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  • Cricetinae
  • American Association for the Advancement of Science (AAAS)  (50)
  • 1990-1994  (44)
  • 1975-1979  (6)
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Publisher
  • American Association for the Advancement of Science (AAAS)  (50)
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Year
  • 1
    Publication Date: 1990-02-09
    Description: The control of cellular senescence by specific human chromosomes was examined in interspecies cell hybrids between diploid human fibroblasts and an immortal, Syrian hamster cell line. Most such hybrids exhibited a limited life span comparable to that of the human fibroblasts, indicating that cellular senescence is dominant in these hybrids. Karyotypic analyses of the hybrid clones that did not senesce revealed that all these clones had lost both copies of human chromosome 1, whereas all other human chromosomes were observed in at least some of the immortal hybrids. The application of selective pressure for retention of human chromosome 1 to the cell hybrids resulted in an increased percentage of hybrids that senesced. Further, the introduction of a single copy of human chromosome 1 to the hamster cells by microcell fusion caused typical signs of cellular senescence. Transfer of chromosome 11 had no effect on the growth of the cells. These findings indicate that human chromosome 1 may participate in the control of cellular senescence and further support a genetic basis for cellular senescence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sugawara, O -- Oshimura, M -- Koi, M -- Annab, L A -- Barrett, J C -- New York, N.Y. -- Science. 1990 Feb 9;247(4943):707-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2300822" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Survival/*genetics ; Chromosome Mapping ; *Chromosomes, Human, Pair 1 ; Clone Cells ; Cricetinae ; Diploidy ; Fibroblasts/*cytology ; Humans ; Hybrid Cells/*cytology ; Hypoxanthine Phosphoribosyltransferase/genetics ; Karyotyping ; Mice ; Ploidies ; Transfection ; Translocation, Genetic ; X Chromosome
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  • 2
    Publication Date: 1990-06-22
    Description: The vast repertoire of immunoglobulins and T cell receptors is generated, in part, by V(D)J recombination, a series of genomic rearrangements that occur specifically in developing lymphocytes. The recombination activating gene, RAG-1, which is a gene expressed exclusively in maturing lymphoid cells, was previously isolated. RAG-1 inefficiently induced V(D)J recombinase activity when transfected into fibroblasts, but cotransfection with an adjacent gene, RAG-2, has resulted in at least a 1000-fold increase in the frequency of recombination. The 2.1-kilobase RAG-2 complementary DNA encodes a putative protein of 527 amino acids whose sequence is unrelated to that of RAG-1. Like RAG-1, RAG-2 is conserved between species that carry out V(D)J recombination, and its expression pattern correlates precisely with that of V(D)J recombinase activity. In addition to being located just 8 kilobases apart, these convergently transcribed genes are unusual in that most, if not all, of their coding and 3' untranslated sequences are contained in single exons. RAG-1 and RAG-2 might activate the expression of the V(D)J recombinase but, more likely, they directly participate in the recombination reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oettinger, M A -- Schatz, D G -- Gorka, C -- Baltimore, D -- GM39458/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 22;248(4962):1517-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2360047" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biological Evolution ; Cattle ; Cell Line ; Chickens ; Cricetinae ; DNA/*genetics ; DNA Nucleotidyltransferases/*genetics ; *DNA-Binding Proteins ; Dogs ; Female ; *Gene Rearrangement, B-Lymphocyte ; *Gene Rearrangement, T-Lymphocyte ; *Homeodomain Proteins ; Humans ; Male ; Mice ; Molecular Sequence Data ; *Multigene Family ; Nuclear Proteins ; Nucleic Acid Hybridization ; Opossums ; Proteins/*genetics ; Rabbits ; Recombination, Genetic/*genetics ; Restriction Mapping ; Transfection ; Turtles ; VDJ Recombinases
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  • 3
    Publication Date: 1990-06-08
    Description: Lighting cycles synchronize (entrain) mammalian circadian rhythms by altering activity of cells in the suprachiasmatic nucleus (SCN) of the hypothalamus, a circadian pacemaker. Exposure of hamsters and rats to light pulses at those phases of the circadian rhythm during which light can shift the rhythm caused increased immunoreactivity for the product of the immediate-early gene c-fos in cells in the region of the SCN that receives retinal fibers. Light pulses also increased messenger RNA for the Fos protein and for the immediate-early protein NGFI-A in the rat SCN. Similar increases in mRNA for NGFI-A were seen in the SCN of hamsters. Thus cells in this portion of the SCN undergo alterations in gene expression in response to retinal illumination, but only at times in the circadian cycle when light is capable of influencing entrainment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rusak, B -- Robertson, H A -- Wisden, W -- Hunt, S P -- New York, N.Y. -- Science. 1990 Jun 8;248(4960):1237-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology, Dalhousie University, Halifax, Nova Scotia, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2112267" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Circadian Rhythm ; Cricetinae ; Darkness ; *Gene Expression ; Light ; Nerve Growth Factors/*genetics ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins c-fos ; *Proto-Oncogenes ; RNA, Messenger/*analysis/genetics ; Rats ; Suprachiasmatic Nucleus/*physiology/radiation effects ; Transcription, Genetic
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  • 4
    Publication Date: 1990-06-15
    Description: Herpes simplex virus type 1 (HSV-1) is a ubiquitous pathogen responsible for considerable morbidity in the general population. The results presented herein establish the basic fibroblast growth factor (FGF) receptor as a means of entry of HSV-1 into vertebrate cells. Inhibitors of basic FGF binding to its receptor and competitive polypeptide antagonists of basic FGF prevented HSV-1 uptake. Chinese hamster ovary (CHO) cells that do not express FGF receptors are resistant to HSV-1 entry; however, HSV-1 uptake is dramatically increased in CHO cells transfected with a complementary DNA encoding a basic FGF receptor. The distribution of this integral membrane protein in vivo may explain the tissue and cell tropism of HSV-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaner, R J -- Baird, A -- Mansukhani, A -- Basilico, C -- Summers, B D -- Florkiewicz, R Z -- Hajjar, D P -- P01 DK 18811/DK/NIDDK NIH HHS/ -- P01 HD 96601/HD/NICHD NIH HHS/ -- P50 HL 18828/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Jun 15;248(4961):1410-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2162560" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; Amino Acid Sequence ; Animals ; Binding, Competitive ; Cell Line ; Cell Membrane/microbiology ; Cricetinae ; DNA/genetics ; Fibroblast Growth Factors/antagonists & inhibitors/metabolism/pharmacology ; Heparitin Sulfate/metabolism ; Molecular Sequence Data ; Peptide Fragments/pharmacology ; Receptors, Cell Surface/genetics/*physiology ; Receptors, Fibroblast Growth Factor ; Simplexvirus/*physiology ; Transfection
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  • 5
    Publication Date: 1991-02-08
    Description: Mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) cause cystic fibrosis. In order to evaluate its function, CFTR was expressed in HeLa, Chinese hamster ovary (CHO), and NIH 3T3 fibroblast cells, and anion permeability was assessed with a fluorescence microscopic assay and the whole-cell patch-clamp technique. Adenosine 3',5'-monophosphate (cAMP) increased anion permeability and chloride currents in cells expressing CFTR, but not in cells expressing a mutant CFTR (delta F508) or in nontransfected cells. The simplest interpretation of these observations is that CFTR is itself a cAMP-activated chloride channel. The alternative interpretation, that CFTR directly or indirectly regulates chloride channels, requires that these cells have endogenous cryptic, chloride channels that are stimulated by cAMP only in the presence of CFTR.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, M P -- Rich, D P -- Gregory, R J -- Smith, A E -- Welsh, M J -- New York, N.Y. -- Science. 1991 Feb 8;251(4994):679-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Iowa College of Medicine, Iowa City 52242.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1704151" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chloride Channels ; Chlorides/*metabolism ; Cricetinae ; Cyclic AMP/*physiology ; Cystic Fibrosis Transmembrane Conductance Regulator ; Humans ; Membrane Proteins/*metabolism/*physiology ; Mice ; Mutation ; Recombinant Proteins ; Structure-Activity Relationship
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-02-23
