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  • Articles  (1,210)
  • Cell & Developmental Biology  (965)
  • Female  (140)
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  • Phosphorylation
  • 1995-1999  (1,210)
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  • 1995  (1,210)
  • Medicine  (1,210)
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  • Articles  (1,210)
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  • 1995-1999  (1,210)
  • 1945-1949
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  • 1
    Publication Date: 1995-09-08
    Description: Centromeres attach chromosomes to the spindle during mitosis, thereby ensuring the equal distribution of chromosomes into daughter cells. Transcriptionally silent heterochromatin of unknown function is associated with centromeres in many organisms. In the fission yeast Schizosaccharomyces pombe, the silent mating-type loci, centromeres, and telomeres are assembled into silent heterochromatin-like domains. The Swi6 chromodomain protein affects this silencing, and now it is shown that Swi6p localizes with these three chromosomal regions. In cells lacking Swi6p, centromeres lag on the spindle during anaphase and chromosomes are lost at high rates. Thus, Swi6p is located at fission yeast centromeres and is required for their proper function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ekwall, K -- Javerzat, J P -- Lorentz, A -- Schmidt, H -- Cranston, G -- Allshire, R -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1429-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Human Genetics Unit, Western General Hospital, Edinburgh, Scotland, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660126" target="_blank"〉PubMed〈/a〉
    Keywords: Centromere/chemistry/*physiology ; Chromosomes, Fungal ; Fluorescent Antibody Technique ; Fungal Proteins/analysis/genetics/*physiology ; Genes, Fungal ; Genes, Mating Type, Fungal ; Heterochromatin/chemistry ; In Situ Hybridization, Fluorescence ; Interphase ; Mitosis ; Mutation ; *Saccharomyces cerevisiae Proteins ; Schizosaccharomyces/cytology/genetics/*physiology ; Telomere/chemistry ; Transcription Factors/analysis/genetics/*physiology
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  • 2
    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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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-09-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erikson, J -- New York, N.Y. -- Science. 1995 Sep 15;269(5230):1508-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7667631" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; *Biomedical Research ; *Breast Neoplasms ; *Consumer Advocacy ; Consumer Organizations ; Ethical Review ; Federal Government ; Female ; Humans ; National Institutes of Health (U.S.) ; Peer Review, Research ; *Research ; United States
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-09-29
    Description: In the nuclei of eukaryotic cells, initiation of DNA replication occurs at a discrete number of foci. One component of these foci is the DNA replication factor RP-A. Here, the process leading to the association of RP-A with foci was reconstituted with cytosolic fractions derived from Xenopus eggs. With the use of this fractionated system, a 170-kilodalton protein required for the assembly of RP-A into foci was identified and purified. The protein appears to be an integral component of the foci at which replication of DNA is initiated in eukaryotic nuclei.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yan, H -- Newport, J -- GM33523/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 29;269(5232):1883-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of California, San Diego, Department of Biology, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569932" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/*metabolism ; Cell-Free System ; Cytosol/chemistry ; *DNA Replication ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/*metabolism ; Female ; Male ; Molecular Weight ; Oocytes ; Orientation ; Proteins/chemistry/*metabolism ; Replication Protein A ; Xenopus
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  • 5
    Publication Date: 1995-10-06
    Description: Furosemide, a chloride cotransport inhibitor, reversibly blocked synchronized burst discharges in hippocampal slices without reducing the pyramidal cell response to single electrical stimuli. Images of the intrinsic optical signal acquired during these slice experiments indicated that furosemide coincidentally blocked changes in extracellular space. In urethane-anesthetized rats, systemically injected furosemide blocked kainic acid-induced electrical discharges recorded from cortex. These results suggest that (i) neuronal synchronization involved in epileptiform activity can be dissociated from synaptic excitability; (ii) nonsynaptic mechanisms, possibly associated with furosemide-sensitive cell volume regulation, may be critical for synchronization of neuronal activity; and (iii) agents that affect extracellular volume may have clinical utility as antiepileptic drugs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hochman, D W -- Baraban, S C -- Owens, J W -- Schwartzkroin, P A -- NS07144/NS/NINDS NIH HHS/ -- NS15317/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 6;270(5233):99-102.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurological Surgery, University of Washington, Seattle 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569957" target="_blank"〉PubMed〈/a〉
    Keywords: 4-Aminopyridine/pharmacology ; Animals ; Anticonvulsants/*pharmacology ; Bicuculline/pharmacology ; Electric Stimulation ; Entorhinal Cortex/physiology ; Extracellular Space/drug effects/physiology ; Female ; Furosemide/*pharmacology ; Hippocampus/drug effects/*physiology ; In Vitro Techniques ; Kainic Acid/pharmacology ; Magnesium/pharmacology ; Male ; Membrane Potentials/drug effects ; Potassium/pharmacology ; Pyramidal Cells/drug effects/*physiology ; Rats ; Rats, Sprague-Dawley ; Status Epilepticus/chemically induced/*physiopathology ; Synaptic Transmission/drug effects
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-10-20
    Description: Over the past two decades, the small soil nematode Caenorhabditis elegans has become established as a major model system for the study of a great variety of problems in biology and medicine. One of its most significant advantages is its simplicity, both in anatomy and in genomic organization. The entire haploid genetic content amounts to 100 million base pairs of DNA, about 1/30 the size of the human value. As a result, C. elegans has also provided a pilot system for the construction of physical maps of larger animal and plant genomes, and subsequently for the complete sequencing of those genomes. By mid-1995, approximately one-fifth of the complete DNA sequence of this animal had been determined. Caenorhabditis elegans provides a test bed not only for the development and application of mapping and sequencing technologies, but also for the interpretation and use of complete sequence information. This article reviews the progress so far toward a realizable goal--the total description of the genome of a simple animal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hodgkin, J -- Plasterk, R H -- Waterston, R H -- New York, N.Y. -- Science. 1995 Oct 20;270(5235):410-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569995" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*genetics ; *Chromosome Mapping ; Gene Expression ; *Genes, Helminth ; *Genome ; Mutation ; *Sequence Analysis, DNA
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-05-12
    Description: Mutations in genes required for associative learning and memory in Drosophila exist, but isolation of the genes has been difficult because most are defined by a single, chemically induced allele. Here, a simplified genetic screen was used to identify candidate genes involved in learning and memory. Second site suppressors of the dunce (dnc) female sterility phenotype were isolated with the use of transposon mutagenesis. One suppressor mutation that was recovered mapped in the amnesiac (amn) gene. Cloning of the locus revealed that amn encodes a previously uncharacterized neuropeptide gene. Thus, with the cloning of amn, specific neuropeptides are implicated in the memory process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feany, M B -- Quinn, W G -- New York, N.Y. -- Science. 1995 May 12;268(5212):869-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754370" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; Codon ; DNA Transposable Elements ; DNA, Complementary/genetics ; Drosophila/*genetics/physiology ; *Drosophila Proteins ; Female ; *Genes, Insect ; Growth Hormone-Releasing Hormone/chemistry/genetics ; Male ; Memory/*physiology ; Molecular Sequence Data ; Mutagenesis, Insertional ; Mutation ; Neuropeptides/chemistry/*genetics ; Pituitary Adenylate Cyclase-Activating Polypeptide ; Sequence Homology, Amino Acid ; Suppression, Genetic
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  • 8
    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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  • 9
    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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  • 10
    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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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-07-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aitken, R J -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):39-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Reproductive Biology Unit, Medical Research Council, Edinburgh, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604276" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Egg Proteins/*metabolism ; Female ; Humans ; Lectins/metabolism ; Male ; Membrane Glycoproteins/*metabolism ; Mice ; Phosphorylation ; Proto-Oncogene Proteins ; Receptor Protein-Tyrosine Kinases/*metabolism ; Receptors, Cell Surface/*metabolism ; Sperm-Ovum Interactions/*physiology ; Spermatozoa/metabolism ; Zona Pellucida/*metabolism
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  • 12
    Publication Date: 1995-05-05
    Description: Fragile X syndrome is the result of the unstable expansion of a trinucleotide repeat in the 5'-untranslated region of the FMR1 gene. Fibroblast subclones from a mildly affected patient, each containing stable FMR1 alleles with 57 to 285 CGG repeats, were shown to exhibit normal steady-state levels of FMR1 messenger RNA. However, FMR protein was markedly diminished from transcript with more than 200 repeats. Such transcripts were associated with stalled 40S ribosomal subunits. These results suggest that a structural RNA transition beyond 200 repeats impedes the linear 40S migration along the 5'-untranslated region. This results in translational inhibition by trinucleotide repeat expansion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, Y -- Zhang, F -- Lokey, L K -- Chastain, J L -- Lakkis, L -- Eberhart, D -- Warren, S T -- HD20521/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1995 May 5;268(5211):731-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Emory University School of Medicine, Atlanta, GA 30322.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7732383" target="_blank"〉PubMed〈/a〉
