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  • Base Sequence  (157)
  • American Association for the Advancement of Science (AAAS)  (157)
  • American Association of Petroleum Geologists (AAPG)
  • 1995-1999  (157)
  • 1995  (157)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (157)
  • American Association of Petroleum Geologists (AAPG)
Years
  • 1995-1999  (157)
Year
  • 1
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    Constitutively activated Jak-STAT pathway in T cells transformed with HTLV-I (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-07
    Description: Human T cell lymphotropic virus I (HTLV-I) is the etiological agent for adult T cell leukemia and tropical spastic paraparesis (also termed HTLV-I-associated myelopathy). HTLV-I-infected peripheral blood T cells exhibit an initial phase of interleukin-2 (IL-2)-dependent growth; over time, by an unknown mechanism, the cells become IL-2-independent. Whereas the Jak kinases Jak1 and Jak3 and the signal transducer and activator of transcription proteins Stat3 and Stat5 are activated in normal T cells in response to IL-2, this signaling pathway was constitutively activated in HTLV-I-transformed cells. In HTLV-I-infected cord blood lymphocytes, the transition from IL-2-dependent to IL-2-independent growth correlated with the acquisition of a constitutively activated Jak-STAT pathway, which suggests that this pathway participates in HTLV-I-mediated T cell transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Migone, T S -- Lin, J X -- Cereseto, A -- Mulloy, J C -- O'Shea, J J -- Franchini, G -- Leonard, W J -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):79-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Immunology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604283" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Line, Transformed ; *Cell Transformation, Viral ; Cells, Cultured ; DNA-Binding Proteins/*metabolism ; Enzyme Activation ; Fetal Blood/cytology ; Human T-lymphotropic virus 1/*physiology ; Humans ; Interleukin-2/pharmacology ; Janus Kinase 1 ; Janus Kinase 3 ; *Milk Proteins ; Molecular Sequence Data ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Receptors, Interleukin-2/metabolism ; STAT3 Transcription Factor ; STAT5 Transcription Factor ; Signal Transduction ; T-Lymphocytes/metabolism/*virology ; Trans-Activators/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Requirement of FGF-4 for postimplantation mouse development (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-13
    Description: Fibroblast growth factors (FGFs) are thought to influence many processes in vertebrate development because of their diverse sites of expression and wide range of biological activities in in vitro culture systems. As a means of elucidating embryonic functions of FGF-4, gene targeting was used to generate mice harboring a disrupted Fgf4 gene. Embryos homozygous for the null allele underwent uterine implantation and induced uterine decidualization but did not develop substantially thereafter. As was consistent with their behavior in vivo, Fgf4 null embryos cultured in vitro displayed severely impaired proliferation of the inner cell mass, whereas growth and differentiation of the inner cell mass were rescued when null embryos were cultured in the presence of FGF-4 protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feldman, B -- Poueymirou, W -- Papaioannou, V E -- DeChiara, T M -- Goldfarb, M -- HD21988/HD/NICHD NIH HHS/ -- HD27198/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 13;267(5195):246-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Integrated Program in Cellular, Molecular, and Biophysical Studies, Columbia University College of Physicians and Surgeons, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809630" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blastocyst/cytology/physiology ; Crosses, Genetic ; Culture Techniques ; Embryonic Development/*physiology ; Embryonic and Fetal Development/*physiology ; Female ; Fibroblast Growth Factor 4 ; Fibroblast Growth Factors/genetics/pharmacology/*physiology ; Gene Targeting ; Heterozygote ; Male ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Morula/drug effects/physiology ; Phenotype ; Pregnancy ; Proto-Oncogene Proteins/genetics/pharmacology/*physiology ; Recombinant Proteins/pharmacology
    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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  • 3
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    Mutations in Fas associated with human lymphoproliferative syndrome and autoimmunity (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-02
    Description: Fas (also known as Apo1 and CD95) is a cell surface receptor involved in apoptotic cell death. Fas expression and function were analyzed in three children (including two siblings) with a lymphoproliferative syndrome, two of whom also had autoimmune disorders. A large deletion in the gene encoding Fas and no detectable cell surface expression characterized the most affected patient. Clinical manifestations in the two related patients were less severe: Fas-mediated apoptosis was impaired and a deletion within the intracytoplasmic domain was detected. These findings illustrate the crucial regulatory role of Fas and may provide a molecular basis for some autoimmune diseases in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rieux-Laucat, F -- Le Deist, F -- Hivroz, C -- Roberts, I A -- Debatin, K M -- Fischer, A -- de Villartay, J P -- New York, N.Y. -- Science. 1995 Jun 2;268(5215):1347-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut National de la Sante et de la Recherche Medicale (INSERM) U 429, Hopital Necker-Enfants Malades, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7539157" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, CD95 ; Antigens, Surface/chemistry/*genetics/physiology ; Apoptosis ; Autoimmune Diseases/*genetics/immunology/pathology ; Base Sequence ; Child ; Female ; *Frameshift Mutation ; Humans ; Infant ; Lymphoproliferative Disorders/*genetics/immunology/pathology ; Male ; Molecular Sequence Data ; Sequence Deletion ; Syndrome ; Thrombocytopenia/genetics/immunology/pathology
    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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  • 4
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    Aggressive behavior and altered amounts of brain serotonin and norepinephrine in mice lacking MAOA (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-23
    Description: Deficiency in monoamine oxidase A (MAOA), an enzyme that degrades serotonin and norepinephrine, has recently been shown to be associated with aggressive behavior in men of a Dutch family. A line of transgenic mice was isolated in which transgene integration caused a deletion in the gene encoding MAOA, providing an animal model of MAOA deficiency. In pup brains, serotonin concentrations were increased up to ninefold, and serotonin-like immunoreactivity was present in catecholaminergic neurons. In pup and adult brains, norepinephrine concentrations were increased up to twofold, and cytoarchitectural changes were observed in the somatosensory cortex. Pup behavioral alterations, including trembling, difficulty in righting, and fearfulness were reversed by the serotonin synthesis inhibitor parachlorophenylalanine. Adults manifested a distinct behavioral syndrome, including enhanced aggression in males.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844866/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844866/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cases, O -- Seif, I -- Grimsby, J -- Gaspar, P -- Chen, K -- Pournin, S -- Muller, U -- Aguet, M -- Babinet, C -- Shih, J C -- K05 MH 00796/MH/NIMH NIH HHS/ -- R01 MH 37020/MH/NIMH NIH HHS/ -- R37 MH 39085/MH/NIMH NIH HHS/ -- R37 MH039085/MH/NIMH NIH HHS/ -- R37 MH039085-23/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1995 Jun 23;268(5218):1763-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre National de la Recherche Scientifique (CNRS), Unite de Recherche Associee (URA), Institut Curie, Orsay, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7792602" target="_blank"〉PubMed〈/a〉
    Keywords: Aggression/*physiology ; Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Southern ; Brain/*metabolism ; Disease Models, Animal ; Dopamine/metabolism ; Female ; Interferon-beta/genetics ; Male ; Mice ; Mice, Inbred C3H ; Mice, Transgenic ; Molecular Sequence Data ; Monoamine Oxidase/*deficiency ; Norepinephrine/*metabolism ; Sequence Deletion ; Serotonin/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Telomeres: beginning to understand the end (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-08
    Description: Telomeres are the protein-DNA structures at the ends of eukaryotic chromosomes. In yeast, and probably most other eukaryotes, telomeres are essential. They allow the cell to distinguish intact from broken chromosomes, protect chromosomes from degradation, and are substrates for novel replication mechanisms. Telomeres are usually replicated by telomerase, a telomere-specific reverse transcriptase, although telomerase-independent mechanisms of telomere maintenance exist. Telomere replication is both cell cycle- and developmentally regulated, and its control is likely to be complex. Because telomere loss causes the kinds of chromosomal changes associated with cancer and aging, an understanding of telomere biology has medical relevance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zakian, V A -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1601-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502069" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Cycle ; Chromosomes/metabolism/physiology ; DNA/analysis/chemistry/metabolism ; DNA Replication ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation ; Humans ; Molecular Sequence Data ; Telomerase/metabolism ; Telomere/chemistry/*physiology
    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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  • 6
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    The RNA component of human telomerase (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-01
    Description: Eukaryotic chromosomes are capped with repetitive telomere sequences that protect the ends from damage and rearrangements. Telomere repeats are synthesized by telomerase, a ribonucleic acid (RNA)-protein complex. Here, the cloning of the RNA component of human telomerase, termed hTR, is described. The template region of hTR encompasses 11 nucleotides (5'-CUAACCCUAAC) complementary to the human telomere sequence (TTAGGG)n. Germline tissues and tumor cell lines expressed more hTR than normal somatic cells and tissues, which have no detectable telomerase activity. Human cell lines that expressed hTR mutated in the template region generated the predicted mutant telomerase activity. HeLa cells transfected with an antisense hTR lost telomeric DNA and began to die after 23 to 26 doublings. Thus, human telomerase is a critical enzyme for the long-term proliferation of immortal tumor cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, J -- Funk, W D -- Wang, S S -- Weinrich, S L -- Avilion, A A -- Chiu, C P -- Adams, R R -- Chang, E -- Allsopp, R C -- Yu, J -- AG09383/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 1;269(5228):1236-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geron Corporation, Menlo Park, CA 94025, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7544491" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Death ; *Cell Division ; Cell Line ; Cloning, Molecular ; DNA Nucleotidylexotransferase/antagonists & ; inhibitors/chemistry/genetics/*metabolism ; HeLa Cells ; Humans ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacology ; Polymerase Chain Reaction ; RNA/chemistry/genetics/*metabolism ; Templates, Genetic ; Transfection ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
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  • 7
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    Participation of the human beta-globin locus control region in initiation of DNA replication (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-03
    Description: The human beta-globin locus control region (LCR) controls the transcription, chromatin structure, and replication timing of the entire locus. DNA replication was found to initiate in a transcription-independent manner within a region located 50 kilobases downstream of the LCR in human, mouse, and chicken cells containing the entire human beta-globin locus. However, DNA replication did not initiate within a deletion mutant locus lacking the sequences that encompass the LCR. This mutant locus replicated in the 3' to 5' direction. Thus, interactions between distantly separated sequences can be required for replication initiation, and factors mediating this interaction appear to be conserved in evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aladjem, M I -- Groudine, M -- Brody, L L -- Dieken, E S -- Fournier, R E -- Wahl, G M -- Epner, E M -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):815-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Expression Laboratory, Salk Institute, San Diego, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481774" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; Cell Line ; Chickens ; *DNA Replication ; Globins/*genetics ; Humans ; Hybrid Cells ; Mice ; Molecular Sequence Data ; *Regulatory Sequences, Nucleic Acid ; Sequence Deletion ; Tumor Cells, Cultured
    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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  • 8
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    Genome maps. VI. Caenorhabditis elegans. Wall chart (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chalfie, M -- Eddy, S -- Hengartner, M O -- Hodgkin, J -- Kohara, Y -- Plasterk, R H -- Waterston, R H -- White, J G -- New York, N.Y. -- Science. 1995 Oct 20;270(5235):415-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Columbia University, New York, NY, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569996" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Caenorhabditis elegans/*genetics ; *Chromosome Mapping ; Gene Expression ; *Genes, Helminth ; *Genome ; Molecular Sequence Data
    Print ISSN: 0036-8075
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  • 9
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    Requirement of serine phosphorylation for formation of STAT-promoter complexes (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-31
    Description: Members of the interleukin-6 family of cytokines bind to and activate receptors that contain a common subunit, gp130. This leads to the activation of Stat3 and Stat1, two cytoplasmic signal transducers and activators of transcription (STATs), by tyrosine phosphorylation. Serine phosphorylation of Stat3 was constitutive and was enhanced by signaling through gp130. In cells of lymphoid and neuronal origins, inhibition of serine phosphorylation prevented the formation of complexes of DNA with Stat3-Stat3 but not with Stat3-Stat1 or Stat1-Stat1 dimers. In vitro serine dephosphorylation of Stat3 also inhibited DNA binding of Stat3-Stat3. The requirement of serine phosphorylation for Stat3-Stat3.DNA complex formation was inversely correlated with the affinity of Stat3-Stat3 for the binding site. Thus, serine phosphorylation appears to enhance or to be required for the formation of stable Stat3-Stat3.DNA complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, X -- Blenis, J -- Li, H C -- Schindler, C -- Chen-Kiang, S -- CA46595/CA/NCI NIH HHS/ -- HL 21006/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Mar 31;267(5206):1990-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Brookdale Center for Molecular Biology, Mount Sinai School of Medicine, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701321" target="_blank"〉PubMed〈/a〉
    Keywords: 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cell Nucleus/metabolism ; Ciliary Neurotrophic Factor ; Cytoplasm/metabolism ; DNA/metabolism ; DNA-Binding Proteins/*metabolism ; Humans ; Interleukin-6/metabolism/*pharmacology ; Isoquinolines/pharmacology ; Mice ; Molecular Sequence Data ; Nerve Tissue Proteins/pharmacology ; Phosphorylation ; Piperazines/pharmacology ; *Promoter Regions, Genetic ; STAT1 Transcription Factor ; STAT3 Transcription Factor ; Serine/*metabolism ; Signal Transduction ; Threonine/metabolism ; Trans-Activators/*metabolism ; Tumor Cells, Cultured ; Tyrosine/metabolism
    Print ISSN: 0036-8075
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  • 10
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    Cytostatic gene therapy for vascular proliferative disorders with a constitutively active form of the retinoblastoma gene product (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-27
    Description: Vascular smooth muscle cell (SMC) proliferation in response to injury is an important etiologic factor in vascular proliferative disorders such as atherosclerosis and restenosis after balloon angioplasty. The retinoblastoma gene product (Rb) is present in the unphosphorylated and active form in quiescent primary arterial SMCs, but is rapidly inactivated by phosphorylation in response to growth factor stimulation in vitro. A replication-defective adenovirus encoding a nonphosphorylatable, constitutively active form of Rb was constructed. Infection of cultured primary rat aortic SMCs with this virus inhibited growth factor-stimulated cell proliferation in vitro. Localized arterial infection with the virus at the time of balloon angioplasty significantly reduced SMC proliferation and neointima formation in both the rat carotid and porcine femoral artery models of restenosis. These results demonstrate the role of Rb in regulating vascular SMC proliferation and suggest a gene therapy approach for vascular proliferative disorders associated with arterial injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, M W -- Barr, E -- Seltzer, J -- Jiang, Y Q -- Nabel, G J -- Nabel, E G -- Parmacek, M S -- Leiden, J M -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):518-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824950" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/genetics/physiology ; Angioplasty, Balloon ; Animals ; Base Sequence ; Blood ; Carotid Arteries/virology ; Cell Division ; Disease Models, Animal ; Femoral Artery/virology ; *Genes, Retinoblastoma ; *Genetic Therapy ; Genetic Vectors ; Humans ; Molecular Sequence Data ; Muscle, Smooth, Vascular/*cytology/pathology/virology ; Rats ; Rats, Sprague-Dawley ; Retinoblastoma Protein/*physiology ; Swine ; Vascular Diseases/pathology/*therapy
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  • 11
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    Detecting dinosaur DNA (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zischler, H -- Hoss, M -- Handt, O -- von Haeseler, A -- van der Kuyl, A C -- Goudsmit, J -- New York, N.Y. -- Science. 1995 May 26;268(5214):1192-3; author reply 1194.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7605504" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cytochrome b Group/*genetics ; DNA, Mitochondrial/*genetics ; *Fossils ; Humans ; Molecular Sequence Data ; Phylogeny
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  • 12
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    Ethylene insensitivity conferred by Arabidopsis ERS gene (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-22
    Description: ERS (ethylene response sensor), a gene in the Arabidopsis thaliana ethylene hormone-response pathway, was uncovered by cross-hybridization with the Arabidopsis ETR1 gene. The deduced ERS protein has sequence similarity with the amino-terminal domain and putative histidine protein kinase domain of ETR1, but it does not have a receiver domain as found in ETR1. A missense mutation identical to the dominant etr1-4 mutation was introduced into the ERS gene. The altered ERS gene conferred dominant ethylene insensitivity to wild-type Arabidopsis. Double-mutant analysis indicates that ERS acts upstream of the CTR1 protein kinase gene in the ethylene-response pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hua, J -- Chang, C -- Sun, Q -- Meyerowitz, E M -- New York, N.Y. -- Science. 1995 Sep 22;269(5231):1712-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569898" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/chemistry/drug effects/*genetics/physiology ; Arabidopsis Proteins ; Base Sequence ; Cloning, Molecular ; Ethylenes/*pharmacology ; *Genes, Plant ; Kanamycin Resistance ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phenotype ; Plant Proteins/chemistry/*genetics/physiology ; Plants, Genetically Modified ; *Receptors, Cell Surface
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  • 13
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    Solution structure of a cisplatin-induced DNA interstrand cross-link (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-15