    Description: The pacemaker role of the suprachiasmatic nucleus in a mammalian circadian system was tested by neural transplantation by using a mutant strain of hamster that shows a short circadian period. Small neural grafts from the suprachiasmatic region restored circadian rhythms to arrhythmic animals whose own nucleus had been ablated. The restored rhythms always exhibited the period of the donor genotype regardless of the direction of the transplant or genotype of the host. The basic period of the overt circadian rhythm therefore is determined by cells of the suprachiasmatic region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ralph, M R -- Foster, R G -- Davis, F C -- Menaker, M -- HD13162/HD/NICHD NIH HHS/ -- HD18686/HD/NICHD NIH HHS/ -- MH09483/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1990 Feb 23;247(4945):975-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Virginia, Charlottesville 22903.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2305266" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Circadian Rhythm/genetics/*physiology ; Cricetinae ; Immunohistochemistry ; Male ; Mutation ; Nerve Tissue/*transplantation ; Neuropeptide Y/analysis ; Suprachiasmatic Nucleus/embryology/*physiology ; Vasopressins/analysis
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-01-19
    Description: The mevalonate-derived portion of a prenylated protein from Chinese hamster ovary cells has been established as diterpenoid (C20). This group is linked to a carboxyl-terminal cysteine as a thioether. It was removed from the protein by hydrazinolysis followed by Raney nickel desulfurization, and the resulting hydrocarbon fraction was analyzed by gas chromatography-mass spectrometry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rilling, H C -- Breunger, E -- Epstein, W W -- Crain, P F -- GM 29812/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jan 19;247(4940):318-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Utah, Salt Lake City 84112.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2296720" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cricetinae ; Diterpenes/*metabolism ; Female ; Gas Chromatography-Mass Spectrometry ; Mevalonic Acid/metabolism ; Molecular Structure ; Ovary ; Protein Precursors/metabolism ; *Protein Processing, Post-Translational ; Proteins/*metabolism
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  • 8
    Publication Date: 1990-11-23
    Description: The CD4 antigen is the high affinity cellular receptor for the human immunodeficiency virus type-1 (HIV-1). Binding of recombinant soluble CD4 (sCD4) or the purified V1 domain of sCD4 to the surface glycoprotein gp120 on virions resulted in rapid dissociation of gp120 from its complex with the transmembrane glycoprotein gp41. This may represent the initial stage in virus-cell and cell-cell fusion. Shedding of gp120 from virions induced by sCD4 may also contribute to the mechanism by which these soluble receptor molecules neutralize HIV-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, J P -- McKeating, J A -- Weiss, R A -- Sattentau, Q J -- New York, N.Y. -- Science. 1990 Nov 23;250(4984):1139-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chester Beatty Laboratories, Institute of Cancer Research, London, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2251501" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/pharmacology ; Antigens, CD4/immunology/*metabolism ; Binding Sites ; Binding, Competitive ; Cell Line ; Cricetinae ; HIV Envelope Protein gp120/*metabolism ; HIV Envelope Protein gp41/metabolism ; HIV-1/*metabolism ; Virion/*metabolism
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-10-12
    Description: Activation of the N-methyl-D-aspartate (NMDA) subclass of glutamate receptors is a critical step in the selection of appropriate synaptic connections in the developing visual systems of cat and frog. Activity-dependent development of mammalian motor neurons was shown to be similarly mediated by activation of the NMDA receptor. The expression of the Cat-301 proteoglycan on motor neurons was developmentally regulated and could be specifically inhibited by blockade of the NMDA receptor at the spinal segmental level. In the adult, Cat-301 immunoreactivity on motor neurons was not diminished by NMDA receptor blockade. The NMDA receptor may regulate the expression of a class of neuronal proteins (of which Cat-301 is one example) that underlie the morphological and physiological features of activity-dependent development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kalb, R G -- Hockfield, S -- EY 06511/EY/NEI NIH HHS/ -- NS 01247/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Oct 12;250(4978):294-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Neuroanatomy, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2145629" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Animals, Newborn ; Antibodies, Monoclonal/analysis/*biosynthesis ; Anticonvulsants/pharmacology ; Cricetinae ; Dizocilpine Maleate/pharmacology ; Fluorescent Antibody Technique ; Motor Neurons/drug effects/*physiology ; Proteoglycans/*biosynthesis ; Receptors, N-Methyl-D-Aspartate/drug effects/*physiology ; Spinal Cord/drug effects/*growth & development/metabolism
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  • 10
    Publication Date: 1991-11-22
    Description: The binding of cytosolic coat proteins to organelles may regulate membrane structure and traffic. Evidence is presented that a small guanosine triphosphate (GTP)-binding protein, the adenosine diphosphate ribosylation factor (ARF), reversibly associates with the Golgi apparatus in an energy, GTP, and fungal metabolite brefeldin A (BFA)-sensitive manner similar to, but distinguishable from, the 110-kilodalton cytosolic coat protein beta-COP. Addition of beta gamma subunits of G proteins inhibited the association of both ARF and beta-COP with Golgi membranes that occurred upon incubation with guanosine 5'-O-(3-thiotriphosphate) (GTP-gamma-S). Thus, heterotrimeric G proteins may function to regulate the assembly of coat proteins onto the Golgi membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Donaldson, J G -- Kahn, R A -- Lippincott-Schwartz, J -- Klausner, R D -- New York, N.Y. -- Science. 1991 Nov 22;254(5035):1197-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1957170" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factors ; Aluminum/pharmacology ; *Aluminum Compounds ; Animals ; Biological Transport ; Brefeldin A ; CHO Cells ; Coatomer Protein ; Cricetinae ; Cyclopentanes/pharmacology ; Endoplasmic Reticulum/metabolism ; Fluorides/pharmacology ; GTP-Binding Proteins/*metabolism ; Golgi Apparatus/*metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; In Vitro Techniques ; Intracellular Membranes/metabolism ; Microtubule-Associated Proteins/metabolism
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  • 11
    Publication Date: 1991-05-10
    Description: A mutated form of the platelet-derived growth factor (PDGF) beta receptor lacking most of its cytoplasmic domain was tested for its ability to block wild-type PDGF receptor function. PDGF induced the formation of complexes consisting of wild-type and truncated receptors. Such complexes were defective in autophosphorylation. When truncated receptors were expressed in excess compared to wild-type receptors, stimulation by PDGF of receptor autophosphorylation, association of phosphatidylinositol-3 kinase with the receptor, and calcium mobilization were blocked. Thus, a truncated receptor can inactivate wild-type receptor function by forming ligand-dependent receptor complexes (probably heterodimers) that are incapable of mediating the early steps of signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ueno, H -- Colbert, H -- Escobedo, J A -- Williams, L T -- P01 HL-43821/HL/NHLBI NIH HHS/ -- R01 HL-32898/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 10;252(5007):844-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1851331" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Centrifugation, Density Gradient ; Cricetinae ; In Vitro Techniques ; Ligands ; Mice ; Mice, Inbred BALB C ; Phosphorylation ; Platelet-Derived Growth Factor ; Receptors, Cell Surface/*antagonists & inhibitors/physiology ; Receptors, Platelet-Derived Growth Factor ; Signal Transduction/*physiology
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-10-04
    Description: Voltage-gated sodium channels, which are responsible for the generation of action potentials in the brain, are phosphorylated by protein kinase C (PKC) in purified form. Activation of PKC decreases peak sodium current up to 80 percent and slows its inactivation for sodium channels in rat brain neurons and for rat brain type IIA sodium channel alpha subunits heterologously expressed in Chinese hamster ovary cells. These effects are specific for PKC because they can be blocked by specific peptide inhibitors of PKC and can be reproduced by direct application of PKC to the cytoplasmic surface of sodium channels in excised inside-out membrane patches. Modulation of brain sodium channels by PKC is likely to have important effects on signal transduction and synaptic transmission in the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Numann, R -- Catterall, W A -- Scheuer, T -- NS15751/NS/NINDS NIH HHS/ -- NS25704/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):115-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1656525" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/physiology ; CHO Cells ; Cloning, Molecular ; Cricetinae ; Diglycerides/pharmacology ; In Vitro Techniques ; Neurons/physiology ; Phosphoproteins/physiology ; Phosphorylation ; Protein Kinase C/*physiology ; Protein Kinases/physiology ; Rats ; Sodium/*physiology ; Sodium Channels/*physiology
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  • 13
    Publication Date: 1992-02-28
