199 amino acids containing a seven-transmembrane motif, flanked by large amino- and carboxyl-terminal domains. This receptor lacks any amino acid sequence similarity with other G protein-coupled receptors, suggesting that it may be a member of a new subfamily. The presence of two introns flanking the central core suggests that GluGR may have evolved by exon shuffling. Expressed in oocytes, GluGR is activated by quisqualate greater than glutamate greater than ibotenate greater than trans-1-aminocyclopentyl-1,3-dicarboxylate, and it is inhibited by 2-amino-3-phosphonopropionate. Activation is blocked by Bordella pertussis toxin. These properties are typical of some metabotropic glutamate receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Houamed, K M -- Kuijper, J L -- Gilbert, T L -- Haldeman, B A -- O'Hara, P J -- Mulvihill, E R -- Almers, W -- Hagen, F S -- AR 17803/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1318-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1656524" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; *Brain Chemistry ; *Cloning, Molecular ; DNA/genetics ; Exons ; GTP-Binding Proteins/*metabolism ; Humans ; Introns ; Molecular Sequence Data ; Nucleic Acid Hybridization ; RNA, Messenger/genetics ; Rats ; Receptors, Glutamate ; Receptors, Neurotransmitter/chemistry/*genetics/metabolism ; Sequence Homology, Nucleic Acid
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    The dominant W42 spotting phenotype results from a missense mutation in the c-kit receptor kinase (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-01-12
    Description: The murine white spotting locus (W) is allelic with the proto-oncogene c-kit, which encodes a transmembrane tyrosine protein kinase receptor for an unknown ligand. Mutations at the W locus affect various aspects of hematopoiesis and the proliferation and migration of primordial germ cells and melanoblasts during development to varying degrees of severity. The W42 mutation has a particularly severe effect in both the homozygous and the heterozygous states. The molecular basis of the W42 mutation was determined. The c-kit protein products in homozygous mutant mast cells were expressed normally but displayed a defective tyrosine kinase activity in vitro. Nucleotide sequence analysis of mutant complementary DNAs revealed a missense mutation that replaces aspartic acid with asparagine at position 790 in the c-kit protein product. Aspartic acid-790 is a conserved residue in all protein kinases. These results provide an explanation for the dominant nature of the W42 mutation and provide insight into the mechanism of c-kit-mediated signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tan, J C -- Nocka, K -- Ray, P -- Traktman, P -- Besmer, P -- P01-CA-16599/CA/NCI NIH HHS/ -- R01-CA-32926/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jan 12;247(4939):209-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Program, Sloan Kettering Institute, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1688471" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; DNA/genetics ; Gene Expression ; Homozygote ; Liver/analysis/cytology/embryology ; Mast Cells/metabolism ; Mice ; Molecular Sequence Data ; *Mutation ; *Phenotype ; Polymerase Chain Reaction ; Protein-Tyrosine Kinases/*genetics ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins c-kit ; RNA/analysis ; Receptors, Cell Surface/genetics ; Signal Transduction
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    De novo design, expression, and characterization of Felix: a four-helix bundle protein of native-like sequence (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-08-24
    Description: The protein Felix was designed de novo to fold into an antiparallel four-helix bundle of specific topology. Its sequence of 79 amino acid residues is not homologous to any known protein sequence, but is "native-like" in that it is nonrepetitive and contains 19 of the 20 naturally occurring amino acids. Felix has been expressed from a synthetic gene cloned in Escherichia coli, and the protein has been purified to homogeneity. Physical characterization of the purified protein indicates that Felix (i) is monomeric in solution, (ii) is predominantly alpha-helical, (iii) contains a designed intramolecular disulfide bond linking the first and fourth helices, and (iv) buries its single tryptophan in an apolar environment and probably in close proximity with the disulfide bond. These physical properties rule out several alternative structures and indicate that Felix indeed folds into approximately the designed three-dimensional structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hecht, M H -- Richardson, J S -- Richardson, D C -- Ogden, R C -- New York, N.Y. -- Science. 1990 Aug 24;249(4971):884-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Duke University, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2392678" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acid Sequence ; Base Sequence ; DNA/genetics ; *Models, Chemical ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; Protein Denaturation ; *Proteins ; *Recombinant Proteins
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    Huntington's gene: so near, yet so far (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-02-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1990 Feb 9;247(4943):624-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1967853" target="_blank"〉PubMed〈/a〉
    Keywords: *Chromosomes, Human, Pair 4 ; DNA/genetics ; Foundations ; Genetic Markers ; Humans ; Huntington Disease/*genetics ; Interinstitutional Relations ; Lod Score ; Polymorphism, Restriction Fragment Length ; Research Support as Topic
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    beta-Arrestin: a protein that regulates beta-adrenergic receptor function (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-06-22
    Description: Homologous or agonist-specific desensitization of beta-adrenergic receptors is thought to be mediated by a specific kinase, the beta-adrenergic receptor kinase (beta ARK). However, recent data suggest that a cofactor is required for this kinase to inhibit receptor function. The complementary DNA for such a cofactor was cloned and found to encode a 418-amino acid protein homologous to the retinal protein arrestin. The protein, termed beta-arrestin, was expressed and partially purified. It inhibited the signaling function of beta ARK-phosphorylated beta-adrenergic receptors by more than 75 percent, but not that of rhodopsin. It is proposed that beta-arrestin in concert with beta ARK effects homologous desensitization of beta-adrenergic receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lohse, M J -- Benovic, J L -- Codina, J -- Caron, M G -- Lefkowitz, R J -- DK19318/DK/NIDDK NIH HHS/ -- HL16037/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 22;248(4962):1547-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Biochemistry and Cell Biology, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2163110" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens/*genetics/isolation & purification/pharmacology ; Arrestin ; Blotting, Northern ; Chromatography, Ion Exchange ; Cloning, Molecular ; *Cyclic AMP-Dependent Protein Kinases ; DNA/genetics ; Eye Proteins/*genetics/isolation & purification/pharmacology ; Gene Expression Regulation ; Molecular Sequence Data ; Phosphodiesterase Inhibitors/*pharmacology ; Phosphorylation ; Protein Kinases/*pharmacology ; RNA, Messenger/analysis ; Receptors, Adrenergic, beta/*drug effects/physiology ; Transfection ; beta-Adrenergic Receptor Kinases
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    Tissue, developmental, and tumor-specific expression of divergent transcripts in Wilms tumor (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-11-16
    Description: The Wilms tumor locus on chromosome 11p13 has been mapped to a region defined by overlapping, tumor-specific deletions. Complementary DNA clones representing transcripts of 2.5 (WIT-1) and 3.5 kb (WIT-2) mapping to this region were isolated from a kidney complementary DNA library. Expression of WIT-1 and WIT-2 was restricted to kidney and spleen. RNase protection revealed divergent transcription of WIT-1 and WIT-2, originating from a DNA region of less than 600 bp. Both transcripts were present at high concentrations in fetal kidney and at much reduced amounts in 5-year-old and adult kidneys. Eleven of 12 Wilms tumors classified as histopathologically heterogeneous exhibited absent or reduced expression of WIT-2, whereas only 4 of 14 histopathologically homogeneous tumors showed reduced expression. These data demonstrate a molecular basis for the pathogenetic heterogeneity in Wilms tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, A -- Campbell, C E -- Bonetta, L -- McAndrews-Hill, M S -- Chilton-MacNeill, S -- Coppes, M J -- Law, D J -- Feinberg, A P -- Yeger, H -- Williams, B R -- New York, N.Y. -- Science. 1990 Nov 16;250(4983):991-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Hospital for Sick Children, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2173145" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blotting, Northern ; DNA/genetics ; Genes, Wilms Tumor/*genetics ; Humans ; Kidney Neoplasms/*genetics ; Molecular Sequence Data ; Transcription, Genetic ; Wilms Tumor/*genetics