    Keywords: Centrifugation, Density Gradient ; Clone Cells ; Down-Regulation/genetics ; Female ; Fibroblasts/chemistry ; Fragile X Mental Retardation Protein ; Fragile X Syndrome/*genetics ; Humans ; Infant ; Male ; Nerve Tissue Proteins/*genetics ; Polymerase Chain Reaction ; Protein Biosynthesis/*genetics ; RNA, Messenger/analysis ; *RNA-Binding Proteins ; Repetitive Sequences, Nucleic Acid/*genetics
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  • 13
    Publication Date: 1995-05-05
    Description: The aryl hydrocarbon (Ah) receptor (AHR) mediates many carcinogenic and teratogenic effects of environmentally toxic chemicals such as dioxin. An AHR-deficient (Ahr-/-) mouse line was constructed by homologous recombination in embryonic stem cells. Almost half of the mice died shortly after birth, whereas survivors reached maturity and were fertile. The Ahr-/- mice showed decreased accumulation of lymphocytes in the spleen and lymph nodes, but not in the thymus. The livers of Ahr-/- mice were reduced in size by 50 percent and showed bile duct fibrosis Ahr-/- mice were also nonresponsive with regard to dioxin-mediated induction of genes encoding enzymes that catalyze the metabolism of foreign compounds. Thus, the AHR plays an important role in the development of the liver and the immune system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fernandez-Salguero, P -- Pineau, T -- Hilbert, D M -- McPhail, T -- Lee, S S -- Kimura, S -- Nebert, D W -- Rudikoff, S -- Ward, J M -- Gonzalez, F J -- P30 ES06096/ES/NIEHS NIH HHS/ -- R01 ES06811/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1995 May 5;268(5211):722-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Carcinogenesis, National Cancer 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/7732381" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Gene Expression Regulation/physiology ; Immunity/*physiology ; Liver/*physiology ; Liver Cirrhosis, Experimental/genetics/pathology ; Lymphoid Tissue/pathology ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Receptors, Aryl Hydrocarbon/genetics/*physiology
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mongella, G -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):789-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fourth World Conference on Women, United Nations, New York, NY 10017, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638591" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/epidemiology/transmission ; Aging ; Biomedical Research ; Female ; *Global Health ; Health Promotion ; Humans ; *Internationality ; Life Expectancy ; Male ; Neoplasms/epidemiology ; Poverty ; Research ; Research Support as Topic ; Resource Allocation ; Sex Characteristics ; Violence ; *Women's Health ; Women's Health Services ; World Health Organization
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-04-28
    Description: Epstein-Barr virus (EBV) nuclear antigen 2 (EBNA2) is a transcriptional activator that is essential for EBV-driven B cell immortalization. EBNA2 is targeted to responsive promoters through interaction with a cellular DNA binding protein, C promoter binding factor 1 (CBF1). A transcriptional repression domain has been identified within CBF1. This domain also interacts with EBNA2, and repression is masked by EBNA2 binding. Thus, EBNA2 acts by countering transcriptional repression. Mutation at amino acid 233 of CBF1 abolishes repression and correlates with a loss-of-function mutation in the Drosophila homolog Su(H).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hsieh, J J -- Hayward, S D -- CA42245/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):560-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Molecular Sciences, 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/7725102" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Viral/chemistry/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Epstein-Barr Virus Nuclear Antigens ; *Gene Expression Regulation ; HeLa Cells ; Humans ; Immunoglobulin J Recombination Signal Sequence-Binding Protein ; Models, Genetic ; Mutation ; *Nuclear Proteins ; Promoter Regions, Genetic ; Trans-Activators/chemistry/*metabolism ; *Transcription, Genetic ; Transfection
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  • 16
    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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  • 17
    Publication Date: 1995-02-10
    Description: The neural basis of sexual orientation in Drosophila was studied by the production of males with regionally feminized brains. Such flies express the female form of the sex determination gene transformer in a limited number of neurons under the control of GAL4 enhancer trap inserts. This method facilitated the creation of lines with a stable pattern of feminization. In tests of sexual preferences, flies that were feminized in a portion of the antennal lobes or in a subset of the corpora pedunculata (mushroom bodies) courted both males and females. These two brain structures, both of which are involved in olfactory processing, may function in the recognition of sex-specific pheromones, in the control of sex-specific behaviors, or both.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferveur, J F -- Stortkuhl, K F -- Stocker, R F -- Greenspan, R J -- New York, N.Y. -- Science. 1995 Feb 10;267(5199):902-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, New York University, NY 10003.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7846534" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bisexuality ; Brain/physiology ; Drosophila melanogaster/genetics/*physiology ; Female ; *Genes, Insect ; Male ; Sex Attractants/physiology ; Sexual Behavior, Animal ; Smell
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-01-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roop, D -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):474-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7529942" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Membrane/metabolism ; Humans ; Ichthyosis/*genetics/metabolism/pathology ; Ichthyosis, Lamellar/*genetics/metabolism/pathology ; Intermediate Filaments/metabolism/ultrastructure ; Keratinocytes/metabolism/*ultrastructure ; Keratins/genetics ; Lipid Metabolism ; Mutation ; Transglutaminases/genetics/metabolism
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-09-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1995 Sep 1;269(5228):1216-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7652566" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cooperative Behavior ; Female ; Game Theory ; Lions/*psychology ; *Territoriality
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):775-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638588" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Chlamydia Infections/complications/immunology ; Endometriosis/*complications/genetics ; Female ; Genetic Predisposition to Disease ; Humans ; Infertility, Female/*etiology/genetics ; Infertility, Male/etiology ; Leiomyoma/*complications/genetics ; Male ; Sexually Transmitted Diseases/*complications/epidemiology/immunology ; Uterine Neoplasms/*complications/genetics
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  • 21
    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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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):773-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638587" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoimmune Diseases/etiology ; Clinical Trials as Topic ; Estrogens/*physiology ; Female ; Genetic Predisposition to Disease ; Genitalia, Female/physiology ; Gonadal Steroid Hormones/*physiology ; Humans ; Immune System/*physiology ; Infection/immunology ; Male ; Menopause ; *Menstrual Cycle
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  • 23
    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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  • 24
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-11-24
    Description: Two-dimensional deconvolution techniques are used here to reconstruct age-specific human immunodeficiency virus (HIV) infection rates in the United States from surveillance data on acquired immunodeficiency syndrome (AIDS). This approach suggests that 630,000 to 897,000 adults and adolescents in the United States were living with HIV infection as of January 1993, including 107,000 to 150,000 women. The estimated incidence of HIV infection declined markedly over time among white males, especially those older than 30 years. In contrast, HIV incidence appears to have remained relatively constant among women and minorities. As of January 1993, prevalence was highest among young adults in their late twenties and thirties and among minorities. An estimated 3 percent of black men and 1 percent of black women in their thirties were living with HIV infection as of that date. If infection rates remain at these levels, HIV must be considered as endemic in the United States.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenberg, P S -- New York, N.Y. -- Science. 1995 Nov 24;270(5240):1372-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Cancer Institute, Rockville, MD 20852-4910, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481828" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*epidemiology ; Adolescent ; Adult ; African Americans/statistics & numerical data ; Age Distribution ; *Disease Outbreaks ; European Continental Ancestry Group/statistics & numerical data ; Female ; HIV Infections/*epidemiology ; Hispanic Americans/statistics & numerical data ; Humans ; Incidence ; Male ; Middle Aged ; Models, Statistical ; Prevalence ; Sex Distribution ; United States/epidemiology
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  • 25
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-04-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fischman, J -- Gibbons, A -- Culotta, E -- New York, N.Y. -- Science. 1995 Apr 21;268(5209):364-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716536" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthropology ; Behavior ; Female ; Fossils ; Genetic Variation ; Haplorhini/physiology ; Hominidae/anatomy & histology ; Humans ; Humerus/anatomy & histology ; Labor, Obstetric ; Male ; Melanesia ; Pregnancy
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  • 26
    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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  • 27
    Publication Date: 1995-11-17
