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  • American Association for the Advancement of Science (AAAS)  (12)
  • PANGAEA
  • 2015-2019
  • 2005-2009
  • 2000-2004
  • 1995-1999  (12)
  • 1996  (12)
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  • 2015-2019
  • 2005-2009
  • 2000-2004
  • 1995-1999  (12)
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  • 1
    Publication Date: 1996-06-21
    Description: ZPR1 is a zinc finger protein that binds to the cytoplasmic tyrosine kinase domain of the epidermal growth factor receptor (EGFR). Deletion analysis demonstrated that this binding interaction is mediated by the zinc fingers of ZPR1 and subdomains X and XI of the EGFR tyrosine kinase. Treatment of mammalian cells with EGF caused decreased binding of ZPR1 to the EGFR and the accumulation of ZPR1 in the nucleus. The effect of EGF to regulate ZPR1 binding is dependent on tyrosine phosphorylation of the EGFR. ZPR1 therefore represents a prototype for a class of molecule that binds to the EGFR and is released from the receptor after activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galcheva-Gargova, Z -- Konstantinov, K N -- Wu, I H -- Klier, F G -- Barrett, T -- Davis, R J -- R01-CA58396/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1797-802.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650580" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/*metabolism/secretion ; Cell Line ; Cell Nucleus/metabolism ; Cloning, Molecular ; Cytoplasm/metabolism ; Epidermal Growth Factor/pharmacology ; Humans ; Immunoblotting ; Male ; Mice ; Molecular Sequence Data ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Structure, Secondary ; RNA, Messenger/genetics/metabolism ; Receptor, Epidermal Growth Factor/chemistry/*metabolism ; Testis/metabolism ; Type C Phospholipases/metabolism ; Vanadates/pharmacology ; *Zinc Fingers ; src Homology Domains
    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: 1996-03-29
    Description: Upon contacting its postsynaptic target, a neuronal growth cone transforms into a presynaptic terminal. A membrane component on the growth cone that facilitates synapse formation was identified by means of a complementary DNA-based screen followed by genetic analysis. The late bloomer (lbl) gene in Drosophila encodes a member of the tetraspanin family of cell surface proteins. LBL protein is transiently expressed on motor axons, growth cones, and terminal arbors. In lbl mutant embryos, the growth cone of the RP3 motoneuron contacts its target muscles, but synapse formation is delayed and neighboring motoneurons display an increase in ectopic sprouting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kopczynski, C C -- Davis, G W -- Goodman, C S -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1867-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, Berkeley 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596956" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Axons/metabolism/ultrastructure ; Cloning, Molecular ; Drosophila/embryology/genetics/physiology ; *Drosophila Proteins ; *Genes, Insect ; Membrane Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Motor Neurons/cytology/metabolism/*physiology ; Muscles/innervation ; Mutation ; Nerve Tissue Proteins/chemistry/genetics/*physiology ; Neuromuscular Junction/*physiology ; Presynaptic Terminals/*physiology/ultrastructure ; Signal Transduction
    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: 1996-10-04
    Description: Identification and characterization of antigen-specific T lymphocytes during the course of an immune response is tedious and indirect. To address this problem, the peptide-major histocompatability complex (MHC) ligand for a given population of T cells was multimerized to make soluble peptide-MHC tetramers. Tetramers of human lymphocyte antigen A2 that were complexed with two different human immunodeficiency virus (HIV)-derived peptides or with a peptide derived from influenza A matrix protein bound to peptide-specific cytotoxic T cells in vitro and to T cells from the blood of HIV-infected individuals. In general, tetramer binding correlated well with cytotoxicity assays. This approach should be useful in the analysis of T cells specific for infectious agents, tumors, and autoantigens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altman, J D -- Moss, P A -- Goulder, P J -- Barouch, D H -- McHeyzer-Williams, M G -- Bell, J I -- McMichael, A J -- Davis, M M -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1996 Oct 4;274(5284):94-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305-5428, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8810254" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/*immunology ; Base Sequence ; CD8-Positive T-Lymphocytes/immunology ; Cell Line ; Coloring Agents ; Epitopes/immunology ; Flow Cytometry ; Gene Products, gag/immunology ; HIV Seropositivity/*immunology ; HLA-A2 Antigen/*immunology ; Humans ; Molecular Sequence Data ; Peptide Fragments/*immunology ; Phenotype ; RNA-Directed DNA Polymerase/immunology ; T-Lymphocytes, Cytotoxic/*immunology ; Viral Matrix Proteins/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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  • 4
    Publication Date: 1996-10-25
    Description: The genome of the yeast Saccharomyces cerevisiae has been completely sequenced through a worldwide collaboration. The sequence of 12,068 kilobases defines 5885 potential protein-encoding genes, approximately 140 genes specifying ribosomal RNA, 40 genes for small nuclear RNA molecules, and 275 transfer RNA genes. In addition, the complete sequence provides information about the higher order organization of yeast's 16 chromosomes and allows some insight into their evolutionary history. The genome shows a considerable amount of apparent genetic redundancy, and one of the major problems to be tackled during the next stage of the yeast genome project is to elucidate the biological functions of all of these genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goffeau, A -- Barrell, B G -- Bussey, H -- Davis, R W -- Dujon, B -- Feldmann, H -- Galibert, F -- Hoheisel, J D -- Jacq, C -- Johnston, M -- Louis, E J -- Mewes, H W -- Murakami, Y -- Philippsen, P -- Tettelin, H -- Oliver, S G -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):546, 563-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Universite Catholique de Louvain, Unite de Biochimie Physiologique, Place Croix du Sud, 2/20, 1348 Louvain-la-Neuve, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849441" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Chromosome Mapping ; Chromosomes, Fungal/genetics ; Computer Communication Networks ; DNA, Fungal/genetics ; Evolution, Molecular ; Fungal Proteins/chemistry/genetics/physiology ; Gene Library ; *Genes, Fungal ; *Genome, Fungal ; International Cooperation ; Multigene Family ; Open Reading Frames ; RNA, Fungal/genetics ; Saccharomyces cerevisiae/*genetics ; Sequence Analysis, DNA