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    Human sickle hemoglobin in transgenic mice (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-02-02
    Description: DNA molecules that contain the human alpha- and beta s-globin genes inserted downstream of erythroid-specific, deoxyribonuclease I super-hypersensitive sites were coinjected into fertilized mouse eggs and a transgenic mouse line was established that synthesizes human sickle hemoglobin (Hb S). These animals were bred to beta-thalassemic mice to reduce endogenous mouse globin levels. When erythrocytes from these mice were deoxygenated, greater than 90 percent of the cells displayed the same characteristic sickled shapes as erythrocytes from humans with sickle cell disease. Compared to controls the mice have decreased hematocrits, elevated reticulocyte counts, lower hemoglobin concentrations, and splenomegaly, which are all indications of the anemia associated with human sickle cell disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ryan, T M -- Townes, T M -- Reilly, M P -- Asakura, T -- Palmiter, R D -- Brinster, R L -- Behringer, R R -- HD-09172/HD/NICHD NIH HHS/ -- HL-35559/HL/NHLBI NIH HHS/ -- HL43508/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Feb 2;247(4942):566-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, School of Medicine, University of Alabama, Birmingham 35294.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2154033" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/blood/genetics ; Animals ; DNA/genetics ; DNA Transposable Elements ; Erythrocytes/ultrastructure ; Genes ; Globins/*genetics ; Hemoglobin, Sickle/*genetics/isolation & purification ; Humans ; Mice ; Mice, Transgenic ; Microscopy, Electron ; Microscopy, Electron, Scanning
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    Cloning of an interleukin-3 receptor gene: a member of a distinct receptor gene family (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-01-19
    Description: Interleukin-3 (IL-3) binds to its receptor with high and low affinities, induces tyrosine phosphorylation, and promotes the proliferation and differentiation of hematopoietic cells. A binding component of the IL-3 receptor was cloned. Fibroblasts transfected with the complementary DNA bound IL-3 with a low affinity [dissociation constant (Kd) of 17.9 +/- 3.6 nM]. No consensus sequence for a tyrosine kinase was present in the cytoplasmic domain. Thus, additional components are required for a functional high affinity IL-3 receptor. A sequence comparison of the IL-3 receptor with other cytokine receptors (erythropoietin, IL-4, IL-6, and the beta chain IL-2 receptor) revealed a common motif of a distinct receptor gene family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Itoh, N -- Yonehara, S -- Schreurs, J -- Gorman, D M -- Maruyama, K -- Ishii, A -- Yahara, I -- Arai, K -- Miyajima, A -- New York, N.Y. -- Science. 1990 Jan 19;247(4940):324-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2404337" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Cloning, Molecular ; DNA/genetics ; DNA Probes ; Escherichia coli/genetics ; Fibroblasts/metabolism ; Interleukin-3/metabolism ; Mice ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Plasmids ; Protein-Tyrosine Kinases/metabolism ; Receptors, Immunologic/*genetics/metabolism ; Receptors, Interleukin-3 ; Sequence Homology, Nucleic Acid ; Transfection
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    Calculating the original family--of exons (1990)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1990-12-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1990 Dec 7;250(4986):1342.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1701567" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Evolution ; DNA/genetics ; *Exons ; Proteins/*genetics ; RNA/genetics
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    Fibroblast growth factor receptor is a portal of cellular entry for herpes simplex virus type 1 (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-15
    Description: Herpes simplex virus type 1 (HSV-1) is a ubiquitous pathogen responsible for considerable morbidity in the general population. The results presented herein establish the basic fibroblast growth factor (FGF) receptor as a means of entry of HSV-1 into vertebrate cells. Inhibitors of basic FGF binding to its receptor and competitive polypeptide antagonists of basic FGF prevented HSV-1 uptake. Chinese hamster ovary (CHO) cells that do not express FGF receptors are resistant to HSV-1 entry; however, HSV-1 uptake is dramatically increased in CHO cells transfected with a complementary DNA encoding a basic FGF receptor. The distribution of this integral membrane protein in vivo may explain the tissue and cell tropism of HSV-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaner, R J -- Baird, A -- Mansukhani, A -- Basilico, C -- Summers, B D -- Florkiewicz, R Z -- Hajjar, D P -- P01 DK 18811/DK/NIDDK NIH HHS/ -- P01 HD 96601/HD/NICHD NIH HHS/ -- P50 HL 18828/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Jun 15;248(4961):1410-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2162560" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; Amino Acid Sequence ; Animals ; Binding, Competitive ; Cell Line ; Cell Membrane/microbiology ; Cricetinae ; DNA/genetics ; Fibroblast Growth Factors/antagonists & inhibitors/metabolism/pharmacology ; Heparitin Sulfate/metabolism ; Molecular Sequence Data ; Peptide Fragments/pharmacology ; Receptors, Cell Surface/genetics/*physiology ; Receptors, Fibroblast Growth Factor ; Simplexvirus/*physiology ; Transfection
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    Interphase and metaphase resolution of different distances within the human dystrophin gene (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-24
    Description: Fluorescence in situ hybridization makes possible direct visualization of single sequences not only on chromosomes, but within decondensed interphase nuclei, providing a potentially powerful approach for high-resolution (1 Mb and below) gene mapping and the analysis of nuclear organization. Interphase mapping was able to extend the ability to resolve and order sequences up to two orders of magnitude beyond localization on banded or unbanded chromosomes. Sequences within the human dystrophin gene separated by less than 100 kb to 1 Mb were visually resolved at interphase by means of standard microscopy. In contrast, distances in the 1-Mb range could not be ordered on the metaphase chromosome length. Analysis of sequences 100 kb to 1 Mb apart indicates a strong correlation between interphase distance and linear DNA distance, which could facilitate a variety of gene-mapping efforts. Results estimate chromatin condensation up to 1 Mb and indicate a comparable condensation for different cell types prepared by different techniques.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lawrence, J B -- Singer, R H -- McNeil, J A -- HD 18066/HD/NICHD NIH HHS/ -- HG 00251/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 24;249(4971):928-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, University of Massachusetts Medical School, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2203143" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Banding ; Chromosome Mapping ; *Chromosomes, Human, Pair 1 ; DNA/genetics ; DNA Probes ; Dystrophin ; Fibroblasts/cytology ; *Genes ; Genome, Human ; Humans ; Interphase ; Metaphase ; Muscle Proteins/*genetics ; Nucleic Acid Hybridization
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    Down to the wire for the NF gene (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-07-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1990 Jul 20;249(4966):236-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2115688" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/genetics ; *Genes ; Humans ; Mutation ; Neurofibromatosis 1/*genetics ; Suppression, Genetic
