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  • Transfection  (98)
  • American Association for the Advancement of Science (AAAS)  (96)
  • Springer  (2)
  • American Institute of Physics
  • 1990-1994  (94)
  • 1980-1984  (4)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (96)
  • Springer  (2)
  • American Institute of Physics
Years
Year
  • 1
    Publication Date: 1990-07-13
    Description: T cell hybridomas that express zeta zeta, but not zeta eta, dimers in their T cell receptors (TCRs) produce interleukin-2 (IL-2) and undergo an inhibition of spontaneous growth when activated by antigen, antibodies to the receptor, or antibodies to Thy-1. Hybridomas without zeta and eta were reconstituted with mutated zeta chains. Cytoplasmic truncations of up to 40% of the zeta molecule reconstituted normal surface assembly of TCRs, but antigen-induced IL-2 secretion and growth inhibition were lost. In contrast, cross-linking antibodies to the TCR activated these cells. A point mutation conferred the same signaling phenotype as did the truncations and caused defective antigen-induced tyrosine kinase activation. Thus zeta allows the binding of antigen/major histocompatibility complex (MHC) to alpha beta to effect TCR signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frank, S J -- Niklinska, B B -- Orloff, D G -- Mercep, M -- Ashwell, J D -- Klausner, R D -- New York, N.Y. -- Science. 1990 Jul 13;249(4965):174-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2371564" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cross-Linking Reagents ; Dose-Response Relationship, Immunologic ; Hybridomas ; Immunity, Cellular ; Immunoblotting ; Interleukin-2/*biosynthesis ; Ligands ; *Lymphocyte Activation ; Major Histocompatibility Complex ; Mice ; Molecular Sequence Data ; Mutation ; Peptide Fragments/genetics/*immunology ; Precipitin Tests ; Receptors, Antigen, T-Cell/genetics/*immunology ; Signal Transduction ; 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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  • 2
    Publication Date: 1992-02-07
    Description: The 39- to 43-amino acid amyloid beta protein (beta AP), which is deposited as amyloid in Alzheimer's disease, is encoded as an internal peptide that begins 99 residues from the carboxyl terminus of a 695- to 770-amino acid glycoprotein referred to as the amyloid beta protein precursor (beta APP). To clarify the processing that produces amyloid, carboxyl-terminal derivatives of the beta APP were analyzed. This analysis showed that the beta APP is normally processed into a complex set of 8- to 12-kilodalton carboxyl-terminal derivatives. The two largest derivatives in human brain have the entire beta AP at or near their amino terminus and are likely to be intermediates in the pathway leading to amyloid deposition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Estus, S -- Golde, T E -- Kunishita, T -- Blades, D -- Lowery, D -- Eisen, M -- Usiak, M -- Qu, X M -- Tabira, T -- Greenberg, B D -- AG06656/AG/NIA NIH HHS/ -- AG08012/AG/NIA NIH HHS/ -- AG08992/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1992 Feb 7;255(5045):726-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuropathology, Case Western Reserve University, Cleveland, OH 44106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1738846" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid/*biosynthesis ; Amyloid beta-Protein Precursor/chemistry/genetics/*metabolism ; Cell Line ; Cell Membrane/chemistry ; Cerebral Cortex/chemistry ; Glycosylation ; Humans ; Immunoblotting ; Immunosorbent Techniques ; Molecular Weight ; Peptide Fragments/chemistry/isolation & purification/*metabolism ; Transfection
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  • 3
    Publication Date: 1992-03-13
    Description: Leukemia inhibitory factor (LIF) and interleukin-6 (IL-6) are multifunctional cytokines with many similar activities. LIF is structurally and functionally related to another cytokine, Oncostatin M (OSM), that binds to the high-affinity LIF receptor but not to the low-affinity LIF receptor. A complementary DNA was isolated that encodes the high-affinity converting subunit of the LIF receptor. The converter conferred high-affinity binding of both LIF and OSM when expressed with the low-affinity LIF receptor and is identical to the signal transducing subunit of the IL-6 receptor, gp130. The gp130 subunit alone confers low-affinity binding of OSM when expressed in COS-7 cells. This receptor system resembles the high-affinity receptors for granulocyte-macrophage colony-stimulating factor, IL-3, and IL-5, which share a common subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gearing, D P -- Comeau, M R -- Friend, D J -- Gimpel, S D -- Thut, C J -- McGourty, J -- Brasher, K K -- King, J A -- Gillis, S -- Mosley, B -- New York, N.Y. -- Science. 