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  • Articles  (390)
  • Mice  (218)
  • Rats  (208)
  • American Association for the Advancement of Science (AAAS)  (390)
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  • 1985  (215)
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  • Articles  (390)
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  • American Association for the Advancement of Science (AAAS)  (390)
  • American Association for the Advancement of Science
  • American Chemical Society
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  • 1990-1994
  • 1985-1989  (390)
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  • 1
    Publication Date: 1986-10-17
    Description: The regulation of nerve growth factor (NGF) protein and NGF messenger RNA (mRNA) in the developing rat brain has been studied to assess the hypothesis that NGF supports the differentiation of cholinergic neurons in the basal forebrain. In the adult, the major targets of these neurons, the hippocampus and neocortex, contain the highest concentrations of NGF mRNA, but comparatively low ratios of NGF protein to its mRNA. In contrast, a high concentration of NGF protein and a low concentration of NGF mRNA were seen in the basal forebrain, consistent with retrograde transport of NGF protein into this region from the neocortex and hippocampus. In these two target regions NGF and NGF mRNA were barely detectable at birth, their concentrations increased to a peak at day 21, and then NGF mRNA, but not NGF protein, declined threefold by day 35. NGF accumulation in the basal forebrain paralleled that in the target regions and preceded an increase in choline acetyltransferase, suggesting that the differentiation of cholinergic projection neurons is indeed regulated by retrogradely transported NGF. In addition, high ratios of NGF protein to NGF mRNA, comparable to that in the basal forebrain, were seen in the olfactory bulb and cerebellum, suggesting that NGF may be transported into these regions by unidentified neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Large, T H -- Bodary, S C -- Clegg, D O -- Weskamp, G -- Otten, U -- Reichardt, L F -- NS21824/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1986 Oct 17;234(4774):352-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3764415" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*growth & development/metabolism ; Brain Chemistry ; Cerebellum/analysis ; Cerebral Cortex/analysis ; Hippocampus/analysis ; Nerve Growth Factors/analysis/*biosynthesis/genetics ; RNA, Messenger/analysis ; Rats ; Rats, Inbred Strains
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  • 2
    Publication Date: 1986-04-04
    Description: A lectin in Giardia lamblia was activated by secretions from the human duodenum, the environment where the parasite lives. Incubation of the secretions with trypsin inhibitors prevented the appearance of lectin activity, implicating proteases as the activating agent. Accordingly, lectin activation was also produced by crystalline trypsin and Pronase; other proteases tested were ineffective. When activated, the lectin agglutinated intestinal cells to which the parasite adheres in vivo. The lectin was most specific to mannose-6-phosphate and apparently was bound to the plasma membrane. Activation of a parasite lectin by a host protease represents a novel mechanism of host-parasite interaction and may contribute to the affinity of Giardia lamblia to the infection site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lev, B -- Ward, H -- Keusch, G T -- Pereira, M E -- P-1-P30-AM 39428-01/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 4;232(4746):71-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3513312" target="_blank"〉PubMed〈/a〉
    Keywords: Agglutination ; Animals ; Duodenum/enzymology/parasitology ; Giardia/*metabolism ; *Host-Parasite Interactions ; Humans ; Intestine, Small/enzymology/*parasitology ; Lectins/*metabolism ; Mice ; Peptide Hydrolases/*metabolism ; Sheep ; Species Specificity ; Trypsin/metabolism
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  • 3
    Publication Date: 1986-01-31
    Description: p-Chloromercuriphenylsulfonic acid (PCMS), a sulfhydryl inhibitor, prevented the mycelial-to-yeast transition of the dimorphic fungal pathogen, Histoplasma capsulatum. The effect of PCMS was specific for the mycelial-to-yeast transformation; it had no effect on growth of either the yeast or mycelial forms or on the yeast-to-mycelial transition. The failure of PCMS-treated mycelia to transform to yeast was permanent and irreversible. PCMS-treated mycelia could not infect mice but could stimulate resistance to infection by a pathogenic strain of Histoplasma capsulatum. These results suggest a new general strategy for vaccine development in diseases caused by dimorphic pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Medoff, G -- Sacco, M -- Maresca, B -- Schlessinger, D -- Painter, A -- Kobayashi, G S -- Carratu, L -- AI 07015/AI/NIAID NIH HHS/ -- AI 07172/AI/NIAID NIH HHS/ -- AI 16228/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 31;231(4737):476-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3001938" target="_blank"〉PubMed〈/a〉
    Keywords: 4-Chloromercuribenzenesulfonate/pharmacology ; Animals ; Cytochromes/metabolism ; Energy Metabolism/drug effects ; Fungal Proteins/biosynthesis ; Histoplasma/drug effects/pathogenicity/*physiology ; Histoplasmosis/etiology ; Kinetics ; Mice ; Oxidative Phosphorylation/drug effects ; Oxygen Consumption/drug effects
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  • 4
    Publication Date: 1986-11-07
    Description: Binding of antibodies to effector cells by way of receptors to their constant regions (Fc receptors) is central to the pathway that leads to clearance of antigens by the immune system. The structure and function of this important class of receptors on immune cells is addressed through the molecular characterization of Fc receptors (FcR) specific for the murine immunoglobulin G isotype. Structural diversity is encoded by two genes that by alternative splicing result in expression of molecules with highly conserved extracellular domains and different transmembrane and intracytoplasmic domains. The proteins encoded by these genes are members of the immunoglobulin supergene family, most homologous to the major histocompatibility complex molecule E beta. Functional reconstitution of ligand binding by transfection of individual FcR genes demonstrates that the requirements for ligand binding are encoded in a single gene. These studies demonstrate the molecular basis for the functional heterogeneity of FcR's, accounting for the possible transduction of different signals in response to a single ligand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ravetch, J V -- Luster, A D -- Weinshank, R -- Kochan, J -- Pavlovec, A -- Portnoy, D A -- Hulmes, J -- Pan, Y C -- Unkeless, J C -- AI 24322/AI/NIAID NIH HHS/ -- GM 36306/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Nov 7;234(4777):718-25.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2946078" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/genetics ; Gene Expression Regulation ; Histocompatibility Antigens Class II/genetics ; Immunoglobulin G ; Lymphocytes/*physiology ; Macrophages/*physiology ; Membrane Proteins ; Mice ; Protein Conformation ; *Receptors, Fc/genetics ; Receptors, IgG ; Transcription, Genetic ; Transfection
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  • 5
    Publication Date: 1986-02-28