    Description: The primary defect arising from Zellweger syndrome appears to be linked to impaired assembly of peroxisomes. A human complementary DNA has been cloned that complements the disease's symptoms (including defective peroxisome assembly) in fibroblasts from a patient with Zellweger syndrome. The cause of the syndrome in this patient was a point mutation that resulted in the premature termination of peroxisome assembly factor-1. The homozygous patient apparently inherited the mutation from her parents, each of whom was heterozygous for that mutation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shimozawa, N -- Tsukamoto, T -- Suzuki, Y -- Orii, T -- Shirayoshi, Y -- Mori, T -- Fujiki, Y -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1132-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Gifu University School of Medicine, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546315" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cricetinae ; DNA Mutational Analysis ; Genes ; Genetic Complementation Test ; Humans ; Membrane Proteins/*genetics ; Microbodies/*ultrastructure ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; Pedigree ; Polymerase Chain Reaction ; Transfection ; Zellweger Syndrome/*genetics
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  • 14
    Publication Date: 1992-04-03
    Description: Steroid-thyroid hormone receptors typically bind as dimers to DNA sequences that contain repeated elements termed half-sites. NGFI-B, an early response protein and orphan member of this receptor superfamily, binds to a DNA sequence that contains only one half-site (5'-AAAGGTCA-3'). A domain separate from the NGFI-B zinc fingers, termed the A box, was identified and is required for recognition of the two adenine-thymidine (A-T) base pairs at the 5' end of the NGFI-B DNA binding element. In addition, a domain downstream of the zinc fingers of the orphan receptor H-2 region II binding protein, termed the T box, determined binding to tandem repeats of the estrogen receptor half-site (5'-AGGTCA-3').〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, T E -- Paulsen, R E -- Padgett, K A -- Milbrandt, J -- NS01018/NS/NINDS NIH HHS/ -- P01 CA49712/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):107-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, 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/1314418" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; CHO Cells ; Cell Nucleus/*physiology ; Cricetinae ; DNA/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Kinetics ; Mice ; Molecular Sequence Data ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Oligodeoxyribonucleotides/metabolism ; Polymerase Chain Reaction ; Receptors, Cell Surface/*metabolism ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Substrate Specificity ; Transcription Factors/genetics/*metabolism ; Transfection ; Zinc Fingers/genetics
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  • 15
    Publication Date: 1992-12-04
    Description: A secreted form of a class I major histocompatibility complex (MHC) molecule was denatured and renatured in vitro in the absence of peptide. The resulting empty class I heterodimer was immunologically reactive and structurally similar to a heterodimer renatured in the presence of an appropriate restricted peptide. Thermal stability profiles indicated that the two forms of heterodimer differed in their resistance to denaturation by heat but that a significant portion of the empty class I heterodimers had a native conformation at physiological temperatures. Free energies calculated from these data gave a direct measure of the stabilization of the class I MHC molecule that resulted from peptide binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fahnestock, M L -- Tamir, I -- Narhi, L -- Bjorkman, P J -- AI28931/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 4;258(5088):1658-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1360705" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CHO Cells ; Circular Dichroism ; Cricetinae ; Drug Stability ; Enzyme-Linked Immunosorbent Assay ; Glutamate-Ammonia Ligase/genetics/metabolism ; Histocompatibility Antigens Class I/*chemistry/genetics ; Hot Temperature ; Humans ; Macromolecular Substances ; *Protein Conformation ; Protein Folding ; Thermodynamics ; Transfection
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  • 16
    Publication Date: 1990-04-13
    Description: Biosynthetic studies of the prion protein (PrP) have shown that two forms of different topology can be generated from the same pool of nascent chains in cell-free translation systems supplemented with microsomal membranes. A transmembrane form is the predominant product generated in wheat germ (WG) extracts, whereas a completely translocated (secretory) form is the major product synthesized in rabbit reticulocyte lysates (RRL). An unusual topogenic sequence within PrP is now shown to direct this system-dependent difference. The actions of this topogenic sequence were independent of on-going translation and could be conferred to heterologous proteins by the engineering of a discrete set of codons. System-dependent topology conferred by addition of RRL to WG translation products suggests that this sequence interacts with one or more cytosolic factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lopez, C D -- Yost, C S -- Prusiner, S B -- Myers, R M -- Lingappa, V R -- AG02132/AG/NIA NIH HHS/ -- NS14069/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Apr 13;248(4952):226-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1970195" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Codon ; Cricetinae ; DNA, Viral/genetics ; Kinetics ; Mesocricetus ; Peptide Mapping ; Plasmids ; PrPSc Proteins ; Prions/*genetics ; Protein Biosynthesis ; Protein Processing, Post-Translational ; Restriction Mapping ; Transcription, Genetic ; Viral Proteins/biosynthesis/*genetics
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  • 17
    Publication Date: 1990-02-16
    Description: Transfection of Chinese hamster ovary cells with complementary DNA encoding the RIIA sodium channel alpha subunit from rat brain led to expression of functional sodium channels with the rapid, voltage-dependent activation and inactivation characteristic of sodium channels in brain neurons. The sodium currents mediated by these transfected channels were inhibited by tetrodotoxin, persistently activated by veratridine, and prolonged by Leiurus alpha-scorpion toxin, indicating that neurotoxin receptor sites 1 through 3 were present in functional form. The RIIA sodium channel alpha subunit cDNA alone is sufficient for stable expression of functional sodium channels with the expected kinetic and pharmacological properties in mammalian somatic cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scheuer, T -- Auld, V J -- Boyd, S -- Offord, J -- Dunn, R -- Catterall, W A -- NS 15751/NS/NINDS NIH HHS/ -- NS 25704/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Feb 16;247(4944):854-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, School of Medicine, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2154850" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*physiology ; Cell Line ; Cricetinae ; Cricetulus ; Electric Conductivity ; Female ; Membrane Potentials/drug effects ; Membrane Proteins/genetics/*physiology ; Ovary ; Rats ; Sodium Channels/drug effects/*physiology ; Tetrodotoxin/pharmacology ; *Transfection
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  • 18
    Publication Date: 1990-08-10
    Description: A library of human-derived complementary DNA from a human-hamster hybrid cell line containing the Xq24-qter region has been constructed. Complementary DNA synthesis was primed from heterogeneous nuclear (hn) RNA by oligonucleotides derived from conserved regions of human Alu repeats. At least 80% of these cloned sequences were of human origin, providing an enrichment of at least two orders of magnitude. Two clones, one containing a fragment of the primary transcript of the human hypoxanthine-guanine phosphoribosyltransferase (HPRT) gene at Xq26 and another recognizing a family of human genes mapping to two regions of Xq24-qter, were characterized. Additional hncDNA clones mapped to a variety of sites in the Xq24-qter region, demonstrating the isolation of many transcriptionally active loci. These clones provide probes for identification of genetic loci on the terminal region of the X chromosome long arm, which is the location of a number of inherited disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corbo, L -- Maley, J A -- Nelson, D L -- Caskey, C T -- New York, N.Y. -- Science. 1990 Aug 10;249(4969):652-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular Genetics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2382140" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line ; Chromosome Mapping ; Cloning, Molecular/methods ; Cricetinae ; DNA, Single-Stranded/genetics/isolation & purification ; Deoxyribonuclease EcoRI ; Humans ; Hybrid Cells/cytology ; Molecular Sequence Data ; Molecular Weight ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; RNA, Heterogeneous Nuclear/*genetics ; Restriction Mapping ; *Transcription, Genetic ; *X Chromosome
    Print ISSN: 0036-8075
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  • 19
    Publication Date: 1990-11-23
