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  • 1
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-21
    Description: Transcription of the mouse alpha-fetoprotein gene is activated in the developing fetal liver and gut and repressed in both tissues shortly after birth. With germline transformation in mice, a cis-acting element was identified upstream of the transcription initiation site of the alpha-fetoprotein gene that was responsible for repression of the gene in adult liver. This negative element acts as a repressor in a position-dependent manner.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vacher, J -- Tilghman, S M -- CA44976/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1732-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biology, Princeton University, NJ 08544.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1702902" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Animals, Newborn ; Chromosome Deletion ; Cloning, Molecular ; DNA-Binding Proteins/metabolism ; Enhancer Elements, Genetic ; Fetus ; *Gene Expression Regulation ; Hepatocyte Nuclear Factor 1 ; Hepatocyte Nuclear Factor 1-alpha ; Hepatocyte Nuclear Factor 1-beta ; Liver/growth & development/*metabolism ; Mice ; *Nuclear Proteins ; Transcription Factors/metabolism ; Transcription, Genetic ; alpha-Fetoproteins/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 1990-12-21
    Description: Ten strains of a new arbovirus belonging to the Bunyamwera group (Bunyaviridae) were recovered from field-collected Aedes albopictus mosquitoes in Potosi, Missouri. This evidence indicates that this species may serve as an arbovirus vector in the United States. The urban-suburban distribution, aggressive biting behavior, and broad viral susceptibility of Ae. albopictus may lead to the transmission of viruses of known public health importance and perhaps of viruses hitherto not transmitted to humans because of the feeding pattern of their usual vectors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Francy, D B -- Karabatsos, N -- Wesson, D M -- Moore, C G Jr -- Lazuick, J S -- Niebylski, M L -- Tsai, T F -- Craig, G B Jr -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1738-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Vector-Borne Infectious Diseases, Centers for Disease Control, U.S. Public Health Service, Fort Collins, CO 80522.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2270489" target="_blank"〉PubMed〈/a〉
    Keywords: Aedes/*microbiology ; Animals ; Arboviruses/*isolation & purification ; Asia ; Humans ; Insect Vectors ; United States
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 1990-12-21
    Description: The mechanism by which transcription factors stimulate DNA replication in eukaryotes is unknown. Bovine papillomavirus DNA synthesis requires the products of the viral E1 gene and the transcriptional activator protein encoded by the E2 gene. Experimental data showed that the 68-kilodalton (kD) E1 protein formed a complex with the 48-kD E2 transcription factor. This complex bound specifically to the viral origin of replication, which contains multiple binding sites for E2. Repressor proteins encoded by the E2 open reading frame failed to complex with E1 suggesting that the 162-amino acid region of E2 that participates in transactivation contained critical determinants for interaction with E1. The physical association between a replication protein and a transcription factor suggests that transcriptional activator proteins may function in targeting replication initiator proteins to their respective origins of replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mohr, I J -- Clark, R -- Sun, S -- Androphy, E J -- MacPherson, P -- Botchan, M R -- CA-30490/CA/NCI NIH HHS/ -- CA-42414/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1694-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkely 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2176744" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Bovine papillomavirus 1/*genetics ; Cell Line ; *DNA Replication ; DNA, Viral/biosynthesis/genetics ; DNA-Binding Proteins/*metabolism ; Genes, Viral ; Open Reading Frames ; Protein Binding ; Repressor Proteins/*metabolism ; Transcription Factors/*metabolism ; Viral Proteins/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 1990-12-21
    Description: In order to examine the mechanisms by which clonal deletion of autoreactive T cells occurs, a peptide antigen was used to induce deletion of antigen-reactive thymocytes in vivo. Mice transgenic for a T cell receptor (TCR) that reacts to this peptide contain thymocytes that progress from the immature to the mature phenotype. Intraperitoneal administration of the peptide antigen to transgenic mice results in a rapid deletion of the immature CD4+ CD8+ TCRlo thymocytes. Apoptosis of cortical thymocytes can be seen within 20 hours of treatment. These results provide direct evidence for the in vivo role of apoptosis in the development of antigen-induced tolerance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murphy, K M -- Heimberger, A B -- Loh, D Y -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1720-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2125367" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD4/*immunology ; Antigens, CD8 ; Antigens, Differentiation, T-Lymphocyte/*immunology ; Mice ; Mice, Transgenic ; Microscopy, Electron ; Molecular Sequence Data ; Ovalbumin/immunology ; Phagocytosis ; Phenotype ; Receptors, Antigen, T-Cell/genetics/*immunology ; T-Lymphocytes/cytology/*immunology/ultrastructure ; Thymus Gland/cytology/*immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 1990-12-21
    Description: A heparin binding mitogenic protein isolated from bovine uterus shares NH2-terminal amino acid sequence with a protein isolated from newborn rat brain. The cDNA's of the bovine, human, and rat genes have been isolated and encode extraordinarily conserved proteins unrelated to known growth or neurotrophic factors, although identity of nearly 50 percent has been found with the predicted sequence of a retinoic acid induced transcript in differentiating mouse embryonal carcinoma cells. Lysates of COS-7 cells transiently expressing this protein were mitogenic for NRK cells and initiated neurite outgrowth from mixed cultures of embryonic rat brain cells. RNA transcripts encoding this protein were widely distributed in tissues and were developmentally regulated. This protein, previously designated as heparin binding growth factor (HBGF)-8, is now renamed pleiotrophin (PTN) to reflect its diverse activities. PTN may be the first member of a family of developmentally regulated cytokines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Y S -- Milner, P G -- Chauhan, A K -- Watson, M A -- Hoffman, R M -- Kodner, C M -- Milbrandt, J -- Deuel, T F -- CA49712/CA/NCI NIH HHS/ -- HL14147/HL/NHLBI NIH HHS/ -- HL31102/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1690-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Jewish Hospital, Washington University Medical Center, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2270483" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Axons/*physiology/ultrastructure ; Base Sequence ; Brain/*metabolism ; *Carrier Proteins ; Cattle ; Cell Division ; Cell Line ; Cloning, Molecular ; Cytokines/*genetics ; Humans ; Mitogens/*genetics ; Molecular Sequence Data ; Organ Specificity ; Rats ; Sequence Homology, Nucleic Acid ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 1990-12-21