    Description: The widely used antitumor drug cis-diamminedichloroplatinum(II) (cisplatin or cis-DDP) reacts with DNA, cross-linking two purine residues through the N7 atoms, which reside in the major groove in B-form DNA. The solution structure of the short duplex [d(CAT-AGCTATG)]2 cross-linked at the GC:GC site was determined by nuclear magnetic resonance (NMR). The deoxyguanosine-bridging cis-diammineplatinum(II) lies in the minor groove, and the complementary deoxycytidines are extrahelical. The double helix is locally reversed to a left-handed form, and the helix is unwound and bent toward the minor groove. These findings were independently confirmed by results from a phase-sensitive gel electrophoresis bending assay. The NMR structure differs markedly from previously proposed models but accounts for the chemical reactivity, the unwinding, and the bending of cis-DDP interstrand cross-linked DNA and may be important in the formation and repair of these cross-links in chromatin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, H -- Zhu, L -- Reid, B R -- Drobny, G P -- Hopkins, P B -- GM32681/GM/NIGMS NIH HHS/ -- GM45804/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1842-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Washington, Seattle 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525382" target="_blank"〉PubMed〈/a〉
    Keywords: Antineoplastic Agents/*pharmacology ; Base Sequence ; Cisplatin/*pharmacology ; DNA/*chemistry/drug effects ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Solutions
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  • 14
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    Measurement of lactose repressor-mediated loop formation and breakdown in single DNA molecules (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-20
    Description: In gene regulatory systems in which proteins bind to multiple sites on a DNA molecule, the characterization of chemical mechanisms and single-step reaction rates is difficult because many chemical species may exist simultaneously in a molecular ensemble. This problem was circumvented by detecting DNA looping by the lactose repressor protein of Escherichia coli in single DNA molecules. The looping was detected by monitoring the nanometer-scale Brownian motion of microscopic particles linked to the ends of individual DNA molecules. This allowed the determination of the rates of formation and breakdown of a protein-mediated DNA loop in vitro. The measurements reveal that mechanical strain stored in the loop does not substantially accelerate loop breakdown, and the measurements also show that subunit dissociation of tetrameric repressor is not the predominant loop breakdown pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finzi, L -- Gelles, J -- New York, N.Y. -- Science. 1995 Jan 20;267(5196):378-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824935" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Biotin ; DNA/chemistry/*metabolism ; Digoxigenin ; Isopropyl Thiogalactoside/pharmacology ; Kinetics ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Repressor Proteins/*metabolism ; Thermodynamics
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  • 15
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    Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-15
    Description: Ubiquitin is a highly conserved polypeptide found in all eukaryotes. The major function of ubiquitin is to target proteins for complete or partial degradation by a multisubunit protein complex called the proteasome. Here, the Drosophila fat facets gene, which is required for the appropriate determination of particular cells in the fly eye, was shown to encode a ubiquitin-specific protease (Ubp), an enzyme that cleaves ubiquitin from ubiquitin-protein conjugates. The Fat facets protein (FAF) acts as a regulatory Ubp that prevents degradation of its substrate by the proteasome. Flies bearing fat facets gene mutations were used to show that a Ubp is cell type--and substrate-specific and a regulator of cell fate decisions in a multicellular organism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Y -- Baker, R T -- Fischer-Vize, J A -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1828-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Texas, Austin 78712, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525378" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; *Cell Differentiation/genetics ; Cysteine/metabolism ; Drosophila/embryology/enzymology/genetics ; Endopeptidases/genetics/*metabolism ; Escherichia coli ; Eye/embryology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligodeoxyribonucleotides ; Recombinant Fusion Proteins/genetics/metabolism ; Ubiquitins/*metabolism ; beta-Galactosidase/genetics
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  • 16
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    Mutations of keratinocyte transglutaminase in lamellar ichthyosis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-27
    Description: Lamellar ichthyosis is a severe congenital skin disorder characterized by generalized large scales and variable redness. Affected individuals in three families exhibited drastically reduced keratinocyte transglutaminase (TGK) activity. In two of these families, expression of TGK transcripts was diminished or abnormal and no TGK protein was detected. Homozygous or compound heterozygous mutations of the TGK gene were identified in all families. These data suggest that defects in TGK cause lamellar ichthyosis and that intact cross-linkage of cornified cell envelopes is required for epidermal tissue homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huber, M -- Rettler, I -- Bernasconi, K -- Frenk, E -- Lavrijsen, S P -- Ponec, M -- Bon, A -- Lautenschlager, S -- Schorderet, D F -- Hohl, D -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):525-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Dermatology, Centre Hospitalier Universitaire Vandois (CHUV), Hopital de Beaumont, Lausanne, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824952" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Membrane/metabolism ; Cells, Cultured ; Codon ; Female ; Gene Deletion ; Genetic Linkage ; Heterozygote ; Homozygote ; Humans ; Ichthyosis, Lamellar/enzymology/*genetics ; Introns ; Keratinocytes/*enzymology/ultrastructure ; Male ; Membrane Proteins/metabolism ; Molecular Sequence Data ; Mutation ; Pedigree ; Point Mutation ; Protein Precursors/metabolism ; Transglutaminases/*genetics/metabolism
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  • 17
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    The white gene of Ceratitis capitata: a phenotypic marker for germline transformation (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-22
    Description: Reliable germline transformation is required for molecular studies and ultimately for genetic control of economically important insects, such as the Mediterranean fruit fly (medfly) Ceratitis capitata. A prerequisite for the establishment and maintenance of transformant lines is selectable or phenotypically dominant markers. To this end, a complementary DNA clone derived from the medfly white gene was isolated, which showed substantial similarity to white genes in Drosophila melanogaster and other Diptera. It is correlated with a spontaneous mutation causing white eyes in the medfly and can be used to restore partial eye color in transgenic Drosophila carrying a null mutation in the endogenous white gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zwiebel, L J -- Saccone, G -- Zacharopoulou, A -- Besansky, N J -- Favia, G -- Collins, F H -- Louis, C -- Kafatos, F C -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):2005-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533095" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Base Sequence ; Cloning, Molecular ; Diptera/chemistry/*genetics ; *Drosophila Proteins ; Drosophila melanogaster/genetics ; Eye Color/genetics ; Eye Proteins/chemistry/*genetics ; *Genes, Insect ; Genetic Markers ; Insect Hormones/chemistry/genetics ; Molecular Sequence Data ; Mutation ; Phenotype ; Sequence Alignment ; *Transformation, Genetic
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  • 18
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    Minor groove recognition of the conserved G.U pair at the Tetrahymena ribozyme reaction site (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-03
    Description: The guanine-uracil (G.U) base pair that helps to define the 5'-splice site of group I introns is phylogenetically highly conserved. In such a wobble base pair, G makes two hydrogen bonds with U in a geometry shifted from that of a canonical Watson-Crick pair. The contribution made by individual functional groups of the G.U pair in the context of the Tetrahymena ribozyme was examined by replacement of the G.U pair with synthetic base pairs that maintain a wobble configuration, but that systematically alter functional groups in the major and minor grooves of the duplex. The substitutions demonstrate that the exocyclic amine of G, when presented on the minor groove surface by the wobble base pair conformation, contributes substantially (2 kilocalories.mole-1) to binding by making a tertiary interaction with the ribozyme active site. It contributes additionally to transition state stabilization. The ribozyme active site also makes tertiary contacts with a tripod of 2'-hydroxyls on the minor groove surface of the splice site helix. This suggests that the ribozyme binds the duplex primarily in the minor groove. The alanyl aminoacyl transfer RNA (tRNA) synthetase recognizes the exocyclic amine of an invariant G.U pair and contacts a similar array of 2'-hydroxyls when binding the tRNA(Ala) acceptor stem, providing an unanticipated parallel between protein-RNA and RNA-RNA interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strobel, S A -- Cech, T R -- New York, N.Y. -- Science. 1995 Feb 3;267(5198):675-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7839142" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Base Sequence ; Binding Sites ; Exons ; Guanine/chemistry/*metabolism ; Guanosine Monophosphate/metabolism ; Hydrogen Bonding ; Introns ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Oligoribonucleotides/*metabolism ; RNA Splicing ; RNA, Catalytic/chemistry/*metabolism ; Tetrahymena/enzymology ; Uracil/chemistry/*metabolism
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  • 19
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    Mechanisms of rhodopsin inactivation in vivo as revealed by a COOH-terminal truncation mutant (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-20
    Description: Although biochemical experiments suggest that rhodopsin and other receptors coupled to heterotrimeric guanosine triphosphate-binding proteins (G proteins) are inactivated by phosphorylation near the carboxyl (COOH)-terminus and the subsequent binding of a capping protein, little is known about the quenching process in vivo. Flash responses were recorded from rods of transgenic mice in which a fraction of the rhodopsin molecules lacked the COOH-terminal phosphorylation sites. In the single photon regime, abnormally prolonged responses, attributed to activation of individual truncated rhodopsins, occurred interspersed with normal responses. The occurrence of the prolonged responses suggests that phosphorylation is required for normal shutoff. Comparison of normal and prolonged single photon responses indicated that rhodopsin begins to be quenched before the peak of the electrical response and that quenching limits the response amplitude.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, J -- Makino, C L -- Peachey, N S -- Baylor, D A -- Simon, M I -- AG12288/AG/NIA NIH HHS/ -- EY0570/EY/NEI NIH HHS/ -- F32 EY06405/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 20;267(5196):374-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena, CA 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824934" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Electroretinography ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phosphorylation ; Photic Stimulation ; Retinal Rod Photoreceptor Cells/metabolism/*physiology ; Rhodopsin/chemistry/genetics/*metabolism
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  • 20
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    Aberrant subcellular localization of BRCA1 in breast cancer (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-03
    Description: The BRCA1 gene product was identified as a 220-kilodalton nuclear phosphoprotein in normal cells, including breast ductal epithelial cells, and in 18 of 20 tumor cell lines derived from tissues other than breast and ovary. In 16 of 17 breast and ovarian cancer lines and 17 of 17 samples of cells obtained from malignant effusions, however, BRCA1 localized mainly in cytoplasm. Absence of BRCA1 or aberrant subcellular location was also observed to a variable extent in histological sections of many breast cancer biopsies. These findings suggest that BRCA1 abnormalities may be involved in the pathogenesis of many breast cancers, sporadic as well as familial.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Y -- Chen, C F -- Riley, D J -- Allred, D C -- Chen, P L -- Von Hoff, D -- Osborne, C K -- Lee, W H -- CA58318/CA/NCI NIH HHS/ -- EY05758/EY/NEI NIH HHS/ -- P50CA58183/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):789-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Medicine/Institute of Biotechnology, University of Texas Health Science Center at San Antonio 78245, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481765" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; BRCA1 Protein ; Base Sequence ; Breast/*chemistry ; Breast Neoplasms/*chemistry/ultrastructure ; Cell Fractionation ; Cell Line ; Cell Nucleus/chemistry ; Cytoplasm/*chemistry ; Female ; Humans ; Male ; Molecular Sequence Data ; Mutation ; Neoplasm Proteins/*analysis/genetics/metabolism ; Neoplasms/chemistry/ultrastructure ; Ovarian Neoplasms/chemistry/ultrastructure ; Pleural Effusion, Malignant/chemistry/pathology ; Transcription Factors/*analysis/genetics/metabolism ; Tumor Cells, Cultured
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  • 21
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    Whole-genome random sequencing and assembly of Haemophilus influenzae Rd (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-28
    Description: An approach for genome analysis based on sequencing and assembly of unselected pieces of DNA from the whole chromosome has been applied to obtain the complete nucleotide sequence (1,830,137 base pairs) of the genome from the bacterium Haemophilus influenzae Rd. This approach eliminates the need for initial mapping efforts and is therefore applicable to the vast array of microbial species for which genome maps are unavailable. The H. influenzae Rd genome sequence (Genome Sequence DataBase accession number L42023) represents the only complete genome sequence from a free-living organism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fleischmann, R D -- Adams, M D -- White, O -- Clayton, R A -- Kirkness, E F -- Kerlavage, A R -- Bult, C J -- Tomb, J F -- Dougherty, B A -- Merrick, J M -- New York, N.Y. -- Science. 1995 Jul 28;269(5223):496-512.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7542800" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics ; Base Composition ; Base Sequence ; *Chromosome Mapping/methods ; Chromosomes, Bacterial ; Cloning, Molecular ; Costs and Cost Analysis ; DNA, Bacterial/*genetics ; Databases, Factual ; Genes, Bacterial ; *Genome, Bacterial ; Haemophilus influenzae/*genetics/physiology ; Molecular Sequence Data ; Operon ; RNA, Bacterial/genetics ; RNA, Ribosomal/genetics ; Repetitive Sequences, Nucleic Acid ; *Sequence Analysis, DNA/methods ; Software
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  • 22
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    Glutamate receptor RNA editing in vitro by enzymatic conversion of adenosine to inosine (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-10
    Description: RNA encoding the B subunit of the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) subtype of ionotropic glutamate receptor (GluR-B) undergoes a posttranscriptional modification in which a genomically encoded adenosine is represented as a guanosine in the GluR-B complementary DNA. In vitro editing of GluR-B RNA transcripts with HeLa cell nuclear extracts was found to result from an activity that converts adenosine to inosine in regions of double-stranded RNA by enzymatic base modification. This activity is consistent with that of a double-stranded RNA-specific adenosine deaminase previously described in Xenopus oocytes and widely distributed in mammalian tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rueter, S M -- Burns, C M -- Coode, S A -- Mookherjee, P -- Emeson, R B -- ES00267/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1995 Mar 10;267(5203):1491-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, TN 37232-6600.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7878468" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/*metabolism ; Animals ; Base Sequence ; Cell Line ; Codon ; Exons ; HeLa Cells ; Humans ; Inosine/*metabolism ; Inosine Monophosphate/metabolism ; Mice ; Molecular Sequence Data ; *RNA Editing ; RNA Precursors/metabolism ; RNA, Double-Stranded/metabolism ; Rats ; Receptors, AMPA/*genetics ; Repetitive Sequences, Nucleic Acid ; Tumor Cells, Cultured
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  • 23
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    Cloning of an intrinsic human TFIID subunit that interacts with multiple transcriptional activators (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-27
    Description: TFIID is a multisubunit protein complex comprised of the TATA-binding protein (TBP) and multiple TBP-associated factors (TAFs). The TAFs in TFIID are essential for activator-dependent transcription. The cloning of a complementary DNA encoding a human TFIID TAF, TAFII55, that has no known homolog in Drosophila TFIID is now described. TAFII55 is shown to interact with the largest subunit (TAFII230) of human TFIID through its central region and with multiple activators--including Sp1, YY1, USF, CTF, adenoviral E1A, and human immunodeficiency virus-type 1 Tat proteins--through a distinct amino-terminal domain. The TAFII55-interacting region of Sp1 was localized to its DNA-binding domain, which is distinct from the glutamine-rich activation domains previously shown to interact with Drosophila TAFII110. Thus, this human TFIID TAF may be a co-activator that mediates a response to multiple activators through a distinct mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chiang, C M -- Roeder, R G -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):531-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824954" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1A Proteins/metabolism ; Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; DNA-Binding Proteins/metabolism ; Erythroid-Specific DNA-Binding Factors ; Gene Products, tat/metabolism ; HeLa Cells ; Humans ; Molecular Sequence Data ; Sp1 Transcription Factor/chemistry/metabolism ; *TATA-Binding Protein Associated Factors ; TATA-Box Binding Protein ; Trans-Activators/chemistry/genetics/*metabolism ; Transcription Factor TFIID ; Transcription Factors/*chemistry/*metabolism ; Upstream Stimulatory Factors ; YY1 Transcription Factor
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  • 24
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    Reconstitution of IKATP: an inward rectifier subunit plus the sulfonylurea receptor (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: A member of the inwardly rectifying potassium channel family was cloned here. The channel, called BIR (Kir6.2), was expressed in large amounts in rat pancreatic islets and glucose-responsive insulin-secreting cell lines. Coexpression with the sulfonylurea receptor SUR reconstituted an inwardly rectifying potassium conductance of 76 picosiemens that was sensitive to adenosine triphosphate (ATP) (IKATP) and was inhibited by sulfonylureas and activated by diazoxide. The data indicate that these pancreatic beta cell potassium channels are a complex composed of at least two subunits--BIR, a member of the inward rectifier potassium channel family, and SUR, a member of the ATP-binding cassette superfamily. Gene mapping data show that these two potassium channel subunit genes are clustered on human chromosome 11 at position 11p15.1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inagaki, N -- Gonoi, T -- Clement, J P 4th -- Namba, N -- Inazawa, J -- Gonzalez, G -- Aguilar-Bryan, L -- Seino, S -- Bryan, J -- DK44311/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1166-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Medicine, Chiba University School of Medicine, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502040" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Adenosine Triphosphate/pharmacology ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Chromosome Mapping ; Chromosomes, Human, Pair 11 ; Cloning, Molecular ; Cricetinae ; Diazoxide/pharmacology ; Humans ; Islets of Langerhans/metabolism ; KATP Channels ; Mice ; Molecular Sequence Data ; Potassium/*metabolism ; Potassium Channels/*chemistry/genetics/*metabolism ; *Potassium Channels, Inwardly Rectifying ; Rats ; Receptors, Drug/*chemistry/metabolism ; Rubidium/metabolism ; Sulfonylurea Compounds/pharmacology ; Sulfonylurea Receptors
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  • 25
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    Induction of MHC class I genes in neurons (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-28