    Description: Recruitment of neutrophils to sites of inflammation is mediated in part by endothelial leukocyte adhesion molecule-1 (ELAM-1), which is expressed on activated endothelial cells of the blood vessel walls. ELAM-1 is a member of the LEC-CAM or selectin family of adhesion molecules that contain a lectin motif thought to recognize carbohydrate ligands. In this report, cell adhesion by ELAM-1 is shown to be mediated by a carbohydrate ligand, sialyl-Lewis X (SLex; NeuAc alpha 2,3Gal beta 1,4(Fuc alpha 1,3)-GlcNAc-), a terminal structure found on cell-surface glycoprotein and glycolipid carbohydrate groups of neutrophils.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Phillips, M L -- Nudelman, E -- Gaeta, F C -- Perez, M -- Singhal, A K -- Hakomori, S -- Paulson, J C -- New York, N.Y. -- Science. 1990 Nov 23;250(4984):1130-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cytel Corp., La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1701274" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/pharmacology ; Antigens, CD15/chemistry/*physiology ; Carbohydrate Conformation ; Carbohydrate Sequence ; Cell Adhesion/*physiology ; Cell Adhesion Molecules/immunology/*physiology ; Cell Line ; Cricetinae ; E-Selectin ; Glycosylation ; Humans ; Ligands ; Molecular Sequence Data ; Neuraminidase/pharmacology ; Neutrophils/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
    Publication Date: 1991-02-15
    Description: Transfer of a normal Chinese hamster X chromosome (carried in a mouse A9 donor cell line) to a nickel-transformed Chinese hamster cell line with an Xq chromosome deletion resulted in senescense of these previously immortal cells. At early passages of the A9/CX donor cells, the hamster X chromosome was highly active, inducing senescence in 100% of the colonies obtained after its transfer into the nickel-transformed cells. However, senescence was reduced to 50% when Chinese hamster X chromosomes were transferred from later passage A9 cells. Full senescing activity of the intact hamster X chromosome was restored by treatment of the donor mouse cells with 5-azacytidine, which induced demethylation of DNA. These results suggest that a senescence gene or genes, which may be located on the Chinese hamster X chromosome, can be regulated by DNA methylation, and that escape from senescence and possibly loss of tumor suppressor gene activity can occur by epigenetic mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klein, C B -- Conway, K -- Wang, X W -- Bhamra, R K -- Lin, X H -- Cohen, M D -- Annab, L -- Barrett, J C -- Costa, M -- ES 04715/ES/NIEHS NIH HHS/ -- ES 04895/ES/NIEHS NIH HHS/ -- ES 05512/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 15;251(4995):796-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Environmental Medicine, New York University Medical Center, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990442" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Fusion ; Cell Line, Transformed ; Cell Survival/*genetics ; Cell Transformation, Neoplastic/chemically induced/*genetics ; Chromosome Deletion ; Cricetinae ; Cricetulus ; Hypoxanthine Phosphoribosyltransferase/genetics ; Mice ; Nickel/*pharmacology ; X Chromosome/*drug effects
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  • 21
    Publication Date: 1991-12-20
    Description: The binding of multivalent immunoglobulin G complexes to Fc receptors (Fc gamma Rs) on macrophages activates multiple immune functions. A murine macrophage cell line, but not a fibroblast cell line, that was transfected with human Fc gamma RIIA mediated phagocytosis and an intracellular Ca2+ concentration ([Ca2+]i) flux upon cross-linking of human Fc gamma RIIA. Transfected macrophages that expressed a truncated receptor lacking 17 carboxy-terminal amino acids phagocytosed small antibody complexes. However, only wild-type transfectants phagocytosed labeled erythrocytes and fluxed [Ca2+]i. Thus, the cytoplasmic domain of human Fc gamma RIIA contains distinct functional regions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Odin, J A -- Edberg, J C -- Painter, C J -- Kimberly, R P -- Unkeless, J C -- AI 24322/AI/NIAID NIH HHS/ -- AI 24671/AI/NIAID NIH HHS/ -- AR 33062/AR/NIAMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1785-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Mount Sinai Medical Center, New York, NY 10029.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1837175" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Antigens, Differentiation/genetics/*physiology ; CHO Cells ; Calcium/*metabolism ; Cell Line ; Cloning, Molecular ; Cricetinae ; Homeostasis ; Humans ; Immunoglobulin G/metabolism ; Kinetics ; Macrophages ; Mice ; *Phagocytosis ; Receptors, Fc/genetics/*physiology ; Receptors, IgG ; Recombinant Proteins/metabolism ; *Transfection
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  • 22
    Publication Date: 1992-05-08
    Description: Controversy exists as to whether the interaction of a guanosine triphosphatase activating protein (GAP) with Ras proteins functions both to initiate and to terminate Ras-dependent signaling events or only to terminate them. GAP-C, a carboxyl-terminal fragment of GAP that is sufficient to stimulate GTPase activity, inhibited the stimulation of transcription produced by some oncoproteins (v-Src, polyoma middle T, wild-type Ras, and oncogenic Ras) but not that produced by v-Mos. Wild-type GAP did not affect transcription induced by oncogenic Ras but reversed the inhibitory effect of GAP-C on transcription induced by oncogenic Ras. These results indicate that GAP is a negative regulator of wild-type Ras and elicits a downstream signal by interacting with Ras-GTP (guanosine triphosphate).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schweighoffer, F -- Barlat, I -- Chevallier-Multon, M C -- Tocque, B -- New York, N.Y. -- Science. 1992 May 8;256(5058):825-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rhone-Poulenc Rorer, Centre de Recherche de Vitry-Alfortville, Vitry Sur Seine.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1317056" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Antigens, Polyomavirus Transforming/genetics ; CHO Cells ; *Cell Cycle Proteins ; *Cell Transformation, Neoplastic ; Chloramphenicol O-Acetyltransferase/genetics/metabolism ; Cricetinae ; *Enhancer Elements, Genetic ; Fungal Proteins/genetics/metabolism ; GTPase-Activating Proteins ; *Genes, ras ; Humans ; Mice ; Oncogene Proteins v-mos ; Oncogenes ; Polyomavirus/*genetics ; Promoter Regions, Genetic ; Protein-Tyrosine Kinases/genetics ; Proteins/*metabolism ; Retroviridae Proteins, Oncogenic/genetics ; Signal Transduction ; Simian virus 40/genetics ; Transcription, Genetic ; *Transcriptional Activation ; Transfection ; ras GTPase-Activating Proteins ; *ras-GRF1
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  • 23
    Publication Date: 1992-01-10
    Description: The progesterone analog RU486, an abortifacient, inhibits the action of progestins in humans but not in chickens or hamsters. Substitution of cysteine at position 575 by glycine in the hormone binding domain (HBD) of the chicken progesterone receptor (cPR) generated a cPR that binds RU486 and whose activity is antagonized by that compound. In fact, all receptors that bind RU486 have a glycine at the corresponding position. The hamster PR, like cPR, has a cysteine. Only glycine--not methionine or leucine--at position 575 allowed binding of RU486 to cPR. Substitution of this glycine by cysteine in the human PR (hPR) abrogated binding of RU486 but not that of an agonist. The corresponding mutation in the human glucocorticoid receptor resulted in a loss of binding of both dexamethasone and RU486. Examination of a series of 11 beta-substituted steroids showed that antagonism is not an intrinsic property of an antihormone, because one hPR antagonist acted as an agonist for a mutated hPR. The positioning of an aromatic 11 beta-substitution in the PR HBD appears to be critical for generating agonistic or antagonistic activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benhamou, B -- Garcia, T -- Lerouge, T -- Vergezac, A -- Gofflo, D -- Bigogne, C -- Chambon, P -- Gronemeyer, H -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):206-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department Endocrinologie, Centre de Recherche Roussel-Uclaf, Romainville, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1372753" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cricetinae ; Female ; Humans ; Mifepristone/*pharmacology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction ; Progesterone/analogs & derivatives/metabolism ; RNA/genetics/isolation & purification ; Receptors, Mineralocorticoid ; Receptors, Progesterone/*drug effects/genetics/metabolism ; Receptors, Steroid/drug effects/genetics/metabolism ; Recombinant Proteins/drug effects/metabolism ; Restriction Mapping ; Uterus/metabolism
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  • 24
    Publication Date: 1992-03-20
    Description: The suprachiasmatic nuclei (SCN) of the hypothalamus comprise the primary pacemaker responsible for generation of circadian rhythms in mammals. Light stimuli that synchronize this circadian clock induce expression of the c-fos gene in rodent SCN, which suggests a possible role for Fos in circadian entrainment. Appropriate light stimuli also induce the expression of jun-B messenger RNA in the SCN of golden hamsters but only slightly elevate c-jun messenger RNA levels. In addition, light increases the amount of a protein complex in the SCN that binds specifically to sites on DNA known to mediate regulation by the AP-1 transcription factor. The photic regulation of both jun-B messenger RNA expression and AP-1 binding activity is dependent on circadian phase: only light stimuli that shift behavioral rhythms induce jun-B and AP-1 expression. Thus, light and the circadian pacemaker interact to regulate a specific set of immediate-early genes in the SCN that may participate in entrainment of the circadian clock.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kornhauser, J M -- Nelson, D E -- Mayo, K E -- Takahashi, J S -- New York, N.Y. -- Science. 1992 Mar 20;255(5051):1581-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Neuroscience, Northwestern University, Evanston, IL 60208.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1549784" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cricetinae ; *Gene Expression Regulation ; Genes, fos/physiology ; Genes, jun/*physiology ; *Light ; Molecular Sequence Data ; Nucleic Acid Hybridization ; *Periodicity ; Proto-Oncogene Proteins c-jun/*biosynthesis ; RNA Probes ; RNA, Messenger/*biosynthesis ; Suprachiasmatic Nucleus/physiology ; Time Factors ; Transcription, Genetic