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    The worm project (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1990 Jun 15;248(4961):1310-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2356467" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Base Sequence ; Caenorhabditis/*genetics/growth & development ; *Chromosome Mapping ; Cloning, Molecular ; DNA/genetics ; Genomic Library ; Human Genome Project ; Nucleotide Mapping
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Type 1 neurofibromatosis gene: correction (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1990 Dec 21;250(4988):1749.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2125369" target="_blank"〉PubMed〈/a〉
    Keywords: Blotting, Southern ; Chromosomes, Human, Pair 17 ; Chromosomes, Human, Pair 22 ; Cloning, Molecular ; DNA/genetics ; Humans ; Neurofibromatosis 1/*genetics ; Translocation, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Sequence-specific binding of human Ets-1 to the T cell receptor alpha gene enhancer (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-09
    Description: Expression of the human T cell receptor (TCR) alpha gene is regulated by a T cell-specific transcriptional enhancer that is located 4.5 kilobases (kb) 3' to the C alpha gene segment. The core enhancer contains two nuclear protein binding sites, T alpha 1 and T alpha 2, which are essential for full enhancer activity. T alpha 1 contains a consensus cyclic adenosine monophosphate (cAMP) response element (CRE) and binds a set of ubiquitously expressed CRE binding proteins. In contrast, the transcription factors that interact with the T alpha 2 site have not been defined. In this report, a lambda gt11 expression protocol was used to isolate a complementary DNA (cDNA) that programs the expression of a T alpha 2 binding protein. DNA sequence analysis demonstrated that this clone encodes the human ets-1 proto-oncogene. Lysogen extracts produced with this cDNA clone contained a beta-galactosidase-Ets-1 fusion protein that bound specifically to a synthetic T alpha 2 oligonucleotide. The Ets-1 binding site was localized to a 17-base pair (bp) region from the 3' end of T alpha 2. Mutation of five nucleotides within this sequence abolished both Ets-1 binding and the activity of the TCR alpha enhancer in T cells. These results demonstrate that Ets-1 binds in a sequence-specific fashion to the human TCR alpha enhancer and suggest that this developmentally regulated proto-oncogene functions in regulating TCR alpha gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ho, I C -- Bhat, N K -- Gottschalk, L R -- Lindsten, T -- Thompson, C B -- Papas, T S -- Leiden, J M -- AI-29673/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1990 Nov 9;250(4982):814-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Ann Arbor, MI.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2237431" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding, Competitive ; Cloning, Molecular ; DNA/genetics ; DNA Mutational Analysis ; *Enhancer Elements, Genetic ; Gene Expression Regulation ; Gene Rearrangement, T-Lymphocyte ; Humans ; Immunoblotting ; Molecular Sequence Data ; Proto-Oncogene Protein c-ets-1 ; Proto-Oncogene Proteins/genetics/*metabolism ; Proto-Oncogene Proteins c-ets ; *Proto-Oncogenes ; Receptors, Antigen, T-Cell/genetics/*metabolism ; Transcription Factors ; Transcription, Genetic
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  • 74
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    Genetic mechanisms of tumor suppression by the human p53 gene (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-14
    Description: Mutations of the gene encoding p53, a 53-kilodalton cellular protein, are found frequently in human tumor cells, suggesting a crucial role for this gene in human oncogenesis. To model the stepwise mutation or loss of both p53 alleles during tumorigenesis, a human osteosarcoma cell line, Saos-2, was used that completely lacked endogenous p53. Single copies of exogenous p53 genes were then introduced by infecting cells with recombinant retroviruses containing either point-mutated or wild-type versions of the p53 cDNA sequence. Expression of wild-type p53 suppressed the neoplastic phenotype of Saos-2 cells, whereas expression of mutated p53 conferred a limited growth advantage to cells in the absence of wild-type p53. Wild-type p53 was phenotypically dominant to mutated p53 in a two-allele configuration. These results suggest that, as with the retinoblastoma gene, mutation of both alleles of the p53 gene is essential for its role in oncogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, P L -- Chen, Y M -- Bookstein, R -- Lee, W H -- CA51495/CA/NCI NIH HHS/ -- EY00278/EY/NEI NIH HHS/ -- EY05758/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 14;250(4987):1576-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, School of Medicine, University of California, San Diego, La Jolla 92093-0612.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2274789" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; *Cinnamates ; Cloning, Molecular ; DNA/genetics ; Drug Resistance/genetics ; Genes, p53/*genetics ; Genetic Vectors ; Humans ; Hygromycin B/analogs & derivatives ; Molecular Sequence Data ; Moloney murine leukemia virus/genetics ; Mutation ; Neomycin ; Osteosarcoma/*genetics ; Plasmids ; Transfection ; Tumor Cells, Cultured
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 75
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    Hot spots for growth hormone gene deletions in homologous regions outside of Alu repeats (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-21
    Description: Familial growth hormone deficiency type 1A is an autosomal recessive disease caused by deletion of both growth hormone-1 (GH1) alleles. Ten patients from heterogeneous geographic origins showed differences in restriction fragment length polymorphism haplotypes in nondeleted regions that flanked GH1, suggesting that these deletions arose from independent unequal recombination events. Deoxyribonucleic acid (DNA) samples from nine of ten patients showed that crossovers occurred within 99% homologous, 594-base pair (bp) segments that flanked GH1. A DNA sample from one patient indicated that the crossover occurred within 454-bp segments that flanked GH1 and contained 274-bp repeats that are 98% homologous. Although Alu repeats, which are frequent sites of recombination, are adjacent to GH1, they were not involved in any of the recombination events studied. These results suggest that length and degree of DNA sequence homology are important in defining recombination sites that resulted in GH1 deletions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vnencak-Jones, C L -- Phillips, J A 3rd -- DK 35592/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1745-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Vanderbilt University School of Medicine, Nashville, TN 37232.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1980158" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Composition ; Base Sequence ; *Chromosome Deletion ; Crossing Over, Genetic ; DNA/genetics ; Deoxyribonuclease EcoRI ; Growth Hormone/*genetics ; Haplotypes ; Humans ; Molecular Sequence Data ; Oligonucleotide Probes ; *Polymorphism, Restriction Fragment Length ; Repetitive Sequences, Nucleic Acid ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Transcription, Genetic
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    Poliovirus mutants resistant to neutralization with soluble cell receptors (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-14
    Description: Poliovirus mutants resistant to neutralization with soluble cellular receptor were isolated. Replication of soluble receptor-resistant (srr) mutants was blocked by a monoclonal antibody directed against the HeLa cell receptor for poliovirus, indicating that the mutants use this receptor to enter cells. The srr mutants showed reduced binding to HeLa cells and cell membranes. However, the reduced binding phenotype did not have a major impact on viral replication, as judged by plaque size and one-step growth curves. These results suggest that the use of soluble receptors as antiviral agents could lead to the selection of neutralization-resistant mutants that are able to bind cell surface receptors, replicate, and cause disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaplan, G -- Peters, D -- Racaniello, V R -- AI20017/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 14;250(4987):1596-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, College of Physicians and Surgeons of Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2177226" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Antiviral Agents ; Baculoviridae/genetics ; Cell Line ; Cell Membrane/metabolism ; Centrifugation, Density Gradient ; DNA/genetics ; Genetic Vectors ; HeLa Cells ; Humans ; Insects ; Mutation ; Neutralization Tests ; Poliovirus/genetics/*physiology ; Receptors, Virus/genetics/*physiology ; Recombinant Proteins/physiology ; Transfection ; Virus Replication