    Description: Whether neurons express major histocompatibility complex (MHC) class I genes has not been firmly established. The techniques of confocal laser microscopy, patch clamp electrophysiology, and reverse transcriptase-polymerase chain reaction were combined here to directly examine the inducibility of MHC class I genes in individual cultured rat hippocampal neurons. Transcription of MHC class I genes was very rare in neurons with spontaneous action potentials. In electrically silent neurons, transcription was noted, with expression of beta 2-microglobulin under tighter control than in class I heavy chain molecules. Surface expression of class I molecules occurred only in electrically silent neurons treated with interferon gamma. Immunosurveillance by cytotoxic T cells may be focused on functionally impaired neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neumann, H -- Cavalie, A -- Jenne, D E -- Wekerle, H -- New York, N.Y. -- Science. 1995 Jul 28;269(5223):549-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroimmunology, Max Planck Institute for Psychiatry, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624779" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/drug effects ; Animals ; Base Sequence ; Cells, Cultured ; *Gene Expression Regulation ; *Genes, MHC Class I ; Hippocampus/cytology ; Histocompatibility Antigens Class I/biosynthesis/genetics ; Interferon-gamma/pharmacology ; Molecular Sequence Data ; Patch-Clamp Techniques ; Polymerase Chain Reaction ; Pyramidal Cells/cytology/*metabolism/physiology ; RNA, Messenger/genetics/metabolism ; Rats ; Rats, Inbred Lew ; Tetrodotoxin/pharmacology ; Transcription, Genetic ; beta 2-Microglobulin/biosynthesis/genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    A morbillivirus that caused fatal disease in horses and humans (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-07
    Description: A morbillivirus has been isolated and added to an increasing list of emerging viral diseases. This virus caused an outbreak of fatal respiratory disease in horses and humans. Genetic analyses show it to be only distantly related to the classic morbilliviruses rinderpest, measles, and canine distemper. When seen by electron microscopy, viruses had 10- and 18-nanometer surface projections that gave them a "double-fringed" appearance. The virus induced syncytia that developed in the endothelium of blood vessels, particularly the lungs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murray, K -- Selleck, P -- Hooper, P -- Hyatt, A -- Gould, A -- Gleeson, L -- Westbury, H -- Hiley, L -- Selvey, L -- Rodwell, B -- New York, N.Y. -- Science. 1995 Apr 7;268(5207):94-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CSIRO Australian Animal Health Laboratory, East Geelong, Victoria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701348" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amino Acid Sequence ; Animals ; Base Sequence ; Cercopithecus aethiops ; Disease Outbreaks/*veterinary ; Female ; Horse Diseases/epidemiology/mortality/*virology ; Horses ; Humans ; Kidney/virology ; Lung/virology ; Male ; Middle Aged ; Molecular Sequence Data ; Morbillivirus/genetics/*isolation & purification ; Morbillivirus Infections/epidemiology/mortality/*veterinary/*virology ; Pregnancy ; Queensland/epidemiology ; Respiratory Tract Infections/veterinary/virology ; Spleen/virology ; Vero Cells ; Virus Cultivation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 27
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    Casein kinase II alpha transgene-induced murine lymphoma: relation to theileriosis in cattle (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-10
    Description: Infection of cattle with the protozoan parasite Theileria parva results in a fatal lymphoproliferative syndrome that is associated with the overexpression of casein kinase II. The role of this enzyme in the pathogenesis of lymphoproliferative disorders was investigated by expressing the catalytic subunit in lymphocytes of transgenic mice. Adult transgenic mice displayed a stochastic propensity to develop lymphoma; co-expression of a c-myc transgene in addition to casein kinase II resulted in neonatal leukemia. Thus, the casein kinase II gene can serve as an oncogene, and its dysregulated expression is capable of transforming lymphocytes in a two-step pathway with c-myc.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seldin, D C -- Leder, P -- 1-K08-HL0286-01/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 10;267(5199):894-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Howard Hughes Medical Institute, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7846532" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Casein Kinase II ; Cattle ; *Cell Transformation, Neoplastic ; Cloning, Molecular ; Gene Expression Regulation, Enzymologic ; Gene Rearrangement, T-Lymphocyte ; Genes, myc ; Leukemia/etiology ; Lymphocytes/enzymology ; Lymphoma/enzymology/*etiology/genetics ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Theileriasis/*enzymology ; Up-Regulation
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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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    Serial analysis of gene expression (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-20
    Description: The characteristics of an organism are determined by the genes expressed within it. A method was developed, called serial analysis of gene expression (SAGE), that allows the quantitative and simultaneous analysis of a large number of transcripts. To demonstrate this strategy, short diagnostic sequence tags were isolated from pancreas, concatenated, and cloned. Manual sequencing of 1000 tags revealed a gene expression pattern characteristic of pancreatic function. New pancreatic transcripts corresponding to novel tags were identified. SAGE should provide a broadly applicable means for the quantitative cataloging and comparison of expressed genes in a variety of normal, developmental, and disease states.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Velculescu, V E -- Zhang, L -- Vogelstein, B -- Kinzler, K W -- CA35494/CA/NCI NIH HHS/ -- CA57345/CA/NCI NIH HHS/ -- GM07309/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 20;270(5235):484-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Oncology Center, Johns Hopkins University, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7570003" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular ; DNA Restriction Enzymes ; DNA, Complementary/genetics ; *Gene Expression ; Gene Library ; *Genetic Techniques ; Humans ; Molecular Sequence Data ; Pancreas/*enzymology ; Polymerase Chain Reaction ; RNA, Messenger/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Structure of the Arabidopsis RPM1 gene enabling dual specificity disease resistance (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-11
    Description: Plants can recognize pathogens through the action of disease resistance (R) genes, which confer resistance to pathogens expressing unique corresponding avirulence (avr) genes. The molecular basis of this gene-for-gene specificity is unknown. The Arabidopsis thaliana RPM1 gene enables dual specificity to pathogens expressing either of two unrelated Pseudomonas syringae avr genes. Despite this function, RPM1 encodes a protein sharing molecular features with recently described single-specificity R genes. Surprisingly, RPM1 is lacking from naturally occurring, disease-susceptible Arabidopsis accessions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grant, M R -- Godiard, L -- Straube, E -- Ashfield, T -- Lewald, J -- Sattler, A -- Innes, R W -- Dangl, J L -- R29 GM 46451/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):843-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Delbruck Laboratory, Koln, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638602" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*genetics/microbiology ; *Arabidopsis Proteins ; Base Sequence ; Genes, Bacterial ; *Genes, Plant ; Genetic Complementation Test ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Plant Diseases/*genetics ; Plant Proteins/chemistry/*genetics ; Plants, Genetically Modified ; Polymorphism, Restriction Fragment Length ; Pseudomonas/genetics/growth & development/pathogenicity ; Transformation, Genetic ; Virulence/genetics
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    Functional isolation and characterization of human hematopoietic stem cells (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-06
    Description: Hematopoietic cells differentiate in steps marked by the acquisition or loss of specific phenotypic characteristics. Human bone marrow cells that were responsive to the early-acting cytokines Kit ligand and interleukin-3 were forced to a metabolic death. The subfraction remaining represented 1 in 10(5) bone marrow mononuclear cells, were determined to be quiescent by cell cycle analysis, and had a stem cell immunophenotype. The cells were highly enriched for long-term culture-initiating cells, were capable of secondary colony formation, and produced both myeloid and lymphoid progeny. Thus, this technically simple strategy led to the efficient purification of cells with characteristics of hematopoietic stem cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berardi, A C -- Wang, A -- Levine, J D -- Lopez, P -- Scadden, D T -- R01-HL44851/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 6;267(5194):104-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Hematology/Oncology, Deaconess Hospital, Harvard Medical School, Boston, MA 02215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7528940" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD/analysis ; Antigens, CD34 ; Base Sequence ; Cell Differentiation ; Cell Division ; Cell Separation/*methods ; Cells, Cultured ; Colony-Forming Units Assay ; DNA, Complementary/genetics ; Flow Cytometry ; Fluorouracil/pharmacology ; Hematopoietic Cell Growth Factors/pharmacology ; Hematopoietic Stem Cells/*cytology/drug effects ; Humans ; Immunophenotyping ; Interleukin-3/pharmacology ; Molecular Sequence Data ; Proto-Oncogene Proteins/analysis ; Proto-Oncogene Proteins c-kit ; Receptor Protein-Tyrosine Kinases/analysis ; Receptors, Colony-Stimulating Factor/analysis ; Stem Cell Factor
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    Molecular basis of the cauliflower phenotype in Arabidopsis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-27
    Description: Genetic studies demonstrate that two Arabidopsis genes, CAULIFLOWER and APETALA1, encode partially redundant activities involved in the formation of floral meristems, the first step in the development of flowers. Isolation of the CAULIFLOWER gene from Arabidopsis reveals that it is closely related in sequence to APETALA1. Like APETALA1, CAULIFLOWER is expressed in young flower primordia and encodes a MADS-domain, indicating that it may function as a transcription factor. Analysis of the cultivated garden variety of cauliflower (Brassica oleracea var. botrytis) reveals that its CAULIFLOWER gene homolog is not functional, suggesting a molecular basis for one of the oldest recognized flower abnormalities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kempin, S A -- Savidge, B -- Yanofsky, M F -- GM07313/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):522-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093-0116.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824951" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Arabidopsis/chemistry/*genetics/physiology ; *Arabidopsis Proteins ; Base Sequence ; Brassica/genetics ; DNA-Binding Proteins/chemistry/*genetics/physiology ; *Genes, Plant ; Genetic Complementation Test ; *Homeodomain Proteins ; In Situ Hybridization ; *MADS Domain Proteins ; Molecular Sequence Data ; Phenotype ; Plant Proteins/chemistry/*genetics/physiology ; RNA, Plant/genetics/metabolism
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    Gene therapy in peripheral blood lymphocytes and bone marrow for ADA- immunodeficient patients (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-20
    Description: Adenosine deaminase (ADA) deficiency results in severe combined immunodeficiency, the first genetic disorder treated by gene therapy. Two different retroviral vectors were used to transfer ex vivo the human ADA minigene into bone marrow cells and peripheral blood lymphocytes from two patients undergoing exogenous enzyme replacement therapy. After 2 years of treatment, long-term survival of T and B lymphocytes, marrow cells, and granulocytes expressing the transferred ADA gene was demonstrated and resulted in normalization of the immune repertoire and restoration of cellular and humoral immunity. After discontinuation of treatment, T lymphocytes, derived from transduced peripheral blood lymphocytes, were progressively replaced by marrow-derived T cells in both patients. These results indicate successful gene transfer into long-lasting progenitor cells, producing a functional multilineage progeny.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bordignon, C -- Notarangelo, L D -- Nobili, N -- Ferrari, G -- Casorati, G -- Panina, P -- Mazzolari, E -- Maggioni, D -- Rossi, C -- Servida, P -- Ugazio, A G -- Mavilio, F -- B.36/Telethon/Italy -- New York, N.Y. -- Science. 1995 Oct 20;270(5235):470-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Telethon Gene Therapy Program for Genetic Diseases, DIBIT, Istituto Scientifico H. S. Raffaele, Milan, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7570000" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Deaminase/administration & ; dosage/blood/*deficiency/*genetics/therapeutic use ; Antibody Formation ; Base Sequence ; Bone Marrow Cells ; Cells, Cultured ; Child, Preschool ; *Gene Transfer Techniques ; *Genetic Therapy ; Genetic Vectors ; Hematopoietic Stem Cell Transplantation ; *Hematopoietic Stem Cells/enzymology ; Humans ; Immunity, Cellular ; Lymphocyte Transfusion ; *Lymphocytes/enzymology/immunology ; Molecular Sequence Data ; Severe Combined Immunodeficiency/enzymology/genetics/immunology/*therapy ; T-Lymphocytes/enzymology/immunology
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    KAI1, a metastasis suppressor gene for prostate cancer on human chromosome 11p11.2 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-12
    Description: A gene from human chromosome 11p11.2 was isolated and was shown to suppress metastasis when introduced into rat AT6.1 prostate cancer cells. Expression of this gene, designated KAI1, was reduced in human cell lines derived from metastatic prostate tumors. KAI1 specifies a protein of 267 amino acids, with four hydrophobic and presumably transmembrane domains and one large extracellular hydrophilic domain with three potential N-glycosylation sites. KAI1 is evolutionarily conserved, is expressed in many human tissues, and encodes a member of a structurally distinct family of leukocyte surface glycoproteins. Decreased expression of this gene may be involved in the malignant progression of prostate and other cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dong, J T -- Lamb, P W -- Rinker-Schaeffer, C W -- Vukanovic, J -- Ichikawa, T -- Isaacs, J T -- Barrett, J C -- CA 58236/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 May 12;268(5212):884-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Carcinogenesis, National Institute of Environmental Health Sciences, National Institute of Health, Research Triangle Park, NC 27709, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754374" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD/chemistry/*genetics/physiology ; Antigens, CD82 ; Base Sequence ; Biological Evolution ; *Chromosomes, Human, Pair 11 ; Gene Expression ; *Genes, Tumor Suppressor ; Humans ; Male ; Membrane Glycoproteins/chemistry/*genetics/physiology ; Mice ; Mice, SCID ; Molecular Sequence Data ; Neoplasm Metastasis/*genetics ; Prostatic Neoplasms/*genetics/pathology ; *Proto-Oncogene Proteins ; Rats ; Transfection ; Tumor Cells, Cultured
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    A VAMP-binding protein from Aplysia required for neurotransmitter release (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-15
    Description: Before the fusion of synaptic vesicles with the plasma membrane, a protein complex is thought to form between VAMP--an integral membrane protein of the vesicle--and two proteins associated with the plasma membrane, SNAP-25 and syntaxin. The yeast two-hybrid interaction cloning system has now been used to identify additional proteins from Aplysia that interact directly with VAMP. A 33-kilodalton membrane protein, termed VAP-33 (VAMP-associated protein of 33 kilodaltons), was identified whose corresponding messenger RNA was detected only in the central nervous system and the gill of Aplysia. Presynaptic injection of antibodies specific for VAP-33 inhibited synaptic transmission, which suggests that VAP-33 is required for the exocytosis of neurotransmitter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Skehel, P A -- Martin, K C -- Kandel, E R -- Bartsch, D -- R37 MH45923-06/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 15;269(5230):1580-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, College of Physicians and Surgeons of Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7667638" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aplysia ; Base Sequence ; Carrier Proteins/chemistry/genetics/*physiology ; Cells, Cultured ; Central Nervous System/chemistry ; Cloning, Molecular ; Exocytosis ; Gills/innervation ; Membrane Proteins/chemistry/genetics/*metabolism/*physiology ; Molecular Sequence Data ; Molecular Weight ; Motor Neurons/physiology ; Nerve Tissue Proteins/*metabolism ; Neurons/*physiology ; Neurons, Afferent/physiology ; Neurotransmitter Agents/*metabolism ; R-SNARE Proteins ; *Synaptic Transmission ; Synaptic Vesicles/physiology ; *Vesicular Transport Proteins
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  • 35
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    Gene trap tagging of PROLIFERA, an essential MCM2-3-5-like gene in Arabidopsis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-12
    Description: Gene trap transposon mutagenesis can identify essential genes whose functions in later development are obscured by an early lethal phenotype. In higher plants, many genes are required for haploid gametophyte viability, so that the phenotypic effects of their disruption cannot be readily observed in the diploid plant body. The PROLIFERA (PRL) gene, identified by gene trap transposon mutagenesis in Arabidopsis, is required for megaga-metophyte and embryo development. Reporter gene expression patterns revealed that PRL was expressed in dividing cells throughout the plant. PRL is related to the MCM2-3-5 family of yeast genes that are required for the initiation of DNA replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Springer, P S -- McCombie, W R -- Sundaresan, V -- Martienssen, R A -- New York, N.Y. -- Science. 1995 May 12;268(5212):877-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754372" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*genetics/growth & development/physiology ; *Arabidopsis Proteins ; Base Sequence ; Cell Cycle Proteins/genetics ; Crosses, Genetic ; DNA Transposable Elements ; Fungal Proteins/genetics ; *Genes, Plant ; Genes, Reporter ; Minichromosome Maintenance Complex Component 7 ; Molecular Sequence Data ; Mutagenesis, Insertional ; Phenotype ; Plant Proteins/chemistry/*genetics ; Seeds/growth & development ; Sequence Alignment
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  • 36
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    Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-07
    Description: Peptide synthetases involved in the nonribosomal synthesis of peptide secondary metabolites possess a highly conserved domain structure. The arrangement of these domains within the multifunctional enzymes determines the number and order of the amino acid constituents of the peptide product. A general approach has been developed for targeted substitution of amino acid-activating domains within the srfA operon, which encodes the protein templates for the synthesis of the lipopeptide antibiotic surfactin in Bacillus subtilis. Exchange of domain-coding regions of bacterial and fungal origin led to the construction of hybrid genes that encoded peptide synthetases with altered amino acid specificities and the production of peptides with modified amino acid sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stachelhaus, T -- Schneider, A -- Marahiel, M A -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):69-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochemie/Fachbereich Chemie, Philipps-University of Marburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604280" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aminoacylation ; Anti-Bacterial Agents/*biosynthesis/chemistry/pharmacology ; Bacillus/genetics ; Bacillus subtilis/genetics ; Bacterial Proteins/*biosynthesis/chemistry/pharmacology ; Base Sequence ; Cloning, Molecular ; Genes, Bacterial ; Genes, Fungal ; Hemolysis/drug effects ; Lipopeptides ; Mass Spectrometry ; Molecular Sequence Data ; Operon ; Penicillium chrysogenum/genetics ; Peptide Synthases/chemistry/*genetics ; *Peptides, Cyclic ; *Protein Engineering ; Recombinant Fusion Proteins/biosynthesis/chemistry/pharmacology ; Transformation, Bacterial
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  • 37
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    A regulatory role for ARF6 in receptor-mediated endocytosis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-24