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  • 25
    Publication Date: 1992-07-10
    Description: The concentration of cytoplasmic free calcium (Ca2+) increases in various stimulated cells in a wave (Ca2+ wave) and in periodic transients (Ca2+ oscillations). These phenomena are explained by inositol 1,4,5-trisphosphate (IP3)-induced Ca2+ release (IICR) and Ca(2+)-induced Ca2+ release (CICR) from separate intracellular stores, but decisive evidence is lacking. A monoclonal antibody to the IP3 receptor inhibited both IICR and CICR upon injection of IP3 and Ca2+ into hamster eggs, respectively. The antibody completely blocked sperm-induced Ca2+ waves and Ca2+ oscillations. The results indicate that Ca2+ release in fertilized hamster eggs is mediated solely by the IP3 receptor, and Ca(2+)-sensitized IICR, but not CICR, generates Ca2+ waves and Ca2+ oscillations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miyazaki, S -- Yuzaki, M -- Nakada, K -- Shirakawa, H -- Nakanishi, S -- Nakade, S -- Mikoshiba, K -- New York, N.Y. -- Science. 1992 Jul 10;257(5067):251-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Tokyo Women's Medical College, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1321497" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Caffeine/pharmacology ; Calcium/*metabolism ; *Calcium Channels ; Cricetinae ; Dose-Response Relationship, Drug ; Fertilization/*physiology ; Immunoblotting ; Inositol 1,4,5-Trisphosphate Receptors ; Male ; Ovum/*metabolism ; Receptors, Cell Surface/drug effects/*physiology ; *Receptors, Cytoplasmic and Nuclear ; Ryanodine/pharmacology ; Spermatozoa/physiology ; Time Factors
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  • 26
    Publication Date: 1990-02-09
    Description: The Na+/H+ antiporter, which regulates intracellular pH in virtually all cells, is one of the best examples of a mitogen- and oncogene-activated membrane target whose activity rapidly changes on stimulation. The activating mechanism is unknown. A Na+/H+ antiporter complementary DNA fragment was expressed in Escherichia coli as a beta-galactosidase fusion protein, and a specific antibody to the fusion protein was prepared. Use of this antibody revealed that the Na+/H+ antiporter is a 110-kilodalton glycoprotein that is phosphorylated in growing cells. Mitogenic activation of resting hamster fibroblasts and A431 human epidermoid cells with epidermal growth factor, thrombin, phorbol esters, or serum, stimulated phosphorylation of the Na+/H+ antiporter with a time course similar to that of the rise in intracellular pH.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sardet, C -- Counillon, L -- Franchi, A -- Pouyssegur, J -- New York, N.Y. -- Science. 1990 Feb 9;247(4943):723-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre de Biochimie-CNRS, Nice, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2154036" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood ; Carrier Proteins/genetics/*metabolism ; Cell Line ; Cricetinae ; DNA/genetics ; Epidermal Growth Factor/pharmacology ; Escherichia coli/genetics ; Fibroblasts/metabolism ; Glycosylation ; Growth Substances/*pharmacology ; Humans ; Immunoblotting ; Mammary Tumor Virus, Mouse/genetics ; Molecular Weight ; Phosphorylation ; Promoter Regions, Genetic ; Recombinant Fusion Proteins/metabolism ; Sodium-Hydrogen Antiporter ; Thrombin/pharmacology ; Transfection ; beta-Galactosidase/genetics
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  • 27
    Publication Date: 1991-11-08
    Description: Intracellular signaling alters integrin adhesive functions in inflammation, immune responses, hemostasis, thrombosis, and retinal development. By truncating the cytoplasmic domain of alpha IIb, the affinity of integrin alpha IIb beta 3 for ligand was increased. Reconstitution with the cytoplasmic domain from integrin alpha 5 did not reverse the increased affinity. Thus, the cytoplasmic domain of the alpha subunit of GPIIb-IIIa controls ligand binding affinity, which suggests mechanisms for inside-out transmembrane signaling through integrins. These findings imply the existence of hitherto unappreciated hereditary and acquired thrombotic disorders in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Toole, T E -- Mandelman, D -- Forsyth, J -- Shattil, S J -- Plow, E F -- Ginsberg, M H -- HL 39150/HL/NHLBI NIH HHS/ -- HL16411/HL/NHLBI NIH HHS/ -- HL28235/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):845-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Committee on Vascular Biology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948065" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CHO Cells ; Cell Aggregation ; Cricetinae ; Cytoplasm/metabolism ; Fibrinogen/metabolism ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Platelet Membrane Glycoproteins/genetics/*physiology ; Transfection
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-07-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shieh, M T -- Spear, P G -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):208-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1649495" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cricetinae ; Fibroblast Growth Factors ; Heparitin Sulfate/metabolism ; Herpes Simplex/*metabolism ; In Vitro Techniques ; Receptors, Cell Surface/*physiology ; Receptors, Fibroblast Growth Factor ; Receptors, Virus/*physiology ; Simplexvirus/*metabolism
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  • 29
    Publication Date: 1992-07-17
    Description: The direct effects of pro-inflammatory cytokines on the contractility of mammalian heart were studied. Tumor necrosis factor alpha, interleukin-6, and interleukin-2 inhibited contractility of isolated hamster papillary muscles in a concentration-dependent, reversible manner. The nitric oxide synthase inhibitor NG-monomethyl-L-arginine (L-NMMA) blocked these negative inotropic effects. L-Arginine reversed the inhibition by L-NMMA. Removal of the endocardial endothelium did not alter these responses. These findings demonstrate that the direct negative inotropic effect of cytokines is mediated through a myocardial nitric oxide synthase. The regulation of pro-inflammatory cytokines and myocardial nitric oxide synthase may provide new therapeutic strategies for the treatment of cardiac disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finkel, M S -- Oddis, C V -- Jacob, T D -- Watkins, S C -- Hattler, B G -- Simmons, R L -- GM-37753/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 17;257(5068):387-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Pittsburgh School of Medicine, PA 15213.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1631560" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arginine/analogs & derivatives/pharmacology ; Cells, Cultured ; Cricetinae ; Cytokines/*pharmacology ; Dose-Response Relationship, Drug ; Drug Interactions ; Endocardium/cytology ; Epithelium/physiology ; Interleukin-2/pharmacology ; Interleukin-6/pharmacology ; Microscopy, Electron ; Myocardial Contraction/*drug effects ; Nitric Oxide/*pharmacology ; Tumor Necrosis Factor-alpha/pharmacology ; omega-N-Methylarginine
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  • 30
    Publication Date: 1993-03-12
    Description: Glucagon and the glucagon receptor are a primary source of control over blood glucose concentrations and are especially important to studies of diabetes in which the loss of control over blood glucose concentrations clinically defines the disease. A complementary DNA clone for the glucagon receptor was isolated by an expression cloning strategy, and the receptor protein was expressed in several kidney cell lines. The cloned receptor bound glucagon and caused an increase in the intracellular concentration of adenosine 3', 5'-monophosphate (cAMP). The cloned glucagon receptor also transduced a signal that led to an increased concentration of intracellular calcium. The glucagon receptor is similar to the calcitonin and parathyroid hormone receptors. It can transduce signals leading to the accumulation of two different second messengers, cAMP and calcium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jelinek, L J -- Lok, S -- Rosenberg, G B -- Smith, R A -- Grant, F J -- Biggs, S -- Bensch, P A -- Kuijper, J L -- Sheppard, P O -- Sprecher, C A -- New York, N.Y. -- Science. 1993 Mar 12;259(5101):1614-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ZymoGenetics Inc., Seattle, WA 98105.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8384375" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcium/pharmacology ; Cell Line ; Cloning, Molecular ; Cricetinae ; Cyclic AMP/metabolism ; Glucagon/metabolism/*pharmacology ; Kidney ; Kinetics ; Liver/*metabolism ; Molecular Sequence Data ; Rats ; Receptors, Gastrointestinal Hormone/genetics/metabolism/*physiology ; Receptors, Glucagon ; *Signal Transduction ; Transfection
