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  • Base Sequence  (287)
  • American Association for the Advancement of Science (AAAS)  (287)
  • American Institute of Physics (AIP)
  • Institute of Physics
  • Oxford University Press
  • 1995-1999  (287)
  • 1996  (130)
  • 1995  (157)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (287)
  • American Institute of Physics (AIP)
  • Institute of Physics
  • Oxford University Press
Years
  • 1995-1999  (287)
Year
  • 101
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    Bipartite Ca2+-binding motif in C2 domains of synaptotagmin and protein kinase C (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-12
    Description: C2 domains are found in many proteins involved in membrane traffic or signal transduction. Although C2 domains are thought to bind calcium ions, the structural basis for calcium binding is unclear. Analysis of calcium binding to C2 domains of synaptotagmin I and protein kinase C-beta by nuclear magnetic resonance spectroscopy revealed a bipartite calcium-binding motif that involves the coordination of two calcium ions by five aspartate residues located on two separate loops. Sequence comparisons indicated that this may be a widely used calcium-binding motif, designated here as the C2 motif.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shao, X -- Davletov, B A -- Sutton, R B -- Sudhof, T C -- Rizo, J -- R01-MH52804-01/MH/NIMH NIH HHS/ -- R29 NS33731-01A1/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):248-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75235, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662510" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/chemistry ; Base Sequence ; Calcium/*metabolism ; *Calcium-Binding Proteins ; Crystallography, X-Ray ; Hydrogen-Ion Concentration ; Magnetic Resonance Spectroscopy ; Membrane Glycoproteins/*chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Nerve Tissue Proteins/*chemistry/*metabolism ; Phospholipids/metabolism ; Protein Conformation ; Protein Folding ; Protein Kinase C/chemistry/*metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Synaptotagmin I ; Synaptotagmins ; Temperature
    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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  • 102
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    Support for the prion hypothesis for inheritance of a phenotypic trait in yeast (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-02
    Description: A cytoplasmically inherited genetic element in yeast, [PSI+], was confirmed to be a prionlike aggregate of the cellular protein Sup35 by differential centrifugation analysis and microscopic localization of a Sup35-green fluorescent protein fusion. Aggregation depended on the intracellular concentration and functional state of the chaperone protein Hsp104 in the same manner as did [PSI+] inheritance. The amino-terminal and carboxy-terminal domains of Sup35 contributed to the unusual behavior of [PSI+]. [PSI+] altered the conformational state of newly synthesized prion proteins, inducing them to aggregate as well, thus fulfilling a major tenet of the prion hypothesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patino, M M -- Liu, J J -- Glover, J R -- Lindquist, S -- GM25874/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 2;273(5275):622-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and the Department of Molecular Genetics and Cell Biology, University of Chicago, 5841 South Maryland Avenue, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662547" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Fungal Proteins/analysis/*chemistry/genetics/physiology ; Green Fluorescent Proteins ; Heat-Shock Proteins/physiology ; Luminescent Proteins/analysis ; Molecular Sequence Data ; Peptide Termination Factors ; Phenotype ; Prions/*chemistry/genetics ; *Protein Conformation ; Recombinant Fusion Proteins/analysis/chemistry ; Saccharomyces cerevisiae/*chemistry/*genetics ; *Saccharomyces cerevisiae Proteins ; Solubility
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  • 103
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    TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal transduction (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-24
    Description: Transforming growth factor-beta (TGF-beta) regulates many aspects of cellular function. A member of the mitogen-activated protein kinase kinase kinase (MAPKKK) family, TAK1, was previously identified as a mediator in the signaling pathway of TGF-beta superfamily members. The yeast two-hybrid system has now revealed two human proteins, termed TAB1 and TAB2 (for TAK1 binding protein), that interact with TAK1. TAB1 and TAK1 were co-immunoprecipitated from mammalian cells. Overproduction of TAB1 enhanced activity of the plasminogen activator inhibitor 1 gene promoter, which is regulated by TGF-beta, and increased the kinase activity of TAK1. TAB1 may function as an activator of the TAK1 MAPKKK in TGF-beta signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shibuya, H -- Yamaguchi, K -- Shirakabe, K -- Tonegawa, A -- Gotoh, Y -- Ueno, N -- Irie, K -- Nishida, E -- Matsumoto, K -- New York, N.Y. -- Science. 1996 May 24;272(5265):1179-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638164" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/chemistry/*metabolism ; Cell Line ; Cloning, Molecular ; Enzyme Activation ; Genes, Reporter ; Humans ; *Intracellular Signaling Peptides and Proteins ; *MAP Kinase Kinase Kinases ; Mice ; Molecular Sequence Data ; Plasminogen Activator Inhibitor 1/genetics ; Promoter Regions, Genetic ; Protein-Serine-Threonine Kinases/*metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics/metabolism ; *Signal Transduction ; Transfection ; Transformation, Genetic ; Transforming Growth Factor beta/*metabolism
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  • 104
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    Receptor-ligand interaction between CD44 and osteopontin (Eta-1) (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-26
    Description: The CD44 family of surface receptors regulates adhesion, movement, and activation of normal and neoplastic cells. The cytokine osteopontin (Eta-1), which regulates similar cellular functions, was found to be a protein ligand of CD44. Osteopontin induces cellular chemotaxis but not homotypic aggregation, whereas the inverse is true for the interaction between CD44 and a carbohydrate ligand, hyaluronate. The different responses of cells after CD44 ligation by either osteopontin or hyaluronate may account for the independent effects of CD44 on cell migration and growth. This mechanism may also be exploited by tumor cells to promote metastasis formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weber, G F -- Ashkar, S -- Glimcher, M J -- Cantor, H -- AI12184/AI/NIAID NIH HHS/ -- AI13600/AI/NIAID NIH HHS/ -- P01 AR34078/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):509-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560266" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD44/*metabolism ; Base Sequence ; *Cell Adhesion ; Cell Aggregation ; Cell Line ; *Chemotaxis ; Cytokines/*metabolism/pharmacology ; Hyaluronic Acid/metabolism/pharmacology ; Ligands ; Mice ; Molecular Sequence Data ; Monocytes/metabolism ; Oligopeptides/pharmacology ; Osteopontin ; Sialoglycoproteins/*metabolism/pharmacology ; Transfection ; Tumor Cells, Cultured
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 105
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    Trial set to focus on peer review (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1162-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8787118" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Biomedical Research ; Confidentiality ; *Disclosure ; Editorial Policies ; Ethics ; Humans ; Interleukin-1/*genetics ; *Patents as Topic ; Peer Review, Research/*legislation & jurisprudence ; Periodicals as Topic ; Publishing ; Washington
    Print ISSN: 0036-8075
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  • 106