    Description: In the yeast Saccharomyces cerevisiae, Ras regulates adenylate cyclase, which is essential for progression through the G1 phase of the cell cycle. However, even when the adenosine 3',5'-monophosphate (cAMP) pathway was bypassed, the double disruption of RAS1 and RAS2 resulted in defects in growth at both low and high temperatures. Furthermore, the simultaneous disruption of RAS1, RAS2, and the RAS-related gene RSR1 was lethal at any temperature. The triple-disrupted cells were arrested late in the mitotic (M) phase, which was accompanied by an accumulation of cells with divided chromosomes and sustained histone H1 kinase activity. The lethality of the triple disruption was suppressed by the multicopies of CDC5, CDC15, DBF2, SPO12, and TEM1, all of which function in the completion of the M phase. Mammalian ras also suppressed the lethality, which suggests that a similar signaling pathway exists in higher eukaryotes. These results demonstrate that S. cerevisiae Ras functions in the completion of the M phase in a manner independent of the Ras-cAMP pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morishita, T -- Mitsuzawa, H -- Nakafuku, M -- Nakamura, S -- Hattori, S -- Anraku, Y -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1213-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biochemistry and Cellular Biology, National Institute of Neuroscience, Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502049" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/genetics/metabolism ; Fungal Proteins/*genetics/physiology ; GTP Phosphohydrolases/genetics/physiology ; Genes, Fungal ; Genes, Suppressor ; *Genes, ras ; *Mitosis ; Mutation ; Phenotype ; Saccharomyces cerevisiae/*cytology/genetics/growth & development ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Temperature ; *rab GTP-Binding Proteins ; ras Proteins/*genetics/physiology
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-10-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1995 Oct 27;270(5236):578-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7570013" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacillus subtilis/cytology/genetics/*physiology ; Bacterial Proteins/*metabolism/*physiology ; Cell Division ; Chlorophyta/cytology ; *Cytoskeletal Proteins ; *Drosophila Proteins ; Drosophila melanogaster/cytology ; Genes, Bacterial ; Juvenile Hormones/physiology ; Nerve Tissue Proteins/physiology ; Neurons/cytology ; Nuclear Proteins/physiology ; Phosphorylation ; Sigma Factor/*metabolism ; Spores, Bacterial/genetics/*physiology ; *Transcription Factors
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  • 29
    Publication Date: 1995-08-11
    Description: In the molecular scheme of living organisms, adenosine 3',5'-monophosphate (cyclic AMP or cAMP) has been a universal second messenger. In eukaryotic cells, the primary receptors for cAMP are the regulatory subunits of cAMP-dependent protein kinase. The crystal structure of a 1-91 deletion mutant of the type I alpha regulatory subunit was refined to 2.8 A resolution. Each of the two tandem cAMP binding domains provides an extensive network of hydrogen bonds that buries the cyclic phosphate and the ribose between two beta strands that are linked by a short alpha helix. Each adenine base stacks against an aromatic ring that lies outside the beta barrel. This structure provides a molecular basis for understanding how cAMP binds cooperatively to its receptor protein, thus mediating activation of the kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Su, Y -- Dostmann, W R -- Herberg, F W -- Durick, K -- Xuong, N H -- Ten Eyck, L -- Taylor, S S -- Varughese, K I -- GM07313/GM/NIGMS NIH HHS/ -- GM34921/GM/NIGMS NIH HHS/ -- RR01644/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):807-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla 92093-0654, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638597" target="_blank"〉PubMed〈/a〉
    Keywords: Affinity Labels ; Amino Acid Sequence ; Binding Sites ; Carrier Proteins/*chemistry/genetics/metabolism ; Computer Graphics ; Crystallization ; Crystallography, X-Ray ; Cyclic AMP/analogs & derivatives/*metabolism ; Cyclic AMP-Dependent Protein Kinases/*chemistry ; Enzyme Activation ; Hydrogen Bonding ; *Intracellular Signaling Peptides and Proteins ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary
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  • 30
    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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  • 31
    Publication Date: 1995-09-08
    Description: Psychological traits are commonly inferred from covariation in sets of behavioral measures that otherwise appear to have little in common. Emotionality in mice is such a trait, defined here by covariation in activity and defecation in a novel environment and emergence into the open arms of an elevated plus maze. Behavioral and quantitative trait analyses were conducted on four measures obtained from 879 mice from an F2 intercross. Three loci, on murine chromosomes 1, 12, and 15, were mapped that influence emotionality. This trait, inferred from studies of strain, sex, and individual differences in rodents, may be related to human susceptibility to anxiety or neuroticism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flint, J -- Corley, R -- DeFries, J C -- Fulker, D W -- Gray, J A -- Miller, S -- Collins, A C -- DA-00197/DA/NIDA NIH HHS/ -- DA-05131/DA/NIDA NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1432-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660127" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior, Animal ; *Chromosome Mapping ; Defecation ; *Emotions ; Female ; Genes ; *Genetic Linkage ; Genetic Variation ; Lod Score ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Phenotype ; Regression Analysis
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-07-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, K -- New York, N.Y. -- Science. 1995 Jul 28;269(5223):489-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7542799" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/physiology ; Cell Polarity ; Drosophila/embryology/genetics/*physiology ; *Drosophila Proteins ; Female ; Genes, Insect ; Insect Hormones/genetics/*physiology ; Microtubules/physiology ; Oocytes/*physiology/ultrastructure ; Oogenesis ; Ovary/cytology/physiology ; RNA/metabolism ; *Signal Transduction ; *Transforming Growth Factor alpha ; Transforming Growth Factors/genetics/*physiology
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  • 33
    Publication Date: 1995-05-12
    Description: The yeast non-Mendelian factor [psi+] has been suggested to be a self-modified protein analogous to mammalian prions. Here it is reported that an intermediate amount of the chaperone protein Hsp104 was required for the propagation of the [psi+] factor. Over-production or inactivation of Hsp104 caused the loss of [psi+]. These results suggest that chaperone proteins play a role in prion-like phenomena, and that a certain level of chaperone expression can cure cells of prions without affecting viability. This may lead to antiprion treatments that involve the alteration of chaperone amounts or activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chernoff, Y O -- Lindquist, S L -- Ono, B -- Inge-Vechtomov, S G -- Liebman, S W -- New York, N.Y. -- Science. 1995 May 12;268(5212):880-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Illinois, Chicago 60607-7020, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754373" target="_blank"〉PubMed〈/a〉
    Keywords: Fungal Proteins/*biosynthesis/genetics/physiology ; Gene Expression ; Heat-Shock Proteins/genetics/*physiology ; Mutation ; Prions/*biosynthesis ; Saccharomyces cerevisiae/genetics/*physiology ; *Saccharomyces cerevisiae Proteins ; Suppression, Genetic
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-03-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1995 Mar 31;267(5206):1896-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701312" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Child ; Chromosomes, Human, Pair 6 ; Dyslexia/diagnosis/epidemiology/*etiology ; Female ; Humans ; Learning Disorders/diagnosis/epidemiology/*etiology ; Magnetic Resonance Imaging ; Male ; National Institutes of Health (U.S.) ; Thalamus/*pathology/physiopathology/*radionuclide imaging ; Tomography, Emission-Computed ; United States/epidemiology
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  • 35
    Publication Date: 1995-07-28
    Description: CD5 is a transmembrane protein that is expressed on the surface of T cells and a subset of B cells. The absence of CD5 rendered thymocytes hyperresponsive to stimulation through the T cell antigen receptor (TCR) in vitro. Selection of T cells expressing three distinct transgenic TCRs was also abnormal in CD5-deficient mice. These observations indicate that CD5 can influence the fate of developing thymocytes by acting as a negative regulator of TCR-mediated signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tarakhovsky, A -- Kanner, S B -- Hombach, J -- Ledbetter, J A -- Muller, W -- Killeen, N -- Rajewsky, K -- New York, N.Y. -- Science. 1995 Jul 28;269(5223):535-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genetics, University of Cologne, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7542801" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/*immunology ; Antigens, CD3/metabolism ; Antigens, CD5 ; Female ; *Lymphocyte Activation ; Male ; Mice ; Mice, Transgenic ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Receptors, Antigen, T-Cell/*immunology ; *Signal Transduction ; T-Lymphocyte Subsets/immunology ; T-Lymphocytes/*immunology ; Thymus Gland/immunology ; ZAP-70 Protein-Tyrosine Kinase
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-01-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Futuyma, D J -- New York, N.Y. -- Science. 1995 Jan 6;267(5194):41-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809608" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Biology ; *Biotechnology ; Female ; *Medicine ; Technology Transfer
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  • 37
    Publication Date: 1995-11-17
    Description: Haploid cells of the yeast Saccharomyces cerevisiae respond to mating pheromones with polarized growth toward the mating partner. This morphological response requires the function of the cell polarity establishment protein Bem1p. Immunochemical and two-hybrid protein interaction assays revealed that Bem1p interacts with two components of the pheromone-responsive mitogen-activated protein (MAP) kinase cascade, Ste20p and Ste5p, as well as with actin. Mutants of Bem1p that are associated with defective pheromone-induced polarized morphogenesis interacted with Ste5p and actin but not with Ste20p. Thus, the association of Bem1p with Ste20p and Ste5p may contribute to the conveyance of spatial information that regulates polarized rearrangement of the actin cytoskeleton during yeast mating.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leeuw, T -- Fourest-Lieuvin, A -- Wu, C -- Chenevert, J -- Clark, K -- Whiteway, M -- Thomas, D Y -- Leberer, E -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1210-3.〈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/7502048" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; *Adaptor Proteins, Signal Transducing ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; *Carrier Proteins ; Cell Polarity ; Fungal Proteins/chemistry/genetics/*metabolism ; GTP-Binding Proteins/metabolism ; Intracellular Signaling Peptides and Proteins ; MAP Kinase Kinase Kinases ; Morphogenesis ; Mutation ; Peptides/pharmacology ; Pheromones/*pharmacology ; Protein-Serine-Threonine Kinases/*metabolism ; Saccharomyces cerevisiae/cytology/*metabolism ; *Saccharomyces cerevisiae Proteins
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-03-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ingram, V M -- New York, N.Y. -- Science. 1995 Mar 31;267(5206):1889-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7741944" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Alzheimer Disease/*metabolism ; Humans ; Neurofibrillary Tangles/*metabolism ; Phosphorylation ; Protein Kinases/metabolism ; tau Proteins/*metabolism