    Description: Adenosine diphosphate-ribosylation factor 6 (ARF6), ARF6 mutants, and ARF1 were transiently expressed in Chinese hamster ovary cells, and the effects on receptor-mediated endocytosis were assessed. Overexpressed ARF6 localized to the cell periphery and led to a redistribution of transferrin receptors to the cell surface and a decrease in the rate of uptake of transferrin. Similar results were obtained when a mutant defective in guanosine triphosphate hydrolysis was expressed. Expression of a dominant negative mutant, ARF6(T27N), resulted in an intracellular distribution of transferrin receptors and an inhibition of transferrin recycling to the cell surface. In contrast, overexpression of ARF1 had little or no effect on these parameters of endocytosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉D'Souza-Schorey, C -- Li, G -- Colombo, M I -- Stahl, P D -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1175-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Physiology, 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/7855600" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factor 1 ; ADP-Ribosylation Factors ; Amino Acid Sequence ; Animals ; Base Sequence ; CHO Cells ; Cell Membrane/metabolism ; Cricetinae ; *Endocytosis ; GTP-Binding Proteins/analysis/genetics/*physiology ; Golgi Apparatus/metabolism/ultrastructure ; Kinetics ; Molecular Sequence Data ; Mutation ; Receptors, Transferrin/metabolism ; Transferrin/metabolism
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    Nicotine enhancement of fast excitatory synaptic transmission in CNS by presynaptic receptors (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-22
    Description: The behavioral and cognitive effects of nicotine suggest that nicotinic acetylcholine receptors (nAChRs) participate in central nervous system (CNS) function. Although nAChR subunit messenger RNA (mRNA) and nicotine binding sites are common in the brain, there is little evidence for synapses mediated by nAChRs in the CNS. To test whether, CNS nAChRs might modify rather than mediate transmission, the regulation of excitatory synaptic transmission by these receptors was examined. Nanomolar concentrations of nicotine enhanced both glutamatergic and cholinergic synaptic transmission by activation of presynaptic nAChRs that increased presynaptic [Ca2]i. Pharmacological and subunit deletion experiments reveal that these presynaptic nAChRs include the alpha 7 subunit. These findings reveal that CNS nAChRs enhance fast excitatory transmission, providing a likely mechanism for the complex behavioral effects of nicotine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McGehee, D S -- Heath, M J -- Gelber, S -- Devay, P -- Role, L W -- NS09395/NS/NINDS NIH HHS/ -- NS22061/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 22;269(5231):1692-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Anatomy, Columbia University, College of Physicians and Surgeons, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569895" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Brain/drug effects/*physiology ; Bungarotoxins/metabolism/pharmacology ; Calcium/physiology ; Chick Embryo ; Culture Techniques ; Ganglia, Sympathetic/drug effects/physiology ; Glutamic Acid/metabolism ; Molecular Sequence Data ; Nicotine/metabolism/*pharmacology ; Nicotinic Agonists/metabolism/*pharmacology ; Presynaptic Terminals/chemistry/drug effects/*physiology ; Receptors, Nicotinic/analysis/*physiology ; Synapses/drug effects/physiology ; Synaptic Transmission/*drug effects ; Thalamic Nuclei/drug effects/physiology
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    Antigen-specific development of primary and memory T cells in vivo (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-04-07
    Description: The expansion and contraction of specific helper T cells in the draining lymph nodes of normal mice after injection with antigen was followed. T cell receptors from purified primary and memory responder cells had highly restricted junctional regions, indicating antigen-driven selection. Selection for homogeneity in the length of the third complementarity-determining region (CDR3) occurs before selection for some of the characteristic amino acids, indicating the importance of this parameter in T cell receptor recognition. Ultimately, particular T cell receptor sequences come to predominate in the secondary response and others disappear, showing the selective preservation or expansion of specific T cell clones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McHeyzer-Williams, M G -- Davis, M M -- New York, N.Y. -- Science. 1995 Apr 7;268(5207):106-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7535476" target="_blank"〉PubMed〈/a〉
    Keywords: Adjuvants, Immunologic ; Amino Acid Sequence ; Animals ; Antigens/*immunology ; Antigens, CD44 ; Base Sequence ; Carrier Proteins/biosynthesis ; Cell Adhesion Molecules/biosynthesis ; Immunologic Memory/*immunology ; L-Selectin ; Lymphocyte Activation/immunology ; Mice ; Molecular Sequence Data ; Receptors, Antigen, T-Cell, alpha-beta/biosynthesis/chemistry ; Receptors, Cell Surface/biosynthesis ; Receptors, Lymphocyte Homing/biosynthesis ; T-Lymphocytes, Helper-Inducer/*immunology
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  • 40
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    A p16INK4a-insensitive CDK4 mutant targeted by cytolytic T lymphocytes in a human melanoma (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-09-01
    Description: A mutated cyclin-dependent kinase 4 (CDK4) was identified as a tumor-specific antigen recognized by HLA-A2. 1-restricted autologous cytolytic T lymphocytes (CTLs) in a human melanoma. The mutated CDK4 allele was present in autologous cultured melanoma cells and metastasis tissue, but not in the patient's lymphocytes. The mutation, an arginine-to-cysteine exchange at residue 24, was part of the CDK4 peptide recognized by CTLs and prevented binding of the CDK4 inhibitor p16INK4a, but not of p21 or of p27KIP1. The same mutation was found in one additional melanoma among 28 melanomas analyzed. These results suggest that mutation of CDK4 can create a tumor-specific antigen and can disrupt the cell-cycle regulation exerted by the tumor suppressor p16INK4a.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolfel, T -- Hauer, M -- Schneider, J -- Serrano, M -- Wolfel, C -- Klehmann-Hieb, E -- De Plaen, E -- Hankeln, T -- Meyer zum Buschenfelde, K H -- Beach, D -- New York, N.Y. -- Science. 1995 Sep 1;269(5228):1281-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medizinische Klinik und Poliklinik, Johannes Gutenberg-Universitat, Mainz, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7652577" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/metabolism/*pharmacology ; *Cell Cycle Proteins ; Cell Line ; Cloning, Molecular ; Cyclin-Dependent Kinase 4 ; Cyclin-Dependent Kinase Inhibitor p15 ; Cyclin-Dependent Kinase Inhibitor p16 ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclin-Dependent Kinase Inhibitor p27 ; *Cyclin-Dependent Kinases ; Cyclins/metabolism/pharmacology ; HLA-A2 Antigen/immunology ; Humans ; Melanoma/enzymology/*immunology ; Microtubule-Associated Proteins/metabolism/pharmacology ; Molecular Sequence Data ; Point Mutation ; Polymerase Chain Reaction ; Protein-Serine-Threonine Kinases/antagonists & ; inhibitors/genetics/*immunology/metabolism ; *Proto-Oncogene Proteins ; T-Lymphocytes, Cytotoxic/*immunology ; Transfection ; Tumor Cells, Cultured ; *Tumor Suppressor Proteins
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    Common virulence factors for bacterial pathogenicity in plants and animals (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-30
    Description: A Pseudomonas aeruginosa strain (UCBPP-PA14) is infectious both in an Arabidopsis thaliana leaf infiltration model and in a mouse full-thickness skin burn model. UCBPP-PA14 exhibits ecotype specificity for Arabidopsis, causing a range of symptoms from none to severe in four different ecotypes. In the mouse model, UCBPP-PA14 is as lethal as other well-studied P. aeruginosa strains. Mutations in the UCBPP-PA14 toxA, plcS, and gacA genes resulted in a significant reduction in pathogenicity in both hosts, indicating that these genes encode virulence factors required for the full expression of pathogenicity in both plants and animals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rahme, L G -- Stevens, E J -- Wolfort, S F -- Shao, J -- Tompkins, R G -- Ausubel, F M -- New York, N.Y. -- Science. 1995 Jun 30;268(5219):1899-902.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604262" target="_blank"〉PubMed〈/a〉
    Keywords: *ADP Ribose Transferases ; Animals ; Arabidopsis/*microbiology ; Bacterial Proteins/genetics ; *Bacterial Toxins ; Base Sequence ; Burns/complications ; Exotoxins/genetics ; Male ; Mice ; Molecular Sequence Data ; Mutation ; Phospholipases/genetics ; Plant Diseases/*microbiology ; Pseudomonas Infections/*microbiology ; Pseudomonas aeruginosa/genetics/growth & development/*pathogenicity ; Virulence/genetics ; *Virulence Factors
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    Inactivation of the mouse Huntington's disease gene homolog Hdh (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-07-21
    Description: Huntington's disease (HD) is a dominant neurodegenerative disorder caused by expansion of a CAG repeat in the gene encoding huntingtin, a protein of unknown function. To distinguish between "loss of function" and "gain of function" models of HD, the murine HD homolog Hdh was inactivated by gene targeting. Mice heterozygous for Hdh inactivation were phenotypically normal, whereas homozygosity resulted in embryonic death. Homozygotes displayed abnormal gastrulation at embryonic day 7.5 and were resorbing by day 8.5. Thus, huntingtin is critical early in embryonic development, before the emergence of the nervous system. That Hdh inactivation does not mimic adult HD neuropathology suggests that the human disease involves a gain of function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duyao, M P -- Auerbach, A B -- Ryan, A -- Persichetti, F -- Barnes, G T -- McNeil, S M -- Ge, P -- Vonsattel, J P -- Gusella, J F -- Joyner, A L -- NS16367/NS/NINDS NIH HHS/ -- NS32765/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 21;269(5222):407-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Neurogenetics Unit, Massachusetts General Hospital, Charlestown 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618107" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line ; Ectoderm/cytology ; Embryonic and Fetal Development ; Female ; Gene Targeting ; Genotype ; Heterozygote ; Homozygote ; Humans ; Huntington Disease/*genetics ; Male ; Mesoderm/cytology ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Nerve Tissue Proteins/*genetics/physiology ; Nuclear Proteins/*genetics/physiology ; Phenotype ; Stem Cells/metabolism
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    Participation of the protein Go in multiple aspects of behavior in C. elegans (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-03-17
    Description: The goa-1 gene encoding the alpha subunit of the heterotrimeric guanosine triphosphate-binding protein (G protein) Go from Caenorhabditis elegans is expressed in most neurons, and in the muscles involved in egg laying and male mating. Reduction-of-function mutations in goa-1 caused a variety of behavioral defects including hyperactive movement, premature egg laying, and male impotence. Expression of the activated Go alpha subunit (G alpha o) in transgenic nematodes resulted in lethargic movement, delayed egg laying, and reduced mating efficiency. Induced expression of activated G alpha o in adults was sufficient to cause these phenotypes, indicating that G alpha o mediates behavior through its role in neuronal function and the functioning of specialized muscles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mendel, J E -- Korswagen, H C -- Liu, K S -- Hajdu-Cronin, Y M -- Simon, M I -- Plasterk, R H -- Sternberg, P W -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1652-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7886455" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Base Sequence ; Behavior, Animal ; Caenorhabditis elegans/genetics/*physiology ; Disorders of Sex Development ; Female ; GTP-Binding Proteins/genetics/*physiology ; Genes, Helminth ; Male ; Molecular Sequence Data ; Movement ; Muscles/innervation/physiology ; Mutation ; Neurons/physiology ; Oviposition ; Phenotype ; Serotonin/pharmacology ; Sexual Behavior, Animal
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    Noncoding DNA, Zipf's law, and language (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-12
    Description: In the report "Continent-ocean chemical heterogeneity in the mantle based on seismic tomography" by Alessandro M. Forte et al. (21 Apr., p. 386), note 14 (p. 388) should have included the following sentence at the end. "We note, however, that this classical measure of significance does not take into account the red spectrum of the observed nonhydrostatic geoid, whose harmonic coefficients cannot be properly regarded as a random distribution; therefore, the statistical significance of the measured correlation coefficient is possibly less than 99%.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Konopka, A K -- Martindale, C -- New York, N.Y. -- Science. 1995 May 12;268(5212):789.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754361" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/chemistry/*genetics ; Genetic Code ; Oligodeoxyribonucleotides/chemistry ; Statistics as Topic
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  • 45
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    Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95 (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-09-22
    Description: The N-methyl-D-aspartate (NMDA) receptor subserves synaptic glutamate-induced transmission and plasticity in central neurons. The yeast two-hybrid system was used to show that the cytoplasmic tails of NMDA receptor subunits interact with a prominent postsynaptic density protein PSD-95. The second PDZ domain in PSD-95 binds to the seven-amino acid, COOH-terminal domain containing the terminal tSXV motif (where S is serine, X is any amino acid, and V is valine) common to NR2 subunits and certain NR1 splice forms. Transcripts encoding PSD-95 are expressed in a pattern similar to that of NMDA receptors, and the NR2B subunit co-localizes with PSD-95 in cultured rat hippocampal neurons. The interaction of these proteins may affect the plasticity of excitatory synapses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kornau, H C -- Schenker, L T -- Kennedy, M B -- Seeburg, P H -- NS-28710/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 22;269(5231):1737-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Biology (ZMBH), University of Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569905" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; Cytoplasm/chemistry ; Genes, Reporter ; Hippocampus/*metabolism ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins ; Molecular Sequence Data ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Neuronal Plasticity ; Neurons/*metabolism ; RNA Splicing ; Rats ; Receptors, N-Methyl-D-Aspartate/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction
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  • 46
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    Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-10-06
    Description: The genetic properties of the [URE3] non-Mendelian element of Saccharomyces cerevisiae suggest that it is a prion (infectious protein) form of Ure2p, a regulator of nitrogen catabolism. In extracts from [URE3] strains, Ure2p was partially resistant to proteinase K compared with Ure2p from wild-type extracts. Overexpression of Ure2p in wild-type strains induced a 20- to 200-fold increase in the frequency with which [URE3] arose. Overexpression of just the amino-terminal 65 residues of Ure2p increased the frequency of [URE3] induction 6000-fold. Without this "prion-inducing domain" the carboxyl-terminal domain performed the nitrogen regulation function of Ure2p, but could not be changed to the [URE3] prion state. Thus, this domain induced the prion state in trans, whereas in cis it conferred susceptibility of the adjoining nitrogen regulatory domain to prion infections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Masison, D C -- Wickner, R B -- New York, N.Y. -- Science. 1995 Oct 6;270(5233):93-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section on Genetics of Simple Eukaryotes, National Institute of Diabetes, Digestive and Kidney Disease, National Institutes of Health, Bethesda, MD 20892-0830, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569955" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Endopeptidase K ; Fungal Proteins/chemistry/*genetics/metabolism ; Genes, Fungal ; Genetic Complementation Test ; Glutathione Peroxidase ; Molecular Sequence Data ; Nitrogen/metabolism ; Plasmids ; Prions/*genetics/metabolism ; Promoter Regions, Genetic ; Saccharomyces cerevisiae/chemistry/*genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Sequence Deletion ; Serine Endopeptidases/metabolism
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    Frequency and distribution of DNA uptake signal sequences in the Haemophilus influenzae Rd genome (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-07-28
    Description: The naturally transformable, Gram-negative bacterium Haemophilus influenzae Rd preferentially takes up DNA of its own species by recognizing a 9-base pair sequence, 5'-AAGTGCGGT, carried in multiple copies in its chromosome. With the availability of the complete genome sequence, 1465 copies of the 9-base pair uptake site have been identified. Alignment of these sites unexpectedly reveals an extended consensus region of 29 base pairs containing the core 9-base pair region and two downstream 6-base pair A/T-rich regions, each spaced about one helix turn apart. Seventeen percent of the sites are in inverted repeat pairs, many of which are located downstream to gene termini and are capable of forming stem-loop structures in messenger RNA that might function as signals for transcription termination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, H O -- Tomb, J F -- Dougherty, B A -- Fleischmann, R D -- Venter, J C -- New York, N.Y. -- Science. 1995 Jul 28;269(5223):538-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7542802" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Chromosome Mapping ; Consensus Sequence ; Conserved Sequence ; DNA, Bacterial/chemistry/*genetics ; Escherichia coli/genetics ; *Genome, Bacterial ; Haemophilus influenzae/*genetics ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligonucleotide Probes ; RNA, Bacterial/chemistry/genetics ; RNA, Messenger/chemistry/genetics ; Repetitive Sequences, Nucleic Acid ; Transcription, Genetic ; *Transformation, Bacterial
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  • 48
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    Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-04
    Description: Eukaryotic DNA polymerase beta (pol beta) can catalyze DNA synthesis during base excision DNA repair. It is shown here that pol beta also catalyzes release of 5'-terminal deoxyribose phosphate (dRP) residues from incised apurinic-apyrimidinic sites, which are common intermediate products in base excision repair. The catalytic domain for this activity resides within an amino-terminal 8-kilodalton fragment of pol beta, which comprises a distinct structural domain of the enzyme. Magnesium is required for the release of dRP from double-stranded DNA but not from a single-stranded oligonucleotide. Analysis of the released products indicates that the excision reaction occurs by beta-elimination rather than hydrolysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsumoto, Y -- Kim, K -- CA06927/CA/NCI NIH HHS/ -- CA63154/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Aug 4;269(5224):699-702.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Radiation Oncology, Fox Chase Cancer Center, Philadelphia, PA 19111, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624801" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apurinic Acid ; Base Sequence ; Binding Sites ; DNA/*metabolism ; DNA Ligases/metabolism ; DNA Polymerase I/*metabolism ; *DNA Repair ; DNA-(Apurinic or Apyrimidinic Site) Lyase ; Deoxyribonuclease IV (Phage T4-Induced) ; Edetic Acid/pharmacology ; Hydrolysis ; Lyases/metabolism ; Molecular Sequence Data ; Polynucleotides ; Protein Structure, Tertiary ; Rats ; Ribosemonophosphates/*metabolism ; Xenopus laevis
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    Structure-based design of transcription factors (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-01-06
    Description: Computer modeling suggested that transcription factors with novel sequence specificities could be designed by combining known DNA binding domains. This structure-based strategy was tested by construction of a fusion protein, ZFHD1, that contained zinc fingers 1 and 2 from Zif268, a short polypeptide linker, and the homeodomain from Oct-1. The fusion protein bound optimally to a sequence containing adjacent homeodomain (TAATTA) and zinc finger (NGGGNG) subsites. When fused to an activation domain, ZFHD1 regulated promoter activity in vivo in a sequence-specific manner. Analysis of known protein-DNA complexes suggests that many other DNA binding proteins could be designed in a similar fashion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pomerantz, J L -- Sharp, P A -- Pabo, C O -- P01-CA42063/CA/NCI NIH HHS/ -- P30-CA14051/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 6;267(5194):93-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809612" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Cloning, Molecular ; Computer Simulation ; DNA-Binding Proteins/*chemistry/genetics/metabolism ; Gene Expression Regulation ; Homeodomain Proteins/chemistry ; Host Cell Factor C1 ; Models, Molecular ; Molecular Sequence Data ; Octamer Transcription Factor-1 ; Promoter Regions, Genetic ; Protein Engineering ; Recombinant Fusion Proteins/*chemistry/metabolism ; Transcription Factors/*chemistry/genetics/metabolism ; Transfection ; *Zinc Fingers