    Description: Transgenic mice expressing a metallothionein-somatostatin fusion gene contain high concentrations of somatostatin in the anterior pituitary gland, a tissue that does not normally produce somatostatin. Immunoreactive somatostatin within the anterior pituitaries was found exclusively within gonadotrophs. Similarly, a metallothionein-human growth-hormone fusion gene was also expressed selectively in gonadotrophs. It is proposed that sequences common to the two fusion genes are responsible for the gonadotroph-specific expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Low, M J -- Lechan, R M -- Hammer, R E -- Brinster, R L -- Habener, J F -- Mandel, G -- Goodman, R H -- AM 01313/AM/NIADDK NIH HHS/ -- AM 30457/AM/NIADDK NIH HHS/ -- AM 31400/AM/NIADDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Feb 28;231(4741):1002-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2868526" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA, Recombinant/metabolism ; Genes ; Genetic Engineering ; Humans ; Immunoenzyme Techniques ; Luteinizing Hormone/metabolism ; Metallothionein/*genetics ; Mice ; Pituitary Gland, Anterior/*metabolism ; Rats ; Somatostatin/*genetics/metabolism
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  • 6
    Publication Date: 1986-02-21
    Description: Partial amino acid sequence analysis of a purified lymphocyte homing receptor demonstrates the presence of two amino termini, one of which corresponds precisely to the amino terminus of ubiquitin. This observation extends the province of this conserved polypeptide to the cell surface and leads to a proposed model of the receptor complex as a core polypeptide modified by glycosylation and ubiquitination. Independent antibodies to ubiquitin serve to identify additional cell surface species, an indication that ubiquitination of cell surface proteins may be more general. It is proposed that functional binding of lymphocytes to lymph node high endothelial venules might involve the ubiquitinated region of the receptor; if true, cell surface ubiquitin could play a more general role in cell-cell interaction and adhesion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Siegelman, M -- Bond, M W -- Gallatin, W M -- St John, T -- Smith, H T -- Fried, V A -- Weissman, I L -- AI 19512/AI/NIAID NIH HHS/ -- CA 09151/CA/NCI NIH HHS/ -- GM 31461/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Feb 21;231(4740):823-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3003913" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Cell Movement ; Endothelium/metabolism ; Glycoproteins/metabolism/*physiology ; Glycoside Hydrolases/metabolism ; High Mobility Group Proteins/*metabolism ; Lymphocytes/*physiology ; Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase ; Membrane Proteins/metabolism/*physiology ; Mice ; Molecular Weight ; Protein Processing, Post-Translational ; Receptors, Cell Surface/metabolism/*physiology ; Ubiquitins/immunology/*metabolism
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  • 7
    Publication Date: 1986-04-04
    Description: Experiments were conducted to isolate and characterize the gene and gene product of a human hematopoietic colony-stimulating factor with pluripotent biological activities. This factor has the ability to induce differentiation of a murine myelomonocytic leukemia cell line WEHI-3B(D+) and cells from patients with newly diagnosed acute nonlymphocytic leukemia (ANLL). A complementary DNA copy of the gene encoding a pluripotent human granulocyte colony-stimulating factor (hG-CSF) was cloned and expressed in Escherichia coli. The recombinant form of hG-CSF is capable of supporting neutrophil proliferation in a CFU-GM assay. In addition, recombinant hG-CSF can support early erythroid colonies and mixed colony formation. Competitive binding studies done with 125I-labeled hG-CSF and cell samples from two patients with newly diagnosed human leukemias as well as WEHI-3B(D+) cells showed that one of the human leukemias (ANLL, classified as M4) and the WEHI-3B(D+) cells have receptors for hG-CSF. Furthermore, the murine WEHI-3B(D+) cells and human leukemic cells classified as M2, M3, and M4 were induced by recombinant hG-CSF to undergo terminal differentiation to macrophages and granulocytes. The secreted form of the protein produced by the bladder carcinoma cell line 5637 was found to be O-glycosylated and to have a molecular weight of 19,600.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Souza, L M -- Boone, T C -- Gabrilove, J -- Lai, P H -- Zsebo, K M -- Murdock, D C -- Chazin, V R -- Bruszewski, J -- Lu, H -- Chen, K K -- CA00966/CA/NCI NIH HHS/ -- CA20194/CA/NCI NIH HHS/ -- CA32516/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Apr 4;232(4746):61-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2420009" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation/drug effects ; Cell Line ; Colony-Forming Units Assay ; Colony-Stimulating Factors/genetics/*pharmacology ; DNA/metabolism ; Escherichia coli/genetics ; Genes ; Granulocyte Colony-Stimulating Factor ; Granulocytes/*physiology ; Humans ; Leukemia/*pathology ; Leukemia, Myeloid/pathology ; Mice ; Plasmids ; Recombinant Proteins/*pharmacology
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  • 8
    Publication Date: 1986-05-23
    Description: Electrical stimulation of fibers in the stratum radiatum causes an excitatory postsynaptic potential in CA1 neurons of the hippocampus. Other excitatory inputs to or direct depolarization of these CA1 neurons during stimulation of the stratum radiatum caused a subsequent increase in the excitatory postsynaptic potential. This enhancement was characterized as a brief potentiation (2 to 3 minutes, similar to posttetanic potentiation) and a long-term potentiation (presumed to be involved in learning and memory). These potentiations are probably induced by an interaction of the postsynaptic cell or other presynaptic terminals with the test presynaptic terminals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sastry, B R -- Goh, J W -- Auyeung, A -- New York, N.Y. -- Science. 1986 May 23;232(4753):988-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3010459" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Brain Mapping ; Calcium/physiology ; Conditioning (Psychology)/physiology ; Electric Stimulation ; Hippocampus/*physiology ; In Vitro Techniques ; Learning/physiology ; Membrane Potentials ; Rats ; Synapses/physiology ; Synaptic Transmission
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  • 9
    Publication Date: 1986-02-07
    Description: Comparison of HTLV-III, the putative AIDS virus, with other related viruses, may help to reveal more about the origin of AIDS in humans. In this study, the nucleotide sequence of the gag and pol genes of an equine infectious anemia virus (EIAV) proviral DNA clone was determined. The sequence was compared with that of HTLV-III and of visna, a pathogenic lentivirus of sheep. The results show that these viruses constitute a family clearly distinct from that of the type C viruses or the BLV-HTLV-I and -II group. Within the family, EIAV, HTLV-III, and visna appear to be equally divergent from a common evolutionary ancestor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stephens, R M -- Casey, J W -- Rice, N R -- N0I-C-23909/PHS HHS/ -- New York, N.Y. -- Science. 1986 Feb 7;231(4738):589-94.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3003905" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Codon ; DNA, Viral/genetics ; Deltaretrovirus/*genetics ; *Genes, Viral ; Horses ; Humans ; Infectious Anemia Virus, Equine/*genetics ; Mice ; Visna-maedi virus/*genetics
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-07-18
    Description: The historical background of studies in Japan on chemical carcinogenesis from environmental sources is described from personal experience.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sugimura, T -- New York, N.Y. -- Science. 1986 Jul 18;233(4761):312-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3088728" target="_blank"〉PubMed〈/a〉