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Molecular cloning of the Bombyx mori prothoracicotropic hormone (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-03-16
    Description: Prothoracicotropic hormone (PTTH), a brain secretory polypeptide of insects, stimulates the prothoracic glands to produce and release ecdysone, the steroid essential to insect development. The complementary DNAs encoding PTTH of the silkmoth Bombyx mori were cloned and characterized, and the complete amino acid sequence was deduced. The data indicated that PTTH is first synthesized as a 224-amino acid polypeptide precursor containing three proteolytic cleavage signals. The carboxyl-terminal component (109 amino acids) that follows the last cleavage signal represents one PTTH subunit. Two PTTH subunits are linked together by disulfide bonds, before or after cleavage from prepro-PTTH, to form a homodimeric PTTH. When introduced into Escherichia coli cells, the complementary DNA directed the expression of an active substance that was functionally indistinguishable from natural PTTH. In situ hybridization showed the localization of the prepro-PTTH mRNA to two dorsolateral neurosecretory cells of the Bombyx brain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawakami, A -- Kataoka, H -- Oka, T -- Mizoguchi, A -- Kimura-Kawakami, M -- Adachi, T -- Iwami, M -- Nagasawa, H -- Suzuki, A -- Ishizaki, H -- New York, N.Y. -- Science. 1990 Mar 16;247(4948):1333-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, School of Science, Nagoya University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2315701" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Bombyx/*genetics/physiology ; Cloning, Molecular ; DNA/genetics ; Gene Expression ; Insect Hormones/*genetics ; Molecular Sequence Data ; Neurosecretory Systems/physiology ; Nucleic Acid Hybridization ; Protein Precursors/genetics
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    Hemolin: an insect-immune protein belonging to the immunoglobulin superfamily (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-21
    Description: Insects have an efficient defense system against infections. Their antibacterial immune proteins have been well characterized. However, the molecular mechanisms by which insects recognize foreignness are not yet known. Data are presented showing that hemolin (previously named P4), a bacteria-inducible hemolymph protein of the giant silk moth Hyalophora cecropia, belongs to the immunoglobulin superfamily. Functional analyses indicate that hemolin is one of the first hemolymph components to bind to the bacterial surface, taking part in a protein complex formation that is likely to initiate the immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sun, S C -- Lindstrom, I -- Boman, H G -- Faye, I -- Schmidt, O -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1729-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2270488" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/genetics ; *Genes, Immunoglobulin ; Hemolymph/immunology ; Immunoglobulins ; Insect Proteins ; Molecular Sequence Data ; Moths/genetics/*immunology ; *Multigene Family ; Proteins/*genetics ; Sequence Homology, Nucleic Acid
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  • 79
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    Suppression of tumorigenicity of human prostate carcinoma cells by replacing a mutated RB gene (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-02-09
    Description: Introduction of a normal retinoblastoma gene (RB) into retinoblastoma cells was previously shown to suppress several aspects of their neoplastic phenotype, including tumorigenicity in nude mice, thereby directly demonstrating a cancer suppression function of RB. To explore the possibility of a similar activity in a common adult tumor, RB expression was examined in three human prostate carcinoma cell lines. One of these, DU145, contained an abnormally small protein translated from an RB messenger RNA transcript that lacked 105 nucleotides encoded by exon 21. To assess the functional consequences of this mutation, normal RB expression was restored in DU145 cells by retrovirus-mediated gene transfer. Cells that maintained stable exogenous RB expression lost their ability to form tumors in nude mice, although their growth rate in culture was apparently unaltered. These results suggest that RB inactivation can play a significant role in the genesis of a common adult neoplasm and that restoration of normal RB-encoded protein in tumors could have clinical utility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bookstein, R -- Shew, J Y -- Chen, P L -- Scully, P -- Lee, W H -- 5758/PHS HHS/ -- New York, N.Y. -- Science. 1990 Feb 9;247(4943):712-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, School of Medicine, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2300823" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA/genetics ; Gene Amplification ; Gene Expression ; Humans ; Male ; Mice ; Mice, Nude ; Molecular Sequence Data ; Mutation ; Nucleic Acid Hybridization ; Prostatic Neoplasms/*genetics/pathology ; RNA, Messenger/genetics ; Retinoblastoma/*genetics ; *Suppression, Genetic ; Transfection ; Tumor Cells, Cultured
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 80
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    A family of three mouse potassium channel genes with intronless coding regions (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-02-23
    Description: To understand the molecular mechanisms responsible for generating physiologically diverse potassium channels in mammalian cells, mouse genomic clones have been isolated with a potassium channel complementary DNA, MBK1, that is homologous to the Drosophila potassium channel gene, Shaker. A family of three closely related potassium channel genes (MK1, MK2, and MK3) that are encoded at distinct genomic loci has been isolated. Sequence analysis reveals that the coding region of each of these three genes exists as a single uninterrupted exon in the mouse genome. This organization precludes the generation of multiple forms of the protein by alternative RNA splicing, a mechanism known to characterize the Drosophila potassium channel genes Shaker and Shab. Thus, mammals may use a different strategy for generating diverse K+ channels by encoding related genes at multiple distinct genomic loci, each of which produces only a single protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chandy, K G -- Williams, C B -- Spencer, R H -- Aguilar, B A -- Ghanshani, S -- Tempel, B L -- Gutman, G A -- AI21366/AI/NIAID NIH HHS/ -- AI24783/AI/NIAID NIH HHS/ -- NS27206/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Feb 23;247(4945):973-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, Irvine 92717.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2305265" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; DNA/genetics ; DNA Probes ; Drosophila/genetics ; Exons ; *Introns ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Nucleic Acid Hybridization ; *Potassium Channels ; Restriction Mapping
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  • 81
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    Biophysical and molecular mechanisms of Shaker potassium channel inactivation (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-10-26
    Description: The potassium channels encoded by the Drosophila Shaker gene activate and inactivate rapidly when the membrane potential becomes more positive. Site-directed mutagenesis and single-channel patch-clamp recording were used to explore the molecular transitions that underlie inactivation in Shaker potassium channels expressed in Xenopus oocytes. A region near the amino terminus with an important role in inactivation has now been identified. The results suggest a model where this region forms a cytoplasmic domain that interacts with the open channel to cause inactivation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoshi, T -- Zagotta, W N -- Aldrich, R W -- NS07158/NS/NINDS NIH HHS/ -- NS23294/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Oct 26;250(4980):533-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Physiology, Stanford University, School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2122519" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; DNA/genetics ; Drosophila melanogaster/*genetics ; Electric Conductivity ; Ion Channel Gating/drug effects/*physiology ; Kinetics ; Membrane Potentials/physiology ; Molecular Sequence Data ; Mutagenesis ; Mutagenesis, Site-Directed ; Oocytes/metabolism ; Potassium Channels/genetics/*physiology ; RNA Splicing ; Structure-Activity Relationship ; Trypsin/pharmacology ; Xenopus