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    Association of the yeast pheromone response G protein beta gamma subunits with the MAP kinase scaffold Ste5p (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-15
    Description: The mating response pathway of the yeast Saccharomyces cerevisiae includes a heterotrimeric guanine nucleotide-binding protein (G protein) that activates a mitogen-activated protein MAP kinase cascade by an unknown mechanism. An amino-terminal fragment of the MAP kinase scaffold protein Ste5p that interfered with pheromone-induced cell cycle arrest was identified. A haploid-specific interaction between the amino terminus of Ste5p and the G protein beta subunit Ste4p was also detected in a two-hybrid assay, and the product of a signaling-defective allele of STE4 was defective in this interaction. In cells with a constitutively activated pheromone response pathway, epitope-tagged Ste4p was coimmunoprecipitated with Ste5p. Thus, association of the G protein and the MAP kinase cassette via the scaffolding protein Ste5p may transmit the G protein signal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whiteway, M S -- Wu, C -- Leeuw, T -- Clark, K -- Fourest-Lieuvin, A -- Thomas, D Y -- Leberer, E -- New York, N.Y. -- Science. 1995 Sep 15;269(5230):1572-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7667635" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Base Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; *Carrier Proteins ; Cell Division ; Fungal Proteins/genetics/*metabolism ; *GTP-Binding Protein beta Subunits ; *GTP-Binding Protein gamma Subunits ; GTP-Binding Proteins/genetics/*metabolism ; *Heterotrimeric GTP-Binding Proteins ; Molecular Sequence Data ; Mutation ; Pheromones/pharmacology ; Plasmids ; Saccharomyces cerevisiae/cytology/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; *Signal Transduction ; Transformation, Genetic
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    Simultaneous identification of bacterial virulence genes by negative selection (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-21
    Description: An insertional mutagenesis system that uses transposons carrying unique DNA sequence tags was developed for the isolation of bacterial virulence genes. The tags from a mixed population of bacterial mutants representing the inoculum and bacteria recovered from infected hosts were detected by amplification, radiolabeling, and hybridization analysis. When applied to a murine model of typhoid fever caused by Salmonella typhimurium, mutants with attenuated virulence were revealed by use of tags that were present in the inoculum but not in bacteria recovered from infected mice. This approach resulted in the identification of new virulence genes, some of which are related to, but functionally distinct from, the inv/spa family of S. typhimurium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hensel, M -- Shea, J E -- Gleeson, C -- Jones, M D -- Dalton, E -- Holden, D W -- New York, N.Y. -- Science. 1995 Jul 21;269(5222):400-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Infectious Diseases and Bacteriology, Royal Postgraduate Medical School, Hammersmith Hospital, London, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618105" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *DNA Transposable Elements ; *Genes, Bacterial ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; *Mutagenesis, Insertional ; Nucleic Acid Hybridization ; Polymerase Chain Reaction ; Salmonella Infections, Animal/*microbiology ; Salmonella typhimurium/genetics/*pathogenicity ; Sequence Tagged Sites ; Virulence/genetics
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  • 52
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    Potential mechanism for sustained antiretroviral efficacy of AZT-3TC combination therapy (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-04
    Description: Combinations of antiretroviral drugs that prevent or delay the appearance of drug-resistant human immunodeficiency virus-type 1 (HIV-1) mutants are urgently required. Mutants resistant to 3'-azidothymidine (AZT, zidovudine) became phenotypically sensitive in vitro by mutation of residue 184 of viral reverse transcriptase to valine, which also induced resistance to (-)2'-deoxy-3'-thiacytidine (3TC). Furthermore, AZT-3TC coresistance was not observed during extensive in vitro selection with both drugs. In vivo AZT-3TC combination therapy resulted in a markedly greater decreased in serum HIV-1 RNA concentrations than treatment with AZT alone, even though valine-184 mutants rapidly emerged. Most samples assessed from the combination group remained AZT sensitive at 24 weeks of therapy, consistent with in vitro mutation studies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Larder, B A -- Kemp, S D -- Harrigan, P R -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1995 Aug 4;269(5224):696-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Antiviral Therapeutic Research Unit, Wellcome Research Laboratories, Beckenham, Kent, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7542804" target="_blank"〉PubMed〈/a〉
    Keywords: Antiviral Agents/*pharmacology/therapeutic use ; Base Sequence ; CD4 Lymphocyte Count ; Cell Line ; Codon ; Drug Resistance, Microbial ; Drug Therapy, Combination ; HIV Infections/*drug therapy/virology ; HIV Reverse Transcriptase ; HIV-1/*drug effects/enzymology/genetics/growth & development ; HeLa Cells ; Humans ; Lamivudine ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Point Mutation ; RNA, Viral/blood ; RNA-Directed DNA Polymerase/genetics ; *Reverse Transcriptase Inhibitors ; Serial Passage ; Zalcitabine/*analogs & derivatives/pharmacology/therapeutic use ; Zidovudine/*pharmacology/therapeutic use
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  • 53
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    Structurally complex and highly active RNA ligases derived from random RNA sequences (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-21
    Description: Seven families of RNA ligases, previously isolated from random RNA sequences, fall into three classes on the basis of secondary structure and regiospecificity of ligation. Two of the three classes of ribozymes have been engineered to act as true enzymes, catalyzing the multiple-turnover transformation of substrates into products. The most complex of these ribozymes has a minimal catalytic domain of 93 nucleotides. An optimized version of this ribozyme has a kcat exceeding one per second, a value far greater than that of most natural RNA catalysts and approaching that of comparable protein enzymes. The fact that such a large and complex ligase emerged from a very limited sampling of sequence space implies the existence of a large number of distinct RNA structures of equivalent complexity and activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ekland, E H -- Szostak, J W -- Bartel, D P -- New York, N.Y. -- Science. 1995 Jul 21;269(5222):364-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618102" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Catalysis ; Cloning, Molecular ; Conserved Sequence ; Introns ; Molecular Sequence Data ; Mutagenesis ; *Nucleic Acid Conformation ; Point Mutation ; RNA, Catalytic/*chemistry/classification/*metabolism ; Sequence Deletion
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  • 54
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    Identification of a member of the MAPKKK family as a potential mediator of TGF-beta signal transduction (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-12-22
    Description: The mitogen-activated protein kinase (MAPK) pathway is a conserved eukaryotic signaling module that converts receptor signals into various outputs. MAPK is activated through phosphorylation by MAPK kinase (MAPKK), which is first activated by MAPKK kinase (MAPKKK). A genetic selection based on a MAPK pathway in yeast was used to identify a mouse protein kinase (TAK1) distinct from other members of the MAPKKK family. TAK1 was shown to participate in regulation of transcription by transforming growth factor-beta (TGF-beta). Furthermore, kinase activity of TAK1 was stimulated in response to TGF-beta and bone morphogenetic protein. These results suggest that TAK1 functions as a mediator in the signaling pathway of TGF-beta superfamily members.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamaguchi, K -- Shirakabe, K -- Shibuya, H -- Irie, K -- Oishi, I -- Ueno, N -- Taniguchi, T -- Nishida, E -- Matsumoto, K -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):2008-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Faculty of Science, Nagoya University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533096" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Bone Morphogenetic Proteins ; Cell Line ; Cloning, Molecular ; Epidermal Growth Factor/pharmacology ; *Gene Expression Regulation ; Genes, Reporter ; *MAP Kinase Kinase Kinases ; Mice ; Molecular Sequence Data ; Protein-Serine-Threonine Kinases/*metabolism ; Proteins/pharmacology ; Saccharomyces cerevisiae/genetics ; *Signal Transduction ; Transfection ; Transforming Growth Factor beta/*pharmacology
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  • 55
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    Revival and identification of bacterial spores in 25- to 40-million-year-old Dominican amber (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-05-19
    Description: A bacterial spore was revived, cultured, and identified from the abdominal contents of extinct bees preserved for 25 to 40 million years in buried Dominican amber. Rigorous surface decontamination of the amber and aseptic procedures were used during the recovery of the bacterium. Several lines of evidence indicated that the isolated bacterium was of ancient origin and not an extant contaminant. The characteristic enzymatic, biochemical, and 16S ribosomal DNA profiles indicated that the ancient bacterium is most closely related to extant Bacillus sphaericus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cano, R J -- Borucki, M K -- New York, N.Y. -- Science. 1995 May 19;268(5213):1060-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biological Sciences, California Polytechnic State University, San Luis Obispo 93407, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7538699" target="_blank"〉PubMed〈/a〉
    Keywords: *Amber ; Animals ; Bacillus/genetics/isolation & purification ; Base Sequence ; Bees/*microbiology ; Biological Evolution ; DNA, Bacterial/chemistry/isolation & purification ; Dominican Republic ; *Fossils ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA, Bacterial/chemistry ; Spores, Bacterial/genetics/isolation & purification/*physiology
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  • 56
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    Similarity of sli-1, a regulator of vulval development in C. elegans, to the mammalian proto-oncogene c-cbl (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-25
    Description: Vulval induction during Caenorhabditis elegans development is mediated by LET-23, a homolog of the mammalian epidermal growth factor receptor tyrosine kinase. The sli-1 gene is a negative regulator of LET-23 and is shown here to encode a protein similar to c-Cbl, a mammalian proto-oncoprotein. SLI-1 and c-Cbl share approximately 55 percent amino acid identity over a stretch of 390 residues, which includes a C3HC4 zinc-binding motif known as the RING finger, and multiple consensus binding sites for Src homology 3 (SH3) domains. SLI-1 and c-Cbl may define a new class of proteins that modify receptor tyrosine kinase-mediated signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoon, C H -- Lee, J -- Jongeward, G D -- Sternberg, P W -- New York, N.Y. -- Science. 1995 Aug 25;269(5227):1102-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7652556" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Caenorhabditis elegans/*genetics/growth & development ; *Caenorhabditis elegans Proteins ; Conserved Sequence ; DNA, Complementary/genetics ; Female ; *Genes, Helminth ; *Genes, Regulator ; Helminth Proteins/chemistry/*genetics/metabolism ; Humans ; Molecular Sequence Data ; Mutation ; Proto-Oncogene Proteins/chemistry/*genetics ; Proto-Oncogene Proteins c-cbl ; Receptor, Epidermal Growth Factor/metabolism ; Sequence Alignment ; Signal Transduction ; *Ubiquitin-Protein Ligases ; Vulva/growth & development
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  • 57
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    Role of yeast insulin-degrading enzyme homologs in propheromone processing and bud site selection (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-20
    Description: The Saccharomyces cerevisiae AXL1 gene product Axl1p shares homology with the insulin-degrading enzyme family of endoproteases. Yeast axl1 mutants showed a defect in a-factor pheromone secretion, and a probable site of processing by Axl1p was identified within the a-factor precursor. In addition, Axl1p appears to function as a morphogenetic determinant for axial bud site selection. Amino acid substitutions within the presumptive active site of Axl1p caused defects in propheromone processing but failed to perturb bud site selection. Thus, Axl1p has been shown to participate in the dual regulation of distinct signaling pathways, and a member of the insulinase family has been implicated in propeptide processing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adames, N -- Blundell, K -- Ashby, M N -- Boone, C -- New York, N.Y. -- Science. 1995 Oct 20;270(5235):464-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569998" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Membrane/metabolism ; Cloning, Molecular ; Fungal Proteins/chemistry/genetics/metabolism/*physiology ; Genes, Fungal ; Insulysin/chemistry/genetics/*physiology ; Lipoproteins/genetics/*metabolism ; Metalloendopeptidases ; Molecular Sequence Data ; Morphogenesis ; Mutagenesis, Site-Directed ; Phenotype ; Pheromones/genetics/*metabolism ; Protein Precursors/genetics/*metabolism ; Protein Processing, Post-Translational ; Saccharomyces cerevisiae/cytology/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Sequence Alignment ; Signal Transduction
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  • 58
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    Enhanced DNA-binding activity of a Stat3-related protein in cells transformed by the Src oncoprotein (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-07
    Description: Cytokines and growth factors induce tyrosine phosphorylation of signal transducers and activators of transcription (STATs) that directly activate gene expression. Cells stably transformed by the Src oncogene tyrosine kinase were examined for STAT protein activation. Assays of electrophoretic mobility, DNA-binding specificity, and antigenicity indicated that Stat3 or a closely related STAT family member was constitutively activated by the Src oncoprotein. Induction of this DNA-binding activity was accompanied by tyrosine phosphorylation of Stat3 and correlated with Src transformation. These findings demonstrate that Src can activate STAT signaling pathways and raise the possibility that Stat3 contributes to oncogenesis by Src.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, C L -- Meyer, D J -- Campbell, G S -- Larner, A C -- Carter-Su, C -- Schwartz, J -- Jove, R -- CA55652/CA/NCI NIH HHS/ -- DK34171/DK/NIDDK NIH HHS/ -- R01 DK034171/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):81-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7541555" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line, Transformed ; *Cell Transformation, Neoplastic ; DNA/*metabolism ; DNA-Binding Proteins/*metabolism ; Growth Inhibitors/pharmacology ; Interferon-gamma/pharmacology ; *Interleukin-6 ; Leukemia Inhibitory Factor ; Lymphokines/pharmacology ; Mice ; Molecular Sequence Data ; Oncogene Protein pp60(v-src)/*physiology ; Phosphorylation ; Phosphotyrosine ; STAT3 Transcription Factor ; *Signal Transduction ; Trans-Activators/*metabolism ; Tyrosine/analogs & derivatives/metabolism
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  • 59
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    Cloning of the beta cell high-affinity sulfonylurea receptor: a regulator of insulin secretion (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-21
    Description: Sulfonylureas are a class of drugs widely used to promote insulin secretion in the treatment of non-insulin-dependent diabetes mellitus. These drugs interact with the sulfonylurea receptor of pancreatic beta cells and inhibit the conductance of adenosine triphosphate (ATP)-dependent potassium (KATP) channels. Cloning of complementary DNAs for the high-affinity sulfonylurea receptor indicates that it is a member of the ATP-binding cassette or traffic ATPase superfamily with multiple membrane-spanning domains and two nucleotide binding folds. The results suggest that the sulfonylurea receptor may sense changes in ATP and ADP concentration, affect KATP channel activity, and thereby modulate insulin release.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aguilar-Bryan, L -- Nichols, C G -- Wechsler, S W -- Clement, J P 4th -- Boyd, A E 3rd -- Gonzalez, G -- Herrera-Sosa, H -- Nguy, K -- Bryan, J -- Nelson, D A -- DK41898/DK/NIDDK NIH HHS/ -- DK44311/DK/NIDDK NIH HHS/ -- HL45742/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Apr 21;268(5209):423-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716547" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cloning, Molecular ; Cricetinae ; Insulin/*secretion ; Islets of Langerhans/*metabolism ; Molecular Sequence Data ; Phosphorylation ; Potassium Channels/chemistry/*genetics/metabolism ; *Potassium Channels, Inwardly Rectifying ; Protein Folding ; Protein Structure, Secondary ; Receptors, Drug/chemistry/*genetics/metabolism ; Sequence Alignment ; Sulfonylurea Compounds/metabolism ; Sulfonylurea Receptors ; Transfection ; Tumor Cells, Cultured
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  • 60
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    Construction of a soluble adenylyl cyclase activated by Gs alpha and forskolin (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-23
    Description: A soluble adenylyl cyclase was constructed by linkage of portions of the cytosolic domains of the mammalian type I and type II enzymes. The soluble enzyme was stimulated by both forskolin and the alpha subunit of the heterotrimeric guanine nucleotide-binding protein (G protein) Gs (Gs alpha). Expression of the construct complemented the catabolic defect in a strain of Escherichia coli that is deficient in adenylyl cyclase activity. The active, approximately 60-kilodalton enzyme accumulated in the cytoplasmic fraction of E. coli to yield activities in excess of 1 nanomole per minute per milligram of protein. The two sets of transmembrane helices of mammalian adenylyl cyclases are thus not necessary for the catalytic or the most characteristic regulatory activities of the enzyme. This system may be useful for both genetic and biochemical analysis of G protein-regulated adenylyl cyclases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tang, W J -- Gilman, A G -- GM34497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jun 23;268(5218):1769-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7792604" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/chemistry/*metabolism ; Amino Acid Sequence ; Base Sequence ; Colforsin/*pharmacology ; Cyclic AMP/metabolism ; Cytoplasm/enzymology ; Enzyme Activation ; Escherichia coli/enzymology ; GTP-Binding Proteins/chemistry/genetics/*physiology ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Molecular Sequence Data ; Solubility ; Transformation, Genetic
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  • 61
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    Identification of a dual specificity kinase that activates the Jun kinases and p38-Mpk2 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-14
    Description: One Ras-dependent protein kinase cascade leading from growth factor receptors to the ERK (extracellular signal-regulated kinases) subgroup of mitogen-activated protein kinases (MAPKs) is dependent on the protein kinase Raf-1, which activates the MEK (MAPK or ERK kinase) dual specificity kinases. A second protein kinase cascade leading to activation of the Jun kinases (JNKs) is dependent on MEKK (MEK kinase). A dual-specificity kinase that activates JNK, named JNKK, was identified that functions between MEKK and JNK. JNKK activated the JNKs but did not activate the ERKs and was unresponsive to Raf-1 in transfected HeLa cells. JNKK also activated another MAPK, p38 (Mpk2; the mammalian homolog of HOG1 from yeast), whose activity is regulated similarly to that of the JNKs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, A -- Minden, A -- Martinetto, H -- Claret, F X -- Lange-Carter, C -- Mercurio, F -- Johnson, G L -- Karin, M -- New York, N.Y. -- Science. 1995 Apr 14;268(5208):286-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California-San Diego School of Medicine, La Jolla 92093-0636, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716521" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Line ; Enzyme Activation ; Epidermal Growth Factor/pharmacology ; HeLa Cells ; Humans ; JNK Mitogen-Activated Protein Kinases ; MAP Kinase Kinase 4 ; *MAP Kinase Kinase Kinase 1 ; *Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Phosphorylation ; Protein Kinases/chemistry/*metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-raf ; Recombinant Fusion Proteins/metabolism ; Substrate Specificity ; Transfection ; p38 Mitogen-Activated Protein Kinases