    Keywords: 4-Nitroquinoline-1-oxide/analysis ; Animals ; Biotransformation ; Carcinogens/*analysis ; Cyanobacteria/analysis ; Environmental Pollution/*analysis ; Food Additives ; Food Handling ; Furylfuramide/toxicity ; Health Policy ; Humans ; Indoles/metabolism ; Japan ; Lyngbya Toxins/toxicity ; Methods ; Methylnitronitrosoguanidine/toxicity ; Mutagenicity Tests ; Oncogenes ; Primary Prevention ; Rats ; Risk ; Stereoisomerism ; Stomach Neoplasms/chemically induced ; Streptomyces/analysis ; Structure-Activity Relationship ; Urinary Bladder Neoplasms/chemically induced
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-07-25
    Description: Electrophysiological recordings of inward currents from whole cells showed that vascular muscle cells have one type of sodium channel and two types of calcium channels. One of the calcium channels, the transient calcium channel, was activated by small depolarizations but then rapidly inactivated. It was equally permeable to calcium and barium and was blocked by cadmium, but not by tetrodotoxin. The other type, the sustained calcium channel, was activated by larger depolarizations, but inactivated very little; it was more permeable to barium than calcium. The sustained calcium channel was more sensitive to block by cadmium than the transient channel, but also was not blocked by tetrodotoxin. The sodium channel inactivated 15 times more rapidly than the transient calcium channel and at more negative voltages. This sodium channel, which is unusual because it is only blocked by a very high (60 microM) tetrodotoxin concentration but not by cadmium, is the first to be characterized in vascular muscle, and together with the two calcium channels, provides a basis for different patterns of excitation in vascular muscles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sturek, M -- Hermsmeyer, K -- HL 16328/HL/NHLBI NIH HHS/ -- HL 32295/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jul 25;233(4762):475-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2425434" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*physiology ; Ion Channels/*physiology ; Membrane Potentials ; *Muscle Contraction ; Muscle, Smooth, Vascular/*physiology ; Rats ; Rats, Inbred WKY ; Sodium/*physiology
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  • 12
    Publication Date: 1986-05-23
    Description: Infection of the central nervous system by mouse hepatitis virus strain A59, a murine neurotropic coronavirus, induces class I major histocompatibility complex antigens on mouse oligodendrocytes and astrocytes, cells that do not normally express these antigens on their surfaces. This induction, which occurs through soluble factors elaborated by infected glial cells, potentially allows immunocytes to interact with the glial cells and may play a critical role in the pathogenesis of virus-induced, immune-mediated demyelination in the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Suzumura, A -- Lavi, E -- Weiss, S R -- Silberberg, D H -- NS11037/NS/NINDS NIH HHS/ -- NS21954/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1986 May 23;232(4753):991-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3010460" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/*immunology ; Cells, Cultured ; Fluorescent Antibody Technique ; H-2 Antigens/*immunology ; Hepatitis, Viral, Animal/*immunology ; Macrophages/immunology ; Mice ; Murine hepatitis virus/immunology ; Neuroglia/*immunology ; Oligodendroglia/*immunology
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-01-31
    Description: Contrary to the orthodox view that optical image quality should "match" the photoreceptor grain, anatomical data from the eyes of various animals suggest that the image quality is significantly superior to the potential resolution of the cone mosaic in most retinal regions. A new theory is presented to explain the existence of this relation and to better appreciate eye design. It predicts that photoreceptors are potentially visible through the natural optics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Snyder, A W -- Bossomaier, T R -- Hughes, A -- New York, N.Y. -- Science. 1986 Jan 31;231(4737):499-501.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3941914" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cats ; Humans ; Models, Neurological ; Photoreceptor Cells/*anatomy & histology ; Rats ; Snakes ; Species Specificity ; *Vision, Ocular ; *Visual Perception
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  • 14
    Publication Date: 1986-08-15
    Description: The genetic and molecular mechanisms that determine the capacity of a virus to utilize distinct pathways of spread in an infected host were examined by using reoviruses. Both reovirus type 1 and reovirus type 3 spread to the spinal cord following inoculation into the hindlimb or forelimb footpad of newborn mice. For type 3 this spread is through nerves and occurs via the microtubule-associated system of fast axonal transport. By contrast, type 1 spreads to the spinal cord through the bloodstream. With the use of reassortant viruses containing various combinations of double-stranded RNA segments (genes) derived from type 1 and type 3, the viral S1 double-stranded RNA segment was shown to be responsible for determining the capacity of reoviruses to spread to the central nervous system through these distinct pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tyler, K L -- McPhee, D A -- Fields, B N -- 2 P01 NS16998/NS/NINDS NIH HHS/ -- 5 R01 AI13178/AI/NIAID NIH HHS/ -- K11-AI00610/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):770-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3016895" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Forelimb ; *Genes, Viral ; Hindlimb ; Mammalian orthoreovirus 3/*genetics/pathogenicity ; Mice ; Reoviridae/*genetics/pathogenicity ; Reoviridae Infections/microbiology ; Sciatic Nerve/physiology ; Species Specificity ; Spinal Cord/*microbiology
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  • 15
    Publication Date: 1986-04-18
    Description: In situ hybridization of an oligonucleotide probe complementary to vasopressin messenger RNA (mRNA) in sections from normal or Brattleboro rat hypothalami revealed hybridization densities in each of three vasopressin-rich nuclei: the supraoptic, paraventricular, and suprachiasmatic. When entrained to a daily light-dark cycle, each rat strain displayed diurnal variation in hybridizable mRNA in the suprachiasmatic, but not in the supraoptic or paraventricular nuclei. The higher values for suprachiasmatic mRNA in the morning correlate well with previously elucidated morning increases in vasopressin immunoreactivity in the cerebrospinal fluid. These results support the utility of in situ hybridization techniques for elucidating physiological influences on regional peptidergic function, are consistent with a prominent role for vasopressinergic suprachiasmatic neurons in generating the cerebrospinal fluid vasopressin rhythm, and suggest that regulation of this mRNA rhythm is not dependent on release of intact peptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Uhl, G R -- Reppert, S M -- New York, N.Y. -- Science. 1986 Apr 18;232(4748):390-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3961487" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoradiography ; *Circadian Rhythm ; Nucleic Acid Hybridization ; Paraventricular Hypothalamic Nucleus/analysis/physiology ; RNA, Messenger/*analysis/isolation & purification ; Rats ; Rats, Brattleboro ; Rats, Inbred Strains ; Suprachiasmatic Nucleus/*analysis/physiology ; Supraoptic Nucleus/analysis/physiology ; Vasopressins/genetics/*physiology