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  • 31
    Publication Date: 1993-09-10
    Description: The function of voltage-gated sodium channels that are responsible for action potential generation in mammalian brain neurons is modulated by phosphorylation by adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase (cA-PK) and by protein kinase C (PKC). Reduction of peak sodium currents by cA-PK in intact cells required concurrent activation of PKC and was prevented by blocking phosphorylation of serine 1506, a site in the inactivation gate of the channel that is phosphorylated by PKC but not by cA-PK. Replacement of serine 1506 with negatively charged amino acids mimicked the effect of phosphorylation. Conversion of the consensus sequence surrounding serine 1506 to one more favorable for cA-PK enhanced modulation of sodium currents by cA-PK. Convergent modulation of sodium channels required phosphorylation of serine 1506 by PKC accompanied by phosphorylation of additional sites by cA-PK. This regulatory mechanism may serve to integrate neuronal signals mediated through these parallel signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, M -- West, J W -- Numann, R -- Murphy, B J -- Scheuer, T -- Catterall, W A -- R01-NS15751/NS/NINDS NIH HHS/ -- T32-GM07270/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 10;261(5127):1439-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8396273" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Amino Acid Sequence ; Animals ; CHO Cells ; Consensus Sequence ; Cricetinae ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phosphorylation ; Protein Kinase C/*metabolism ; Protein Kinases/*metabolism ; Sodium/metabolism ; Sodium Channels/*metabolism
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  • 32
    Publication Date: 1993-06-25
    Description: Oncogenic Ras proteins transform animal cells to a malignant phenotype only when modified by farnesyl residues attached to cysteines near their carboxyl termini. The farnesyltransferase that catalyzes this reaction recognizes tetrapeptides of the sequence CAAX, where C is cysteine, A is an aliphatic amino acid, and X is a carboxyl-terminal methionine or serine. Replacement of the two aliphatic residues with a benzodiazepine-based mimic of a peptide turn generated potent inhibitors of farnesyltransferase [50 percent inhibitory concentration (IC50) 〈 1 nM]. Unlike tetrapeptides, the benzodiazepine peptidomimetics enter cells and block attachment of farnesyl to Ras, nuclear lamins, and several other proteins. At micromolar concentrations, these inhibitors restored a normal growth pattern to Ras-transformed cells. The benzodiazepine peptidomimetics may be useful in the design of treatments for tumors in which oncogenic Ras proteins contribute to abnormal growth, such as that of the colon, lung, and pancreas.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉James, G L -- Goldstein, J L -- Brown, M S -- Rawson, T E -- Somers, T C -- McDowell, R S -- Crowley, C W -- Lucas, B K -- Levinson, A D -- Marsters, J C Jr -- HL 20948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jun 25;260(5116):1937-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8316834" target="_blank"〉PubMed〈/a〉
    Keywords: *Alkyl and Aryl Transferases ; Amino Acid Sequence ; Animals ; Antineoplastic Agents/chemistry/*pharmacology ; Benzodiazepinones/chemistry/*pharmacology ; CHO Cells ; Cell Division/drug effects ; Cell Line, Transformed ; Cell Transformation, Neoplastic/drug effects ; Cricetinae ; Drug Design ; Farnesyltranstransferase ; Molecular Sequence Data ; Oligopeptides/pharmacology ; Oncogene Proteins/*metabolism ; Protein Prenylation/*drug effects ; Transferases/*antagonists & inhibitors
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  • 33
    Publication Date: 1994-04-15
    Description: The first step in oral absorption of many medically important peptide-based drugs is mediated by an intestinal proton-dependent peptide transporter. This transporter facilitates the oral absorption of beta-lactam antibiotics and angiotensin-converting enzyme inhibitors from the intestine into enterocytes lining the luminal wall. A monoclonal antibody that blocked uptake of cephalexin was used to identify and clone a gene that encodes an approximately 92-kilodalton membrane protein that was associated with the acquisition of peptide transport activity by transport-deficient cells. The amino acid sequence deduced from the complementary DNA sequence of the cloned gene indicated that this transport-associated protein shares several conserved structural elements with the cadherin superfamily of calcium-dependent, cell-cell adhesion proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dantzig, A H -- Hoskins, J A -- Tabas, L B -- Bright, S -- Shepard, R L -- Jenkins, I L -- Duckworth, D C -- Sportsman, J R -- Mackensen, D -- Rosteck, P R Jr -- New York, N.Y. -- Science. 1994 Apr 15;264(5157):430-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN 46285.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8153632" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport ; CHO Cells ; Cadherins/*chemistry ; Carrier Proteins/*chemistry/genetics/isolation & purification/metabolism ; Cephalexin/*metabolism ; Cloning, Molecular ; Cricetinae ; Glycosylation ; Humans ; Hydrogen-Ion Concentration ; Intestinal Mucosa/*metabolism ; Leucine/analogs & derivatives/metabolism ; *Membrane Transport Proteins ; Mice ; Mice, Inbred A ; Molecular Sequence Data ; Open Reading Frames ; Sequence Homology, Amino Acid ; Transfection ; Tumor Cells, Cultured
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  • 34
    Publication Date: 1993-11-05
    Description: Stimulation of T cell proliferation generally requires two signals: The first signal is provided by the T cell receptor binding to antigen, and the second signal or costimulus is provided by a different receptor-ligand interaction. In mouse and human, the CD28-B7 interaction has been identified as a source of costimulatory signals. We have identified a cell surface molecule (GL1) that is distinct from B7 and abundantly expressed on activated B cells. On activated B cells GL1, rather than B7, is the predominant ligand for the T cell-activation molecule CTLA-4. GL1 provides a critical signal for T cell-dependent responses in vitro and in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hathcock, K S -- Laszlo, G -- Dickler, H B -- Bradshaw, J -- Linsley, P -- Hodes, R J -- New York, N.Y. -- Science. 1993 Nov 5;262(5135):905-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7694361" target="_blank"〉PubMed〈/a〉
    Keywords: Abatacept ; Animals ; Antibodies, Monoclonal ; Antigens, CD/metabolism ; Antigens, CD18 ; Antigens, CD80/immunology/*metabolism ; Antigens, Differentiation/*metabolism ; Antigens, Surface/immunology/*metabolism ; B-Lymphocytes/*immunology ; CHO Cells ; CTLA-4 Antigen ; Cricetinae ; *Immunoconjugates ; Interleukin-2/biosynthesis ; *Lymphocyte Activation ; Mice ; T-Lymphocytes/*immunology
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  • 35
    Publication Date: 1993-04-16
    Description: A fundamental problem in the identification and isolation of tumor suppressor and other growth-inhibiting genes is the loss of power of genetic complementation at the subchromosomal level. A direct genetic strategy was developed to isolate subchromosomal transferable fragments (STFs) from any chromosome, each containing a selectable marker within the human DNA, that could be transferred to any mammalian cell. As a test of the method, several overlapping STFs from 11p15 were shown to cause in vitro growth arrest of rhabdomyosarcoma cells. This activity mapped between the beta-globin and insulin genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koi, M -- Johnson, L A -- Kalikin, L M -- Little, P F -- Nakamura, Y -- Feinberg, A P -- CA54358/CA/NCI NIH HHS/ -- T32GM07314/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Apr 16;260(5106):361-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Internal Medicine, University of Michigan Medical School, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8469989" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; CHO Cells ; Cell Division ; Cell Line ; *Chromosomes, Human, Pair 11 ; Cricetinae ; DNA/*genetics ; *Genes, Tumor Suppressor ; Genetic Markers ; *Genetic Techniques ; Globins/genetics ; Humans ; Insulin/genetics ; Mice ; Molecular Sequence Data ; Rhabdomyosarcoma/*pathology ; Tumor Cells, Cultured
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  • 36
    Publication Date: 1994-10-14
    Description: Three genetic complementation groups of rodent cells are defective for both repair of x-ray-induced double-strand breaks and V(D)J recombination. Cells from one group lack a DNA end-binding activity that is biochemically and antigenically similar to the Ku autoantigen. Transfection of complementary DNA (cDNA) that encoded the 86-kilodalton subunit of Ku rescued these mutant cells for DNA end-binding activity, x-ray resistance, and V(D)J recombination activity. These results establish a role for Ku in DNA repair and recombination. Furthermore, as a component of a DNA-dependent protein kinase, Ku may initiate a signaling pathway induced by DNA damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smider, V -- Rathmell, W K -- Lieber, M R -- Chu, G -- New York, N.Y. -- Science. 1994 Oct 14;266(5183):288-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Stanford University Medical Center, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939667" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, Nuclear ; Cell Line ; Cell Line, Transformed ; Cell Survival/*radiation effects ; Cricetinae ; DNA/*metabolism ; *DNA Helicases ; *DNA Repair ; DNA, Complementary ; DNA-Binding Proteins/genetics/*physiology ; Gene Rearrangement ; Genetic Complementation Test ; Humans ; Nuclear Proteins/genetics/*physiology ; Radiation Tolerance ; *Recombination, Genetic ; Transfection