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  • 62
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    Minimization of a polypeptide hormone (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-08
    Description: A stepwise approach for reducing the size of a polypeptide hormone, atrial natriuretic peptide (ANP), from 28 residues to 15 while retaining high biopotency is described. Systematic structural and functional analysis identified a discontinuous functional epitope for receptor binding and activation, most of which was placed onto a smaller ring (Cys6 to Cys17) that was created by repositioning the ANP native disulfide bond (Cys7 to Cys23). High affinity was subsequently restored by optimizing the remaining noncritical residues by means of phage display. Residues that flanked the mini-ring structure were then deleted in stages, and affinity losses were rectified by additional phage-sorting experiments. Thus, structural and functional data on hormones, coupled with phage display methods, can be used to shrink the hormones to moieties more amendable to small-molecule design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, B -- Tom, J Y -- Oare, D -- Yen, R -- Fairbrother, W J -- Wells, J A -- Cunningham, B C -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1657-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Protein Engineering, Genenteeh, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502074" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Atrial Natriuretic Factor/*chemistry/genetics/immunology/metabolism ; Base Sequence ; Cell Line ; Cyclic GMP/metabolism ; Epitopes ; Guanylate Cyclase/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Conformation ; *Protein Engineering ; Receptors, Atrial Natriuretic Factor/metabolism
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    Induction of apoptosis in uninfected lymphocytes by HIV-1 Tat protein (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-21
    Description: Infection by human immunodeficiency virus-type 1 (HIV-1) is typified by the progressive depletion of CD4 T lymphocytes and deterioration of immune function in most patients. A central unresolved issue in acquired immunodeficiency syndrome (AIDS) pathogenesis is the mechanism underlying this T cell depletion. HIV-1 Tat protein was shown to induce cell death by apoptosis in a T cell line and in cultured peripheral blood mononuclear cells from uninfected donors. This Tat-induced apoptosis was inhibitable by growth factors and was associated with enhanced activation of cyclin-dependent kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, C J -- Friedman, D J -- Wang, C -- Metelev, V -- Pardee, A B -- AI-35511/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 21;268(5209):429-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cell Growth and Regulation, Dana-Farber Cancer Institute, Boston, MA, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716549" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Base Sequence ; *CDC2-CDC28 Kinases ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinases/metabolism ; Enzyme Activation ; Gene Products, tat/pharmacology/*physiology ; Genes, tat ; *Hiv-1 ; Humans ; Leukocytes, Mononuclear/*cytology/enzymology ; Molecular Sequence Data ; Protein-Serine-Threonine Kinases/metabolism ; Recombinant Proteins/pharmacology ; T-Lymphocytes/*cytology/enzymology ; Transfection ; Tumor Cells, Cultured ; tat Gene Products, Human Immunodeficiency Virus
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acids (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-24
    Description: Mandelate racemase and muconate lactonizing enzyme are structurally homologous but catalyze different reactions, each initiated by proton abstraction from carbon. The structural similarity to mandelate racemase of a previously unidentified gene product was used to deduce its function as a galactonate dehydratase. In this enzyme superfamily that has evolved to catalyze proton abstraction from carbon, three variations of homologous active site architectures are now represented: lysine and histidine bases in the active site of mandelate racemase, only a lysine base in the active site of muconate lactonizing enzyme, and only a histidine base in the active site of galactonate dehydratase. This discovery supports the hypothesis that new enzymatic activities evolve by recruitment of a protein catalyzing the same type of chemical reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Babbitt, P C -- Mrachko, G T -- Hasson, M S -- Huisman, G W -- Kolter, R -- Ringe, D -- Petsko, G A -- Kenyon, G L -- Gerlt, J A -- GM-34572/GM/NIGMS NIH HHS/ -- GM-40570/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1159-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855594" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Histidine/metabolism ; Hydro-Lyases/chemistry/genetics/*metabolism ; *Intramolecular Lyases ; Isomerases/chemistry/*metabolism ; Lysine/metabolism ; Molecular Sequence Data ; Open Reading Frames ; Operon ; *Protons ; Pseudomonas putida/*enzymology/genetics ; Racemases and Epimerases/chemistry/*metabolism
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    FAP-1: a protein tyrosine phosphatase that associates with Fas (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-21
    Description: Fas is a cell surface receptor that controls a poorly understood signal transduction pathway that leads to cell death by means of apoptosis. A protein tyrosine phosphatase, FAP-1, capable of interacting with the cytosolic domain of Fas, was identified. The carboxyl terminal 15 amino acids of Fas are necessary and sufficient for interaction with FAP-1. FAP-1 expression is highest in tissues and cell lines that are relatively resistant to Fas-mediated cytotoxicity. Gene transfer-mediated elevations in FAP-1 partially abolished Fas-induced apoptosis in a T cell line. These findings are consistent with an inhibitory effect of FAP-1 on Fas signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sato, T -- Irie, S -- Kitada, S -- Reed, J C -- New York, N.Y. -- Science. 1995 Apr 21;268(5209):411-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉La Jolla Cancer Research Foundation, Oncogene and Tumor Suppressor Gene Program, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7536343" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD95 ; Antigens, Surface/genetics/*metabolism ; Apoptosis ; Base Sequence ; Cell Line ; Cloning, Molecular ; DNA, Complementary/genetics ; Humans ; Mice ; Molecular Sequence Data ; Protein Tyrosine Phosphatases/genetics/*metabolism ; Receptors, Cell Surface/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; T-Lymphocytes/cytology
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    A human telomeric protein (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-08
    Description: Telomeres are multifunctional elements that shield chromosome ends from degradation and end-to-end fusions, prevent activation of DNA damage checkpoints, and modulate the maintenance of telomeric DNA by telomerase. A major protein component of human telomeres has been identified and cloned. This factor, TRF, contains one Myb-type DNA-binding repeat and an amino-terminal acidic domain. Immunofluorescent labeling shows that TRF specifically colocalizes with telomeric DNA in human interphase cells and is located at chromosome ends during metaphase. The presence of TRF along the telomeric TTAGGG repeat array demonstrates that human telomeres form a specialized nucleoprotein complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chong, L -- van Steensel, B -- Broccoli, D -- Erdjument-Bromage, H -- Hanish, J -- Tempst, P -- de Lange, T -- GM49046/GM/NIGMS NIH HHS/ -- P30 CA08748-29/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1663-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Cell Biology and Genetics, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502076" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Nucleus/chemistry ; Cloning, Molecular ; DNA-Binding Proteins/analysis/*chemistry/genetics/isolation & purification ; HeLa Cells ; Humans ; Interphase ; Metaphase ; Molecular Sequence Data ; Molecular Weight ; Repetitive Sequences, Nucleic Acid ; Sequence Alignment ; Telomere/*chemistry ; Transfection
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    Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-08
    Description: The Elongin (SIII) complex activates elongation by mammalian RNA polymerase II by suppressing transient pausing of the polymerase at many sites within transcription units. Elongin is a heterotrimer composed of A, B, and C subunits of 110, 18, and 15 kilodaltons, respectively. Here, the mammalian Elongin A gene was isolated and expressed, and the Elongin (SIII) complex reconstituted with recombinant subunits. Elongin A is shown to function as the transcriptionally active component of Elongin (SIII) and Elongin B and C as regulatory subunits. Whereas Elongin C assembles with Elongin A to form an AC complex with increased specific activity, Elongin B, a member of the ubiquitin-homology gene family, appears to serve a chaperone-like function, facilitating assembly and enhancing stability of the Elongin (SIII) complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aso, T -- Lane, W S -- Conaway, J W -- Conaway, R C -- GM41628/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1439-43.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular and Cell Biology, Oklahoma Medical Research Foundation, Oklahoma City 73104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660129" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Genes, Tumor Suppressor ; *Ligases ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; RNA Polymerase II/*metabolism ; RNA, Messenger/biosynthesis ; Recombinant Proteins/metabolism ; Temperature ; Transcription Factors/chemistry/genetics/isolation & purification/*metabolism ; *Transcription, Genetic ; *Tumor Suppressor Proteins ; *Ubiquitin-Protein Ligases ; Von Hippel-Lindau Tumor Suppressor Protein
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    Structure of Bam HI endonuclease bound to DNA: partial folding and unfolding on DNA binding (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-04
    Description: The crystal structure of restriction endonuclease Bam HI complexed to DNA has been determined at 2.2 angstrom resolution. The DNA binds in the cleft and retains a B-DNA type of conformation. The enzyme, however, undergoes a series of conformational changes, including rotation of subunits and folding of disordered regions. The most striking conformational change is the unraveling of carboxyl-terminal alpha helices to form partially disordered "arms." The arm from one subunit fits into the minor groove while the arm from the symmetry related subunit follows the DNA sugar-phosphate backbone. Recognition of DNA base pairs occurs primarily in the major groove, with a few interactions occurring in the minor groove. Tightly bound water molecules play an equally important role as side chain and main chain atoms in the recognition of base pairs. The complex also provides new insights into the mechanism by which the enzyme catalyzes the hydrolysis of DNA phosphodiester groups.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newman, M -- Strzelecka, T -- Dorner, L F -- Schildkraut, I -- Aggarwal, A K -- GM-44006/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Aug 4;269(5224):656-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624794" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Binding Sites ; Catalysis ; Computer Graphics ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; Deoxyribonuclease BamHI/*chemistry/*metabolism ; Deoxyribonuclease EcoRI/chemistry ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Conformation ; *Protein Folding ; Protein Structure, Secondary
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    Bent helix formation between RNA hairpins with complementary loops (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-09
    Description: The initial interaction between the ColE1 plasmid specific transcripts RNA I and RNA II, which function as antisense regulators of plasmid replication, comprises a transient complex between complementary loops found within the RNA secondary structures. Multidimensional heteronuclear magnetic resonance spectroscopy was used to characterize complexes formed between model RNA hairpins having seven nucleotide complementary loops. Seven base pairs are formed in the loop-loop helix, with continuous helical stacking of the loop residues on the 3' side of their helical stems. A sharp bend in the loop-loop helix, documented by gel electrophoresis, narrows the major groove and allows bridging of the phosphodiester backbones across the major groove in order to close the hairpin loops at their 5'-ends. The bend is further enhanced by the binding of Rom, a ColE1 encoded protein that regulates replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marino, J P -- Gregorian, R S Jr -- Csankovszki, G -- Crothers, D M -- GM 21966/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jun 9;268(5216):1448-54.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Yale University, New Haven, CT 06511, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7539549" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/chemistry/metabolism ; Bacteriocin Plasmids/*genetics ; Base Composition ; Base Sequence ; Computer Graphics ; Electrophoresis, Polyacrylamide Gel ; Helix-Loop-Helix Motifs ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Protein Structure, Secondary ; RNA/*chemistry/metabolism ; RNA, Bacterial/*chemistry/metabolism
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    Stable transfection of malaria parasite blood stages (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-02
    Description: Genetic manipulation of malaria parasites would revolutionize the study of this group of pathogens and have implications for vaccine and drug development. This report describes the stable, drug-selectable genetic transformation of the clinically relevant intracellular blood stages of a malaria parasite. A plasmid transfection vector carrying the gene locus that encodes a drug-resistant form of the bifunctional enzyme dihydrofolate reductase-thymidylate synthase from the rodent malaria parasite Plasmodium berghei was constructed. Derivatives of this vector were introduced into merozoites of P. berghei by electroporation, and parasites were selected for successful transformation in the rodent host on the basis of resistance to pyrimethamine. The plasmids were present in a circular, unrearranged form that replicated episomally to an observed maximum of 15 copies per cell in drug-resistant populations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van Dijk, M R -- Waters, A P -- Janse, C J -- New York, N.Y. -- Science. 1995 Jun 2;268(5215):1358-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Parasitology, University of Leiden, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7761856" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA Replication ; Drug Resistance ; Electroporation ; Erythrocytes/parasitology ; Genes, Protozoan ; Genetic Vectors ; Molecular Sequence Data ; Multienzyme Complexes/*genetics ; Plasmids ; Plasmodium berghei/drug effects/*genetics/growth & development ; Point Mutation ; Pyrimethamine/*pharmacology ; Rats ; Rats, Wistar ; Replication Origin ; Tetrahydrofolate Dehydrogenase/*genetics ; Thymidylate Synthase/*genetics ; *Transfection
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    The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-22
    Description: Hydrolysis of guanosine triphosphate (GTP) by the small guanosine triphosphatase (GTPase) adenosine diphosphate ribosylation factor-1 (ARF1) depends on a GTPase-activating protein (GAP). A complementary DNA encoding the ARF1 GAP was cloned from rat liver and predicts a protein with a zinc finger motif near the amino terminus. The GAP function required an intact zinc finger and additional amino-terminal residues. The ARF1 GAP was localized to the Golgi complex and was redistributed into a cytosolic pattern when cells were treated with brefeldin A, a drug that prevents ARF1-dependent association of coat proteins with the Golgi. Thus, the GAP is likely to be recruited to the Golgi by an ARF1-dependent mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cukierman, E -- Huber, I -- Rotman, M -- Cassel, D -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):1999-2002.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Technion-Israel Institute of Technology, Haifa, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533093" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factor 1 ; ADP-Ribosylation Factors ; Alternative Splicing ; Amino Acid Sequence ; Animals ; Base Sequence ; Brefeldin A ; Cloning, Molecular ; Cyclopentanes/pharmacology ; Cytosol/metabolism ; DNA, Complementary ; GTP-Binding Proteins/*metabolism ; GTPase-Activating Proteins ; Golgi Apparatus/*metabolism ; Guanosine Triphosphate/metabolism ; Liver/metabolism ; Molecular Sequence Data ; Proteins/chemistry/genetics/isolation & purification/*metabolism ; Rats ; *Zinc Fingers
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    Mismatch repair deficiency in phenotypically normal human cells (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-05
    Description: Tumor cells in patients with hereditary nonpolyposis colorectal cancer (HNPCC) are characterized by a genetic hypermutability caused by defects in DNA mismatch repair. A subset of HNPCC patients was found to have widespread mutations not only in their tumors, but also in their non-neoplastic cells. Although these patients had numerous mutations in all tissues examined, they had very few tumors. The hypermutability was associated with a profound defect in mismatch repair at the biochemical level. These results have implications for the relation between mutagenesis and carcinogenesis, and they suggest that mismatch repair deficiency is compatible with normal human development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parsons, R -- Li, G M -- Longley, M -- Modrich, P -- Liu, B -- Berk, T -- Hamilton, S R -- Kinzler, K W -- Vogelstein, B -- CA35494/CA/NCI NIH HHS/ -- CA62924/CA/NCI NIH HHS/ -- GM45190/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 May 5;268(5211):738-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johns Hopkins Oncology Center, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7632227" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Line, Transformed ; Clone Cells ; Colorectal Neoplasms, Hereditary Nonpolyposis/*genetics ; DNA Repair/*genetics ; DNA, Satellite/analysis ; Humans ; Intestinal Mucosa/chemistry ; Lymphocytes/chemistry ; Molecular Sequence Data ; Mutation ; Phenotype ; Repetitive Sequences, Nucleic Acid
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    An ethylene-inducible component of signal transduction encoded by never-ripe (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-15
    Description: The ripening-impaired tomato mutant Never-ripe (Nr) is insensitive to the plant hormone ethylene. The gene that cosegregates with the Nr locus encodes a protein with homology to the Arabidopsis ethylene receptor ETR1 but is lacking the response regulator domain found in ETR1 and related prokaryotic two-component signal transducers. A single amino acid change in the sensor domain confers ethylene insensitivity when expressed in transgenic tomato plants. Modulation of NR gene expression during fruit ripening controls response to the hormone ethylene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilkinson, J Q -- Lanahan, M B -- Yen, H C -- Giovannoni, J J -- Klee, H J -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1807-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Monsanto Company, Chesterfield, MO 63198, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525371" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/genetics ; Base Sequence ; DNA Primers ; Ethylenes/*metabolism ; Genes, Plant ; Lycopersicon esculentum/*genetics/growth & development/metabolism ; Molecular Sequence Data ; Mutation ; Plant Proteins/*genetics/metabolism ; *Receptors, Cell Surface ; Sequence Homology, Amino Acid ; *Signal Transduction
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    A subclass of bHLH proteins required for cardiac morphogenesis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-22
    Description: Skeletal muscle development is controlled by a family of muscle-specific basic helix-loop-helix (bHLH) transcription factors. Two bHLH genes, dHAND and eHAND, have now been isolated that are expressed in the bilateral heart primordia and subsequently throughout the primitive tubular heart and its derivatives during chick and mouse embryogenesis. Incubation of stage 8 chick embryos with dHAND and eHAND antisense oligonucleotides revealed that either oligonucleotide alone had no effect on embryonic development, whereas together they arrested development at the looping heart tube stage. Thus, dHAND and eHAND may play redundant roles in the regulation of the morphogenetic events of vertebrate heart development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Srivastava, D -- Cserjesi, P -- Olson, E N -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):1995-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Texas M. D. Anderson Cancer Center, Houston 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533092" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Amino Acid Sequence ; Animals ; Base Sequence ; Basic Helix-Loop-Helix Transcription Factors ; Cardiovascular System/embryology/metabolism ; Chick Embryo ; DNA-Binding Proteins/biosynthesis/chemistry/*genetics/physiology ; Embryonic and Fetal Development ; Gene Expression ; Heart/*embryology ; *Helix-Loop-Helix Motifs ; In Situ Hybridization ; MEF2 Transcription Factors ; Mesoderm/metabolism ; Mice ; Molecular Sequence Data ; Morphogenesis ; Myocardium/metabolism ; *Myogenic Regulatory Factors ; Oligonucleotides, Antisense/pharmacology ; Transcription Factors/biosynthesis/chemistry/*genetics/physiology ; Zebrafish Proteins