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  • 16
    Publication Date: 1986-06-13
    Description: Administration of cholecystokinin (CCK) to rats caused a dose-dependent increase in plasma levels of the neurohypophyseal hormone oxytocin (OT). The OT secretion was comparable to that found in response to nausea-producing chemical agents that cause learned taste aversions. The effect of CCK on OT secretion was blunted after gastric vagotomy, as was the inhibition of food intake induced by CCK. Food ingestion also led to elevated plasma OT in rats, but CCK and aversive agents caused even greater OT stimulation. Thus, after administration of large doses of CCK, vagally mediated activation of central nausea pathways seems to be predominantly responsible for the subsequent decrease in food intake. Despite their dissimilar affective states, both nausea and satiety may activate a common hypothalamic oxytocinergic pathway that controls the inhibition of ingestion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verbalis, J G -- McCann, M J -- McHale, C M -- Stricker, E M -- AM-16166/AM/NIADDK NIH HHS/ -- MH-25140/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1986 Jun 13;232(4756):1417-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3715453" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avoidance Learning/physiology ; Cholecystokinin/*pharmacology ; Feeding Behavior/*physiology ; Nausea/*physiopathology ; Oxytocin/*secretion ; Paraventricular Hypothalamic Nucleus/physiology ; Rats ; Satiation/*physiology ; Vagotomy
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  • 17
    Publication Date: 1986-05-09
    Description: Antigenic or mitogenic stimulation of T cells induces the secretion of an array of protein hormones that regulate immune responses. Molecular cloning has contributed strongly to our present understanding of the nature of this regulation. A complementary DNA (cDNA) library prepared from a cloned concanavalin A-activated mouse T-helper cell line was screened for abundant and induction-specific cDNA's. One such randomly chosen cDNA was found to encode mouse preproenkephalin messenger RNA (mRNA). Preproenkephalin mRNA represented about 0.4 percent of the mRNA in the activated cell line but was absent in resting cells of this line. Other induced T-helper cell lines have 0.1 to 0.5 percent of their mRNA as preproenkephalin mRNA. Induced T-helper cell culture supernatants have [Met]enkephalin-immunoreactive material. The production by activated T cells of a peptide neurotransmitter identifies a signal that can potentially permit T cells to modulate the nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zurawski, G -- Benedik, M -- Kamb, B J -- Abrams, J S -- Zurawski, S M -- Lee, F D -- New York, N.Y. -- Science. 1986 May 9;232(4751):772-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2938259" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cattle ; Cell Line ; Cloning, Molecular ; DNA/genetics ; Enkephalins/*biosynthesis/genetics ; Humans ; *Lymphocyte Activation ; Mice ; Protein Precursors/*biosynthesis/genetics ; RNA, Messenger/*biosynthesis ; Rats ; T-Lymphocytes, Helper-Inducer/drug effects/metabolism/*physiology
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  • 18
    Publication Date: 1986-09-05
    Description: Expression of the ras oncogene is thought to be one of the contributing events in the initiation of certain types of human cancer. To determine the cellular activities that are directly triggered by ras proteins, the early consequences of microinjection of the human H-ras proteins into quiescent rat embryo fibroblasts were investigated. Within 30 minutes to 1 hour after injection, cells show a marked increase in surface ruffles and fluid-phase pinocytosis. The rapid enhancement of membrane ruffling and pinocytosis is induced by both the proto-oncogenic and the oncogenic forms of the H-ras protein. The effects produced by the oncogenic protein persist for more than 15 hours after injection, whereas the effects of the proto-oncogenic protein are short-lived, being restricted to a 3-hour interval after injection. The stimulatory effect of the ras oncogene protein on ruffling and pinocytosis is dependent on the amount of injected protein and is accompanied by an apparent stimulation of phospholipase A2 activity. These rapid changes in cell membrane activities induced by ras proteins may represent primary events in the mechanism of action of ras proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bar-Sagi, D -- Feramisco, J R -- CA07896/CA/NCI NIH HHS/ -- CA39811/CA/NCI NIH HHS/ -- GM28277/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 5;233(4768):1061-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3090687" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Cycle/drug effects ; Cell Membrane/*drug effects/ultrastructure ; Cells, Cultured ; Culture Media ; DNA/biosynthesis ; GTP-Binding Proteins/*pharmacology ; Humans ; Microinjections ; Oncogene Proteins, Viral/*pharmacology ; Phospholipases A/metabolism ; Phospholipases A2 ; Phospholipids/metabolism ; Pinocytosis/*drug effects ; Rats ; Time Factors
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-07-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barnes, D M -- New York, N.Y. -- Science. 1986 Jul 11;233(4760):155-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3726526" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*anatomy & histology/growth & development ; Chickens ; Genes ; Humans ; Language Development ; Male ; Neurons/physiology ; Rats ; Synapses/physiology ; Visual Cortex/anatomy & histology/physiology
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-01-24
    Description: The dynamics of the attachment of lymphocytes to the endothelium of high endothelial venules in murine Peyer's patches were studied in vivo. Lymphocytes adhered readily to the endothelium lining these vessels, but most of the adhering cells detached within a few seconds. Many lymphocytes, however, experienced multiple collisions with the high endothelial venules, and this substantially increased the efficiency of lymphocyte collection by these vessels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bjerknes, M -- Cheng, H -- Ottaway, C A -- New York, N.Y. -- Science. 1986 Jan 24;231(4736):402-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3941903" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Endothelium/physiology ; Female ; In Vitro Techniques ; Lymphocytes/*physiology ; Mice ; Mice, Inbred BALB C ; Microscopy, Fluorescence ; Peyer's Patches/*physiology
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  • 21
    Publication Date: 1986-08-08
    Description: The production and action of immunoregulatory cytokines, including interleukin-1 (IL-1), are inhibited by glucocorticoid hormones in vivo and in vitro. Conversely, glucocorticoid blood levels were increased by factors released by human leukocytes exposed to Newcastle disease virus preparations. This activity was neutralized by an antibody to IL-1. Therefore the capacity of IL-1 to stimulate the pituitary-adrenal axis was tested. Administration of subpyrogenic doses of homogeneous human monocyte-derived IL-1 or the pI 7 form of human recombinant IL-1 to mice and rats increased blood levels of adrenocorticotropic hormone (ACTH) and glucocorticoids. Another monokine, tumor necrosis factor, and the lymphokines IL-2 and gamma-interferon had no such effects when administered in doses equivalent to or higher than those of IL-1. The stimulatory effect of IL-1 on the pituitary-adrenal axis seemed not to be mediated by the secondary release of products from mature T lymphocytes since IL-1 was endocrinologically active when injected into athymic nude mice. These results strongly support the existence of an immunoregulatory feedback circuit in which IL-1 acts as an afferent and glucocorticoid as an efferent hormonal signal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Besedovsky, H -- del Rey, A -- Sorkin, E -- Dinarello, C A -- AI15614/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 8;233(4764):652-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014662" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenocorticotropic Hormone/blood/physiology ; Animals ; Corticosterone/blood/physiology ; Female ; Glucocorticoids/blood/immunology/*physiology ; Humans ; Interleukin-1/immunology/pharmacology/*physiology ; Leukocytes/drug effects/physiology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Mice, Nude ; Newcastle disease virus/immunology ; Rats ; Rats, Inbred Strains