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    Molecular cloning and disease association of hepatitis G virus: a transfusion-transmissible agent (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-26
    Description: An RNA virus, designated hepatitis G virus (HGV), was identified from the plasma of a patient with chronic hepatitis. Extension from an immunoreactive complementary DNA clone yielded the entire genome (9392 nucleotides) encoding a polyprotein of 2873 amino acids. The virus is closely related to GB virus C (GBV-C) and distantly related to hepatitis C virus, GBV-A, and GBV-B. HGV was associated with acute and chronic hepatitis. Persistent viremia was detected for up to 9 years in patients with hepatitis. The virus is transfusion-transmissible. It has a global distribution and is present within the volunteer blood donor population in the United States.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Linnen, J -- Wages, J Jr -- Zhang-Keck, Z Y -- Fry, K E -- Krawczynski, K Z -- Alter, H -- Koonin, E -- Gallagher, M -- Alter, M -- Hadziyannis, S -- Karayiannis, P -- Fung, K -- Nakatsuji, Y -- Shih, J W -- Young, L -- Piatak, M Jr -- Hoover, C -- Fernandez, J -- Chen, S -- Zou, J C -- Morris, T -- Hyams, K C -- Ismay, S -- Lifson, J D -- Hess, G -- Foung, S K -- Thomas, H -- Bradley, D -- Margolis, H -- Kim, J P -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):505-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genelabs Technologies, Redwood City, CA 94063, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560265" target="_blank"〉PubMed〈/a〉
    Keywords: Acute Disease ; Amino Acid Sequence ; Base Sequence ; Blood Donors ; Blood Transfusion/*adverse effects ; Blood-Borne Pathogens ; Chronic Disease ; Cloning, Molecular ; Consensus Sequence ; Disease Transmission, Infectious ; Flaviviridae/genetics ; Genome, Viral ; Hepatitis Viruses/chemistry/*genetics/isolation & purification ; Hepatitis, Viral, Human/epidemiology/transmission/*virology ; Humans ; Molecular Sequence Data ; Polymerase Chain Reaction ; RNA Viruses/chemistry/*genetics/isolation & purification ; RNA, Viral/blood/genetics ; Sequence Alignment ; United States/epidemiology ; Viral Proteins/chemistry/genetics ; Viremia/epidemiology/virology
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  • 107
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    Interaction between a putative mechanosensory membrane channel and a collagen (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-19
    Description: The degenerin family of proteins in Caenorhabditis elegans is homologous to subunits of the mammalian amiloride-sensitive epithelial sodium channels. Mutations in nematode degenerins cause cell death, probably because of defects in channel function. Genetic evidence was obtained that the unc-105 gene product represents a degenerin homolog affecting C. elegans muscles and that this putative channel interacts with type IV collagen in the extracellular matrix underlying the muscle cell. This interaction may serve as a mechanism of stretch-activated muscle contraction, and this system could provide a molecular model for the activation of mechanosensitive ion channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, J -- Schrank, B -- Waterston, R H -- GM23883/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):361-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, 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/8662524" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; Caenorhabditis elegans/chemistry/genetics/*metabolism ; *Caenorhabditis elegans Proteins ; Cloning, Molecular ; Collagen/*metabolism ; Extracellular Matrix/metabolism ; Genes, Helminth ; Genetic Complementation Test ; Helminth Proteins/chemistry/genetics/*metabolism/*physiology ; Ion Channel Gating ; Models, Biological ; Molecular Sequence Data ; Muscle Contraction ; Muscles/physiology ; Mutation ; Sensation ; Signal Transduction ; Sodium Channels/chemistry/genetics/*metabolism/*physiology ; Suppression, Genetic
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  • 108
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    Long-term lymphohematopoietic reconstitution by a single CD34-low/negative hematopoietic stem cell (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-12
    Description: Hematopoietic stem cells (HSCs) supply all blood cells throughout life by making use of their self-renewal and multilineage differentiation capabilities. A monoclonal antibody raised to the mouse homolog of CD34 (mCD34) was used to purify mouse HSCs to near homogeneity. Unlike in humans, primitive adult mouse bone marrow HSCs were detected in the mCD34 low to negative fraction. Injection of a single mCD34(lo/-), c-Kit+, Sca-1(+), lineage markers negative (Lin-) cell resulted in long-term reconstitution of the lymphohematopoietic system in 21 percent of recipients. Thus, the purified HSC population should enable analysis of the self-renewal and multilineage differentiation of individual HSCs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Osawa, M -- Hanada, K -- Hamada, H -- Nakauchi, H -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):242-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Institute of Basic Medical Sciences and Center for Tsukuba Advanced Research Alliance, University of Tsukuba, Tsukuba Science-City, Ibaraki 305, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662508" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD34/*analysis ; Base Sequence ; *Bone Marrow Cells ; Cell Differentiation ; Cell Lineage ; Cell Separation ; DNA Primers ; *Hematopoiesis ; Hematopoietic Stem Cell Transplantation ; Hematopoietic Stem Cells/*cytology/immunology ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Time Factors
    Print ISSN: 0036-8075
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  • 109
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    Intercalation, DNA kinking, and the control of transcription (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-09
    Description: Biological processes involved in the control and regulation of transcription are dependent on protein-induced distortions in DNA structure that enhance the recruitment of proteins to their specific DNA targets. This function is often accomplished by accessory factors that bind sequence specifically and locally bend or kink the DNA. The recent determination of the three-dimensional structures of several protein-DNA complexes, involving proteins that perform such architectural tasks, brings to light a common theme of side chain intercalation as a mechanism capable of driving the deformation of the DNA helix. The protein scaffolds orienting the intercalating side chain (or side chains) are structurally diverse, presently comprising four distinct topologies that can accomplish the same task. The intercalating side chain (or side chains), however, is exclusively hydrophobic. Intercalation can either kink or bend the DNA, unstacking one or more adjacent base pairs and locally unwinding the DNA over as much as a full turn of helix. Despite these distortions, the return to B-DNA helical parameters generally occurs within the adjacent half-turns of DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Werner, M H -- Gronenborn, A M -- Clore, G M -- New York, N.Y. -- Science. 1996 Feb 9;271(5250):778-84.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8628992" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; DNA/*chemistry/metabolism ; DNA Helicases/chemistry/metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Hydrogen Bonding ; Intercalating Agents/chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Transcription Factors/chemistry/*metabolism ; *Transcription, Genetic
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  • 110
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    A role for CD81 in early T cell development (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-12