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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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    Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: The Tat protein of bovine immunodeficiency virus (BIV) binds to its target RNA, TAR, and activates transcription. A 14-amino acid arginine-rich peptide corresponding to the RNA-binding domain of BIV Tat binds specifically to BIV TAR, and biochemical and in vivo experiments have identified the amino acids and nucleotides required for binding. The solution structure of the RNA-peptide complex has now been determined by nuclear magnetic resonance spectroscopy. TAR forms a virtually continuous A-form helix with two unstacked bulged nucleotides. The peptide adopts a beta-turn conformation and sits in the major groove of the RNA. Specific contacts are apparent between critical amino acids in the peptide and bases and phosphates in the RNA. The structure is consistent with all biochemical data and demonstrates ways in which proteins can recognize the major groove of RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Puglisi, J D -- Chen, L -- Blanchard, S -- Frankel, A D -- AI08591/AI/NIAID NIH HHS/ -- AI29135/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1200-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, Santa Cruz 95064, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502045" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Composition ; Base Sequence ; Gene Products, tat/*chemistry/metabolism ; Hydrogen Bonding ; Immunodeficiency Virus, Bovine/*chemistry ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Secondary ; RNA, Viral/*chemistry/metabolism
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  • 76
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    The TBP-TFIIA interaction in the response to acidic activators in vivo (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-07
    Description: A yeast TBP mutant (N2-1) is described here that is defective specifically in responding to acidic activators in vivo. N2-1 does not support activation by Gal4, Ace1, and Gcn4, but appears unaffected for constitutive transcription, repression by the Cyc8-Tup1 and Not complexes, and transcription by polymerase I (Pol) and Pol III. In vitro, N2-1 fails to interact with TFIIA, but it associates normally with a TATA element, an acidic activation domain, and TFIIB. Fusion of the small subunit of TFIIA to N2-1 restores activation function in vivo. Thus, an efficient interaction between TBP and TFIIA is required for transcriptional activation in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stargell, L A -- Struhl, K -- GM30186/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):75-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604282" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA-Binding Proteins/genetics/*metabolism/physiology ; DNA-Directed RNA Polymerases/metabolism ; Fungal Proteins/physiology ; Hydrogen-Ion Concentration ; Immediate-Early Proteins/physiology ; Molecular Sequence Data ; Mutation ; *Nuclear Proteins ; Nuclear Receptor Subfamily 4, Group A, Member 2 ; Protein Kinases/physiology ; *Repressor Proteins ; Saccharomyces cerevisiae/*genetics/growth & development ; *Saccharomyces cerevisiae Proteins ; *TATA Box ; TATA-Box Binding Protein ; Trans-Activators/*physiology ; Transcription Factor TFIIA ; Transcription Factors/genetics/*metabolism/physiology ; *Transcriptional Activation
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  • 77
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    Early-onset epilepsy and postnatal lethality associated with an editing-deficient GluR-B allele in mice (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-12-08
    Description: The arginine residue at position 586 of the GluR-B subunit renders heteromeric alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA)-sensitive glutamate receptor channels impermeable to calcium. The codon for this arginine is introduced at the precursor messenger RNA (pre-mRNA) stage by site-selective adenosine editing of a glutamine codon. Heterozygous mice engineered by gene targeting to harbor an editing-incompetent GluR-B allele synthesized unedited GluR-B subunits and, in principal neurons and interneurons, expressed AMPA receptors with increased calcium permeability. These mice developed seizures and died by 3 weeks of age, showing that GluR-B pre-mRNA editing is essential for brain function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brusa, R -- Zimmermann, F -- Koh, D S -- Feldmeyer, D -- Gass, P -- Seeburg, P H -- Sprengel, R -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1677-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neuroendocrinology, University of Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502080" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; Calcium/metabolism ; Epilepsy/*genetics/pathology ; Gene Targeting ; Glutamic Acid/metabolism ; Heterozygote ; Hippocampus/pathology ; In Situ Hybridization ; Male ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Nerve Degeneration ; Neurons/*metabolism ; Polymerase Chain Reaction ; Purkinje Cells/metabolism ; Pyramidal Cells/metabolism ; *RNA Editing ; RNA Precursors/genetics/metabolism ; Receptors, AMPA/chemistry/*genetics/metabolism
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  • 78
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    Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-02-03
    Description: Mammalian mitogen-activated protein (MAP) kinases include extracellular signal-regulated protein kinase (ERK), c-Jun amino-terminal kinase (JNK), and p38 subgroups. These MAP kinase isoforms are activated by dual phosphorylation on threonine and tyrosine. Two human MAP kinase kinases (MKK3 and MKK4) were cloned that phosphorylate and activate p38 MAP kinase. These MKK isoforms did not activate the ERK subgroup of MAP kinases, but MKK4 did activate JNK. These data demonstrate that the activators of p38 (MKK3 and MKK4), JNK (MKK4), and ERK (MEK1 and MEK2) define independent MAP kinase signal transduction pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Derijard, B -- Raingeaud, J -- Barrett, T -- Wu, I H -- Han, J -- Ulevitch, R J -- Davis, R J -- AI15136/AI/NIAID NIH HHS/ -- CA58396/CA/NCI NIH HHS/ -- GM37696/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 3;267(5198):682-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester 01605.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7839144" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Line ; Cloning, Molecular ; Enzyme Activation ; Humans ; JNK Mitogen-Activated Protein Kinases ; MAP Kinase Kinase 3 ; *MAP Kinase Kinase 4 ; Mitogen-Activated Protein Kinase 1 ; *Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Phosphorylation ; Protein-Serine-Threonine Kinases/chemistry/*metabolism ; Protein-Tyrosine Kinases/chemistry/*metabolism ; *Signal Transduction ; Substrate Specificity ; Transfection ; p38 Mitogen-Activated Protein Kinases
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  • 79
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    A specialized pathway affecting virulence glycoconjugates of Leishmania (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-29
    Description: For virulence and transmission, the protozoan parasite Leishmania must assemble a complex glycolipid on the cell surface, the lipophosphoglycan (LPG). Functional complementation identified the gene LPG2, which encodes an integral Golgi membrane protein implicated in intracellular compartmentalization of LPG biosynthesis. Ipg2- mutants lack only characteristic disaccharide-phosphate repeats, normally present on both LPG and other surface or secreted molecules considered critical for infectivity. In contrast, a related yeast gene, VAN2/VRG4, is essential and required for general Golgi function. These results suggest that LPG2 participates in a specialized virulence pathway, which may offer an attractive target for chemotherapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Descoteaux, A -- Luo, Y -- Turco, S J -- Beverley, S M -- AI31078/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 29;269(5232):1869-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569927" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carbohydrate Sequence ; Cell Compartmentation ; Genes, Fungal ; *Genes, Protozoan ; Genetic Complementation Test ; Glycosphingolipids/*biosynthesis/chemistry/genetics/*physiology ; Glycosylation ; Golgi Apparatus/*metabolism ; Leishmania donovani/genetics/metabolism/*pathogenicity ; Membrane Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Protozoan Proteins/chemistry/genetics/*physiology ; Virulence/genetics ; Yeasts/genetics
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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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    Cytotoxic T lymphocyte lysis inhibited by viable HIV mutants (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-24
    Description: Immune evasion by the human immunodeficiency virus (HIV) is unexplained but may involve the mutation of viral antigens. When cytotoxic T lymphocytes engaged CD4-positive cells that were acutely infected with HIV bearing natural variant epitopes in reverse transcriptase, substantial inhibition of specific antiviral lysis was observed. Mutant viruses capable of these transactive effects could facilitate the persistence of a broad range of HIV variants in the face of an active and specific immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meier, U C -- Klenerman, P -- Griffin, P -- James, W -- Koppe, B -- Larder, B -- McMichael, A -- Phillips, R -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1995 Nov 24;270(5240):1360-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nuffield Department of Clinical Medicine, John Radcliffe Hospital, Headington, Oxford, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481824" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigenic Variation ; Base Sequence ; CD4-Positive T-Lymphocytes/immunology/virology ; Cell Line ; *Cytotoxicity, Immunologic ; Epitopes/genetics ; HIV Antigens/genetics/*immunology ; HIV Reverse Transcriptase ; HIV-1/enzymology/genetics/*immunology ; HLA-B8 Antigen/immunology ; Humans ; *Immune Tolerance ; Molecular Sequence Data ; RNA-Directed DNA Polymerase/genetics/*immunology ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes, Cytotoxic/*immunology
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  • 81
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    Pathogenicity of live, attenuated SIV after mucosal infection of neonatal macaques (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-03-24
    Description: Adult macaques do not develop disease after infection with a nef deletion mutant of the simian immunodeficiency virus (SIV) and are protected against challenge with pathogenic virus. This finding led to the proposal to use nef-deleted viruses as live, attenuated vaccines to prevent human acquired immunodeficiency syndrome (AIDS). In contrast, neonatal macaques developed persistently high levels of viremia after oral exposure to and SIV nef, vpr, and negative regulatory element (NRE) deletion mutant. Severe hemolytic anemia, thrombocytopenia, and CD4+ T cell depletion were observed, indicating that neither nef nor vpr determine pathogenicity in neonates. Because such constructs have retained their pathogenic potential, they should not be used as candidate live, attenuated virus vaccines against human AIDS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baba, T W -- Jeong, Y S -- Pennick, D -- Bronson, R -- Greene, M F -- Ruprecht, R M -- R01-A132330/PHS HHS/ -- R01-A135533/PHS HHS/ -- New York, N.Y. -- Science. 1995 Mar 24;267(5205):1820-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Tufts University School of Medicine, Boston, MA 02111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7892606" target="_blank"〉PubMed〈/a〉
    Keywords: *AIDS Vaccines/adverse effects/genetics/immunology ; Administration, Oral ; Animals ; Animals, Newborn/*immunology/virology ; Base Sequence ; Gene Products, nef/genetics ; Gene Products, vpr/genetics ; Macaca mulatta/immunology ; Molecular Sequence Data ; Mucous Membrane/immunology ; Regulatory Sequences, Nucleic Acid/genetics ; Simian Acquired Immunodeficiency Syndrome/immunology/*prevention & ; control/*transmission ; Simian Immunodeficiency Virus/genetics/immunology/*pathogenicity ; Vaccines, Attenuated/adverse effects/immunology ; Virus Replication/genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 82
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    Assessing molecular phylogenies (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-01-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nei, M -- Takezaki, N -- Sitnikova, T -- GM20293-23/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 13;267(5195):253-4; author reply 255-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809633" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Biological Evolution ; Computer Simulation ; DNA/genetics ; Models, Statistical ; *Phylogeny ; Probability
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  • 83
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    A role for exonuclease I from S. pombe in mutation avoidance and mismatch correction (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-02-24
    Description: Exonuclease I (Exo I) from Schizosaccharomyces pombe, a 5'--〉3' double-stranded DNA exonuclease, is induced during meiotic prophase I. The exo1 gene is a member of a family of related DNA repair genes, including RAD2/rad13/xpgc and YKL510/rad2, conserved from yeast to humans. An exo1 mutant displays a mutator phenotype and alters activity of the ade6-M387 marker effect. These results suggest that Exo I acts in a pathway that corrects mismatched base pairs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Szankasi, P -- Smith, G R -- GM32194/GM/NIGMS NIH HHS/ -- P30 CA15704-20/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1166-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855597" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Base Composition ; Base Sequence ; Crosses, Genetic ; *DNA Repair ; DNA Replication ; DNA, Fungal/*metabolism ; Exodeoxyribonucleases/chemistry/genetics/*metabolism ; Meiosis ; Molecular Sequence Data ; *Mutation ; Recombination, Genetic ; Schizosaccharomyces/enzymology/*genetics/physiology
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  • 84
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    Mutations in the dystrophin-associated protein gamma-sarcoglycan in chromosome 13 muscular dystrophy (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-11-03
    Description: Severe childhood autosomal recessive muscular dystrophy (SCARMD) is a progressive muscle-wasting disorder common in North Africa that segregates with microsatellite markers at chromosome 13q12. Here, it is shown that a mutation in the gene encoding the 35-kilodalton dystrophin-associated glycoprotein, gamma-sarcoglycan, is likely to be the primary genetic defect in this disorder. The human gamma-sarcoglycan gene was mapped to chromosome 13q12, and deletions that alter its reading frame were identified in three families and one of four sporadic cases of SCARMD. These mutations not only affect gamma-sarcoglycan but also disrupt the integrity of the entire sarcoglycan complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noguchi, S -- McNally, E M -- Ben Othmane, K -- Hagiwara, Y -- Mizuno, Y -- Yoshida, M -- Yamamoto, H -- Bonnemann, C G -- Gussoni, E -- Denton, P H -- Kyriakides, T -- Middleton, L -- Hentati, F -- Ben Hamida, M -- Nonaka, I -- Vance, J M -- Kunkel, L M -- Ozawa, E -- NS23740/NS/NINDS NIH HHS/ -- P01-NS26630/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):819-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Neuroscience, National Center for Neurology and Psychiatry, Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481775" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; *Chromosomes, Human, Pair 13 ; *Cytoskeletal Proteins ; DNA, Complementary/genetics ; Dystrophin/chemistry/genetics/metabolism ; Humans ; Linkage Disequilibrium ; Membrane Glycoproteins/chemistry/*genetics/metabolism ; Molecular Sequence Data ; Molecular Weight ; Muscle, Skeletal/chemistry/metabolism ; Muscular Dystrophies/*genetics ; Mutation ; Phenotype ; Rabbits ; Sarcoglycans ; Sequence Deletion
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  • 85
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    Head-on collision between a DNA replication apparatus and RNA polymerase transcription complex (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-02-24
    Description: An in vitro system reconstituted from purified proteins has been used to examine what happens when the DNA replication apparatus of bacteriophage T4 collides with an Escherichia coli RNA polymerase ternary transcription complex that is poised to move in the direction opposite to that of the moving replication fork. In the absence of a DNA helicase, the replication fork stalls for many minutes after its encounter with the RNA polymerase. However, when the T4 gene 41 DNA helicase is present, the replication fork passes the RNA polymerase after a pause of a few seconds. This brief pause is longer than the pause observed for a codirectional collision between the same two polymerases, suggesting that there is an inherent disadvantage to having replication and transcription directions oriented head to head. As for a codirectional collision, the RNA polymerase remains competent to resume faithful RNA chain elongation after the DNA replication fork passes; most strikingly, the RNA polymerase has switched from its original template strand to use the newly synthesized daughter DNA strand as the template.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, B -- Alberts, B M -- GM-24020/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1131-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855590" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage T4 ; Base Sequence ; DNA Helicases/metabolism ; *DNA Replication ; DNA, Bacterial/genetics/metabolism ; DNA, Circular/metabolism ; DNA, Viral/biosynthesis/genetics ; DNA-Directed DNA Polymerase/metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Escherichia coli ; Molecular Sequence Data ; RNA, Messenger/*biosynthesis ; Replicon/*physiology ; Templates, Genetic ; *Transcription, Genetic
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  • 86
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    Requirement of MIP-1 alpha for an inflammatory response to viral infection (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-15
    Description: Macrophage inflammatory protein-1 alpha (MIP-1 alpha) is a chemokine that has pro-inflammatory and stem cell inhibitory activities in vitro. Its biologic role in vivo was examined in mice in which the gene encoding MIP-1 alpha had been disrupted. Homozygous MIP-1 alpha mutant (-/-) mice were resistant to Coxsackievirus-induced myocarditis seen in infected wild-type (+/+) mice. Influenza virus-infected -/- mice had reduced pneumonitis and delayed clearance of the virus compared with infected +/+ mice. The -/- mice had no overt hematopoietic abnormalities. These results demonstrate that MIP-1 alpha is an important mediator of virus-induced inflammation in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cook, D N -- Beck, M A -- Coffman, T M -- Kirby, S L -- Sheridan, J F -- Pragnell, I B -- Smithies, O -- GM20069/GM/NIGMS NIH HHS/ -- HL37001/HL/NHLBI NIH HHS/ -- R29HL46195/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 15;269(5230):1583-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of North Carolina, Chapel Hill 27599-7525, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7667639" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Viral/blood ; B-Lymphocytes/immunology ; Base Sequence ; Chemokine CCL4 ; Coxsackievirus Infections/*immunology/virology ; Cytokines/genetics/*physiology ; *Enterovirus B, Human/growth & development/immunology ; Gene Targeting ; Hematopoiesis ; *Influenza A virus/growth & development/immunology ; Lymphocyte Activation ; Macrophage Inflammatory Proteins ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Monokines/genetics/*physiology ; Myocarditis/*immunology/virology ; Neutralization Tests ; Orthomyxoviridae Infections/*immunology/virology ; Stem Cells ; T-Lymphocytes/immunology
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  • 87
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    An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-01