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    Germ line p53 mutations in a familial syndrome of breast cancer, sarcomas, and other neoplasms (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-10
    Description: Familial cancer syndromes have helped to define the role of tumor suppressor genes in the development of cancer. The dominantly inherited Li-Fraumeni syndrome (LFS) is of particular interest because of the diversity of childhood and adult tumors that occur in affected individuals. The rarity and high mortality of LFS precluded formal linkage analysis. The alternative approach was to select the most plausible candidate gene. The tumor suppressor gene, p53, was studied because of previous indications that this gene is inactivated in the sporadic (nonfamilial) forms of most cancers that are associated with LFS. Germ line p53 mutations have been detected in all five LFS families analyzed. These mutations do not produce amounts of mutant p53 protein expected to exert a trans-dominant loss of function effect on wild-type p53 protein. The frequency of germ line p53 mutations can now be examined in additional families with LFS, and in other cancer patients and families with clinical features that might be attributed to the mutation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malkin, D -- Li, F P -- Strong, L C -- Fraumeni, J F Jr -- Nelson, C E -- Kim, D H -- Kassel, J -- Gryka, M A -- Bischoff, F Z -- Tainsky, M A -- 34936/PHS HHS/ -- 5-T32-CA09299/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Nov 30;250(4985):1233-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Genetics, Massachusetts General Hospital Cancer Center, Charlestown 02129.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1978757" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Breast Neoplasms/*genetics ; Chromosomes, Human, Pair 17 ; Cloning, Molecular ; Codon ; DNA/genetics ; Deoxyribonucleases, Type II Site-Specific ; *Genes, p53 ; Genetic Testing ; Germ Cells ; Humans ; Molecular Sequence Data ; *Mutation ; Neoplastic Syndromes, Hereditary/*genetics ; Pedigree ; Polymerase Chain Reaction ; Polymorphism, Restriction Fragment Length ; Repetitive Sequences, Nucleic Acid ; Sarcoma/*genetics ; Tumor Suppressor Protein p53/genetics
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    Chromosomal region of the cystic fibrosis gene in yeast artificial chromosomes: a model for human genome mapping (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-10-05
    Description: A general strategy for cloning and mapping large regions of human DNA with yeast artificial chromosomes (YAC's) is described. It relies on the use of the polymerase chain reaction to detect DNA landmarks called sequence-tagged sites (STS's) within YAC clones. The method was applied to the region of human chromosome 7 containing the cystic fibrosis (CF) gene. Thirty YAC clones from this region were analyzed, and a contig map that spans more than 1,500,000 base pairs was assembled. Individual YAC's as large as 790 kilobase pairs and containing the entire CF gene were constructed in vivo by meiotic recombination in yeast between pairs of overlapping YAC's.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Green, E D -- Olson, M V -- GM40606/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Oct 5;250(4977):94-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218515" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Mapping ; *Chromosomes, Fungal ; *Chromosomes, Human, Pair 7 ; Cloning, Molecular/*methods ; Cystic Fibrosis/*genetics ; DNA/genetics ; *Genome, Human ; Humans ; Models, Genetic ; Molecular Sequence Data ; Oligonucleotide Probes ; Polymerase Chain Reaction/methods ; Recombination, Genetic ; Saccharomyces cerevisiae/*genetics
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  • 84
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    Functional domains and upstream activation properties of cloned human TATA binding protein (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-29
    Description: The TATA binding protein, TFIID, plays a central role in the initiation of eukaryotic mRNA synthesis. Here, we present a human cDNA clone for this factor. Comparison of its predicted protein sequence with those from Drosophila and yeast reveals a highly conserved carboxyl-terminal 180 amino acids. By contrast, the amino-terminal region of TFIID has diverged in both sequence and length. A striking feature of the human protein is a stretch of 38 glutamine residues in the NH2-terminal region. Expression of human TFIID in both Escherichia coli and HeLa cells produces a protein that binds specifically to a TATA box and promotes basal transcription; the conserved COOH-terminal portion of the protein is sufficient for both of these activities. Recombinant TFIID forms a stable complex on a TATA box either alone or in combination with either of the general transcription factors, TFIIA or TFIIB. Full-length recombinant TFIID is able to support Sp1 activated transcription in a TFIID-depleted nuclear extract, while a deletion of the NH2-terminal half of the protein is not. These results indicate the importance of the NH2-terminal region for upstream activation functions and suggest that additional factors (co-activators) are required for mediating interactions with specific regulators.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peterson, M G -- Tanese, N -- Pugh, B F -- Tjian, R -- New York, N.Y. -- Science. 1990 Jun 29;248(4963):1625-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2363050" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Nucleus/metabolism ; Cloning, Molecular/methods ; DNA/genetics ; DNA, Neoplasm/genetics ; *Gene Expression Regulation ; Glutamine ; HeLa Cells/metabolism ; Humans ; Molecular Sequence Data ; Oligonucleotide Probes ; *Promoter Regions, Genetic ; RNA, Messenger/genetics ; Recombinant Proteins/isolation & purification/metabolism ; Transcription Factor TFIID ; Transcription Factors/*genetics/isolation & purification/metabolism ; *Transcription, Genetic
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  • 85
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    Direct gene transfer into mouse muscle in vivo (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-03-23
    Description: RNA and DNA expression vectors containing genes for chloramphenicol acetyltransferase, luciferase, and beta-galactosidase were separately injected into mouse skeletal muscle in vivo. Protein expression was readily detected in all cases, and no special delivery system was required for these effects. The extent of expression from both the RNA and DNA constructs was comparable to that obtained from fibroblasts transfected in vitro under optimal conditions. In situ cytochemical staining for beta-galactosidase activity was localized to muscle cells following injection of the beta-galactosidase DNA vector. After injection of the DNA luciferase expression vector, luciferase activity was present in the muscle for at least 2 months.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolff, J A -- Malone, R W -- Williams, P -- Chong, W -- Acsadi, G -- Jani, A -- Felgner, P L -- HD00669-05/HD/NICHD NIH HHS/ -- HD03352/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1990 Mar 23;247(4949 Pt 1):1465-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Waisman Center, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1690918" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avian Sarcoma Viruses/genetics ; Beetles/genetics ; Chloramphenicol O-Acetyltransferase/biosynthesis/genetics ; DNA/genetics ; Escherichia coli/genetics ; *Gene Expression ; Genetic Vectors ; Histocytochemistry ; Luciferases/biosynthesis/genetics ; Mice ; Muscles/*enzymology ; RNA/genetics ; *Transfection ; beta-Galactosidase/biosynthesis/genetics
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  • 86
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    Norwalk virus genome cloning and characterization (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-14