    Description: Early stages of T cell development are thought to include a series of coordinated interactions between thymocytes and other cells of the thymus. A monoclonal antibody specific for mouse CD81 was identified that blocked the appearance of alpha beta but not gamma delta T cells in fetal organ cultures initiated with day 14.5 thymus lobes. In reaggregation cultures with CD81-transfected fibroblasts, CD4-CD8- thymocytes differentiated into CD4+CD8+ T cells. Thus, interactions between immature thymocytes and stromal cells expressing CD81 are required and may be sufficient to induce early events associated with T cell development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boismenu, R -- Rhein, M -- Fischer, W H -- Havran, W L -- AI32751/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):198-200.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539618" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antigens, CD/genetics/immunology/*physiology ; Antigens, CD4/analysis ; Antigens, CD8/analysis ; Antigens, CD81 ; Base Sequence ; CHO Cells ; Cell Differentiation ; Cricetinae ; Membrane Proteins/immunology/*physiology ; Mice ; Molecular Sequence Data ; Organ Culture Techniques ; Receptors, Antigen, T-Cell, alpha-beta/*analysis ; Receptors, Antigen, T-Cell, gamma-delta/analysis ; Stromal Cells/immunology ; T-Lymphocyte Subsets/cytology/*immunology ; Thymus Gland/cytology/*immunology ; Transfection
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  • 111
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    Cell cycle regulation of E2F site occupation in vivo (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: DNA-binding E2F complexes have been identified throughout the mammalian cell cycle, including the transcriptionally inactive complexes with pocket proteins, which occur early in the prereplicative G1 phase of the cycle, and the transactivating free E2F, which increases in late G1. Here, a regulatory B-myb promoter site was shown to bind with high affinity to free E2F and to E2F-pocket protein complexes in an indistinguishable way in vitro. In contrast, in vivo footprinting with NIH 3T3 cells demonstrated E2F site occupation specifically in early G1, when the B-myb promoter is inactive. These observations indicate that a novel mechanism governs E2F-DNA interactions during the cell cycle and emphasize the relevance of E2F site-directed transcriptional repression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zwicker, J -- Liu, N -- Engeland, K -- Lucibello, F C -- Muller, R -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1595-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Molekularbiologie und Tumorforschung, Philipps-Universitat Marburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599118" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Base Sequence ; *Carrier Proteins ; *Cell Cycle Proteins ; DNA/*metabolism ; DNA-Binding Proteins/*genetics/metabolism ; E2F Transcription Factors ; *G1 Phase ; Mice ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; *Promoter Regions, Genetic ; Retinoblastoma-Binding Protein 1 ; Retinoblastoma-Like Protein p107 ; *S Phase ; *Trans-Activators ; Transcription Factor DP1 ; Transcription Factors/*genetics/*metabolism ; Transcription, Genetic
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  • 112
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    Computational molecular biology. Software matchmakers help make sense of sequences (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taubes, G -- New York, N.Y. -- Science. 1996 Aug 2;273(5275):588-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8701312" target="_blank"〉PubMed〈/a〉
    Keywords: *Algorithms ; *Amino Acid Sequence ; Base Sequence ; Computer Communication Networks ; *Databases, Factual ; Evolution, Molecular ; Markov Chains ; Models, Molecular ; Molecular Sequence Data ; Neural Networks (Computer) ; *Protein Conformation ; Sequence Alignment
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  • 113
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    Essential yeast protein with unexpected similarity to subunits of mammalian cleavage and polyadenylation specificity factor (CPSF) (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-29
    Description: The 3' ends of most eukaryotic messenger RNAs are generated by internal cleavage and polyadenylation. In mammals, there is a strict dependence of both reactions on the sequence AAUAAA, which occurs upstream of polyadenylation [poly(A)] sites and which is recognized by CPSF. In contrast, cis-acting signals for yeast 3'-end generation are highly divergent from those of mammals, suggesting that trans-acting factors other than poly(A) polymerase would not be conserved. The essential yeast protein Brr5/Ysh1 shows sequence similarity to subunits of mammalian CPSF and is required for 3'-end processing in vivo and in vitro. These results demonstrate a structural and functional conservation of the yeast and mammalian 3'-end processing machineries despite a lack of conservation of the cis sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chanfreau, G -- Noble, S M -- Guthrie, C -- GM21119/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 29;274(5292):1511-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, UCSF School of Medicine, San Francisco, CA 94143-0448. guthrie@cgl.ucsf.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8929408" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cattle ; *Conserved Sequence ; Crystallography, X-Ray ; Fungal Proteins/*chemistry/genetics/metabolism ; Molecular Sequence Data ; Mutation ; Poly A/metabolism ; RNA Precursors/metabolism ; *RNA Processing, Post-Transcriptional ; RNA, Fungal/metabolism ; RNA, Messenger/metabolism ; RNA-Binding Proteins/*chemistry/genetics/metabolism ; Saccharomyces cerevisiae/*chemistry/genetics ; mRNA Cleavage and Polyadenylation Factors
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    Human foamy virus replication: a pathway distinct from that of retroviruses and hepadnaviruses (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: Human foamy virus (HFV) is the prototype of the Spumavirus genus of Retroviridae. In all other retroviruses, the pol gene products, including reverse transcriptase, are synthesized as Gag-Pol fusion proteins and are cleaved to functional enzymes during viral budding or release. In contrast, the Pol protein of HFV is translated from a spliced messenger RNA and lacks Gag domains. Infectious HFV particles contain double-stranded DNA similar in size to full-length provirus, suggesting that reverse transcription has taken place in viral particles before new rounds of infection, reminiscent of hepadnaviruses. These data suggest that foamy viruses possess a replication pathway containing features of both retroviruses and hepadnaviruses but distinct from both.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, S F -- Baldwin, D N -- Gwynn, S R -- Yendapalli, S -- Linial, M L -- CA18282/CA/NCI NIH HHS/ -- F32 CA60357/CA/NCI NIH HHS/ -- HL53762/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1579-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599113" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; Cricetinae ; Fusion Proteins, gag-pol/biosynthesis/genetics/metabolism ; Gene Products, gag/biosynthesis/genetics ; Gene Products, pol/*biosynthesis/genetics/metabolism ; Genes, gag ; Genes, pol ; Genome, Viral ; Hepatitis B virus/genetics/metabolism/physiology ; Humans ; Molecular Sequence Data ; RNA Splicing ; RNA, Viral/genetics ; RNA-Directed DNA Polymerase/metabolism ; Retroviridae/genetics/metabolism/physiology ; Spumavirus/genetics/metabolism/*physiology ; *Virus Replication
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Accessing genetic information with high-density DNA arrays (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-25