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  • 22
    Publication Date: 1986-06-27
    Description: Age-associated increases in collagen cross-linking and accumulation of advanced glycosylation products are both accelerated by diabetes, suggesting that glucose-derived cross-link formation may contribute to the development of chronic diabetic complications as well as certain physical changes of aging. Aminoguanidine, a nucleophilic hydrazine compound, prevented both the formation of fluorescent advanced nonenzymatic glycosylation products and the formation of glucose-derived collagen cross-links in vitro. Aminoguanidine administration to rats was equally effective in preventing diabetes-induced formation of fluorescent advanced nonenzymatic glycosylation products and cross-linking of arterial wall connective tissue protein in vivo. The identification of aminoguanidine as an inhibitor of advanced nonenzymatic glycosylation product formation now makes possible precise experimental definition of the pathogenetic significance of this process and suggests a potential clinical role for aminoguanidine in the future treatment of chronic diabetic complications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brownlee, M -- Vlassara, H -- Kooney, A -- Ulrich, P -- Cerami, A -- AM 19655/AM/NIADDK NIH HHS/ -- R01-AM 33861/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Jun 27;232(4758):1629-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3487117" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arteries/*drug effects/metabolism ; Collagen/metabolism ; Connective Tissue/drug effects/metabolism ; Diabetes Mellitus, Experimental/*drug therapy/metabolism ; Glucose/metabolism ; Guanidines/*pharmacology/therapeutic use ; Male ; Rats ; Rats, Inbred Lew ; Serum Albumin, Bovine/metabolism
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  • 23
    Publication Date: 1986-01-17
    Description: T lymphocytes recognize foreign antigen together with allele-specific determinants on membrane-bound class I and class II (Ia) gene products of the major histocompatibility complex. To identify amino acids of class II molecules critical to this recognition process, the genes encoding the beta chains of the I-Ak molecule were cloned from a wild-type B-cell hybridoma and from an immunoselected variant subline showing distinct serological and T-cell stimulatory properties. Nucleotide sequencing and DNA-mediated gene transfer established that a single base transition (G----A) encoding a change from glutamic acid to lysine at position 67 in the I-Ak beta molecule accounted for all the observed phenotypic changes of the variant cells. These results confirm the importance of residues 62 to 78 in the amino terminal domain of I-A beta for class II-restricted T-cell recognition of antigen and demonstrate the ability of a single substitution in this region to alter this recognition event.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, M A -- Glimcher, L A -- Nielsen, E A -- Paul, W E -- Germain, R N -- New York, N.Y. -- Science. 1986 Jan 17;231(4735):255-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3484558" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/genetics/immunology ; Base Sequence ; Cloning, Molecular ; Histocompatibility Antigens Class II/*immunology ; Humans ; Hybridomas/immunology ; Major Histocompatibility Complex ; Mice ; Mice, Inbred BALB C ; T-Lymphocytes/*immunology
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  • 24
    Publication Date: 1986-04-25
    Description: Nerve growth factor (NGF) and its receptor are important in the development of cells derived from the neural crest. Mouse L cell transformants have been generated that stably express the human NGF receptor gene transfer with total human DNA. Affinity cross-linking, metabolic labeling and immunoprecipitation, and equilibrium binding with 125I-labeled NGF revealed that this NGF receptor had the same size and binding characteristics as the receptor from human melanoma cells and rat PC12 cells. The sequences encoding the NGF receptor were molecularly cloned using the human Alu repetitive sequence as a probe. A cosmid clone that contained the human NGF receptor gene allowed efficient transfection and expression of the receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chao, M V -- Bothwell, M A -- Ross, A H -- Koprowski, H -- Lanahan, A A -- Buck, C R -- Sehgal, A -- NS-17551/NS/NINDS NIH HHS/ -- NS-23343-01/NS/NINDS NIH HHS/ -- NS21072/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Apr 25;232(4749):518-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3008331" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Transformation, Neoplastic/drug effects ; *Cloning, Molecular ; DNA, Recombinant ; Genes ; Humans ; Melanoma/metabolism ; Mice ; Oncogenes ; Rats ; Receptors, Cell Surface/*genetics ; Receptors, Nerve Growth Factor ; Repetitive Sequences, Nucleic Acid ; Tunicamycin/pharmacology
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  • 25
    Publication Date: 1986-07-25
    Description: Rat thyroid cells in culture, rendered quiescent by hormone deprivation, can be stimulated to undergo DNA synthesis in the absence of serum by the addition of purified thyrotropin. The primary effect in response to thyrotropin action in thyroid cells is the induction of the c-fos oncogene, followed by c-myc expression. This suggests that thyrotropin acts as a competence growth factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Colletta, G -- Cirafici, A M -- Vecchio, G -- New York, N.Y. -- Science. 1986 Jul 25;233(4762):458-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3726540" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Cell Division/drug effects ; Cells, Cultured ; Cycloheximide/pharmacology ; DNA/biosynthesis ; Oncogenes/*drug effects ; Rats ; Thyroid Gland/*cytology/drug effects/metabolism ; Thyrotropin/*pharmacology
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  • 26
    Publication Date: 1986-03-14
    Description: Approximately 80 percent of all human sera that react with antigens of HTLV-III, the etiologic agent of the acquired immune deficiency syndrome (AIDS), recognize protein bands at 66 and 51 kilodaltons. A mouse hybridoma was produced that was specific to these proteins. Repeated cloning of the hybridoma did not separate the two reactivities. The p66/p51 was purified from HTLV-III lysates by immunoaffinity chromatography and subjected to NH2-terminal Edman degradation. Single amino acid residues were obtained in 17 successive degradation cycles. The sequence determined was a perfect translation of the nucleotide sequence of a portion of the HTLV-III pol gene. The purified p66/51 had reverse transcriptase activity and the monoclonal immunoglobulin G specifically removed the enzyme activity from crude viral extract as well as purified enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉di Marzo Veronese, F -- Copeland, T D -- DeVico, A L -- Rahman, R -- Oroszlan, S -- Gallo, R C -- Sarngadharan, M G -- New York, N.Y. -- Science. 1986 Mar 14;231(4743):1289-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2418504" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/immunology ; Animals ; Antibodies, Monoclonal ; Antigens, Viral/genetics/immunology/isolation & purification ; Base Sequence ; Chromatography, Affinity ; Deltaretrovirus/*enzymology/genetics/immunology ; Electrophoresis, Polyacrylamide Gel ; Genes, Viral ; Humans ; Hybridomas/immunology ; Mice ; Mice, Inbred BALB C ; RNA-Directed DNA Polymerase/genetics/*immunology/isolation & purification