1992 Mar 13;255(5050):1434-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Research and Development Corporation, Seattle, WA 98101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1542794" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, CD ; Binding, Competitive ; Cell Line, Transformed ; Cytokine Receptor gp130 ; Growth Inhibitors/*metabolism ; Interleukin-6/*metabolism ; Leukemia Inhibitory Factor ; Lymphokines/*metabolism ; Membrane Glycoproteins/*metabolism ; Oncostatin M ; Peptides/*metabolism ; Radioligand Assay ; *Receptors, Cytokine ; Receptors, Immunologic/*metabolism ; Receptors, OSM-LIF ; Recombinant Proteins/metabolism ; 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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  • 4
    Publication Date: 1990-06-01
    Description: Better understanding of the pathogenesis of acquired immunodeficiency syndrome (AIDS) would be greatly facilitated by a relevant animal model that uses molecularly cloned virus of defined sequence to induce the disease. Such a system would also be of great value for AIDS vaccine research. An infectious molecular clone of simian immunodeficiency virus (SIV) was identified that induces AIDS in common rhesus monkeys in a time frame suitable for laboratory investigation. These results provide another strong link in the chain of evidence for the viral etiology of AIDS. More importantly, they define a system for molecular dissection of the determinants of AIDS pathogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kestler, H -- Kodama, T -- Ringler, D -- Marthas, M -- Pedersen, N -- Lackner, A -- Regier, D -- Sehgal, P -- Daniel, M -- King, N -- AI25328/AI/NIAID NIH HHS/ -- RR00168/RR/NCRR NIH HHS/ -- RR00169/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Jun 1;248(4959):1109-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉New England Regional Primate Research Center, Harvard Medical School, Southborough, MA 01772.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2160735" target="_blank"〉PubMed〈/a〉
    Keywords: *Acquired Immunodeficiency Syndrome ; Animals ; Antibodies, Viral/biosynthesis ; Cloning, Molecular ; *Disease Models, Animal ; Leukocytes, Mononuclear/microbiology ; Macaca mulatta ; Macrophages/microbiology ; Opportunistic Infections/etiology ; *Retroviridae Infections/complications/immunology ; *Simian Immunodeficiency Virus/genetics/immunology/isolation & ; purification/pathogenicity ; Transfection ; Virus Replication
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  • 5
    Publication Date: 1990-08-03
    Description: Phosphoenolpyruvate carboxykinase (PEPCK) governs the rate-limiting step in gluconeogenesis. Glucocorticoids and adenosine 3',5'-monophosphate (cAMP) increase PEPCK gene transcription and gluconeogenesis, whereas insulin has the opposite effect. Insulin is dominant, since it prevents cAMP and glucocorticoid-stimulated transcription. Glucocorticoid and cAMP response elements have been located in the PEPCK gene and now a 15-base pair insulin-responsive sequence (IRS) is described. Evidence for a binding activity that recognizes this sequence is presented.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, R M -- Lucas, P C -- Forest, C D -- Magnuson, M A -- Granner, D K -- DK 20593/DK/NIDDK NIH HHS/ -- DK 35107/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):533-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Physiology and Biophysics, Vanderbilt University Medical School, Nashville, TN 37232-0615.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2166335" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line ; Chloramphenicol O-Acetyltransferase/genetics/metabolism ; Cyclic AMP/analogs & derivatives/physiology ; Dexamethasone/pharmacology ; *Genes, Regulator ; Insulin/*pharmacology ; Molecular Sequence Data ; Phosphoenolpyruvate Carboxykinase (GTP)/*genetics/metabolism ; RNA, Messenger/drug effects/genetics ; Recombinant Fusion Proteins/metabolism ; Thionucleotides ; Transcription, Genetic/*drug effects ; Transfection
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  • 6