    Description: Rapid access to genetic information is central to the revolution taking place in molecular genetics. The simultaneous analysis of the entire human mitochondrial genome is described here. DNA arrays containing up to 135,000 probes complementary to the 16.6-kilobase human mitochondrial genome were generated by light-directed chemical synthesis. A two-color labeling scheme was developed that allows simultaneous comparison of a polymorphic target to a reference DNA or RNA. Complete hybridization patterns were revealed in a matter of minutes. Sequence polymorphisms were detected with single-base resolution and unprecedented efficiency. The methods described are generic and can be used to address a variety of questions in molecular genetics including gene expression, genetic linkage, and genetic variability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chee, M -- Yang, R -- Hubbell, E -- Berno, A -- Huang, X C -- Stern, D -- Winkler, J -- Lockhart, D J -- Morris, M S -- Fodor, S P -- 5RO1HG00813/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):610-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Affymetrix, 3380 Central Expressway, Santa Clara, CA 95051, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849452" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Base Composition ; Base Sequence ; Cloning, Molecular ; DNA, Mitochondrial/*genetics ; Fluorescein ; Fluoresceins ; Gene Expression ; Genetic Variation ; *Genome ; Humans ; Mitochondria/*genetics ; *Nucleic Acid Hybridization ; *Oligonucleotide Probes ; Phycoerythrin ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Sequence Analysis, DNA
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    Egr-1-induced endothelial gene expression: a common theme in vascular injury (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-08
    Description: A number of pathophysiologically relevant genes, including platelet-derived growth factor B-chain (PDGF-B), are induced in the vasculature after acute mechanical injury. In rat aorta, the activated expression of these genes was preceded by a marked increase in the amount of the early-growth-response gene product Egr-1 at the endothelial wound edge. Egr-1 interacts with a novel element in the proximal PDGF-B promoter, as well as with consensus elements in the promoters of other genes induced by endothelial injury. This interaction is crucial for injury-induced PDGF-B promoter-dependent expression. Sp1, whose binding site in the PDGF-B promoter overlaps that of Egr-1, occupies this element in unstimulated cells and is displaced by increasing amounts of Egr-1. These findings implicate Egr-1 in the up-regulated expression of PDGF-B and other potent mediators in mechanically injured arterial endothelial cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khachigian, L M -- Lindner, V -- Williams, A J -- Collins, T -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1427-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vascular Research Division, Department of Pathology, Brigham and Women's Hospital, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596917" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta/injuries/metabolism ; Base Sequence ; Binding Sites ; DNA-Binding Proteins/genetics/*metabolism ; Early Growth Response Protein 1 ; Endothelium, Vascular/injuries/*metabolism ; *Gene Expression Regulation ; Genes, Reporter ; Humans ; *Immediate-Early Proteins ; Male ; Molecular Sequence Data ; Platelet-Derived Growth Factor/biosynthesis/*genetics ; *Promoter Regions, Genetic ; Rats ; Rats, Sprague-Dawley ; Recombinant Proteins/metabolism ; Sp1 Transcription Factor/metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Transcription Factors/genetics/*metabolism ; *Zinc Fingers
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    Crystal structure of the yeast TFIIA/TBP/DNA complex (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-10
    Description: The crystal structure of the yeast TFIIA/TBP/TATA promoter complex was solved to 3 angstrom resolution by double-edge multiple wavelength anomalous diffraction from two different species of anomalous scattering elements in the same crystal. The large and small subunits of TFIIA associate intimately to form both domains of a two-domain folding pattern. TFIIA binds as a heterodimer to the side of the TBP/TATA complex opposite to the side that binds TFIIB and does not alter the TBP/DNA interaction. The six-stranded beta-sandwich domain interacts with the amino-terminal end of TBP through a stereospecific parallel beta-strand interface and with the backbone of the TATA box and the 5'-flanking B-DNA segment. The four-helix-bundle domain projects away from the TBP/TATA complex, thereby presenting a substantial surface for further protein-protein interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geiger, J H -- Hahn, S -- Lee, S -- Sigler, P B -- New York, N.Y. -- Science. 1996 May 10;272(5263):830-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629014" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Crystallography, X-Ray ; DNA, Fungal/*chemistry/metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Nucleic Acid Conformation ; Promoter Regions, Genetic ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Saccharomyces cerevisiae/chemistry/genetics/metabolism ; TATA Box ; TATA-Box Binding Protein ; Transcription Factor TFIIA ; Transcription Factor TFIIB ; Transcription Factors/*chemistry/metabolism ; Transcription, Genetic
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    GS28, a 28-kilodalton Golgi SNARE that participates in ER-Golgi transport (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-24
    Description: Little is known about the integral membrane proteins that participate in the early secretory pathway of mammalian cells. The complementary DNA encoding a 28-kilodalton protein (p28) of the cis-Golgi was cloned and sequenced. The protein was predicted to contain a central coiled-coil domain with a carboxyl-terminal membrane anchor. An in vitro assay for endoplasmic reticulum-Golgi transport was used to show that p28 participates in the docking and fusion stage of this transport event. Biochemical studies established that p28 is a core component of the Golgi SNAP receptor (SNARE) complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Subramaniam, V N -- Peter, F -- Philp, R -- Wong, S H -- Hong, W -- New York, N.Y. -- Science. 1996 May 24;272(5265):1161-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Membrane Biology Laboratory, Institute of Molecular and Cell Biology, National University of Singapore.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638159" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biological Transport ; Carrier Proteins/analysis ; Cell Line ; Cloning, Molecular ; DNA, Complementary/genetics ; Egtazic Acid/pharmacology ; Endoplasmic Reticulum/*metabolism ; Golgi Apparatus/*chemistry/metabolism ; *Membrane Glycoproteins ; Membrane Proteins/analysis/*chemistry/genetics/isolation & ; purification/*metabolism ; Molecular Sequence Data ; N-Ethylmaleimide-Sensitive Proteins ; SNARE Proteins ; Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins ; *Vesicular Transport Proteins ; Vesicular stomatitis Indiana virus ; Viral Envelope Proteins/metabolism
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    Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase from Xenopus egg extracts (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-06
    Description: Cdc2, the cyclin-dependent kinase that controls mitosis, is negatively regulated by phosphorylation on its threonine-14 and tyrosine-15 residues. Cdc25, the phosphatase that dephosphorylates both of these residues, undergoes activation and phosphorylation by multiple kinases at mitosis. Plx1, a kinase that associates with and phosphorylates the amino-terminal domain of Cdc25, was purified extensively from Xenopus egg extracts. Cloning of its complementary DNA revealed that Plx1 is related to the Polo family of protein kinases. Recombinant Plx1 phosphorylated Cdc25 and stimulated its activity in a purified system. Cdc25 phosphorylated by Plx1 reacted strongly with MPM-2, a monoclonal antibody to mitotic phosphoproteins. These studies indicate that Plx1 may participate in control of mitotic progression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kumagai, A -- Dunphy, W G -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1377-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, 216-76, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703070" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; CDC2 Protein Kinase/metabolism ; Cell Cycle Proteins/chemistry/*metabolism ; Cloning, Molecular ; Cyclins/metabolism ; Enzyme Activation ; Molecular Sequence Data ; Mutation ; Oocytes/enzymology ; Peptide Mapping ; Phosphoprotein Phosphatases/chemistry/*metabolism ; Phosphorylation ; Phosphoserine/analysis ; Phosphothreonine/analysis ; Protein-Serine-Threonine Kinases/chemistry/genetics/*isolation & ; purification/metabolism ; Recombinant Proteins/metabolism ; Xenopus ; *Xenopus Proteins ; cdc25 Phosphatases