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  • 39
    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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  • 40
    Publication Date: 1995-10-27
    Description: During pregnancy a semiallogeneic fetus survives despite the presence of maternal T cells specific for paternally inherited histocompatibility antigens. A mouse transgenic for a T cell receptor recognizing the major histocompatibility (MHC) antigen H-2Kb was used to follow the fate of T cells reactive to paternal alloantigens. In contrast to syngeneic and third-party allogeneic pregnancies, mice bearing a Kb-positive conceptus had reduced numbers of Kb-reactive T cells and accepted Kb-positive tumor grafts. T cell phenotype and responsiveness were restored after delivery. Thus, during pregnancy maternal T cells acquire a transient state of tolerance specific for paternal alloantigens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tafuri, A -- Alferink, J -- Moller, P -- Hammerling, G J -- Arnold, B -- New York, N.Y. -- Science. 1995 Oct 27;270(5236):630-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tumor Immunology Program, Deutsches Krebsforschungszentrum (DKFZ), Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7570020" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CD4-Positive T-Lymphocytes/immunology ; CD8-Positive T-Lymphocytes/immunology ; Fathers ; Female ; Fetus/*immunology ; Graft Rejection ; H-2 Antigens/*immunology ; *Immune Tolerance ; Male ; Mice ; Mice, Inbred C57BL ; Mice, SCID ; Mice, Transgenic ; Neoplasm Transplantation ; Phenotype ; Placenta/immunology ; Pregnancy ; Pregnancy, Animal/*immunology ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes/*immunology
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-07-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1995 Jul 21;269(5222):295-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618095" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes/standards ; Boston ; Breast Neoplasms/drug therapy ; Cancer Care Facilities/*standards ; Clinical Protocols/*standards ; Clinical Trials as Topic/standards ; Cyclophosphamide/adverse effects ; Drug Overdose ; Fatal Outcome ; Female ; Humans ; *Medication Errors ; Medication Systems, Hospital/*standards
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-07-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):30-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604275" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Animals ; Bacterial Proteins ; Bacterial Vaccines/immunology ; Cell Movement/*physiology ; DNA-Binding Proteins/*genetics/physiology ; Escherichia coli/genetics/physiology ; Genes, Bacterial ; Humans ; Macaca mulatta ; Mutation ; Shigella flexneri/genetics/immunology/*physiology ; Transcription Factors/*genetics/physiology
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-11-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 1995 Nov 10;270(5238):904-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481784" target="_blank"〉PubMed〈/a〉
    Keywords: *AIDS Vaccines/immunology ; Acquired Immunodeficiency Syndrome/*prevention & control ; Animals ; *Clinical Trials as Topic/economics ; Cohort Studies ; Costs and Cost Analysis ; Female ; HIV/classification ; HIV Antibodies/biosynthesis ; *HIV Envelope Protein gp120/immunology ; HIV Infections/*prevention & control ; Humans ; International Cooperation ; Male ; Pan troglodytes ; Patient Selection ; Thailand ; United States
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-02-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, J L -- Hanson, D L -- Chu, S Y -- Ward, J W -- Jaffe, H W -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1078-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855583" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS-Related Opportunistic Infections/drug therapy/virology ; Acquired Immunodeficiency Syndrome/*complications/drug therapy ; Acyclovir/therapeutic use ; Female ; Foscarnet/*therapeutic use ; Ganciclovir/therapeutic use ; Herpesviridae Infections/drug therapy/virology ; Humans ; Male ; Retrospective Studies ; Risk Factors ; Sarcoma, Kaposi/*complications/drug therapy/virology
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  • 45
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-07-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thompson, C -- New York, N.Y. -- Science. 1995 Jul 21;269(5222):301-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618098" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/chemistry/genetics/*immunology ; Child ; Cloning, Molecular ; Complement Activation/*immunology ; Disease Susceptibility ; Humans ; *Immunity, Innate ; Immunologic Deficiency Syndromes/*etiology ; Mannose-Binding Lectins ; Mutation ; Phagocytosis/*immunology ; Protein Conformation ; Protein Structure, Secondary
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  • 46
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-10-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 1995 Oct 6;270(5233):30-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569947" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Developed Countries ; Developing Countries ; Female ; HIV Infections/epidemiology/transmission/*virology ; HIV-1/classification/growth & development/*pathogenicity ; Humans ; Langerhans Cells/*virology ; Male ; Thailand/epidemiology ; Vagina/virology
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  • 47
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-02-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1091-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855588" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*physiology ; *Arabidopsis Proteins ; *Biological Clocks/genetics ; Carrier Proteins/genetics ; *Circadian Rhythm/genetics ; *Genes, Plant ; Light-Harvesting Protein Complexes ; Luciferases/genetics ; Mutation ; *Photosynthetic Reaction Center Complex Proteins ; *Photosystem II Protein Complex ; *Plant Proteins ; Recombinant Fusion Proteins
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  • 48
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-01-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maestro, R -- Boiocchi, M -- New York, N.Y. -- Science. 1995 Jan 6;267(5194):15-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809600" target="_blank"〉PubMed〈/a〉
    Keywords: Carrier Proteins/*genetics ; Cyclin-Dependent Kinase Inhibitor p16 ; *Genes, Tumor Suppressor ; Humans ; Melanoma/*etiology/genetics ; Mutation ; Neoplasms, Radiation-Induced/*genetics ; Protein Kinase Inhibitors ; Ultraviolet Rays/*adverse effects
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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-01-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1995 Jan 13;267(5195):177-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809622" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/*chemistry ; Cloning, Molecular ; Glycosylation ; Models, Molecular ; Phosphorylation ; Receptors, Glutamate/*chemistry/genetics
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-02-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nowak, R -- New York, N.Y. -- Science. 1995 Feb 3;267(5198):616.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7839136" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; *Functional Laterality ; Humans ; Magnetic Resonance Imaging ; Male ; *Music ; *Pitch Discrimination ; Temporal Lobe/*anatomy & histology
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  • 51
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-11-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1995 Nov 10;270(5238):910.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481787" target="_blank"〉PubMed〈/a〉
    Keywords: Anticarcinogenic Agents/adverse effects/*therapeutic use ; Breast Neoplasms/*prevention & control ; *Carcinogens ; *Clinical Trials as Topic ; Endometrial Neoplasms/chemically induced ; Female ; Heart Diseases/prevention & control ; Humans ; Osteoporosis/prevention & control ; Patient Selection ; Tamoxifen/*adverse effects/*therapeutic use
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  • 52
    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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  • 53
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sherman, L A -- Temple, R -- Merkatz, R B -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):793-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Drug Evaluation and Research, FDA, Rockville, MD 20857, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638593" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; *Clinical Trials as Topic ; Drug Approval ; Federal Government ; Female ; *Guidelines as Topic ; Humans ; Male ; Paternalism ; *Patient Selection ; Pregnant Women ; Research Design ; *Research Subjects ; Sex Characteristics ; United States ; *United States Food and Drug Administration
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  • 54
    Publication Date: 1995-06-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mani, S K -- Allen, J M -- Clark, J H -- Blaustein, J D -- O'Malley, B W -- New York, N.Y. -- Science. 1995 Jun 30;268(5219):1833.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604251" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Estradiol/*pharmacology ; Female ; Male ; Neurotransmitter Agents/*physiology ; Rats ; Sexual Behavior, Animal/drug effects/*physiology
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  • 55
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mann, C -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):766-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638586" target="_blank"〉PubMed〈/a〉
    Keywords: *Biomedical Research ; Clinical Trials as Topic ; Cultural Characteristics ; Developing Countries ; Female ; Humans ; *Internationality ; Male ; Maternal Health Services ; *Patient Selection ; Poverty ; *Research ; Research Design ; *Research Subjects ; Resource Allocation ; Sex Characteristics ; *Women's Health
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  • 56
    Publication Date: 1995-07-28
    Description: The gene product of the ob locus is important in the regulation of body weight. The ob product was shown to be present as a 16-kilodalton protein in mouse and human plasma but was undetectable in plasma from C57BL/6J ob/ob mice. Plasma levels of this protein were increased in diabetic (db) mice, a mutant thought to be resistant to the effects of ob. Daily intraperitoneal injections of either mouse or human recombinant OB protein reduced the body weight of ob/ob mice by 30 percent after 2 weeks of treatment with no apparent toxicity but had no effect on db/db mice. The protein reduced food intake and increased energy expenditure in ob/ob mice. Injections of wild-type mice twice daily with the mouse protein resulted in a sustained 12 percent weight loss, decreased food intake, and a reduction of body fat from 12.2 to 0.7 percent. These data suggest that the OB protein serves an endocrine function to regulate body fat stores.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Halaas, J L -- Gajiwala, K S -- Maffei, M -- Cohen, S L -- Chait, B T -- Rabinowitz, D -- Lallone, R L -- Burley, S K -- Friedman, J M -- DK41096/DK/NIDDK NIH HHS/ -- RR00862/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 28;269(5223):543-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics, Howard Hughes Medical Institute, Rockfeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624777" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/drug effects ; Animals ; Blood Glucose/analysis ; Body Composition/drug effects ; Diabetes Mellitus/blood/physiopathology ; Eating/drug effects ; Energy Metabolism/drug effects ; Female ; Humans ; Leptin ; Mice ; Mice, Inbred C57BL ; Mice, Obese ; Obesity/blood/genetics/*physiopathology ; Proteins/analysis/genetics/*pharmacology/physiology ; Recombinant Proteins/administration & dosage/pharmacology ; Weight Loss/*drug effects