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-02-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, M M -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1078-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Beckman Center, Stanford University School of Medicine, Stanford, CA 94305-5428, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599081" target="_blank"〉PubMed〈/a〉
    Keywords: *Antibodies, Catalytic/chemistry/genetics/immunology ; Antibody Affinity ; Antigen-Antibody Reactions ; Catalysis ; *Evolution, Molecular ; Gene Rearrangement ; Genes, Immunoglobulin ; Haptens ; Mutagenesis ; Thermodynamics
    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
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-08-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S J -- van der Merwe, P A -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1241-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703062" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD2/*chemistry/genetics/metabolism ; Glycosylation ; Humans ; Immunoglobulins/chemistry ; Ligands ; Membrane Glycoproteins/*chemistry/genetics/metabolism ; Mutation ; Polysaccharides/chemistry ; *Protein Conformation ; Protein Folding ; Solubility
    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: 1996-10-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gupta, V -- Nivarthi, S S -- Keffer, D -- McCormick, A V -- Davis, H T -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):164.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17847219" target="_blank"〉PubMed〈/a〉
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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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-08-16
    Description: Modeling results show that collisions among Edgeworth-Kuiper Belt Objects (EKOs), a vast swarm of small bodies orbiting beyond Neptune, have been a major process affecting this population and its progeny, the short-period comets. Most EKOs larger than about 100 kilometers in diameter survive over the age of the solar system, but at smaller sizes collisional breakup is frequent, producing a cascade of fragments having a power law size-frequency distribution. Collisions are also a plausible mechanism for injecting EKOs 1 to 10 kilometers in diameter into dynamical resonances, where they can be transported into the inner solar system to become short-period comets. The fragmental nature of these comets may explain their physical properties, such as shape, color, and strength.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Farinella -- Davis -- New York, N.Y. -- Science. 1996 Aug 16;273(5277):938-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉P. Farinella, Dipartimento di Matematica, Universita di Pisa, Via Buonarroti 2, 56127 Pisa, Italy. D. R. Davis, Planetary Science Institute, 620 North Sixth Avenue, Tucson, AZ 85705-8331, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688073" target="_blank"〉PubMed〈/a〉
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  • 9
    Publication Date: 1996-12-20
    Description: An important feature of the human immune system is the ability of T cells to respond to small quantities of antigen. Class II major histocompatibility complex (MHC)-restricted T cells that expressed a costimulatory natural killer (NK) cell receptor for class I MHC proteins were cloned. In the presence of low doses of superantigen, the proliferative response of these T cell clones was three- to ninefold greater when the T cells were costimulated by way of the NK receptor. Thus, the action of costimulatory NK receptors on T cells may play a significant role in initiating and sustaining immune responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mandelboim, O -- Davis, D M -- Reyburn, H T -- Vales-Gomez, M -- Sheu, E G -- Pazmany, L -- Strominger, J L -- CA 47554/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2097-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, MA 02138, USA. jlstrom@fas.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8953044" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocytes/immunology ; Cell Line ; Clone Cells ; HLA Antigens/immunology ; HLA-C Antigens/immunology ; HLA-G Antigens ; Histocompatibility Antigens Class I/*immunology ; Histocompatibility Antigens Class II/*immunology ; Humans ; *Lymphocyte Activation ; Receptors, Immunologic/*immunology ; Superantigens/immunology ; T-Lymphocytes/*immunology ; 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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  • 10
    Publication Date: 1996-11-01
    Description: The outermost layer of the human placenta is devoid of classical class I human leukocyte antigens (HLA-A, HLA-B, and HLA-C) and class II proteins (HLA-DR, HLA-DQ, and HLA-DP). Although this prevents recognition by maternal T lymphocytes, the lack of class I molecules leaves these cells susceptible to attack by natural killer (NK) cells. However, trophoblast cells directly in contact with the maternal tissues express the class I molecule HLA-G, which may be involved in protecting the trophoblast from recognition by NK cells. Here evidence is provided that expression of HLA-G is sufficient to protect otherwise susceptible target cells from lysis by activated NK1 and NK2 cell lines and clones that are specific for distinct groups of HLA-C alleles. The receptors on NK cells that recognize HLA-G are also identified.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pazmany, L -- Mandelboim, O -- Vales-Gomez, M -- Davis, D M -- Reyburn, H T -- Strominger, J L -- CA-47554/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 1;274(5288):792-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8864122" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD56/analysis ; Cell Line ; Clone Cells ; *Cytotoxicity, Immunologic ; HLA Antigens/genetics/*physiology ; HLA-C Antigens/genetics/physiology ; HLA-G Antigens ; Histocompatibility Antigens Class I/genetics/*physiology ; Humans ; Killer Cells, Natural/*immunology ; Receptors, Immunologic/physiology ; Receptors, KIR ; Transfection ; Tumor Cells, Cultured
    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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