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    Enzymatic synthesis of a quorum-sensing autoinducer through use of defined substrates (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-14
    Description: Many bacteria, including several pathogens of plants and humans, use a pheromone called an autoinducer to regulate gene expression in a cell density-dependent manner. Agrobacterium autoinducer [AAI, N-(3-oxo-octanoyl)-L-homoserine lactone] of A. tumefaciens is synthesized by the Tral protein, which is encoded by the tumor-inducing plasmid. Purified hexahistidinyl-Tral (H6-Tral) used S-adenosylmethionine to make the homoserine lactone moiety of AAI, but did not use related compounds. H6-Tral used 3-oxo-octanoyl-acyl carrier protein to make the 3-oxo-octanoyl moiety of AAI, but did not use 3-oxo-octanoyl-coenzyme A. These results demonstrate the enzymatic synthesis of an autoinducer through the use of purified substrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉More, M I -- Finger, L D -- Stryker, J L -- Fuqua, C -- Eberhard, A -- Winans, S C -- GM42893/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1655-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Microbiology, Cornell University, Ithaca, New York 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658141" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/antagonists & inhibitors/metabolism ; Acyl Carrier Protein/metabolism ; Agrobacterium tumefaciens/*genetics/metabolism ; Base Sequence ; Cerulenin/pharmacology ; Chromatography, Gel ; Chromatography, High Pressure Liquid ; Cloning, Molecular ; DNA Helicases/*metabolism ; DNA Primers ; Escherichia coli ; Escherichia coli Proteins ; Fatty Acids/metabolism ; *Gene Expression Regulation, Bacterial/drug effects ; Homoserine/*analogs & derivatives/biosynthesis ; Malonyl Coenzyme A/metabolism ; Molecular Sequence Data ; NADP/metabolism ; Plasmids ; S-Adenosylmethionine/metabolism
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    Phenotypes of mouse diabetes and rat fatty due to mutations in the OB (leptin) receptor (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-16
    Description: Mice harboring mutations in the obese (ob) and diabetes (db) genes display similar phenotypes, and it has been proposed that these genes encode the ligand and receptor, respectively, for a physiologic pathway that regulates body weight. The cloning of ob, and the demonstration that it encodes a secreted protein (leptin) that binds specifically to a receptor (OB-R) in the brain, have validated critical aspects of this hypothesis. Here it is shown by genetic mapping and genomic analysis that mouse db, rat fatty (a homolog of db), and the gene encoding the OB-R are the same gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chua, S C Jr -- Chung, W K -- Wu-Peng, X S -- Zhang, Y -- Liu, S M -- Tartaglia, L -- Leibel, R L -- DK26687/DK/NIDDK NIH HHS/ -- DK47473/DK/NIDDK NIH HHS/ -- HD28047/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 16;271(5251):994-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Human Behavior and Metabolism, Rockefeller University, New York 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8584938" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blotting, Southern ; Carrier Proteins/*genetics ; Chromosome Mapping ; Cloning, Molecular ; DNA Mutational Analysis ; Diabetes Mellitus/*genetics ; Genetic Markers ; Leptin ; Mice ; Mice, Inbred C57BL ; Mice, Inbred Strains ; Molecular Sequence Data ; Obesity/*genetics ; Phenotype ; Polymerase Chain Reaction ; Proteins/genetics ; Rats ; Rats, Inbred Strains ; *Receptors, Cell Surface ; Receptors, Cytokine/*genetics ; Receptors, Leptin
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    Retinal degeneration in mice lacking the gamma subunit of the rod cGMP phosphodiesterase (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-17
    Description: The retinal cyclic guanosine 3',5'-monophosphate (cGMP) phosphodiesterase (PDE) is a key regulator of phototransduction in the vertebrate visual system. PDE consists of a catalytic core of alpha and beta subunits associated with two inhibitory gamma subunits. A gene-targeting approach was used to disrupt the mouse PDEgamma gene. This mutation resulted in a rapid retinal degeneration resembling human retinitis pigmentosa. In homozygous mutant mice, reduced rather than increased PDE activity was apparent; the PDEalphabeta dimer was formed but lacked hydrolytic activity. Thus, the inhibitory gamma subunit appears to be necessary for integrity of the photoreceptors and expression of PDE activity in vivo.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2757426/" 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/PMC2757426/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsang, S H -- Gouras, P -- Yamashita, C K -- Kjeldbye, H -- Fisher, J -- Farber, D B -- Goff, S P -- EY08285/EY/NEI NIH HHS/ -- K08 EY000408/EY/NEI NIH HHS/ -- K08 EY000408-01/EY/NEI NIH HHS/ -- T32 GM 073667-14/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 May 17;272(5264):1026-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, College of Physicians and Surgeons, New York 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638127" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-GMP Phosphodiesterases/deficiency/genetics/*metabolism ; Animals ; Base Sequence ; Chimera ; Crosses, Genetic ; Cyclic GMP/*metabolism ; Electroretinography ; Enzyme Activation ; Female ; Gene Targeting ; Humans ; Light ; Male ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; Phenotype ; Retina/metabolism/*pathology/physiopathology ; Retinal Degeneration/*enzymology/pathology/physiopathology ; Retinal Rod Photoreceptor Cells/*enzymology/metabolism/pathology ; Retinitis Pigmentosa/pathology
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    Modification of phytohormone response by a peptide encoded by ENOD40 of legumes and a nonlegume (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-19
    Description: The gene ENOD40 is expressed during early stages of legume nodule development. A homolog was isolated from tobacco, which, as does ENOD40 from legumes, encodes an oligopeptide of about 10 amino acids. In tobacco protoplasts, these peptides change the response to auxin at concentrations as low as 10(-12) to 10(-16)M. The peptides encoded by ENOD40 appear to act as plant growth regulators.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van de Sande, K -- Pawlowski, K -- Czaja, I -- Wieneke, U -- Schell, J -- Schmidt, J -- Walden, R -- Matvienko, M -- Wellink, J -- van Kammen, A -- Franssen, H -- Bisseling, T -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):370-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Zuchtungsforschung, Koln, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662527" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Division ; Fabaceae/chemistry/*genetics/growth & development ; *Genes, Plant ; Green Fluorescent Proteins ; Indoleacetic Acids/*pharmacology ; Luminescent Proteins/biosynthesis ; Molecular Sequence Data ; Naphthaleneacetic Acids/pharmacology ; Open Reading Frames ; Plant Growth Regulators ; Plant Proteins/biosynthesis/*genetics/*physiology ; Plant Roots/growth & development/metabolism ; *Plants, Medicinal ; *Plants, Toxic ; Protoplasts/cytology ; RNA, Long Noncoding ; RNA, Untranslated/*physiology ; Recombinant Fusion Proteins ; Tobacco/chemistry/*genetics/growth & development ; Transfection
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    Rearrangement-enhancing element upstream of the mouse immunoglobulin kappa chain J cluster (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-08