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  • 57
    Publication Date: 1995-01-20
    Description: Antifungal saponins occur in many plant species and may provide a preformed chemical barrier to attack by phytopathogenic fungi. Some fungal pathogens can enzymatically detoxify host plant saponins, which suggests that saponin detoxification may determine the host range of these fungi. A gene encoding a saponin detoxifying enzyme was cloned from the cereal-infecting fungus Gaeumannomyces graminis. Fungal mutants generated by targeted gene disruption were no longer able to infect the saponin-containing host oats but retained full pathogenicity to wheat (which does not contain saponins). Thus, the ability of a phytopathogenic fungus to detoxify a plant saponin can determine its host range.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bowyer, P -- Clarke, B R -- Lunness, P -- Daniels, M J -- Osbourn, A E -- New York, N.Y. -- Science. 1995 Jan 20;267(5196):371-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sainsburg Laboratory, John Innes Centre, Norwich, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824933" target="_blank"〉PubMed〈/a〉
    Keywords: Ascomycota/enzymology/*genetics/physiology ; Avena/*microbiology ; Cloning, Molecular ; *Fungal Proteins ; Genes, Fungal ; Molecular Sequence Data ; Mutation ; Neurospora crassa/genetics ; Saponins/*analysis/*antagonists & inhibitors/metabolism ; Transformation, Genetic ; Triticum/*microbiology ; beta-Glucosidase/*genetics/isolation & purification/metabolism
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  • 58
    Publication Date: 1995-02-17
    Description: Although the myogenic regulator MyoD is expressed in proliferating myoblasts, differentiation of these cells is limited to the G0 phase of the cell cycle. Forced expression of cyclin D1, but not cyclins A, B, or E, inhibited the ability of MyoD to transactivate muscle-specific genes and correlated with phosphorylation of MyoD. Transfection of myoblasts with cyclin-dependent kinase (Cdk) inhibitors p21 and p16 augmented muscle-specific gene expression in cells maintained in high concentrations of serum, suggesting that an active cyclin-Cdk complex suppresses MyoD function in proliferating cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Skapek, S X -- Rhee, J -- Spicer, D B -- Lassar, A B -- 1F32AR08214-01A1/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 17;267(5200):1022-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7863328" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/biosynthesis/physiology ; Cell Cycle ; Cell Differentiation ; Cell Line ; Cyclin D1 ; Cyclin-Dependent Kinase Inhibitor p16 ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclin-Dependent Kinases/*metabolism ; Cyclins/biosynthesis/*physiology ; Enzyme Activation ; Mice ; Muscle, Skeletal/*cytology/metabolism ; MyoD Protein/*antagonists & inhibitors/metabolism ; Oncogene Proteins/*physiology ; Phosphorylation ; Transcriptional Activation ; Transfection
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  • 59
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    American Association for the Advancement of Science (AAAS)
    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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  • 60
    Publication Date: 1995-06-09
    Description: Minor histocompatibility antigen disparities between human leukocyte antigen (HLA)-matched bone marrow donors and recipients are a major risk factor for graft versus host disease (GVHD). An HLA-A2.1-restricted cytotoxic T cell clone that recognized the minor histocompatibility antigen HA-2 was previously isolated from a patient with severe GVHD after HLA-identical bone marrow transplantation. The HLA-A2.1-bound peptide representing HA-2 has now been identified. This peptide appears to originate from a member of the non-filament-forming class I myosin family. Because HA-2 has a phenotype frequency of 95 percent in the HLA-A2.1-positive population, it is a candidate for immunotherapeutic intervention in bone marrow transplantation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉den Haan, J M -- Sherman, N E -- Blokland, E -- Huczko, E -- Koning, F -- Drijfhout, J W -- Skipper, J -- Shabanowitz, J -- Hunt, D F -- Engelhard, V H -- AI20963/AI/NIAID NIH HHS/ -- AI33993/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1995 Jun 9;268(5216):1476-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunohaematology, University Hospital, Leiden, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7539551" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bone Marrow Transplantation ; Epitopes ; Female ; Graft vs Host Disease/*immunology ; HLA-A2 Antigen/immunology ; Humans ; Mass Spectrometry ; Minor Histocompatibility Antigens/chemistry/*immunology ; Molecular Sequence Data ; Neoplasm Proteins/chemistry/*immunology ; Oligopeptides/chemistry/immunology ; T-Lymphocytes, Cytotoxic/immunology
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  • 61
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-09-08
    Description: A method of gene targeting that allows the inducible inactivation of a target gene in mice is presented. The method uses an interferon-responsive promoter to control the expression of Cre recombinase. Here, Cre was used to delete a segment of the DNA polymerase beta gene flanked by IoxP recombinase recognition sites. Deletion was complete in liver and nearly complete in lymphocytes within a few days, whereas partial deletion was obtained in other tissues. This method can be used for the inducible inactivation of any other gene in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuhn, R -- Schwenk, F -- Aguet, M -- Rajewsky, K -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1427-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genetics, University of Cologne, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660125" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crosses, Genetic ; DNA Nucleotidyltransferases/genetics ; DNA Polymerase I/genetics ; Female ; *GTP-Binding Proteins ; Gene Targeting/*methods ; Genetic Vectors ; *Integrases ; Interferon-alpha/pharmacology ; Interferon-beta/pharmacology ; Liver/drug effects/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Inbred CBA ; Mice, Transgenic ; Myxovirus Resistance Proteins ; Poly I-C/pharmacology ; Promoter Regions, Genetic ; Proteins/genetics ; Recombination, Genetic ; Sequence Deletion ; *Viral Proteins
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  • 62
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-01-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weiner, J -- New York, N.Y. -- Science. 1995 Jan 6;267(5194):30-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809606" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Birds ; Female ; Fishes ; Genetic Variation ; Male ; Reproduction ; Reproduction, Asexual ; *Selection, Genetic
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  • 63
    Publication Date: 1995-03-03
    Description: Many members of the cytokine receptor superfamily initiate intracellular signaling by activating members of the Jak family of tyrosine kinases. Activation of the same Jaks by multiple cytokines raises the question of how these cytokines activate distinct intracellular signaling pathways. Selection of particular substrates--the transcriptional activator Stat3 and protein tyrosine phosphatase PTP1D--that characterize responses to the ciliary neurotrophic factor-interleukin-6 cytokine family depended not on which Jak was activated, but was instead determined by specific tyrosine-based motifs in the receptor components--gp130 and LIFR--shared by these cytokines. Further, these tyrosine-based motifs were modular, because addition of a Stat3-specifying motif to another cytokine receptor, that for erythropoietin, caused it to activate Stat3 in a ligand-dependent fashion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stahl, N -- Farruggella, T J -- Boulton, T G -- Zhong, Z -- Darnell, J E Jr -- Yancopoulos, G D -- New York, N.Y. -- Science. 1995 Mar 3;267(5202):1349-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Inc., Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7871433" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antigens, CD ; Cell Line ; Cytokine Receptor gp130 ; DNA-Binding Proteins/*metabolism ; *Growth Inhibitors ; Interleukin-6/pharmacology ; Intracellular Signaling Peptides and Proteins ; Leukemia Inhibitory Factor ; *Lymphokines ; Membrane Glycoproteins/chemistry/*metabolism ; Molecular Sequence Data ; Phosphorylation ; Point Mutation ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/metabolism ; Protein-Tyrosine Kinases/*metabolism ; Receptors, Cytokine/chemistry/*metabolism ; Receptors, OSM-LIF ; Recombinant Fusion Proteins/metabolism ; STAT3 Transcription Factor ; *Signal Transduction ; Trans-Activators/*metabolism ; Tyrosine/metabolism
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  • 64
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-04-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heinrichs, C -- Munson, P J -- Counts, D R -- Cutler, G B Jr -- Baron, J -- New York, N.Y. -- Science. 1995 Apr 21;268(5209):442-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716552" target="_blank"〉PubMed〈/a〉
    Keywords: Body Height ; Body Weight ; Cephalometry ; Female ; *Growth ; Humans ; Infant ; Kinetics ; Male ; Regression Analysis
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  • 65
    Publication Date: 1995-10-27
    Description: Cell fate is determined by cell-specific activation of transcription factor sigma F after asymmetric division during sporulation by Bacillus subtilis. The activity of sigma F is governed by SpoIIAA, SpoIIAB, and SpoIIE, a membrane protein localized at the polar septum. SpoIIAB binds to and inhibits sigma F, and SpoIIAA inhibits SpoIIAB, which prevents SpoIIAB from binding to sigma F. SpoIIAB is also a serine kinase that inactivates SpoIIAA. Here, it is demonstrated that SpoIIE dephosphorylates SpoIIAA-P and overcomes SpoIIAB-mediated inhibition of sigma F. The finding that SpoIIE is a serine phosphatase links asymmetric division to the pathway governing cell-specific gene transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duncan, L -- Alper, S -- Arigoni, F -- Losick, R -- Stragier, P -- GM18568/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 27;270(5236):641-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7570023" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Bacillus subtilis/cytology/genetics/*physiology ; Bacterial Proteins/antagonists & inhibitors/*metabolism ; Cell Division ; Molecular Sequence Data ; Phosphoprotein Phosphatases/*metabolism ; Phosphorylation ; Recombinant Fusion Proteins/metabolism ; Sigma Factor/antagonists & inhibitors/*metabolism ; Spores, Bacterial/*physiology ; *Transcription Factors ; *Transcription, Genetic