    Description: Influx of calcium through membrane channels is an important initial step in signal transduction of growth signals. Therefore, the effects of Ras protein injection on calcium currents across the soma membrane of an identified neuron of the snail Hermissenda were examined. With the use of these post-mitotic cells, a voltage-sensitive, inward calcium current was increased 10 to 20 minutes after Harvey-ras oncoproteins were injected. The effects of oncogenic Harvey ras p21 protein (v-Ras) occurred quickly and were sustained, whereas the effects of proto-oncogenic ras protein (c-Ras) were transient. This relative potency is consistent with the activities of these oncoproteins in stimulating cell proliferation. Thus, this calcium channel may be a target for Ras action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Collin, C -- Papageorge, A G -- Lowy, D R -- Alkon, D L -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1743-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular and Cellular Neurobiology, NINDS-NIH, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2176747" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Barium/pharmacology ; Calcium Channels/drug effects/*physiology ; In Vitro Techniques ; Membrane Potentials/drug effects ; Microinjections ; Neurons/*physiology ; Oncogene Protein p21(ras)/administration & dosage/*pharmacology ; Potassium Channels/drug effects/physiology ; Proto-Oncogene Proteins p21(ras)/administration & dosage/*pharmacology ; Snails
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 1990-12-21
    Description: Insects have an efficient defense system against infections. Their antibacterial immune proteins have been well characterized. However, the molecular mechanisms by which insects recognize foreignness are not yet known. Data are presented showing that hemolin (previously named P4), a bacteria-inducible hemolymph protein of the giant silk moth Hyalophora cecropia, belongs to the immunoglobulin superfamily. Functional analyses indicate that hemolin is one of the first hemolymph components to bind to the bacterial surface, taking part in a protein complex formation that is likely to initiate the immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sun, S C -- Lindstrom, I -- Boman, H G -- Faye, I -- Schmidt, O -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1729-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2270488" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/genetics ; *Genes, Immunoglobulin ; Hemolymph/immunology ; Immunoglobulins ; Insect Proteins ; Molecular Sequence Data ; Moths/genetics/*immunology ; *Multigene Family ; Proteins/*genetics ; Sequence Homology, Nucleic Acid
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-21
    Description: T lymphocyte activation requires recognition by the T cell of peptide fragments of foreign antigen bound to a self major histocompatibility complex (MHC) molecule. Genetic evidence suggests that part of the class II region of the MHC influences the expression, in trans, of MHC class I antigens on the cell surface, by regulating the availability of peptides that bind to and stabilize the class I molecule. Two closely related genes in this region, HAM1 and HAM2, were cloned and had sequence similarities to a superfamily of genes involved in the ATP-dependent transport of a variety of substrates across cell membranes. Thus, these MHC-linked transport protein genes may be involved in transporting antigen, or peptide fragments thereof, from the cytoplasm into a membrane-bounded compartment containing newly synthesized MHC molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Monaco, J J -- Cho, S -- Attaya, M -- GM38774/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1723-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Medical College of Virginia/Virginia Commonwealth University, Richmond 23298-0678.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2270487" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/*genetics ; Cell Line ; Cloning, Molecular ; *Major Histocompatibility Complex ; Mice ; Molecular Sequence Data ; *Multigene Family ; Protein Conformation ; Sequence Homology, Nucleic Acid ; T-Lymphocytes/*immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-21
    Description: A major mechanism for generating tolerance in developing T cells is the intrathymic clonal deletion of T cells that have receptors for those self antigens that are presented on hematopoietic cells. The mechanisms of tolerance induction to antigens not expressed in the thymus remain unclear. Tolerance to self antigens can be generated extrathymically through the induction of clonal nonresponsiveness in T cells with self-reactive receptors. A second mechanism of extrathymic tolerance was identified: clonal elimination of mature T cells with self-reactive receptors that had previously displayed functional reactivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, L A -- Chin, L T -- Longo, D L -- Kruisbeek, A M -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1726-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biological Response Modifiers Program, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2125368" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Antigens, CD4/analysis ; Antigens, CD8 ; Antigens, Differentiation, T-Lymphocyte/analysis ; Clone Cells ; *Immune Tolerance ; Kinetics ; *Lymphocyte Depletion ; Mice ; Mice, Inbred DBA ; Mice, Inbred Strains ; Spleen/immunology ; T-Lymphocytes/cytology/*immunology ; Thymus Gland/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1657-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2270477" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Viral/immunology ; Histocompatibility Antigens Class I/genetics/*immunology ; Humans ; *Immunity, Cellular ; *Major Histocompatibility Complex ; Models, Molecular ; Protein Conformation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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