    Description: Transcriptional regulatory elements have been shown to be necessary but not sufficient for the developmental regulation of immunoglobulin gene rearrangement in mouse precursor B cells. In the chicken lambda light chain locus, additional elements in the V-J intervening sequence are involved in negative and positive regulation of rearrangement. Here, mutation of the mouse homolog of a chicken element, located in the V(K)-J(K) intervening sequence upstream of the J(K) cluster, was shown to significantly decrease rearrangement. This cis-acting recombination-enhancing element affects the rearrangement process without being involved in regulating transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferradini, L -- Gu, H -- De Smet, A -- Rajewsky, K -- Reynaud, C A -- Weill, J C -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1416-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INSERM U373, Institut Necker, Faculte de Medecine, Universite Paris V, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596914" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; B-Lymphocytes/cytology/immunology ; Base Sequence ; Chimera ; Enhancer Elements, Genetic ; *Gene Rearrangement, B-Lymphocyte ; Gene Rearrangement, T-Lymphocyte ; Gene Targeting ; *Genes, Immunoglobulin ; Immunoglobulin J-Chains/*genetics ; Immunoglobulin Variable Region/genetics ; Immunoglobulin kappa-Chains/*genetics ; Introns ; Mice ; Mice, Inbred C57BL ; Mice, SCID ; Molecular Sequence Data ; Mutation ; Recombination, Genetic ; *Regulatory Sequences, Nucleic Acid ; Stem Cells
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    The immunological evolution of catalysis (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-23
    Description: The germline genes used by the mouse to generate the esterolytic antibody 48G7 were cloned and expressed in an effort to increase our understanding of the detailed molecular mechanisms by which the immune system evolves catalytic function. The nine replacement mutations that were fixed during affinity maturation increased affinity for the transition state analogue by a factor of 10(4), primarily the result of a decrease in the dissociation rate of the hapten-antibody complex. There was a corresponding increase in the rate of reaction of antibody with substrate, k(cat)/k(m), from 1.7 x 10(2)M(-1) min(-1) to 1.4 x 10(4)M(-1) min(-1). The three-dimensional crystal structure of the 48G7-transition state analogue complex at 2.0 angstroms resolution indicates that one of the nine residues in which somatic mutations have been fixed directly contact the hapten. Thus, in the case of 48G7, affinity maturation appears to play a conformational role, either in reorganizing the active site geometry of limiting side-chain and backbone flexibility of the germline antibody. The crystal structure and analysis of somatic and directed active site mutants underscore the role of transition state stabilization in the evolution of this catalytic antibody.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patten, P A -- Gray, N S -- Yang, P L -- Marks, C B -- Wedemayer, G J -- Boniface, J J -- Stevens, R C -- Schultz, P G -- R01 AL24695/PHS HHS/ -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1086-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599084" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Catalytic/chemistry/genetics/*immunology/metabolism ; Antibody Affinity ; Antigen-Antibody Complex ; Antigen-Antibody Reactions ; Base Sequence ; Binding Sites ; Catalysis ; Cloning, Molecular ; Crystallization ; Crystallography, X-Ray ; *Evolution, Molecular ; Genes, Immunoglobulin ; Haptens/immunology ; Immunoglobulin Fab Fragments/genetics/immunology ; Immunoglobulin Heavy Chains/genetics/immunology ; Immunoglobulin Light Chains/genetics/immunology ; Mice ; Molecular Sequence Data ; Mutation ; Protein Conformation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Congenital jaundice in rats with a mutation in a multidrug resistance-associated protein gene (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-23
    Description: The human Dubin-Johnson syndrome and its animal model, the TR(-) rat, are characterized by a chronic conjugated hyperbilirubinemia. TR(-) rats are defective in the canalicular multispecific organic anion transporter (cMOAT), which mediates hepatobiliary excretion of numerous organic anions. The complementary DNA for rat cmoat, a homolog of the human multidrug resistance gene (hMRP1), was isolated and shown to be expressed in the canalicular membrane of hepatocytes. In the TR(-) rat, a single-nucleotide deletion in this gene resulted in a reduced messenger RNA level and absence of the protein. It is likely that this mutation accounts for the TR(-) phenotype.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paulusma, C C -- Bosma, P J -- Zaman, G J -- Bakker, C T -- Otter, M -- Scheffer, G L -- Scheper, R J -- Borst, P -- Oude Elferink, R P -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1126-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Gastrointestinal and Liver Diseases, Center for Liver and Intestinal Research, Academic Medical Center, Amsterdam, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599091" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/analysis/chemistry/*genetics ; Amino Acid Sequence ; Animals ; Anion Transport Proteins ; Base Sequence ; Carrier Proteins/analysis/chemistry/*genetics ; Cell Membrane/chemistry ; DNA, Complementary/genetics ; Frameshift Mutation ; Humans ; Hyperbilirubinemia, Hereditary/*genetics ; Liver/*chemistry/cytology ; Molecular Sequence Data ; Molecular Weight ; Multidrug Resistance-Associated Proteins ; Phenotype ; Rats ; Rats, Wistar ; Sequence Alignment ; Sequence Deletion
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    The POU factor Oct-6 and Schwann cell differentiation (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-26
    Description: The POU transcription factor Oct-6, also known as SCIP or Tst-1, has been implicated as a major transcriptional regulator in Schwann cell differentiation. Microscopic and immunochemical analysis of sciatic nerves of Oct-6(-/-) mice at different stages of postnatal development reveals a delay in Schwann cell differentiation, with a transient arrest at the promyelination stage. Thus, Oct-6 appears to be required for the transition of promyelin cells to myelinating cells. Once these cells progress past this point, Oct-6 is no longer required, and myelination occurs normally.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jaegle, M -- Mandemakers, W -- Broos, L -- Zwart, R -- Karis, A -- Visser, P -- Grosveld, F -- Meijer, D -- New York, N.Y. -- Science. 1996 Jul 26;273(5274):507-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Genetics Center, Department of Cell Biology and Genetics, Erasmus University, Post Office Box 1738, 3000 DR Rotterdam, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662541" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Axons/ultrastructure ; Base Sequence ; Cell Differentiation ; Gene Expression ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Myelin P0 Protein/genetics/metabolism ; Myelin Proteins/genetics/metabolism ; Myelin Sheath/physiology ; Octamer Transcription Factor-6 ; Recombination, Genetic ; Schwann Cells/*cytology/physiology ; Sciatic Nerve/cytology/growth & development ; Stem Cells ; Transcription Factors/*genetics/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    A model of host-microbial interactions in an open mammalian ecosystem (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-06