    Description: Members of the Rho family of small guanosine triphosphatases (GTPases) regulate the organization of the actin cytoskeleton; Rho controls the assembly of actin stress fibers and focal adhesion complexes, Rac regulates actin filament accumulation at the plasma membrane to produce lamellipodia and membrane ruffles, and Cdc42 stimulates the formation of filopodia. When microinjected into quiescent fibroblasts, Rho, Rac, and Cdc42 stimulated cell cycle progression through G1 and subsequent DNA synthesis. Furthermore, microinjection of dominant negative forms of Rac and Cdc42 or of the Rho inhibitor C3 transferase blocked serum-induced DNA synthesis. Unlike Ras, none of the Rho GTPases activated the mitogen-activated protein kinase (MAPK) cascade that contains the protein kinases c-Raf1, MEK (MAPK or ERK kinase), and ERK (extracellular signal-regulated kinase). Instead, Rac and Cdc42, but not Rho, stimulated a distinct MAP kinase, the c-Jun kinase JNK/SAPK (Jun NH2-terminal kinase or stress-activated protein kinase). Rho, Rac, and Cdc42 control signal transduction pathways that are essential for cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olson, M F -- Ashworth, A -- Hall, A -- New York, N.Y. -- Science. 1995 Sep 1;269(5228):1270-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University College, London, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7652575" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Base Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cell Cycle Proteins/*metabolism ; Cell Line ; DNA/biosynthesis ; *G1 Phase ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; JNK Mitogen-Activated Protein Kinases ; MAP Kinase Kinase 1 ; Mice ; Microinjections ; *Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-raf ; *Signal Transduction ; Transfection ; cdc42 GTP-Binding Protein, Saccharomyces cerevisiae ; rac GTP-Binding Proteins ; rhoA GTP-Binding Protein
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  • 88
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    Sequence and characterization of a coactivator for the steroid hormone receptor superfamily (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-24
    Description: A yeast two-hybrid system was used to identify a protein that interacts with and enhances the human progesterone receptor (hPR) transcriptional activity without altering the basal activity of the promoter. Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). Coexpression of SRC-1 reversed the ability of the estrogen receptor to squelch activation by hPR. Also, the amino terminal truncated form of SRC-1 acted as a dominant-negative repressor. Together, these results indicate that SRC-1 encodes a coactivator that is required for full transcriptional activity of the steroid receptor superfamily.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Onate, S A -- Tsai, S Y -- Tsai, M J -- O'Malley, B W -- HD08188/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 24;270(5240):1354-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481822" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cyclic AMP Response Element-Binding Protein/metabolism ; Gene Expression ; HeLa Cells ; Histone Acetyltransferases ; Hormone Antagonists/metabolism/pharmacology ; Humans ; Mifepristone/metabolism/pharmacology ; Molecular Sequence Data ; Nuclear Receptor Coactivator 1 ; Promegestone/pharmacology ; Receptors, Progesterone/*metabolism ; Receptors, Steroid/*metabolism ; Recombinant Fusion Proteins/metabolism ; Trans-Activators/*metabolism ; Transcription Factors/*chemistry/genetics/*metabolism ; *Transcriptional Activation ; Transfection
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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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    ILR1, an amidohydrolase that releases active indole-3-acetic acid from conjugates (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-23
    Description: In plants, the growth regulator indole-3-acetic acid (IAA) is found both free and conjugated to a variety of amino acids, peptides, and carbohydrates. IAA conjugated to leucine has effects in Arabidopsis thaliana similar to those of free IAA. The ilr1 mutant is insensitive to exogenous IAA-Leu and was used to positionally clone the Arabidopsis ILR1 gene. ILR1 encodes a 48-kilodalton protein that cleaves IAA-amino acid conjugates in vitro and is homologous to bacterial amidohydrolase enzymes. DNA sequences similar to that of ILR1 are found in other plant species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bartel, B -- Fink, G R -- New York, N.Y. -- Science. 1995 Jun 23;268(5218):1745-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7792599" target="_blank"〉PubMed〈/a〉
    Keywords: Amidohydrolases/chemistry/*genetics/metabolism ; Amino Acid Sequence ; Amino Acids ; Arabidopsis/enzymology/*genetics ; *Arabidopsis Proteins ; Base Sequence ; Cloning, Molecular ; *Genes, Plant ; Hydrolysis ; Indoleacetic Acids/*metabolism/pharmacology ; Leucine/metabolism ; Molecular Sequence Data ; Mutation ; Plant Growth Regulators/*metabolism ; Sequence Alignment
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  • 90
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    GTBP, a 160-kilodalton protein essential for mismatch-binding activity in human cells (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-30
    Description: DNA mismatch recognition and binding in human cells has been thought to be mediated by the hMSH2 protein. Here it is shown that the mismatch-binding factor consists of two distinct proteins, the 100-kilodalton hMSH2 and a 160-kilodalton polypeptide, GTBP (for G/T binding protein). Sequence analysis identified GTBP as a new member of the MutS homolog family. Both proteins are required for mismatch-specific binding, a result consistent with the finding that tumor-derived cell lines devoid of either protein are also devoid of mismatch-binding activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palombo, F -- Gallinari, P -- Iaccarino, I -- Lettieri, T -- Hughes, M -- D'Arrigo, A -- Truong, O -- Hsuan, J J -- Jiricny, J -- New York, N.Y. -- Science. 1995 Jun 30;268(5219):1912-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Istituto di Ricerche di Biologia Molecolare P. Angeletti, Pomezia, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604265" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Composition ; Base Sequence ; Cloning, Molecular ; Colorectal Neoplasms ; *DNA Repair/genetics ; DNA, Neoplasm/*metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; HeLa Cells ; Humans ; Molecular Sequence Data ; Molecular Weight ; Nucleic Acid Heteroduplexes/*metabolism ; Sequence Analysis ; Tumor Cells, Cultured
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  • 91
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    The development of crustacean limbs and the evolution of arthropods (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-24
    Description: Arthropods exhibit great diversity in the position, number, morphology, and function of their limbs. The evolutionary relations among limb types and among the arthropod groups that bear them (insects, crustaceans, myriapods, and chelicerates) are controversial. Here, the use of molecular probes, including an antibody to proteins encoded by arthropod and vertebrate Distal-less (Dll and Dlx) genes, provided evidence that common genetic mechanisms underlie the development of all arthropod limbs and their branches and that all arthropods derive from a common ancestor. However, differences between crustacean and insect body plans were found to correlate with differences in the deployment of particular homeotic genes and in the ways that these genes regulate limb development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Panganiban, G -- Sebring, A -- Nagy, L -- Carroll, S -- New York, N.Y. -- Science. 1995 Nov 24;270(5240):1363-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, University of Wisconsin, Madison 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481825" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Artemia/genetics/growth & development ; Arthropods/embryology/genetics/*growth & development ; Base Sequence ; *Biological Evolution ; Cell Differentiation ; Crustacea/embryology/genetics/*growth & development ; Decapoda (Crustacea)/embryology/genetics/growth & development ; Extremities/embryology/growth & development ; *Gene Expression Regulation, Developmental ; *Genes, Homeobox ; Homeodomain Proteins/genetics/immunology ; Molecular Sequence Data ; Morphogenesis
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  • 92
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    Age of bacteria from amber (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beckenbach, A T -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):2015-6; author reply 2016-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533098" target="_blank"〉PubMed〈/a〉
    Keywords: *Amber ; Bacillus/*genetics/isolation & purification ; Base Sequence ; DNA, Bacterial/*genetics ; Molecular Sequence Data ; RNA, Bacterial/genetics ; RNA, Ribosomal, 16S/genetics ; Sequence Alignment ; Sequence Analysis, DNA
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  • 93
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    Cleavage of an amide bond by a ribozyme (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-13
    Description: A variant form of a group I ribozyme, optimized by in vitro evolution for its ability to catalyze magnesium-dependent phosphoester transfer reactions involving DNA substrates, also catalyzes the cleavage of an unactivated alkyl amide when that linkage is presented in the context of an oligodeoxynucleotide analog. Substrates containing an amide bond that joins either two DNA oligos, or a DNA oligo and a short peptide, are cleaved in a magnesium-dependent fashion to generate the expected products. The first-order rate constant, kcat, is 0.1 x 10(-5) min-1 to 1 x 10(-5) min-1 for the DNA-flanked substrates, which corresponds to a rate acceleration of more than 10(3) as compared with the uncatalyzed reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dai, X -- De Mesmaeker, A -- Joyce, G F -- New York, N.Y. -- Science. 1995 Jan 13;267(5195):237-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809628" target="_blank"〉PubMed〈/a〉
    Keywords: Amides/*metabolism ; Animals ; Base Composition ; Base Sequence ; Kinetics ; Magnesium/metabolism ; Molecular Sequence Data ; Oligodeoxyribonucleotides/*metabolism ; Oligopeptides/metabolism ; RNA, Catalytic/*metabolism ; Tetrahymena/enzymology
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  • 94
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    Repositioning of a domain in a modular polyketide synthase to promote specific chain cleavage (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-09
    Description: Macrocyclic polyketides exhibit an impressive range of medically useful activities, and there is great interest in manipulating the genes that govern their synthesis. The 6-deoxyerythronolide B synthase (DEBS) of Saccharopolyspora erythraea, which synthesizes the aglycone core of the antibiotic erythromycin A, has been modified by repositioning of a chain-terminating cyclase domain to the carboxyl-terminus of DEBS1, the multienzyme that catalyzes the first two rounds of polyketide chain extension. The resulting mutant markedly accelerates formation of the predicted triketide lactone, compared to a control in which the repositioned domain is inactive. Repositioning of the cyclase should be generally useful for redirecting polyketide synthesis to obtain polyketides of specified chain lengths.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cortes, J -- Wiesmann, K E -- Roberts, G A -- Brown, M J -- Staunton, J -- Leadlay, P F -- New York, N.Y. -- Science. 1995 Jun 9;268(5216):1487-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cambridge Centre for Molecular Recognition, University of Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7770773" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Cloning, Molecular ; Erythromycin/biosynthesis ; Genes, Bacterial ; Genetic Vectors ; Molecular Sequence Data ; Multienzyme Complexes/chemistry/genetics/*metabolism ; *Protein Engineering ; Saccharopolyspora/*enzymology/genetics ; Transformation, Genetic
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  • 95
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    Mating patterns in malaria parasite populations of Papua New Guinea (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-22
    Description: Description of the genetic structure of malaria parasite populations is central to an understanding of the spread of multiple-locus drug and vaccine resistance. The Plasmodium falciparum mating patterns from madang, Papua New Guinea, where intense transmission of malaria occurs, are described here. A high degree of inbreeding occurs in the absence of detectable linkage disequilibrium. This contrasts with other studies, indicating that the genetic structure of malaria parasite populations is neither clonal nor panmictic but will vary according to the transmission characteristics of the region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paul, R E -- Packer, M J -- Walmsley, M -- Lagog, M -- Ranford-Cartwright, L C -- Paru, R -- Day, K P -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1995 Sep 22;269(5231):1709-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Oxford, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569897" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Anopheles/parasitology ; Antimalarials/pharmacology ; Base Sequence ; Drug Resistance/genetics ; Female ; *Genes, Protozoan ; Genetic Variation ; Genotype ; Heterozygote ; Humans ; Inbreeding ; Insect Vectors/parasitology ; Linkage Disequilibrium ; Malaria, Falciparum/*parasitology/transmission ; Male ; Merozoite Surface Protein 1 ; Molecular Sequence Data ; Papua New Guinea ; Plasmodium falciparum/drug effects/*genetics/physiology ; Protein Precursors/genetics ; Protozoan Proteins/genetics ; Reproduction
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  • 96
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    Mercury-199 NMR of the metal receptor site in MerR and its protein-DNA complex (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-21
    Description: Structural insights have been provided by mercury-199 nuclear magnetic resonance (NMR) into the metal receptor site of the MerR metalloregulatory protein alone and in a complex with the regulatory target, DNA. The one- and two-dimensional NMR data are consistent with a trigonal planar Hg-thiolate coordination environment consisting only of Cys side chains and resolve structural aspects of both metal ion recognition and the allosteric mechanism. These studies establish 199Hg NMR techniques as useful probes of the metal coordination environment of regulatory proteins, copper enzymes, and zinc transcription factor complexes as large as 50 kilodaltons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Utschig, L M -- Bryson, J W -- O'Halloran, T V -- GM-08061/GM/NIGMS NIH HHS/ -- GM-38784/GM/NIGMS NIH HHS/ -- GM-45972/GM/NIGMS NIH HHS/ -- R01 GM038784/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Apr 21;268(5209):380-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Northwestern University, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716541" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Site ; Bacterial Proteins/*chemistry/metabolism ; Base Sequence ; DNA/*metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; Magnetic Resonance Spectroscopy ; Mercury/*metabolism ; Mercury Isotopes ; Metalloproteins/chemistry ; Molecular Sequence Data ; Protons ; Thermodynamics
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  • 97
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    Specific DNA-RNA hybrid binding by zinc finger proteins (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-04-14
    Description: Zinc finger proteins of the Cys2His2 type represent a large class of proteins that have been assumed to function by means of specific interactions with DNA. Experiments motivated by structural characteristics of zinc finger protein-DNA complexes revealed that certain zinc finger proteins bound DNA-RNA hybrids with affinities comparable to or greater than those for DNA duplexes. The interactions between the zinc finger proteins and the DNA-RNA hybrids were dependent on which strand was RNA and were sequence-specific. Thus, interactions with DNA-RNA hybrids should be considered with regard to the biological roles of zinc finger proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shi, Y -- Berg, J M -- GM46257/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 14;268(5208):282-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7536342" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; DNA/chemistry/*metabolism ; Molecular Sequence Data ; Nucleic Acid Hybridization ; RNA/chemistry/*metabolism ; RNA-Binding Proteins/chemistry/*metabolism ; Sp1 Transcription Factor/metabolism ; Zinc Fingers/*physiology
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  • 98
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    Fas ligand-induced apoptosis as a mechanism of immune privilege (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: The eye is a privileged site that cannot tolerate destructive inflammatory responses. Inflammatory cells entering the anterior chamber of the eye in response to viral infection underwent apoptosis that was dependent on Fas (CD95)-Fas ligand (FasL) and produced no tissue damage. In contrast, viral infection in gld mice, which lack functional FasL, resulted in an inflammation and invasion of ocular tissue without apoptosis. Fas-positive but not Fas-negative tumor cells were killed by apoptosis when placed within isolated anterior segments of the eyes of normal but not FasL-negative mice. FasL messenger RNA and protein were detectable in the eye. Thus, Fas-FasL interactions appear to be an important mechanism for the maintenance of immune privilege.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Griffith, T S -- Brunner, T -- Fletcher, S M -- Green, D R -- Ferguson, T A -- EY02687/EY/NEI NIH HHS/ -- EY06765/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1189-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ophthalmology and Visual Sciences, Washington University School of Medicine, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502042" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anterior Chamber/*immunology/virology ; Antigens, CD95/physiology ; *Apoptosis ; Base Sequence ; Eye/metabolism ; Fas Ligand Protein ; Gene Expression ; *Immune Tolerance ; Keratitis, Herpetic/immunology ; Leukemia L1210 ; Lymphocytes/cytology/immunology ; Membrane Glycoproteins/analysis/genetics/*physiology ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Neutrophils/cytology/immunology ; RNA, Messenger/analysis/genetics ; Tumor Cells, Cultured
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  • 99
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    Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-02
    Description: The substrate-specific protein chaperone Hsp90 (heat shock protein 90) from Saccharomyces cerevisiae functions in diverse signal transduction pathways. A mutation in YDJ1, a member of the DnaJ chaperone family, was recovered in a synthetic-lethal screen with Hsp90 mutants. In an otherwise wild-type background, the ydj1 mutation exerted strong and specific effects on three Hsp90 substrates, derepressing two (the estrogen and glucocorticoid receptors) and reducing the function of the third (the tyrosine kinase p60v-src). Analysis of one of these substrates, the glucocorticoid receptor, indicated that Ydj1 exerts its effects through physical interaction with Hsp90 substrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kimura, Y -- Yahara, I -- Lindquist, S -- New York, N.Y. -- Science. 1995 Jun 2;268(5215):1362-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Cell Biology, University of Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7761857" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Fungal Proteins/genetics/*physiology ; HSP40 Heat-Shock Proteins ; HSP90 Heat-Shock Proteins/genetics/*physiology ; *Heat-Shock Proteins ; Molecular Chaperones/genetics/*physiology ; Molecular Sequence Data ; Oncogene Protein pp60(v-src)/metabolism ; Point Mutation ; Protein Conformation ; Receptors, Estrogen/metabolism ; Receptors, Glucocorticoid/metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins ; *Signal Transduction
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  • 100
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    A nucleic acid triple helix formed by a peptide nucleic acid-DNA complex (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-15
    Description: The crystal structure of a nucleic acid triplex reveals a helix, designated P-form, that differs from previously reported nucleic acid structures. The triplex consists of one polypurine DNA strand complexed to a polypyrimidine hairpin peptide nucleic acid (PNA) and was successfully designed to promote Watson-Crick and Hoogsteen base pairing. The P-form helix is underwound, with a base tilt similar to B-form DNA. The bases are displaced from the helix axis even more than in A-form DNA. Hydrogen bonds between the DNA backbone and the Hoogsteen PNA backbone explain the observation that polypyrimidine PNA sequences form highly stable 2:1 PNA-DNA complexes. This structure expands the number of known stable helical forms that nucleic acids can adopt.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Betts, L -- Josey, J A -- Veal, J M -- Jordan, S R -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1838-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Glaxo Wellcome, Research Triangle Park, NC 27709, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525381" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Crystallography, X-Ray ; DNA/*chemistry ; Models, Molecular ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry ; Oligopeptides/*chemistry ; Protein Conformation
    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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