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  • 37
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-10-21
    Description: The endoplasmic reticulum (ER) contains molecular chaperones that facilitate the folding of proteins in mammalian cells. Biosynthetic labeling was used to study the interactions of two chaperones, BiP and calnexin, with vesicular stomatitis virus (VSV) glycoprotein (G protein). Coimmunoprecipitation of G protein with the chaperones showed that BiP bound maximally to early folding intermediates of G protein, whereas calnexin bound after a short lag to more folded molecules. Castanospermine, an inhibitor of ER glucosidases, blocked the binding of proteins to calnexin and inhibited G protein folding. Interaction with calnexin was necessary for efficient folding of G protein and for retention of partially folded forms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hammond, C -- Helenius, A -- P01 CA46128/CA/NCI NIH HHS/ -- R01 GM38346/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 21;266(5184):456-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939687" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CHO Cells ; Calcium-Binding Proteins/chemistry/*metabolism ; Calnexin ; Carrier Proteins/chemistry/*metabolism ; Cell Membrane/metabolism ; Cricetinae ; Cytoplasm/metabolism ; Glycoproteins/*chemistry/metabolism ; Heat-Shock Proteins/chemistry/metabolism ; Indolizines/pharmacology ; *Membrane Glycoproteins ; *Molecular Chaperones ; Protein Folding ; Vesicular stomatitis Indiana virus/*chemistry/physiology ; Viral Envelope Proteins/*chemistry/metabolism
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  • 38
    Publication Date: 1993-04-09
    Description: Mammalian circadian rhythms are regulated by a pacemaker within the suprachiasmatic nuclei (SCN) of the hypothalamus. The molecular mechanisms controlling the synchronization of the circadian pacemaker are unknown; however, immediate early gene (IEG) expression in the SCN is tightly correlated with entrainment of SCN-regulated rhythms. Antibodies were isolated that recognize the activated, phosphorylated form of the transcription factor cyclic adenosine monophosphate response element binding protein (CREB). Within minutes after exposure of hamsters to light, CREB in the SCN became phosphorylated on the transcriptional regulatory site, Ser133. CREB phosphorylation was dependent on circadian time: CREB became phosphorylated only at times during the circadian cycle when light induced IEG expression and caused phase shifts of circadian rhythms. These results implicate CREB in neuronal signaling in the hypothalamus and suggest that circadian clock gating of light-regulated molecular responses in the SCN occurs upstream of phosphorylation of CREB.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ginty, D D -- Kornhauser, J M -- Thompson, M A -- Bading, H -- Mayo, K E -- Takahashi, J S -- Greenberg, M E -- F31 MH10241/MH/NIMH NIH HHS/ -- F32 NS08764/NS/NINDS NIH HHS/ -- NS 28829/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Apr 9;260(5105):238-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8097062" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; *Circadian Rhythm ; Colforsin/pharmacology ; Cricetinae ; Cyclic AMP Response Element-Binding Protein/immunology/*metabolism ; Darkness ; Gene Expression Regulation ; Genes, fos ; Glutamates/pharmacology ; Glutamic Acid ; *Light ; Molecular Sequence Data ; PC12 Cells ; Phosphorylation ; Potassium Chloride/pharmacology ; Suprachiasmatic Nucleus/drug effects/*metabolism
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  • 39
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-08-05
    Description: The osmotic balance between the cytoplasmic and extracellular compartments of cells is critical for the control of cell volume. A mammalian protein kinase, Jnk, which is a distant relative of the mitogen-activated protein kinase group, was activated by phosphorylation on threonine and tyrosine in osmotically shocked cells. The activation of Jnk may be relevant to the biological response to osmotic shock because the expression of human Jnk in the yeast Saccharomyces cerevisiae rescued a defect in growth on hyper-osmolar media. These data indicate that related protein kinases may mediate osmosensing signal transduction in yeast and mammalian cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galcheva-Gargova, Z -- Derijard, B -- Wu, I H -- Davis, R J -- New York, N.Y. -- Science. 1994 Aug 5;265(5173):806-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester 01605.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8047888" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CHO Cells ; Calcium-Calmodulin-Dependent Protein Kinases/genetics ; Cricetinae ; Cricetulus ; Enzyme Activation ; Genetic Complementation Test ; JNK Mitogen-Activated Protein Kinases ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Osmotic Pressure ; Protein-Serine-Threonine Kinases/*physiology ; Saccharomyces cerevisiae/genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Amino Acid ; Signal Transduction/*physiology ; Water-Electrolyte Balance/*physiology
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  • 40
    Publication Date: 1994-09-02
    Description: The radiosensitive mutant xrs-6, derived from Chinese hamster ovary cells, is defective in DNA double-strand break repair and in ability to undergo V(D)J recombination. The human XRCC5 DNA repair gene, which complements this mutant, is shown here through genetic and biochemical evidence to be the 80-kilodalton subunit of the Ku protein. Ku binds to free double-stranded DNA ends and is the DNA-binding component of the DNA-dependent protein kinase. Thus, the Ku protein is involved in DNA repair and in V(D)J recombination, and these results may also indicate a role for the Ku-DNA-dependent protein kinase complex in those same processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taccioli, G E -- Gottlieb, T M -- Blunt, T -- Priestley, A -- Demengeot, J -- Mizuta, R -- Lehmann, A R -- Alt, F W -- Jackson, S P -- Jeggo, P A -- AI 20047/AI/NIAID NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1994 Sep 2;265(5177):1442-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Children's Hospital, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8073286" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, Nuclear ; Base Sequence ; CHO Cells ; Cell Survival/radiation effects ; Cloning, Molecular ; Cricetinae ; DNA Damage ; *DNA Helicases ; DNA Repair/*genetics ; DNA-Binding Proteins/*genetics/metabolism ; *Genes, Immunoglobulin ; Genetic Complementation Test ; Humans ; Hybrid Cells ; Molecular Sequence Data ; Nuclear Proteins/*genetics/metabolism ; Receptors, Antigen, T-Cell/*genetics ; *Recombination, Genetic ; Transfection
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-01-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nowak, R -- New York, N.Y. -- Science. 1994 Jan 7;263(5143):30-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7903824" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cilia/physiology ; Cricetinae ; Extracellular Matrix/*physiology ; Fallopian Tubes/*physiology ; Female ; Genes, Homeobox ; *Genes, Plant ; Humans ; Plants, Toxic ; Smoke/*adverse effects ; Tobacco ; Zea mays/*genetics/growth & development
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  • 42
    Publication Date: 1992-08-07
    Description: In vitro, when the B7 molecule on the surface of antigen-presenting cells binds to the T cell surface molecules CD28 and CTLA-4, a costimulatory signal for T cell activation is generated. CTLA4Ig is a soluble form of the extracellular domain of CTLA-4 and binds B7 with high avidity. CTLA4Ig treatment in vivo suppressed T cell-dependent antibody responses to sheep erythrocytes or keyhole limpet hemocyanin. Large doses of CTLA4Ig suppressed responses to a second immunization. Thus, costimulation by B7 is important for humoral immune responses in vivo, and interference with costimulation may be useful for treatment of antibody-mediated autoimmune disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Linsley, P S -- Wallace, P M -- Johnson, J -- Gibson, M G -- Greene, J L -- Ledbetter, J A -- Singh, C -- Tepper, M A -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):792-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bristol-Myers Squibb Pharmaceutical Research Institute, Seattle, WA 98121.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1496399" target="_blank"〉PubMed〈/a〉
    Keywords: Abatacept ; Animals ; Antibody Formation/*drug effects ; Antigens, CD ; Antigens, Differentiation/*immunology/metabolism ; CHO Cells ; CTLA-4 Antigen ; Cricetinae ; Erythrocytes/immunology ; Hemocyanin/immunology ; Humans ; Immunization ; *Immunoconjugates ; Immunosuppressive Agents/pharmacokinetics/*pharmacology ; Lymphocyte Activation ; Metabolic Clearance Rate ; Mice ; Mice, Inbred BALB C ; Mice, Inbred Strains ; Recombinant Fusion Proteins/pharmacokinetics/pharmacology ; T-Lymphocytes/*immunology
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  • 43
    Publication Date: 1993-04-09