    Description: The maintenance and significance of the complex populations of microbes present in the mammalian intestine are poorly understood. Comparison of conventionally housed and germ-free NMRI mice revealed that production of fucosylated glycoconjugates and an alpha1, 2-fucosyltransferase messenger RNA in the small-intestinal epithelium requires the normal microflora. Colonization of germ-free mice with Bacteroides thetaiotaomicron, a component of this flora, restored the fucosylation program, whereas an isogenic strain carrying a transposon insertion that disrupts its ability to use L-fucose as a carbon source did not. Simplified models such as this should aid the study of open microbial ecosystems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bry, L -- Falk, P G -- Midtvedt, T -- Gordon, J I -- DK30292/DK/NIDDK NIH HHS/ -- DK37960/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1380-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Pharmacology, 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/8703071" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacteroides/growth & development/metabolism/*physiology ; Base Sequence ; Cell Differentiation ; Cell Lineage ; Colony Count, Microbial ; Ecosystem ; Fucose/*metabolism ; Fucosyltransferases/genetics/metabolism ; Germ-Free Life ; Glycoconjugates/*metabolism ; Intestinal Mucosa/cytology/*microbiology ; Intestine, Small/cytology/metabolism/*microbiology ; Male ; Mice ; Mice, Inbred Strains ; Molecular Sequence Data ; Polymerase Chain Reaction ; RNA, Messenger/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Adaptive evolution of human immunodeficiency virus-type 1 during the natural course of infection (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-26
    Description: The rate of progression to disease varies considerably among individuals infected with human immunodeficiency virus-type 1 (HIV-1). Analyses of semiannual blood samples obtained from six infected men showed that a rapid rate of CD4 T cell loss was associated with relative evolutionary stasis of the HIV-1 quasispecies virus population. More moderate rates of CD4 T cell loss correlated with genetic evolution within three of four subjects. Consistent with selection by the immune constraints of these subjects, amino acid changes were apparent within the appropriate epitopes of human leukocyte antigen class I-restricted cytotoxic T lymphocytes. Thus, the evolutionary dynamics exhibited by the HIV-1 quasispecies virus populations under natural selection are compatible with adaptive evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolinsky, S M -- Korber, B T -- Neumann, A U -- Daniels, M -- Kunstman, K J -- Whetsell, A J -- Furtado, M R -- Cao, Y -- Ho, D D -- Safrit, J T -- AI32535/AI/NIAID NIH HHS/ -- AI35522/AI/NIAID NIH HHS/ -- AI45218/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Apr 26;272(5261):537-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Northwestern University Medical School, Chicago, IL 60611, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614801" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/immunology/virology ; Amino Acid Sequence ; Animals ; *Antigenic Variation ; Base Sequence ; Biological Evolution ; CD4 Lymphocyte Count ; Cohort Studies ; Disease Progression ; HIV Antibodies/immunology ; HIV Antigens/immunology ; HIV Infections/*immunology/*virology ; HIV-1/*genetics/immunology/pathogenicity/physiology ; Histocompatibility Antigens Class I/immunology ; Humans ; Male ; Mice ; Mice, SCID ; Molecular Sequence Data ; Mutation ; Phenotype ; RNA, Viral/blood ; T-Lymphocytes, Cytotoxic/*immunology ; Virulence ; Virus Replication
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Human homolog of patched, a candidate gene for the basal cell nevus syndrome (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-14
    Description: The basal cell nevus syndrome (BCNS) is characterized by developmental abnormalities and by the postnatal occurrence of cancers, especially basal cell carcinomas (BCCs), the most common human cancer. Heritable mutations in BCNS patients and a somatic mutation in a sporadic BCC were identified in a human homolog of the Drosophila patched (ptc) gene. The ptc gene encodes a transmembrane protein that in Drosophila acts in opposition to the Hedgehog signaling protein, controlling cell fates, patterning, and growth in numerous tissues. The human PTC gene appears to be crucial for proper embryonic development and for tumor suppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, R L -- Rothman, A L -- Xie, J -- Goodrich, L V -- Bare, J W -- Bonifas, J M -- Quinn, A G -- Myers, R M -- Cox, D R -- Epstein, E H Jr -- Scott, M P -- AR3995/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1668-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Howard Hughes Medical Institute, Stanford University School of Medicine, California 94305-5427, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658145" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amino Acid Sequence ; Animals ; Basal Cell Nevus Syndrome/*genetics ; Base Sequence ; Cloning, Molecular ; DNA, Neoplasm ; Drosophila ; *Drosophila Proteins ; Female ; Frameshift Mutation ; *Genes, Tumor Suppressor ; Humans ; Insect Hormones/genetics ; Male ; Membrane Proteins/*genetics ; Middle Aged ; Molecular Sequence Data ; Polymerase Chain Reaction ; Polymorphism, Single-Stranded Conformational ; Protein Conformation ; Receptors, Cell Surface
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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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
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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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
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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
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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
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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
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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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
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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
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  • 138
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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
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  • 139
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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
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  • 140
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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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  • 141
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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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  • 142
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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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  • 143
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    Solution structure of a cisplatin-induced DNA interstrand cross-link (1995)
    American Association for the Advancement of Science (AAAS)
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    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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  • 144
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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)
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    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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  • 145
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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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  • 146
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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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  • 147
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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)
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    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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  • 148
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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)
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    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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  • 149
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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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  • 150
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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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    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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    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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    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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    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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    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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    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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    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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    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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    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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  • 162
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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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  • 163
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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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  • 164
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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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  • 165
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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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  • 166
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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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  • 167
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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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  • 168
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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)
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    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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  • 169
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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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  • 170
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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)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 171
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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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  • 172
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    Inactivation of the mouse Huntington's disease gene homolog Hdh (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 173
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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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  • 174
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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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    Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 176
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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)
    Details
    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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  • 177
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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)
    Details
    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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  • 178
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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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  • 179
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    Structure-based design of transcription factors (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 180
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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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    Potential mechanism for sustained antiretroviral efficacy of AZT-3TC combination therapy (1995)
    American Association for the Advancement of Science (AAAS)
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    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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    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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  • 184
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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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    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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  • 186
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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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    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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  • 188
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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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 189
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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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  • 190
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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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  • 191
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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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  • 192
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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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  • 193
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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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  • 194
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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)
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    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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  • 195
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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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  • 196
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    A human telomeric protein (1995)
    American Association for the Advancement of Science (AAAS)
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    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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  • 197
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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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  • 198
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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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  • 199
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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
    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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    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
    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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