    Description: Major epidemic outbreaks of acute gastroenteritis result from infections with Norwalk or Norwalk-like viruses. Virus purified from stool specimens of volunteers experimentally infected with Norwalk virus was used to construct recombinant complementary DNA (cDNA) and derive clones representing most of the viral genome. The specificity of the clones was shown by their hybridization with post- (but not pre-) infection stool samples from volunteers infected with Norwalk virus and with purified Norwalk virus. A correlation was observed between the appearance of hybridization signals in stool samples and clinical symptoms of acute gastroenteritis in volunteers. Hybridization assays between overlapping clones, restriction enzyme analyses, and partial nucleotide sequence information of the clones indicated that Norwalk virus contains a single-stranded RNA genome of positive sense, with a polyadenylated tail at the 3' end and a size of at least 7.5 kilobases. A consensus amino acid sequence motif typical of viral RNA-dependent RNA polymerases was identified in one of the Norwalk virus clones. The availability of Norwalk-specific cDNA and the new sequence information of the viral genome should permit the development of sensitive diagnostic assays and studies of the molecular biology of the virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xi, J N -- Graham, D Y -- Wang, K N -- Estes, M K -- 223-88-2182/PHS HHS/ -- RR 00350/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 14;250(4987):1580-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2177224" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Cloning, Molecular ; DNA/genetics ; DNA Restriction Enzymes ; Feces/microbiology ; Gastroenteritis/microbiology ; Gene Amplification ; *Genes, Viral ; Humans ; Microscopy, Electron ; Molecular Sequence Data ; Norwalk virus/*genetics/ultrastructure ; Nucleic Acid Hybridization ; Plasmids ; RNA Probes ; RNA Replicase/genetics ; RNA, Viral/genetics ; Virion/genetics
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  • 87
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    Mini-mouse: disruption of the pygmy locus in a transgenic insertional mutant (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-02-23
    Description: A founder transgenic mouse harbored two different integration patterns of a transgene at the same locus, each of which gave rise to a similar autosomal recessive mutation. Mice of the mutant phenotype were of small stature but had normal levels of growth hormone. The disrupted locus was cloned, and a genetic and molecular analysis showed that the insertional mutants were allelic to a spontaneous mutant, pygmy. The mice should be a useful model for the growth hormone-resistant human dwarf syndromes and could lead to a greater understanding of the pathways involved in growth and development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xiang, X -- Benson, K F -- Chada, K -- GM38731/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Feb 23;247(4945):967-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway 08854.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2305264" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/genetics ; Disease Models, Animal ; Dwarfism/*genetics ; Female ; Growth Hormone/blood ; Male ; Mice ; Mice, Mutant Strains ; Mice, Transgenic ; Mutation ; Nucleic Acid Hybridization ; Pedigree ; Restriction Mapping
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 88
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    A receptor for tumor necrosis factor defines an unusual family of cellular and viral proteins (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-05-25
    Description: Tumor necrosis factor alpha and beta (TNF-alpha and TNF-beta) bind surface receptors on a variety of cell types to mediate a wide range of immunological responses, inflammatory reactions, and anti-tumor effects. A cDNA clone encoding an integral membrane protein of 461 amino acids was isolated from a human lung fibroblast library by direct expression screening with radiolabeled TNF-alpha. The encoded receptor was also able to bind TNF-beta. The predicted cysteine-rich extracellular domain has extensive sequence similarity with five proteins, including nerve growth factor receptor and a transcriptionally active open reading frame from Shope fibroma virus, and thus defines a family of receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, C A -- Davis, T -- Anderson, D -- Solam, L -- Beckmann, M P -- Jerzy, R -- Dower, S K -- Cosman, D -- Goodwin, R G -- New York, N.Y. -- Science. 1990 May 25;248(4958):1019-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Corporation, Seattle, WA 98101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2160731" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Blotting, Northern ; Cloning, Molecular ; DNA/genetics ; Humans ; Membrane Proteins/genetics ; Molecular Sequence Data ; Multigene Family ; Receptors, Cell Surface/*genetics ; Receptors, Tumor Necrosis Factor ; Tumor Necrosis Factor-alpha/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 89
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    A 49-kilodalton phosphoprotein in the Drosophila photoreceptor is an arrestin homolog (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-04-27
    Description: The gene encoding the 49-kilodalton protein that undergoes light-induced phosphorylation in the Drosophila photoreceptor has been isolated and characterized. The encoded protein has 401 amino acid residues and a molecular mass of 44,972 daltons, and it shares approximately 42 percent amino acid sequence identity with arrestin (S-antigen), which has been proposed to quench the light-induced cascade of guanosine 3',5'-monophosphate hydrolysis in vertebrate photoreceptors. Unlike the 49-kilodalton protein, however, arrestin, which appears to bind to phosphorylated rhodopsin, has not itself been reported to undergo phosphorylation. In vitro, Ca2+ was the only agent found that would stimulate the phosphorylation of the 49-kilodalton protein. The phosphorylation of this arrestin-like protein in vivo may therefore be triggered by a Ca2+ signal that is likely to be regulated by light-activated phosphoinositide-specific phospholipase C.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamada, T -- Takeuchi, Y -- Komori, N -- Kobayashi, H -- Sakai, Y -- Hotta, Y -- Matsumoto, H -- EY06595/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1990 Apr 27;248(4954):483-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City 73190.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2158671" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antigens ; Arrestin ; Binding Sites ; Calcium/pharmacology ; Cloning, Molecular ; Cyclic GMP/metabolism ; DNA/genetics ; Drosophila melanogaster/*genetics ; Enzyme Activation/drug effects ; *Eye Proteins ; Isoelectric Point ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Phosphatidylinositol Diacylglycerol-Lyase ; *Phosphoproteins/genetics/metabolism ; Phosphoric Diester Hydrolases/metabolism ; Phosphorylation ; Photoreceptor Cells/*analysis ; Protein Biosynthesis ; Restriction Mapping ; Sequence Homology, Nucleic Acid
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  • 90
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    Telomeres and their synthesis (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blackburn, E H -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):489-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2200120" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosomes/*physiology ; DNA/genetics ; *DNA Replication ; Humans ; Molecular Sequence Data ; Repetitive Sequences, Nucleic Acid
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 91
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    Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-28
    Description: In the central nervous system (CNS), the principal mediators of fast synaptic excitatory neurotransmission are L-glutamate-gated ion channels that are responsive to the glutamate agonist alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA). In each member of a family of four abundant AMPA receptors, a small segment preceding the predicted fourth transmembrane region has been shown to exist in two versions with different amino acid sequences. These modules, designated "flip" and "flop," are encoded by adjacent exons of the receptor genes and impart different pharmacological and kinetic properties on currents evoked by L-glutamate or AMPA, but not those evoked by kainate. For each receptor, the alternatively spliced messenger RNAs show distinct expression patterns in rat brain, particularly in the CA1 and CA3 fields of the hippocampus. These results identify a switch in the molecular and functional properties of glutamate receptors operated by alternative splicing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sommer, B -- Keinanen, K -- Verdoorn, T A -- Wisden, W -- Burnashev, N -- Herb, A -- Kohler, M -- Takagi, T -- Sakmann, B -- Seeburg, P H -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1580-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neuroendocrinology, Center for Molecular Biology, University of Heidelberg, F.R.G.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1699275" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/*metabolism ; DNA/genetics ; Exons ; Genomic Library ; Glutamates/*metabolism/pharmacology ; Ibotenic Acid/*analogs & derivatives/metabolism/pharmacology ; Ion Channels/*physiology ; Kinetics ; Molecular Sequence Data ; Oligonucleotide Probes ; Organ Specificity ; *RNA Splicing ; RNA, Messenger/*genetics ; Rats ; Receptors, AMPA ; Receptors, Glutamate ; Receptors, Neurotransmitter/drug effects/*genetics/physiology ; Recombinant Proteins/metabolism ; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid