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  • 27
    Publication Date: 1986-07-25
    Description: The hepatitis B virus (HBV) envelope protein carrying the surface antigen (HBsAg) is assembled with cellular lipids in mammalian cells into empty viral envelopes. In a study to evaluate the capacity of such particles to present foreign peptide sequences in a biologically active form, in-phase insertions were created in the S gene encoding the major envelope protein. One of the sequences inserted was a synthetic DNA fragment encoding a poliovirus neutralization epitope. Mammalian cells expressing the modified gene secreted hybrid particles closely resembling authentic 22-nanometer HBsAg particles. These particles reacted with a poliovirus-specific monoclonal antibody and induced neutralizing antibodies against poliovirus. The results indicate that empty viral envelopes of HBV may provide a means for the presentation of peptide sequences and for their export from mammalian cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Delpeyroux, F -- Chenciner, N -- Lim, A -- Malpiece, Y -- Blondel, B -- Crainic, R -- van der Werf, S -- Streeck, R E -- New York, N.Y. -- Science. 1986 Jul 25;233(4762):472-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2425433" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Viral/genetics/*immunology ; Epitopes/genetics/*immunology ; Genetic Engineering ; Hepatitis B Surface Antigens/genetics/*immunology ; Mice ; Neutralization Tests ; Poliovirus/*immunology ; Viral Envelope Proteins/genetics/immunology
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-03-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Easton, T A -- New York, N.Y. -- Science. 1986 Mar 14;231(4743):1235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3945820" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Homosexuality ; Humans ; Male ; *Perfume ; Rats ; *Sexual Behavior
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  • 29
    Publication Date: 1986-06-20
    Description: The hormone 17 beta-estradiol acts through its receptor system to induce MCF-7 human breast cancer cells to form tumors in athymic mice. In vitro studies have identified the production of estrogen-induced growth factors from MCF-7 cells that may have a role in growth control. These induced growth factors were sufficient to stimulate MCF-7 tumor growth in ovariectomized athymic mice, thus partially replacing estradiol. Growth factors may act as estrogen-induced "second messengers" in estrogen-responsive growth of human breast cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dickson, R B -- McManaway, M E -- Lippman, M E -- New York, N.Y. -- Science. 1986 Jun 20;232(4757):1540-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3715461" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Breast Neoplasms/*pathology ; Cell Division ; Cell Line ; Culture Media ; Estradiol/*physiology ; Female ; Humans ; Mice ; Mice, Nude ; Neoplasm Transplantation ; Ovariectomy ; Receptors, Estradiol/*physiology ; Receptors, Estrogen/*physiology ; Transplantation, Heterologous
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  • 30
    Publication Date: 1986-07-25
    Description: The H-2 histocompatibility complex of the mouse is a multigene family, some members of which are essential for the immune response to foreign antigens. The structure and organization of these genes have been established by molecular cloning, and their regulation and function is being defined by expression of the cloned genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flavell, R A -- Allen, H -- Burkly, L C -- Sherman, D H -- Waneck, G L -- Widera, G -- New York, N.Y. -- Science. 1986 Jul 25;233(4762):437-43.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3726537" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; H-2 Antigens/*genetics ; *Major Histocompatibility Complex ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Polymorphism, Genetic
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  • 31
    Publication Date: 1986-05-02
    Description: Cardiocytes in the atria contain a prohormone that gives rise to atrial natriuretic peptides (ANP's), which have intrinsic hemodynamic regulatory activity. The distribution of ANP's in the brain suggests the involvement of these peptides in central cardiovascular regulation. In conscious rats with chronic indwelling catheters, volume loading with isotonic saline or glucose increased the amount of circulating immunoreactive ANP's by a factor of 4 to 5, as determined by radioimmunoassay. Hyperosmotic challenge with a hypertonic NaCl solution or anesthesia with halothane caused similar increases in plasma ANP's. Results obtained with the denervated-heart preparation indicate that neuronal influences are important in the release of ANP's induced by volume loading. As judged from reversed-phase high-performance liquid chromatography of extracted plasma and radioimmunoassay of collected fractions, the circulating physiologically important ANP's in the conscious rodent appear to be alpha-rANP(5-28) (atriopeptin III) and either alpha-rANP(3-28) [ANF(8-33)] or alpha-rANP(1-28) (ANF).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eskay, R -- Zukowska-Grojec, Z -- Haass, M -- Dave, J R -- Zamir, N -- New York, N.Y. -- Science. 1986 May 2;232(4750):636-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2938258" target="_blank"〉PubMed〈/a〉
    Keywords: Anesthesia ; Animals ; Atrial Natriuretic Factor/blood/isolation & purification/physiology/*secretion ; Blood Volume ; Chromatography, High Pressure Liquid ; Consciousness/physiology ; Halothane/pharmacology ; Heart/innervation ; Heart Atria/drug effects/secretion ; Male ; Osmotic Pressure ; Pentobarbital/pharmacology ; Peptide Fragments/isolation & purification ; Radioimmunoassay ; Rats ; Rats, Inbred Strains
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  • 32
    Publication Date: 1986-05-16
    Description: Two human T-cell leukemias carrying a t(8;14)(q24;q11) chromosome translocation were studied for rearrangements and expression of the c-myc oncogene. For one leukemia, rearrangement was detected in a region immediately distal (3') to the c-myc locus; no rearrangements of c-myc were observed in the second case (DeF). However, studies with hybrids between human and mouse leukemic T cells indicated that in the leukemic cells of DeF, the breakpoint in chromosome 14 occurred between genes for the variable (V alpha) and the constant (C alpha) regions for the alpha chain of the T-cell receptor. The C alpha locus had translocated to a region more than 38 kilobases 3' to the involved c-myc oncogene. Since human c-myc transcripts were expressed only in hybrids carrying the 8q+ chromosome but not in hybrids containing the normal chromosome 8, it is concluded that the translocation of the C alpha locus 3' to the c-myc oncogene can result in its transcriptional deregulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erikson, J -- Finger, L -- Sun, L -- ar-Rushdi, A -- Nishikura, K -- Minowada, J -- Finan, J -- Emanuel, B S -- Nowell, P C -- Croce, C M -- CA10815/CA/NCI NIH HHS/ -- CA25875/CA/NCI NIH HHS/ -- CA39860/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 May 16;232(4752):884-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3486470" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Burkitt Lymphoma/genetics ; Chromosomes, Human, 13-15 ; Chromosomes, Human, 6-12 and X ; Humans ; Hybrid Cells ; Karyotyping ; Leukemia/*genetics ; Male ; Mice ; Middle Aged ; Nucleic Acid Hybridization ; *Oncogenes ; Receptors, Antigen, T-Cell/*genetics ; *T-Lymphocytes ; *Translocation, Genetic