    Description: Cells maintain the integrity of their genome through an intricate network of repair systems that recognize and remove lesions from DNA. The only known site-directed recombination process in vertebrates is the V(D)J recombination of lymphocyte antigen receptor genes. A large panel of cell lines deficient in DNA repair were tested for the ability to perform V(D)J recombination after introduction of the RAG-1 and RAG-2 genes. Two mutants failed to generate normal V(D)J recombination, and further analysis provided evidence for two distinct nonlymphoid-specific genes that encode factors involved in both DNA repair and V(D)J recombination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taccioli, G E -- Rathbun, G -- Oltz, E -- Stamato, T -- Jeggo, P A -- Alt, F W -- AI 20047/AI/NIAID NIH HHS/ -- CA45277/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Apr 9;260(5105):207-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Children's Hospital, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8469973" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; CHO Cells ; Cell Line ; Cricetinae ; DNA Nucleotidyltransferases/genetics/metabolism ; *DNA Repair ; *Gene Rearrangement, T-Lymphocyte ; *Genes, RAG-1 ; Immunoglobulin Heavy Chains ; Molecular Sequence Data ; Mutation ; Receptors, Antigen, T-Cell/*genetics ; Recombination, Genetic ; VDJ Recombinases
    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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  • 44
    Publication Date: 1993-10-29
    Description: The Spermann organizer induces neural tissue from dorsal ectoderm and dorsalizes lateral and ventral mesoderm in Xenopus. The secreted factor noggin, which is expressed in the organizer, can mimic the dorsalizing signal of the organizer. Data are presented showing that noggin directly induces neural tissue, that it induces neural tissue in the absence of dorsal mesoderm, and that it acts at the appropriate stage to be an endogenous neural inducing signal. Noggin induces cement glands and anterior brain markers, but not hindbrain or spinal cord markers. Thus, noggin has the expression pattern and activity expected of an endogenous neural inducer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lamb, T M -- Knecht, A K -- Smith, W C -- Stachel, S E -- Economides, A N -- Stahl, N -- Yancopolous, G D -- Harland, R M -- New York, N.Y. -- Science. 1993 Oct 29;262(5134):713-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235591" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastocyst/metabolism ; CHO Cells ; Carrier Proteins ; Cricetinae ; Embryonic Induction/*physiology ; Gastrula/metabolism ; Humans ; Mesoderm/metabolism ; Nervous System/*embryology ; Proteins/*physiology ; RNA, Messenger/metabolism ; Recombinant Proteins ; Xenopus
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 45
    Publication Date: 1979-09-14
    Description: Inoculation of suckling hamsters with 2 x 10(8) live cells of Escherichia coli K12 strain chi1776, carrying the complete genome of polyoma virus in a recombinant plasmid, failed to induce tumors in any of 32 recipients. Also, lambda phage DNA and particles with a monomeric insert of polyoma DNA did not induce tumors. Purified recombinant plasmid DNA, as well as phage particles and DNA containing a head-to-tail dimer of polyoma DNA, showed a low degree of oncogenicity, comparable to that of polyoma DNA prepared from mouse cells. These findings support the previous conclusions, based on infectivity assays in mice, that propagation of polyoma virus DNA as a component of recombinant DNA molecules in E. coli K12 reduces its biologic activity many orders of magnitude relative to the virus itself.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Israel, M A -- Chan, H W -- Martin, M A -- Rowe, W P -- New York, N.Y. -- Science. 1979 Sep 14;205(4411):1140-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/224458" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Coliphages/genetics ; Cricetinae ; *DNA, Recombinant ; DNA, Viral/*genetics ; Escherichia coli/*genetics ; Neoplasms, Experimental/*etiology ; Plasmids ; Polyomavirus/*genetics ; Risk
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 46
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-09-14
    Description: When pyramidal tract axons are cut in the adult hamster, fibers degenerate in both anterograde and retrograde directions from the lesion. If the same operation is performed on infant hamsters, however, there is massive regrowth of the severed axons via a new brainstem pathway to their appropriate terminal sites in the medulla and spinal cord. In contrast to previous studies, these results suggest that axons in the mammalian central nervous system damaged early in life may regenerate in a functionally useful way.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kalil, K -- Reh, T -- New York, N.Y. -- Science. 1979 Sep 14;205(4411):1158-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/472734" target="_blank"〉PubMed〈/a〉
    Keywords: Age Factors ; Animals ; Animals, Newborn/*physiology ; Axons/physiology ; Behavior, Animal/physiology ; Brain Stem/growth & development ; Cricetinae ; Functional Laterality ; *Nerve Regeneration ; Neural Pathways/growth & development ; Pyramidal Tracts/*growth & development ; Spinal Cord/growth & development
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 47
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-11-30
    Description: Wild-type Chinese hamster V79 cells (6-thioguanine-sensitive) reduce the recovery of 6-thioguanine-resistant cells when they are cultured together at high densities, through a form of intercellular communication (metabolic cooperation). Cooperation is inhibited by 12-O-tetradecanoyl phorbol-13-acetate, rescuing the 6-thioguanine-resistant cells. These results may be useful in the study of an aspect of the mechanism of tumor promotion and in assaying for promoters.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yotti, L P -- Chang, C C -- Trosko, J E -- New York, N.Y. -- Science. 1979 Nov 30;206(4422):1089-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/493994" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Communication/*drug effects ; Cell Membrane/drug effects ; Cricetinae ; Dose-Response Relationship, Drug ; Drug Resistance ; Phorbol Esters/*pharmacology ; Phorbols/*pharmacology ; Structure-Activity Relationship ; Tetradecanoylphorbol Acetate/pharmacology ; Thioguanine/pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 48
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-06-29
    Description: A domestic dog residing in New England suffered a fatal febrile illness caused by a Babesia infection. The morphology of these intraerythrocytic protozoa and the range of hosts that could be infected experimentally suggested that the parasite was B. gibsoni. Although this tick-bourne disease is enzootic in wild and domestic Canidae in Africa and Asia, it appears to be new to the Americas.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, J F -- Magnarelli, L A -- Donner, C S -- Spielman, A -- Piesman, J -- New York, N.Y. -- Science. 1979 Jun 29;204(4400):1431-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/451574" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arthropod Vectors ; Babesia/classification/cytology ; Babesiosis/epidemiology/*parasitology/transmission ; Cricetinae ; Dog Diseases/*parasitology ; Dogs ; Erythrocytes/parasitology ; Mice ; United States
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 49
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-07-27
    Description: The channels in the junctions of various mammalian cell types--primary cultures and lines--were probed with a series of linear fluorescent amino acid and peptide molecules of different size and charge. Permeability is limited by probe size and electronegativity, these two factors apparently being related reciprocally. In respect to both factors, mammalian junctional channels are more restrictive than insect channels; hence the mammalian channels are narrower, more polar, or both. The channels of the various mammalian cell types differed slightly from each other; in some types the serum of the culture medium affected the channel permeability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flagg-Newton, J -- Simpson, I -- Loewenstein, W R -- New York, N.Y. -- Science. 1979 Jul 27;205(4404):404-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/377490" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Membrane/physiology ; *Cell Membrane Permeability ; Cells, Cultured ; Cricetinae ; Fluorescent Antibody Technique ; Kidney ; Mice ; Mice, Inbred BALB C ; Species Specificity
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  • 50
    Publication Date: 1979-10-19
    Description: Experimental infection of hamster ciliated tracheal epithelium in organ culture with virulent Mycoplasma pneumoniae resulted in the deterioration o ciliary necklaces and an altered distribution of membrane-associated particles on the shafts of the affected cilia. To our knowledge that is the first report of an altered disposition of ciliary membrane-associated particles in response to a specific infectious agent.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carson, J L -- Collier, A M -- Clyde, W A Jr -- New York, N.Y. -- Science. 1979 Oct 19;206(4416):349-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/113877" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/ultrastructure ; Cilia/ultrastructure ; Cricetinae ; Culture Techniques ; Epithelium/ultrastructure ; Mycoplasma Infections/*pathology ; Mycoplasma pneumoniae ; Trachea/*pathology/ultrastructure
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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