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  • 92
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    Molecule of the year. Diamond: glittering prize for materials science (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guyer, R L -- Koshland, D E Jr -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1640-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2176743" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Carbon ; Cattle ; DNA/genetics ; Diamond ; Genetic Therapy ; Growth Hormone/genetics/pharmacology ; Humans ; Neurofibromatosis 1/genetics ; Recombinant Proteins/pharmacology ; *Technology
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  • 93
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    Random peptide libraries: a source of specific protein binding molecules (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-07-27
    Description: Libraries of random peptide sequences were constructed and screened to identify peptides that specifically bind to proteins. In one of these about 2 X 10(7) different 15-residue peptide sequences were expressed on the surface of the coliphage M13. Each phage encoded a single random sequence and expressed it as a fusion complex with pIII, a minor coat protein present at five molecules per phage. Phage encoding nine different streptavidin-binding peptide sequences were isolated from this library. The core consensus sequence was His-Pro-Gln and binding of these phage to streptavidin was inhibited by biotin. This type of library makes it possible to identify peptides that bind to proteins (or other macromolecules) that have no previously known affinity for peptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Devlin, J J -- Panganiban, L C -- Devlin, P E -- New York, N.Y. -- Science. 1990 Jul 27;249(4967):404-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Cetus Corporation, Emeryville, CA 94608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2143033" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; Amino Acid Sequence ; Bacterial Proteins/metabolism ; Bacteriophage lambda/genetics/metabolism ; Bacteriophages/genetics/isolation & purification/metabolism ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Escherichia coli/genetics ; Gene Expression ; Genetic Vectors ; Molecular Sequence Data ; Peptides/genetics/*metabolism ; Polymerase Chain Reaction ; Protein Binding ; *Proteins/*metabolism ; Recombinant Fusion Proteins ; Streptavidin ; Transfection
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  • 94
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    EGF receptor and erbB-2 tyrosine kinase domains confer cell specificity for mitogenic signaling (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-04-06
    Description: The epidermal growth factor (EGF) receptor (EGFR) can efficiently couple with mitogenic signaling pathways when it is transfected into interleukin-3 (IL-3)-dependent 32D hematopoietic cells. When expression vectors for erbB-2, which is structurally related to EGFR, or its truncated counterpart, delta NerbB-2, were introduced into 32D cells, neither was capable of inducing proliferation. This was despite overexpression and constitutive tyrosine kinase activity of their products at levels associated with potent transformation of fibroblast target cells. Thus, EGFR and erbB-2 couple with distinct mitogenic signaling pathways. The region responsible for the specificity of intracellular signal transduction was localized to a 270-amino acid stretch encompassing their respective tyrosine kinase domains. Thus, tissue- or cell-specific regulation of growth factor receptor signaling can occur at a point after the initial interaction of growth factor with receptor. Such specificity in signal transduction may account for the selection of certain oncogenes in some malignancies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Di Fiore, P P -- Segatto, O -- Taylor, W G -- Aaronson, S A -- Pierce, J H -- New York, N.Y. -- Science. 1990 Apr 6;248(4951):79-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2181668" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Division ; Cell Line ; DNA/genetics ; DNA, Recombinant ; Fibroblasts/cytology/metabolism ; Gene Expression ; Genetic Vectors ; Hematopoietic Stem Cells/cytology/metabolism ; Immunoblotting ; Mice ; *Mitogens ; Molecular Sequence Data ; Protein-Tyrosine Kinases/genetics/*physiology ; Proto-Oncogene Proteins/genetics/*physiology ; Receptor, Epidermal Growth Factor/genetics/*physiology ; Sequence Homology, Nucleic Acid ; Signal Transduction ; Transfection
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  • 95
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    Isolation of a cDNA from the virus responsible for enterically transmitted non-A, non-B hepatitis (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-03-16
    Description: Major epidemic outbreaks of viral hepatitis in underdeveloped countries result from a type of non-A, non-B hepatitis distinct from the parenterally transmitted form. The viral agent responsible for this form of epidemic, or enterically transmitted non-A, non-B hepatitis (ET-NANBH), has been serially transmitted in cynomolgus macaques (cynos) and has resulted in typical elevation in liver enzymes and the detection of characteristic virus-like particles (VLPs) in both feces and bile. Infectious bile was used for the construction of recombinant complementary DNA libraries. One clone, ET1.1, was exogenous to uninfected human and cyno genomic liver DNA, as well as to genomic DNA from infected cyno liver. ET1.1 did however, hybridize to an approximately 7.6-kilobase RNA species present only in infected cyno liver. The translated nucleic acid sequence of a portion of ET1.1 had a consensus amino acid motif consistent with an RNA-directed RNA polymerase; this enzyme is present in all positive strand RNA viruses. Furthermore, ET1.1 specifically identified similar sequences in complementary DNA prepared from infected human fecal samples collected from five geographically distinct ET-NANBH outbreaks. Therefore, ET1.1 represents a portion of the genome of the principal viral agent, to be named hepatitis E virus, which is responsible for epidemic outbreaks of ET-NANBH.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reyes, G R -- Purdy, M A -- Kim, J P -- Luk, K C -- Young, L M -- Fry, K E -- Bradley, D W -- New York, N.Y. -- Science. 1990 Mar 16;247(4948):1335-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Virology Department, Genelabs Incorporated, Redwood City, CA 94063.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2107574" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Hepatitis E/*microbiology ; Hepatitis Viruses/*genetics ; Hepatitis, Viral, Human/*microbiology ; Humans ; Macaca fascicularis ; Molecular Sequence Data ; Polymerase Chain Reaction ; RNA Viruses/genetics ; RNA, Viral/genetics ; Restriction Mapping
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  • 96
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    Molecular cloning and functional expression of the cardiac sarcolemmal Na(+)-Ca2+ exchanger (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-10-26