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  • 66
    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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  • 67
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1596-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7886445" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior, Animal ; Caenorhabditis elegans/genetics/*physiology ; GTP-Binding Proteins/genetics/*physiology ; Genes, Helminth ; Male ; Mutation ; *Signal Transduction
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  • 68
    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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  • 69
    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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  • 70
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-06-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bohen, S P -- Kralli, A -- Yamamoto, K R -- New York, N.Y. -- Science. 1995 Jun 2;268(5215):1303-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892-4255, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7761850" target="_blank"〉PubMed〈/a〉
    Keywords: Fungal Proteins/genetics/*physiology ; HSP40 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins/physiology ; HSP90 Heat-Shock Proteins/physiology ; *Heat-Shock Proteins ; Molecular Chaperones/*physiology ; Mutation ; Oncogene Protein pp60(v-src)/metabolism ; Protein Folding ; Receptors, Estrogen/metabolism ; Receptors, Glucocorticoid/metabolism ; Receptors, Steroid/*metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins ; *Signal Transduction
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  • 71
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-01-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):459-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824945" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens/immunology ; Autoimmune Diseases/immunology ; Graft Rejection ; Humans ; Ligands ; Lymphocyte Activation ; Membrane Proteins/metabolism ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Receptors, Antigen, T-Cell/chemistry/*immunology/metabolism ; Signal Transduction ; T-Lymphocytes/*immunology ; ZAP-70 Protein-Tyrosine Kinase
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  • 72
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-11-10
    Description: To determine the interaction energy between cross-strand pairs of side chains on an antiparallel beta sheet, pairwise amino acid substitutions were made on the solvent-exposed face of the B1 domain of streptococcal protein G. The measured interaction energies were substantial (1.8 kilocalories per mole) and comparable to the magnitude of the beta sheet propensities. The experimental results paralleled the statistical frequency with which the residue pairs are found in beta sheets of known structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, C K -- Regan, L -- New York, N.Y. -- Science. 1995 Nov 10;270(5238):980-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481801" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/genetics ; Hot Temperature ; Hydrogen Bonding ; Mutation ; Protein Conformation ; Protein Denaturation ; *Protein Engineering ; Protein Folding ; *Protein Structure, Secondary ; Streptococcus/chemistry ; Thermodynamics
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  • 73
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1995 Aug 11;269(5225):765-801.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638585" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; Humans ; Research ; *Women's Health
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  • 74
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- Kumar, S R -- Thach, A B -- Kiat-Winarko, T -- Frambach, D A -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1577; author reply 1580-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7741897" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Alzheimer Disease/*diagnosis ; Female ; Humans ; Male ; Pupil/*drug effects ; *Tropicamide
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 75
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-11-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, P A -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1219-20; author reply 1220-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502054" target="_blank"〉PubMed〈/a〉
    Keywords: *AIDS Vaccines ; Animals ; Animals, Newborn ; Female ; HIV Infections/*prevention & control/transmission ; Humans ; Macaca mulatta ; Male ; Simian Immunodeficiency Virus/pathogenicity ; Vaccination ; Vaccines, Attenuated
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  • 76
    Publication Date: 1995-08-04
    Description: The related mouse Engrailed genes En-1 and En-2 are expressed from the one- and approximately five-somite stages, respectively, in a similar presumptive mid-hindbrain domain. However, mutations in En-1 and En-2 produce different phenotypes. En-1 mutant mice die at birth with a large mid-hindbrain deletion, whereas En-2 mutants are viable, with cerebellar defects. To determine whether these contrasting phenotypes reflect differences in temporal expression or biochemical activity of the En proteins, En-1 coding sequences were replaced with En-2 sequences by gene targeting. This rescued all En-1 mutant defects, demonstrating that the difference between En-1 and En-2 stems from their divergent expression patterns.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hanks, M -- Wurst, W -- Anson-Cartwright, L -- Auerbach, A B -- Joyner, A L -- New York, N.Y. -- Science. 1995 Aug 4;269(5224):679-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular and Developmental Biology, Samuel Lunenfeld Research Institute, Mt. Sinai Hospital, Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624797" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/abnormalities/embryology ; Chimera ; Crosses, Genetic ; Female ; *Gene Expression Regulation, Developmental ; *Gene Targeting ; *Genes, Homeobox ; Homeodomain Proteins/*genetics/physiology ; Limb Deformities, Congenital ; Male ; Mice ; Mutation ; Nerve Tissue Proteins/*genetics/physiology ; Phenotype ; Promoter Regions, Genetic ; Recombination, Genetic ; Stem Cells ; Sternum/abnormalities
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 77
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-07-07
    Description: Mouse sperm recognize and bind to ZP3, one of three glycoproteins in the egg's zona pellucida. A mouse sperm protein, sp56, was identified that has the characteristics expected of the sperm protein responsible for recognition of ZP3. The complementary DNA encoding sp56 was isolated, and its primary sequence indicates that sp56 is a member of a superfamily of protein receptors. It was shown that sp56 expression is restricted to mouse spermatids and that the presence or absence of sp56 on sperm from different species accounts for species specificity of sperm-egg recognition in mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bookbinder, L H -- Cheng, A -- Bleil, J D -- R01 HD 27847/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):86-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Scripps Research Institute, Department of Molecular Biology, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604284" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cricetinae ; Egg Proteins/*metabolism ; Female ; Guinea Pigs ; Humans ; Male ; Membrane Glycoproteins/*metabolism ; Mice ; Molecular Sequence Data ; Molecular Weight ; Organ Specificity ; RNA, Messenger/analysis/genetics ; Receptors, Cell Surface/*biosynthesis/chemistry/genetics/metabolism ; Species Specificity ; Sperm-Ovum Interactions/*physiology ; Spermatids/metabolism ; Spermatozoa/*metabolism ; Zona Pellucida/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 78
    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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  • 79
    Publication Date: 1995-12-08
    Description: Transcriptional silencing at the HMRa locus of Saccharomyces cerevisiae requires the function of the origin recognition complex (ORC), the replication initiator of yeast. Expression of a Drosophila melanogaster Orc2 complementary DNA in the yeast orc2-1 strain, which is defective for replication and silencing, complemented the silencing defect but not the replication defect; this result indicated that the replication and silencing functions of ORC were separable. The orc2-1 mutation mapped to the region of greatest homology between the Drosophila and yeast proteins. The silent state mediated by DmOrc2 was epigenetic; it was propagated during mitotic divisions in a relatively stable way, whereas the nonsilent state was metastable. In contrast, the silent state was erased during meiosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ehrenhofer-Murray, A E -- Gossen, M -- Pak, D T -- Botchan, M R -- Rine, J -- GM31105/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1671-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502078" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; *DNA Replication ; DNA-Binding Proteins/genetics/*physiology ; Drosophila Proteins ; Drosophila melanogaster/*genetics ; Fungal Proteins/genetics/physiology ; *Gene Expression Regulation ; Genes, Fungal ; Genes, Insect ; Genetic Complementation Test ; Mutation ; Origin Recognition Complex ; Regulatory Sequences, Nucleic Acid ; *Replication Origin ; Repressor Proteins/genetics/*physiology ; Saccharomyces cerevisiae/*genetics/physiology ; Saccharomyces cerevisiae Proteins ; Temperature ; Transformation, Genetic
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  • 80
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-11-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Worton, R -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):755-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Hospital for Sick Children, Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481760" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Chromosome Mapping ; Chromosomes, Human, Pair 13 ; Chromosomes, Human, Pair 4 ; Cytoskeletal Proteins/*genetics/physiology ; Dystroglycans ; Dystrophin/*genetics/physiology ; Humans ; Membrane Glycoproteins/*genetics/physiology ; Muscles/chemistry ; Muscular Dystrophies/*genetics/metabolism ; Mutation ; Phenotype ; Sarcoglycans ; Sequence Deletion
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  • 81
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-11-17