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  • 33
    Publication Date: 1986-11-07
    Description: Intracellular electrical recordings in an in vitro slice preparation of the brainstem medial pontine reticular formation, a region thought to be important in mediation of desynchronized sleep phenomena, demonstrate a population of neurons that have a calcium-dependent, low threshold spike. This low threshold spike was inactivated at relatively depolarized membrane potential levels and, when this spike was deinactivated, it induced a burst of action potentials. The membrane potential dependence of the spike may underlie changes in action potential firing patterns associated with behavioral state change because the baseline membrane potential in neurons of the medial pontine reticular population depolarizes during passage from waking and slow wave sleep to desynchronized sleep, which is characterized by the absence of burst firing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greene, R W -- Haas, H L -- McCarley, R W -- MH 39,683/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1986 Nov 7;234(4777):738-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3775364" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Calcium/physiology ; Electric Stimulation ; In Vitro Techniques ; Membrane Potentials ; Pons/cytology/*physiology ; Rats
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  • 34
    Publication Date: 1986-05-16
    Description: A specific DNA probe was used to study the effect of recombinant rat, mouse, and human gamma-interferon (gamma-IFN) on the course of sporozoite-induced malaria infections. In mice and rats infected with sporozoites of Plasmodium berghei, mouse and rat gamma-IFN's strongly inhibited the development of the exoerythrocytic forms in the liver liver cells of the hosts, but not the development of the erythrocytic stages. The degree of inhibition of the exoerythrocytic forms was proportional to the dose of gamma-IFN administered, but was independent of the number of sporozoites used for challenge. A 30 percent reduction in the development of exoerythrocytic forms in rat liver was achieved when 150 units (about 15 nanograms of protein) of rat gamma-IFN were injected a few hours before sporozoite challenge; the reduction was 90 percent or more with higher doses of gamma-IFN. The effect was less pronounced if the gamma-IFN was administered 18 hours before or a few hours after challenge. Human gamma-IFN also diminished the parasitemia in chimpanzees infected with sporozoites of the human malaria parasite Plasmodium vivax. The target of gamma-IFN activity may be the infected hepatocytes themselves, as shown by in vitro experiments in which small doses of the human lymphokine inhibited the development of exoerythrocytic forms of Plasmodium berghei in a human hepatoma cell line. These results suggest that immunologically induced interferon may be involved in controlling malaria infection under natural conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferreira, A -- Schofield, L -- Enea, V -- Schellekens, H -- van der Meide, P -- Collins, W E -- Nussenzweig, R S -- Nussenzweig, V -- New York, N.Y. -- Science. 1986 May 16;232(4752):881-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3085218" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Humans ; Interferon-gamma/pharmacology/*therapeutic use ; Liver/cytology ; Malaria/*drug therapy ; Mice ; Pan troglodytes ; Plasmodium berghei/drug effects ; Plasmodium vivax/drug effects ; Toxoplasma/drug effects
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  • 35
    Publication Date: 1986-01-24
    Description: Steady-state cellular levels of phosphatidylinositol-4,5-bisphosphate (PIP2), 1,2-diacylglycerol (DAG), and inositol phosphates have been measured in two different fibroblast cell lines (NIH 3T3 and NRK cells) before and after transformation with three different ras genes. At high cell density the ratio of DAG to PIP2 was 2.5- to 3-fold higher in the ras-transformed cells than in their untransformed counterparts. The sum of the water-soluble breakdown products of the polyphosphoinositides, inositol-1,4-bisphosphate and inositol-1,4,5-trisphosphate, was also elevated in ras-transformed NRK cells compared with nontransformed NRK cells. These findings suggest that the ras (p21) protein may act by affecting these levels, possibly as a regulatory element in the PIP2 breakdown pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fleischman, L F -- Chahwala, S B -- Cantley, L -- GM 36133/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 24;231(4736):407-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3001936" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Transformation, Neoplastic/*analysis ; Diglycerides/analysis ; Humans ; Inositol 1,4,5-Trisphosphate ; Inositol Phosphates/analysis ; *Oncogenes ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositols/*analysis ; Rats
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  • 36
    Publication Date: 1986-12-05
    Description: Clonal cell lines derived from specific types of central neurons can be used to identify and characterize properties specific to those neurons. With somatic cell fusion techniques, nine clonal hybrid cell lines have been developed from the septal region of the mouse basal forebrain. Two lines express characteristics typical of cholinergic neurons--choline acetyltransferase activity and immunoreactivity, neurite formation with neurofilament protein immunoreactivity, and aggregation in rotation-mediated cell culture. These cell lines may be useful for studying the trophic interactions that support the development and maintenance of central cholinergic connections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hammond, D N -- Wainer, B H -- Tonsgard, J H -- Heller, A -- HD04583/HD/NICHD NIH HHS/ -- NS07195/NS/NINDS NIH HHS/ -- NS17661/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Dec 5;234(4781):1237-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3775382" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/cytology ; Cell Line ; Choline O-Acetyltransferase/metabolism ; Cholinergic Fibers/*physiology ; Clone Cells ; Hybrid Cells ; Mice ; Mice, Inbred C57BL ; Neuroblastoma/metabolism ; Neurons/*physiology
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  • 37
    Publication Date: 1986-05-30
    Description: Primary Sjogren's syndrome is an autoimmune disorder characterized by dryness of the mouth and eyes. The human leukocyte antigen (HLA) locus DQ is related to the primary Sjogren's syndrome autoantibodies that bind the RNA proteins Ro/SSA and La/SSB. Both DQ1 and DQ2 alleles are associated with high concentrations of these autoantibodies. An analysis of all possible combinations at DQ has shown that the entire effect was due to heterozygotes expressing the DQ1 and DQ2 alleles. These data suggest that gene interaction between DQ1 and DQ2 (or alleles at associated loci), possibly from gene complementation of trans-associated surface molecules, influences the autoimmune response in primary Sjogren's syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harley, J B -- Reichlin, M -- Arnett, F C -- Alexander, E L -- Bias, W B -- Provost, T T -- AM 31133/AM/NIADDK NIH HHS/ -- AM 34159/AM/NIADDK NIH HHS/ -- HL 30748/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 May 30;232(4754):1145-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3458307" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Autoantibodies/*biosynthesis/genetics ; HLA-DQ Antigens ; HLA-DR Antigens ; Histocompatibility Antigens Class II/*genetics/immunology ; Mice ; Sjogren's Syndrome/*genetics/immunology