    Publication Date: 1990-06-22
    Description: The vast repertoire of immunoglobulins and T cell receptors is generated, in part, by V(D)J recombination, a series of genomic rearrangements that occur specifically in developing lymphocytes. The recombination activating gene, RAG-1, which is a gene expressed exclusively in maturing lymphoid cells, was previously isolated. RAG-1 inefficiently induced V(D)J recombinase activity when transfected into fibroblasts, but cotransfection with an adjacent gene, RAG-2, has resulted in at least a 1000-fold increase in the frequency of recombination. The 2.1-kilobase RAG-2 complementary DNA encodes a putative protein of 527 amino acids whose sequence is unrelated to that of RAG-1. Like RAG-1, RAG-2 is conserved between species that carry out V(D)J recombination, and its expression pattern correlates precisely with that of V(D)J recombinase activity. In addition to being located just 8 kilobases apart, these convergently transcribed genes are unusual in that most, if not all, of their coding and 3' untranslated sequences are contained in single exons. RAG-1 and RAG-2 might activate the expression of the V(D)J recombinase but, more likely, they directly participate in the recombination reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oettinger, M A -- Schatz, D G -- Gorka, C -- Baltimore, D -- GM39458/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 22;248(4962):1517-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2360047" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biological Evolution ; Cattle ; Cell Line ; Chickens ; Cricetinae ; DNA/*genetics ; DNA Nucleotidyltransferases/*genetics ; *DNA-Binding Proteins ; Dogs ; Female ; *Gene Rearrangement, B-Lymphocyte ; *Gene Rearrangement, T-Lymphocyte ; *Homeodomain Proteins ; Humans ; Male ; Mice ; Molecular Sequence Data ; *Multigene Family ; Nuclear Proteins ; Nucleic Acid Hybridization ; Opossums ; Proteins/*genetics ; Rabbits ; Recombination, Genetic/*genetics ; Restriction Mapping ; Transfection ; Turtles ; VDJ Recombinases
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  • 7
    Publication Date: 1990-09-21
    Description: Thyrotropin (TSH), luteinizing hormone (LH), and chorionic gonadotropin (CG) are structurally related glycoprotein hormones, which bind to receptors that share a high degree of sequence similarity. However, comparison of the primary amino acid sequences of the TSH and LH-CG receptors reveals two unique insertions of 8 and 50 amino acids in the extracellular domain of the TSH receptor. The functional significance of these insertions were determined by site-directed mutagenesis. Deletion of the 50-amino acid tract (residues 317 to 366) had no effect on TSH binding or on TSH and thyroid-stimulating immunoglobulin (TSI) biological activities. In contrast, either deletion or substitution of the eight-amino acid region (residues 38 to 45) abolished these activities. This eight-amino acid tract near the amino terminus of the TSH receptor appears to be an important site of interaction for both TSH and TSI.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wadsworth, H L -- Chazenbalk, G D -- Nagayama, Y -- Russo, D -- Rapoport, B -- DK-19289/DK/NIDDK NIH HHS/ -- DK-36182/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 21;249(4975):1423-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Veterans Administration Medical Center, San Francisco, CA 94121.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2169649" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cell Line ; Chromosome Deletion ; Clone Cells ; Cyclic AMP/metabolism ; Humans ; Molecular Sequence Data ; Mutation ; Oligonucleotide Probes ; Receptors, Thyrotropin/*genetics/metabolism ; Thyrotropin/*metabolism/pharmacology ; Transfection
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  • 8
    Publication Date: 1990-06-15