    Description: Cadherins mediate cell adhesion and are essential for normal development. Embryonic stem cells were transfected with a dominant negative N-cadherin mutant (NCAD delta) under the control of promoters active in small intestinal epithelial cells and then introduced into C57BL/6 mouse blastocysts. Analysis of adult chimeric mice revealed that expression of NCAD delta along the entire crypt-villus axis, but not in the villus epithelium alone, produced an inflammatory bowel disease resembling Crohn's disease. NCAD delta perturbed proliferation, migration, and death programs in crypts, which lead to adenomas. This model provides insights about cadherin function in an adult organ and the factors underlying inflammatory bowel disease and intestinal neoplasia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hermiston, M L -- Gordon, J I -- DK30292/DK/NIDDK NIH HHS/ -- DK39760/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1203-7.〈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/7502046" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoma/*etiology/metabolism/pathology ; Animals ; Apoptosis ; Cadherins/biosynthesis/genetics/*physiology ; Cell Division ; Cell Line ; Cell Movement ; Chimera ; Crohn Disease/etiology/immunology/metabolism/pathology ; Immunity, Mucosal ; Inflammatory Bowel Diseases/*etiology/immunology/metabolism/pathology ; Intestinal Mucosa/immunology/metabolism/*pathology ; Intestinal Neoplasms/*etiology/metabolism/pathology ; Intestine, Small/pathology ; Jejunum/pathology ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Mutation ; Stem Cells ; Transfection
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  • 82
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wuethrich, B -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1594.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7886444" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chickens/*virology ; Disease Outbreaks/prevention & control/*veterinary ; Influenza A virus/genetics/immunology/*pathogenicity ; Influenza in Birds/*epidemiology/prevention & control/virology ; Mexico/epidemiology ; Mutation ; Viral Vaccines ; Virulence
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 83
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-11-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abelson, P H -- New York, N.Y. -- Science. 1995 Nov 10;270(5238):895.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481778" target="_blank"〉PubMed〈/a〉
    Keywords: *Adolescent ; Adolescent Behavior ; Female ; Health Education ; Humans ; Life Style ; Male ; Peer Group ; Television
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  • 84
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-04-14
    Description: Thermodynamic mutant cycles provide a formalism for studying energetic coupling between amino acids on the interaction surface in a protein-protein complex. This approach was applied to the Shaker potassium channel and to a high-affinity peptide inhibitor (scorpion toxin) that binds to its pore entryway. The assignment of pairwise interactions defined the spatial arrangement of channel amino acids with respect to the known inhibitor structure. A strong constraint was placed on the Shaker channel pore-forming region by requiring its amino-terminal border to be 12 to 15 angstroms from the central axis. This method is directly applicable to sodium, calcium, and other ion channels where inhibitor or modulatory proteins bind with high affinity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hidalgo, P -- MacKinnon, R -- GM43949/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 14;268(5208):307-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716527" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Oocytes ; Potassium Channels/*chemistry/genetics/metabolism ; Scorpion Venoms/*metabolism ; Shaker Superfamily of Potassium Channels ; Thermodynamics ; Toxins, Biological/*metabolism ; Xenopus laevis
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  • 85
    Publication Date: 1995-02-24
    Description: The cycling bioluminescence of Arabidopsis plants carrying a firefly luciferase fusion construct was used to identify mutant individuals with aberrant cycling patterns. Both long- and short-period mutants were recovered. A semidominant short-period mutation, timing of CAB expression (toc1), was mapped to chromosome 5. The toc1 mutation shortens the period of two distinct circadian rhythms, the expression of chlorophyll a/b-binding protein (CAB) genes and the movements of primary leaves, although toc1 mutants do not show extensive pleiotropy for other phenotypes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Millar, A J -- Carre, I A -- Strayer, C A -- Chua, N H -- Kay, S A -- GM44640/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1161-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Science Foundation (NSF) Center for Biological Timing, 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/7855595" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*physiology ; *Arabidopsis Proteins ; Biological Clocks/*genetics ; Carrier Proteins/*genetics ; Circadian Rhythm/*genetics ; Crosses, Genetic ; Darkness ; Gene Expression Regulation, Plant ; *Genes, Plant ; Light ; Light-Harvesting Protein Complexes ; Luciferases/genetics ; Luminescence ; Movement ; Mutation ; Phenotype ; *Photosynthetic Reaction Center Complex Proteins ; *Photosystem II Protein Complex ; Plant Leaves/physiology ; *Plant Proteins ; Plants, Genetically Modified ; Recombinant Fusion Proteins
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  • 86
    Publication Date: 1995-07-28
    Description: The recent positional cloning of the mouse ob gene and its human homology has provided the basis to investigate the potential role of the ob gene product in body weight regulation. A biologically active form of recombinant mouse OB protein was overexpressed and purified to near homogeneity from a bacterial expression system. Peripheral and central administration of microgram doses of OB protein reduced food intake and body weight of ob/ob and diet-induced obese mice but not in db/db obese mice. The behavioral effects after brain administration suggest that OB protein can act directly on neuronal networks that control feeding and energy balance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Campfield, L A -- Smith, F J -- Guisez, Y -- Devos, R -- Burn, P -- New York, N.Y. -- Science. 1995 Jul 28;269(5223):546-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Metabolic Diseases, Hoffmann-La Roche Incorporated, Nutley, NJ 07110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624778" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/drug effects/*physiology ; Diabetes Mellitus/genetics/physiopathology ; Diet ; Dose-Response Relationship, Drug ; Eating/*drug effects ; Female ; Injections, Intraperitoneal ; Injections, Intravenous ; Injections, Intraventricular ; Leptin ; Male ; Mice ; Mice, Inbred AKR ; Mice, Inbred C57BL ; Mice, Obese ; Nerve Net/drug effects/*physiology ; Obesity/genetics/*physiopathology ; Proteins/administration & dosage/*pharmacology/physiology ; Recombinant Proteins/administration & dosage/pharmacology ; Weight Loss/*drug effects
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  • 87
    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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  • 88
    Publication Date: 1995-02-10
    Description: Integrin receptors mediate cell adhesion, signal transduction, and cytoskeletal organization. How a single transmembrane receptor can fulfill multiple functions was clarified by comparing roles of receptor occupancy and aggregation. Integrin occupancy by monovalent ligand induced receptor redistribution, but minimal tyrosine phosphorylation signaling or cytoskeletal protein redistribution. Aggregation of integrins by noninhibitory monoclonal antibodies on beads induced intracellular accumulations of pp125FAK and tensin, as well as phosphorylation, but no accumulation of other cytoskeletal proteins such as talin. Combining antibody-mediated clustering with monovalent ligand occupancy induced accumulation of seven cytoskeletal proteins, including alpha-actinin, talin, and F-actin, thereby mimicking multivalent interactions with fibronectin or polyvalent peptides. Integrins therefore mediate a complex repertoire of functions through the distinct effects of receptor aggregation, receptor occupancy, or both together.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miyamoto, S -- Akiyama, S K -- Yamada, K M -- New York, N.Y. -- Science. 1995 Feb 10;267(5199):883-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Developmental Biology, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892-4370.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7846531" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal ; Cell Adhesion Molecules/metabolism ; Cell Membrane/*metabolism ; Cells, Cultured ; Cytoskeletal Proteins/*metabolism ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Humans ; Integrins/*physiology ; Ligands ; Microfilament Proteins/metabolism ; Molecular Sequence Data ; Oligopeptides/metabolism ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Signal Transduction ; Tyrosine/metabolism
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  • 89
    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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  • 90
    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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  • 91
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
    Publication Date: 1995-07-28
    Description: T cell hybridomas require the immediate-early gene NGFI-B (nur77) for T cell receptor (TCR)-mediated apoptosis, a model for negative selection of self-reactive T cells. TCR-mediated death was examined in mice bearing an NGFI-B loss-of-function mutation, either by administration of antibodies to CD3 (anti-CD3) or in two well-characterized transgenic models expressing self-reactive TCRs. Both the extent and the rate of thymocyte death were unimpaired. Anti-CD3-induced death was normal in CD4+ peripheral T cells, in which death is mediated predominantly by the Fas signaling pathway. Thus, no unique requirement for NGFI-B is observed for thymic or peripheral T cell death.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, S L -- Wesselschmidt, R L -- Linette, G P -- Kanagawa, O -- Russell, J H -- Milbrandt, J -- P01 CA49712/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 28;269(5223):532-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, 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/7624775" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies ; Antigens, CD3/immunology/physiology ; *Apoptosis ; Cells, Cultured ; Clonal Deletion ; Crosses, Genetic ; DNA-Binding Proteins/genetics/*physiology ; Female ; Gene Targeting ; Hybridomas ; Male ; Mice ; Mice, Transgenic ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Receptors, Antigen, T-Cell, alpha-beta/*physiology ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid/genetics/*physiology ; Stem Cells ; T-Lymphocyte Subsets/cytology ; T-Lymphocytes/*cytology/immunology ; Thymus Gland/cytology ; Transcription Factors/genetics/*physiology
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  • 93
    Publication Date: 1995-07-07