    Description: The Na(+)-Ca2+ exchanger of the cardiac sarcolemma can rapidly transport Ca2+ during excitation-contraction coupling. To begin molecular studies of this transporter, polyclonal antibodies were used to identify a complementary DNA (cDNA) clone encoding the Na(+)-Ca2+ exchanger protein. The cDNA hybridizes with a 7-kilobase RNA on a Northern blot and has an open reading frame of 970 amino acids. Hydropathy analysis suggests that the protein has multiple transmembrane helices, and a small region of the sequence is similar to that of the Na(+)- and K(+)-dependent adenosine triphosphatase. Polyclonal antibodies to a synthetic peptide from the deduced amino acid sequence react with sarcolemmal proteins of 70, 120, and 160 kilodaltons on immunoblots. RNA, synthesized from the cDNA clone, induces expression of Na(+)-Ca2+ exchange activity when injected into Xenopus oocytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nicoll, D A -- Longoni, S -- Philipson, K D -- AHL07386/AH/BHP HRSA HHS/ -- HL27821/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Oct 26;250(4980):562-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, UCLA School of Medicine 90024-1760.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1700476" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/pharmacology ; Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/*genetics ; Chemistry, Physical ; *Cloning, Molecular ; DNA/genetics ; DNA Probes ; Dogs ; *Gene Expression ; Glycosylation ; Immunoblotting ; Molecular Sequence Data ; Molecular Weight ; Myocardium/*chemistry ; Nucleic Acid Hybridization ; Physicochemical Phenomena ; RNA/genetics ; RNA, Complementary ; Sarcolemma/*chemistry ; Sodium-Calcium Exchanger
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    Tumor cells exhibit deregulation of the cell cycle histone gene promoter factor HiNF-D (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-03-23
    Description: Cell cycle-regulated gene expression is essential for normal cell growth and development and loss of stringent growth control is associated with the acquisition of the transformed phenotype. The selective synthesis of histone proteins during the S phase of the cell cycle is required to render cells competent for the ordered packaging of replicating DNA into chromatin. Regulation of H4 histone gene transcription requires the proliferation-specific promoter binding factor HiNF-D. In normal diploid cells, HiNF-D binding activity is regulated during the cell cycle; nuclear protein extracts prepared from normal cells in S phase contain distinct and measurable HiNF-D binding activity, while this activity is barely detectable in G1 phase cells. In contrast, in tumor-derived or transformed cell lines, HiNF-D binding activity is constitutively elevated throughout the cell cycle and declines only with the onset of differentiation. The change from cell cycle-mediated to constitutive interaction of HiNF-D with the promoter of a cell growth-controlled gene is consistent with, and may be functionally related to, the loss of stringent cell growth regulation associated with neoplastic transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holthuis, J -- Owen, T A -- van Wijnen, A J -- Wright, K L -- Ramsey-Ewing, A -- Kennedy, M B -- Carter, R -- Cosenza, S C -- Soprano, K J -- Lian, J B -- New York, N.Y. -- Science. 1990 Mar 23;247(4949 Pt 1):1454-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, University of Massachusetts Medical School, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2321007" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Cycle/*genetics ; Cell Line, Transformed ; Cells, Cultured ; DNA/genetics ; DNA-Binding Proteins/*metabolism ; Gene Expression Regulation, Neoplastic ; Histones/*genetics ; Humans ; Molecular Sequence Data ; Nuclear Proteins/*metabolism ; *Promoter Regions, Genetic ; RNA, Messenger/analysis ; Rats ; Sequence Homology, Nucleic Acid ; Transcription, Genetic ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 98
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    Spontaneous neurodegeneration in transgenic mice with mutant prion protein (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-14
    Description: Transgenic mice were created to assess genetic linkage between Gerstmann-Straussler-Scheinker syndrome and a leucine substitution at codon 102 of the human prion protein gene. Spontaneous neurologic disease with spongiform degeneration and gliosis similar to that in mouse scrapie developed at a mean age of 166 days in 35 mice expressing mouse prion protein with the leucine substitution. Thus, many of the clinical and pathological features of Gerstmann-Straussler-Scheinker syndrome are reproduced in transgenic mice containing a prion protein with a single amino acid substitution, illustrating that a neurodegenerative process similar to a human disease can be genetically modeled in animals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hsiao, K K -- Scott, M -- Foster, D -- Groth, D F -- DeArmond, S J -- Prusiner, S B -- AG02132/AG/NIA NIH HHS/ -- NS14069/NS/NINDS NIH HHS/ -- NS22786/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Dec 14;250(4987):1587-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1980379" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/pathology ; Brain Diseases/*genetics/microbiology/pathology ; Codon ; DNA/genetics ; Disease Models, Animal ; Endopeptidase K ; Gerstmann-Straussler-Scheinker Disease/*genetics/microbiology/pathology ; Leucine ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; *Mutation ; Nucleic Acid Hybridization ; Pedigree ; PrPSc Proteins ; Prions/*genetics ; Serine Endopeptidases/metabolism ; Transfection ; Vacuoles/pathology ; Viral Proteins/*genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 99
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    Expression of gene rrg is associated with reversion of NIH 3T3 transformed by LTR-c-H-ras (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-17
    Description: A partial complementary DNA was isolated for a gene (rrg) that is normally expressed in mouse NIH 3T3 cells, but is down-regulated after cellular transformation by long terminal repeat (LTR)-activated c-H-ras (LTR-c-H-ras). This gene was reexpressed in a nontumorigenic persistent revertant cell line created by prolonged treatment of the transformed cells with mouse interferon alpha/beta. Persistent revertants stably transfected with rrg complementary DNA antisense expression vectors appeared transformed, had decreased amounts of rrg messenger RNA, and were tumorigenic in nude mice. Stable transfection with sense constructs did not alter the normal morphology, message level, or nontumorigenicity of the persistent revertant cell line.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Contente, S -- Kenyon, K -- Rimoldi, D -- Friedman, R M -- R01 CA 37351-04A1/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 17;249(4970):796-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814-4799.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1697103" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line, Transformed ; Cloning, Molecular ; DNA/genetics ; *Gene Expression ; *Genes, ras ; Humans ; Interferon Type I/pharmacology ; Mice ; Mice, Nude ; Neoplasms, Experimental/etiology ; Nucleic Acid Hybridization ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins p21(ras) ; RNA/analysis/genetics ; RNA, Antisense ; RNA, Messenger/genetics ; Rats ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 100
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    Neurotrophin-3: a neurotrophic factor related to NGF and BDNF (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-03-23
    Description: The development and maintenance of the nervous system depends on proteins known as neurotrophic factors. Although the prototypical neurotrophic factor, nerve growth factor (NGF), has been intensively studied for decades, the discovery and characterization of additional such factors has been impeded by their low abundance. Sequence homologies between NGF and the recently cloned brain-derived neurotrophic factor (BDNF) were used to design a strategy that has now resulted in the cloning of a gene encoding a novel neurotrophic factor, termed neurotrophin-3 (NT-3). The distribution of NT-3 messenger RNA and its biological activity on a variety of neuronal populations clearly distinguish NT-3 from NGF and BDNF, and provide compelling evidence that NT-3 is an authentic neurotrophic factor that has its own characteristic role in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maisonpierre, P C -- Belluscio, L -- Squinto, S -- Ip, N Y -- Furth, M E -- Lindsay, R M -- Yancopoulos, G D -- New York, N.Y. -- Science. 1990 Mar 23;247(4949 Pt 1):1446-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Inc., Tarrytown, New York 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2321006" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain-Derived Neurotrophic Factor ; Cells, Cultured ; Cloning, Molecular ; DNA/genetics ; Mice ; Molecular Sequence Data ; Nerve Growth Factors/biosynthesis/*genetics/physiology ; Nerve Tissue Proteins/biosynthesis/*genetics/physiology ; Neurons/physiology ; Polymerase Chain Reaction ; Rats ; Restriction Mapping ; Sequence Homology, Nucleic Acid
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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