    Description: Herpes simplex virus type 1 (HSV-1) is a ubiquitous pathogen responsible for considerable morbidity in the general population. The results presented herein establish the basic fibroblast growth factor (FGF) receptor as a means of entry of HSV-1 into vertebrate cells. Inhibitors of basic FGF binding to its receptor and competitive polypeptide antagonists of basic FGF prevented HSV-1 uptake. Chinese hamster ovary (CHO) cells that do not express FGF receptors are resistant to HSV-1 entry; however, HSV-1 uptake is dramatically increased in CHO cells transfected with a complementary DNA encoding a basic FGF receptor. The distribution of this integral membrane protein in vivo may explain the tissue and cell tropism of HSV-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaner, R J -- Baird, A -- Mansukhani, A -- Basilico, C -- Summers, B D -- Florkiewicz, R Z -- Hajjar, D P -- P01 DK 18811/DK/NIDDK NIH HHS/ -- P01 HD 96601/HD/NICHD NIH HHS/ -- P50 HL 18828/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Jun 15;248(4961):1410-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2162560" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; Amino Acid Sequence ; Animals ; Binding, Competitive ; Cell Line ; Cell Membrane/microbiology ; Cricetinae ; DNA/genetics ; Fibroblast Growth Factors/antagonists & inhibitors/metabolism/pharmacology ; Heparitin Sulfate/metabolism ; Molecular Sequence Data ; Peptide Fragments/pharmacology ; Receptors, Cell Surface/genetics/*physiology ; Receptors, Fibroblast Growth Factor ; Simplexvirus/*physiology ; Transfection
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  • 9
    Publication Date: 1991-02-01
    Description: Neurotransmitter receptors are generally clustered in the postsynaptic membrane. The mechanism of clustering was analyzed with fibroblast cell lines that were stably transfected with the four subunits for fetal (alpha, beta, gamma, delta) or adult (alpha, beta, epsilon, delta) type mouse muscle nicotinic acetylcholine receptors (AChRs). Immunofluorescent staining indicated that AChRs were dispersed on the surface of these cells. When transiently transfected with an expression construct encoding a 43-kilodalton protein that is normally concentrated under the postsynaptic membrane, AChRs expressed in these cells became aggregated in large cell-surface clusters, colocalized with the 43-kilodalton protein. This suggests that 43-kilodalton protein can induce AChR clustering and that cluster induction involves direct contact between AChR and 43-kilodalton protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Phillips, W D -- Kopta, C -- Blount, P -- Gardner, P D -- Steinbach, J H -- Merlie, J P -- R01 NS022356/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 1;251(4993):568-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, 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/1703661" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/pharmacology ; Animals ; Cell Membrane/physiology ; Fetus ; Fibroblasts/cytology/physiology ; Fluorescent Antibody Technique ; Ion Channels/drug effects/physiology ; Macromolecular Substances ; Mice ; Molecular Weight ; Muscles/physiology ; Receptors, Nicotinic/analysis/genetics/*physiology ; Recombinant Proteins/analysis/metabolism ; Transfection
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  • 10
    Publication Date: 1991-01-04
    Description: An expression cloning strategy was devised to isolate the keratinocyte growth factor (KGF) receptor complementary DNA. NIH/3T3 fibroblasts, which secrete this epithelial cell-specific mitogen, were transfected with a keratinocyte expression complementary DNA library. Among several transformed foci identified, one demonstrated the acquisition of specific high-affinity KGF binding sites. The pattern of binding competition by related fibroblast growth factors (FGFs) indicated that this receptor had high affinity for acidic FGF as well as KGF. The rescued 4.2-kilobase complementary DNA was shown to encode a predicted membrane-spanning tyrosine kinase related to but distinct from the basic FGF receptor. This expression cloning approach may be generally applicable to the isolation of genes that constitute limiting steps in mitogenic signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miki, T -- Fleming, T P -- Bottaro, D P -- Rubin, J S -- Ron, D -- Aaronson, S A -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):72-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1846048" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; Cell Line ; *Cloning, Molecular ; DNA/*genetics ; Fibroblast Growth Factor 10 ; Fibroblast Growth Factor 7 ; Fibroblast Growth Factors/metabolism ; Fibroblasts/metabolism ; *Gene Expression ; Growth Substances/metabolism ; Mice ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Plasmids ; Receptor, Fibroblast Growth Factor, Type 2 ; Receptors, Cell Surface/*genetics/metabolism ; *Receptors, Fibroblast Growth Factor ; Recombinant Proteins/metabolism ; Transfection ; Transformation, Genetic
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