    Description: In the light-driven proton pump bacteriorhodopsin, proton transfer from the retinal Schiff base to aspartate-85 is the crucial reaction of the transport cycle. In halorhodopsin, a light-driven chloride ion pump, the equivalent of residue 85 is threonine. When aspartate-85 was replaced with threonine, the mutated bacteriorhodopsin became a chloride ion pump when expressed in Halobacterium salinarium and, like halorhodopsin, actively transported chloride ions in the direction opposite from the proton pump. Chloride was bound to it, as revealed by large shifts of the absorption maximum of the chromophore, and its photointermediates included a red-shifted state in the millisecond time domain, with its amplitude and decay rate dependent on chloride concentration. Bacteriorhodopsin and halorhodopsin thus share a common transport mechanism, and the interaction of residue 85 with the retinal Schiff base determines the ionic specificity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sasaki, J -- Brown, L S -- Chon, Y S -- Kandori, H -- Maeda, A -- Needleman, R -- Lanyi, J K -- GM29498/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):73-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics, Faculty of Science, Kyoto University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604281" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/chemistry ; Bacteriorhodopsins/chemistry/genetics/*metabolism ; Biological Transport ; Chlorides/*metabolism ; Halorhodopsins ; Hot Temperature ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Ion Pumps/chemistry/*metabolism ; Light ; Mutation ; Proton Pumps ; Schiff Bases ; Threonine/chemistry
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  • 94
    Publication Date: 1995-07-14
    Description: Simple repetitive DNA sequences are unstable in human colorectal cancers and a variety of other cancers. Mutations in the DNA mismatch repair genes MSH2, MLH1, and PMS1 result in elevated rates of spontaneous mutation and cause a marked increase in the instability of simple repeats. Compared with the wild type, a null mutation in the yeast RTH1 gene, which encodes a 5' to 3' exonuclease, was shown to increase the rate of instability of simple repetitive DNA by as much as 280 times and to increase the spontaneous mutation rate by 30 times. Epistasis analyses were consistent with the hypothesis that this RTH1-encoded nuclease has a role in the MSH2-MLH-1-PMS1 mismatch repair pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, R E -- Kovvali, G K -- Prakash, L -- Prakash, S -- CA 41261/CA/NCI NIH HHS/ -- GM 19261/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):238-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Science, University of Texas Medical Branch, Galveston 77555-1061, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618086" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; *Carrier Proteins ; *DNA Repair ; DNA, Fungal/genetics ; DNA-Binding Proteins/genetics ; Exodeoxyribonuclease V ; Exodeoxyribonucleases/*genetics/metabolism ; Fungal Proteins/genetics ; *Genes, Fungal ; MutS Homolog 2 Protein ; Mutation ; *Neoplasm Proteins ; *Repetitive Sequences, Nucleic Acid ; Saccharomyces cerevisiae/enzymology/*genetics ; *Saccharomyces cerevisiae Proteins
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  • 95
    Publication Date: 1995-01-06
    Description: Specificity of protein kinases and phosphatases may be achieved through compartmentalization with preferred substrates. In neurons, adenosine 3', 5'-monophosphate (cAMP)-dependent protein kinase (PKA) is localized at postsynaptic densities by association of its regulatory subunit with an A kinase anchor protein, AKAP79. Interaction cloning experiments demonstrated that AKAP79 also binds protein phosphatase 2B, or calcineurin (CaN). A ternary complex of PKA, AKAP, and CaN was isolated from bovine brain, and colocalization of the kinase and the phosphatase was established in neurites of cultured hippocampal neurons. The putative CaN-binding domain of AKAP79 is similar to that of the immunophilin FKBP-12, and AKAP79 inhibited CaN phosphatase activity. These results suggest that both PKA and CaN are targeted to subcellular sites by association with a common anchor protein and thereby regulate the phosphorylation state of key neuronal substrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coghlan, V M -- Perrino, B A -- Howard, M -- Langeberg, L K -- Hicks, J B -- Gallatin, W M -- Scott, J D -- DK09059/DK/NIDDK NIH HHS/ -- GM48231/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 6;267(5194):108-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, Portland 97201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7528941" target="_blank"〉PubMed〈/a〉
    Keywords: A Kinase Anchor Proteins ; *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Binding Sites ; *Brain Chemistry ; Calcineurin ; Calmodulin-Binding Proteins/analysis/antagonists & inhibitors/*metabolism ; Carrier Proteins/analysis ; Cattle ; Cells, Cultured ; Cyclic AMP-Dependent Protein Kinases/analysis/*metabolism ; Hippocampus/chemistry ; Molecular Sequence Data ; Neurites/chemistry ; Phosphoprotein Phosphatases/analysis/antagonists & inhibitors/*metabolism ; Phosphorylation ; Proteins/*metabolism/pharmacology ; Rats ; Recombinant Proteins/pharmacology ; Tacrolimus/pharmacology
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  • 96
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):777-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638589" target="_blank"〉PubMed〈/a〉
    Keywords: *Acquired Immunodeficiency Syndrome/epidemiology/prevention & ; control/transmission ; Animals ; Anti-Infective Agents/administration & dosage/therapeutic use ; Cervix Uteri/virology ; Developing Countries ; Female ; HIV/physiology ; HIV Infections/epidemiology/prevention & control/transmission ; Humans ; Male ; Nonoxynol/therapeutic use ; *Research ; Risk Factors ; Sex Distribution ; Sexual Behavior ; Sexually Transmitted Diseases/complications ; Vagina/virology
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  • 97
    Publication Date: 1995-11-03
    Description: The period (per) gene likely encodes a component of the Drosophila circadian clock. Circadian oscillations in the abundance of per messenger RNA and per protein (PER) are thought to arise from negative feedback control of per gene transcription by PER. A recently identified second clock locus, timeless (tim), apparently regulates entry of PER into the nucleus. Reported here are the cloning of complementary DNAs derived from the tim gene in a two-hybrid screen for PER-interacting proteins and the demonstration of a physical interaction between the tim protein (TIM) and PER in vitro. A restricted segment of TIM binds directly to a part of the PER dimerization domain PAS. PERL, a mutation that causes a temperature-sensitive lengthening of circadian period and a temperature-sensitive delay in PER nuclear entry, exhibits a temperature-sensitive defect in binding to TIM. These results suggest that the interaction between TIM and PER determines the timing of PER nuclear entry and therefore the duration of part of the circadian cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gekakis, N -- Saez, L -- Delahaye-Brown, A M -- Myers, M P -- Sehgal, A -- Young, M W -- Weitz, C J -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):811-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481773" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Clocks/genetics ; Cell Nucleus/metabolism ; Circadian Rhythm/*genetics ; Cloning, Molecular ; Cytoplasm/metabolism ; DNA, Complementary/genetics ; *Drosophila Proteins ; Drosophila melanogaster/genetics/*metabolism ; Feedback ; Gene Expression Regulation ; Genes, Insect ; Mutation ; Nuclear Proteins/genetics/*metabolism ; Period Circadian Proteins ; Proteins/genetics/isolation & purification/*metabolism ; Recombinant Fusion Proteins/metabolism ; Temperature
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  • 98
    Publication Date: 1995-03-03
    Description: Cell cycle checkpoints enhance genetic fidelity by causing arrest at specific stages of the cell cycle when previous events have not been completed. The tumor suppressor p53 has been implicated in a G1 checkpoint. To investigate whether p53 also participates in a mitotic checkpoint, cultured fibroblasts from p53-deficient mouse embryos were exposed to spindle inhibitors. The fibroblasts underwent multiple rounds of DNA synthesis without completing chromosome segregation, thus forming tetraploid and octaploid cells. Deficiency of p53 was also associated with the development of tetraploidy in vivo. These results suggest that murine p53 is a component of a spindle checkpoint that ensures the maintenance of diploidy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cross, S M -- Sanchez, C A -- Morgan, C A -- Schimke, M K -- Ramel, S -- Idzerda, R L -- Raskind, W H -- Reid, B J -- R01CA55814/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Mar 3;267(5202):1353-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7871434" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Cycle ; Cells, Cultured ; DNA/biosynthesis ; Demecolcine/pharmacology ; Diploidy ; Female ; Genes, p53 ; Male ; Mice ; *Mitosis ; Nocodazole/pharmacology ; Ploidies ; Spindle Apparatus/*physiology ; Tumor Suppressor Protein p53/*physiology
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  • 99
    Publication Date: 1995-03-31
    Description: Channel adaptation is a fundamental feature of sarcoplasmic reticulum calcium release channels (called ryanodine receptors, RyRs). It permits successive increases in the intracellular concentration of calcium (Ca2+) to repeatedly but transiently activate channels. Adaptation of RyRs in the absence of magnesium (Mg2+) and adenosine triphosphate is an extremely slow process (taking seconds). Photorelease of Ca2+ from nitrophenyl-EGTA, a photolabile Ca2+ chelator, demonstrated that RyR adaptation is rapid (milliseconds) in canine heart muscle when physiological Mg2+ concentrations are present. Phosphorylation of the RyR by protein kinase A increased the responsiveness of the channel to Ca2+ and accelerated the kinetics of adaptation. These properties of the RyR from heart may also be relevant to other cells in which multiple agonist-dependent triggering events regulate cellular functions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4242209/" 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/PMC4242209/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Valdivia, H H -- Kaplan, J H -- Ellis-Davies, G C -- Lederer, W J -- HL25675/HL/NHLBI NIH HHS/ -- HL30315/HL/NHLBI NIH HHS/ -- HL36974/HL/NHLBI NIH HHS/ -- R01 GM053395/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Mar 31;267(5206):1997-2000.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Maryland Medical School, Baltimore 21201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701323" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Adenosine Triphosphate/metabolism/pharmacology ; Animals ; Calcium/*metabolism ; Calcium Channels/drug effects/*metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Dogs ; Kinetics ; Lipid Bilayers ; Magnesium/*pharmacology ; Muscle Proteins/drug effects/*metabolism ; Myocardium/*metabolism ; Phosphorylation ; Ryanodine Receptor Calcium Release Channel
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  • 100
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-08-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1995 Aug 18;269(5226):917-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638610" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/ethnology/*genetics ; Amyloid beta-Peptides/biosynthesis ; Chromosomes, Human, Pair 1/*genetics ; DNA, Complementary ; Female ; Gene Expression ; Genes ; Germany/ethnology ; Humans ; Male ; Membrane Proteins/genetics ; Mutation ; Presenilin-1 ; Sequence Homology, Nucleic Acid
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