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  • 38
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-05-16
    Description: A new serine protease was encoded by a clone isolated from a murine cytotoxic T-lymphocyte complementary DNA library by an RNA-hybridization competition protocol. Complementary transcripts were detected in cytotoxic T lymphocytes, spleen cells from nude mice, a rat natural killer cell leukemia, and in two of eight T-helper clones (both cytotoxic), but not in normal mouse kidney, liver, spleen, or thymus, nor in several tested T- and B-cell tumors. T-cell activation with concanavalin A plus interleukin-2 induced spleen cells to express this gene with kinetics correlating with the acquisition of cytolytic capacity. The nucleotide sequence of this gene encoded an amino acid sequence of approximately 25,700 daltons, with 25 to 35 percent identity to members of the serine protease family. The active site "charge-relay" residues (His57, Asp102, and Ser195 of the chymotrypsin numbering system) are conserved, as well as the trypsin-specific Asp (position 189 in trypsin). A Southern blot analysis indicated that this gene is conserved in humans, mouse, and chicken. This serine protease may have a role in lymphocyte lysis and a "lytic cascade."〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gershenfeld, H K -- Weissman, I L -- AI 19512/AI/NIAID NIH HHS/ -- CA09032/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 May 16;232(4752):854-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2422755" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cloning, Molecular ; Concanavalin A/pharmacology ; DNA/genetics ; Endopeptidases/*genetics ; Mice ; Mice, Inbred C57BL ; Mice, Inbred CBA ; Mice, Nude ; Nucleic Acid Hybridization ; RNA/genetics ; Serine Endopeptidases ; T-Lymphocytes, Cytotoxic/drug effects/*metabolism
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  • 39
    Publication Date: 1986-02-14
    Description: Examination of the histocompatibility region of the nonobese diabetic (NOD) mouse with antibodies against class II glycoproteins (products of immune response genes of the major histocompatibility complex I-A and I-E), hybrid T-cell clones, and mixed-lymphocyte cultures and analysis of restriction fragment length polymorphisms indicate that the NOD mouse has a unique class II major histocompatibility complex with no expression of surface I-E, no messenger RNA for I-E alpha, and an I-A not recognized by any monoclonal antibodies or hybrid T-cell clones studied. In crosses of NOD mice with control C3H mice, the development of diabetes was dependent on homozygosity for the NOD mouse's unique major histocompatibility region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hattori, M -- Buse, J B -- Jackson, R A -- Glimcher, L -- Dorf, M E -- Minami, M -- Makino, S -- Moriwaki, K -- Kuzuya, H -- Imura, H -- AM07009-01/AM/NIADDK NIH HHS/ -- AM32083-03/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Feb 14;231(4739):733-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3003909" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; DNA Restriction Enzymes/metabolism ; Diabetes Mellitus, Type 1/*genetics ; Genes, Recessive ; Genetic Linkage ; Genotype ; H-2 Antigens/genetics ; Histocompatibility Antigens Class II/*genetics ; Interleukin-2/biosynthesis ; *Major Histocompatibility Complex ; Mice ; Mice, Mutant Strains/*genetics ; Spleen/physiology
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  • 40
    Publication Date: 1986-11-14
    Description: The chromosomal localization of the genes encoding the four subunits of muscle nicotinic receptor was determined by analyzing restriction fragment length polymorphisms between two mouse species Mus musculus domesticus (DBA/2) and Mus spretus (SPE). Analysis of the progeny of the interspecies mouse backcross (DBA/2 X SPE) X DBA/2 showed that the alpha-subunit gene cosegregates with the alpha-cardiac actin gene on chromosome 17, that the beta-subunit gene is located on chromosome 11, and that the gamma- and delta-subunit genes cosegregate and are located on chromosome 1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heidmann, O -- Buonanno, A -- Geoffroy, B -- Robert, B -- Guenet, J L -- Merlie, J P -- Changeux, J P -- New York, N.Y. -- Science. 1986 Nov 14;234(4778):866-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3022377" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Animals ; *Chromosome Mapping ; Crosses, Genetic ; DNA/genetics ; DNA Restriction Enzymes ; Mice ; Mice, Inbred DBA ; Muridae ; Muscles/*analysis ; Nucleic Acid Hybridization ; Polymorphism, Genetic ; Receptors, Nicotinic/*genetics ; Species Specificity
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  • 41
    Publication Date: 1986-09-05
    Description: Damage to the vessel wall is a signal for endothelial migration and replication and for platelet release at the site of injury. Addition of transforming growth factor-beta (TGF-beta) purified from platelets to growing aortic endothelial cells inhibited [3H]thymidine incorporation in a concentration-dependent manner. A transient inhibition of DNA synthesis was also observed in response to wounding; cell migration and replication are inhibited during the first 24 hours after wounding. By 48 hours after wounding both TGF-beta-treated and -untreated cultures showed similar responses. Flow microfluorimetric analysis of cell cycle distribution indicated that after 24 hours of exposure to TGF-beta the cells were blocked from entering S phase, and the fraction of cells in G1 was increased. The inhibition of the initiation of regeneration by TGF-beta could allow time for recruitment of smooth muscle cells into the site of injury by other platelet components.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heimark, R L -- Twardzik, D R -- Schwartz, S M -- HL-18645/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 5;233(4768):1078-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3461562" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Platelets/*physiology ; Cell Cycle/drug effects ; Cell Movement/drug effects ; Cells, Cultured ; Endothelium/cytology/*physiology ; Flow Cytometry ; *Growth Inhibitors ; Humans ; In Vitro Techniques ; Peptides/*pharmacology ; Rats ; Regeneration ; Transforming Growth Factors
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-12-12
    Description: Transformation of C3H10T1/2 cells by exposure to ultraviolet (UV) irradiation followed by tetradecanoyl phorbol acetate (TPA) has been used as a model of two-stage carcinogenesis. However, cells cloned from UV-TPA-induced foci (UV-TDTx cells) had a unique phenotype. Cloned UV-TDTx cells appeared transformed in pure culture but were unable to form foci when cocultured with C3H10T1/2 cells. However, in the presence of TPA, UV-TDTx cells form foci in mixed culture with C3H10T1/2 cells. This phenotype was the only one observed for UV-TPA transformants. These data suggest that communal suppression of cell division is a discrete phenomenon that must be overcome as one step in the multistage process of transformation, and this protocol permits the routine isolation of transformed cells responsive to density-dependent growth suppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herschman, H R -- Brankow, D W -- New York, N.Y. -- Science. 1986 Dec 12;234(4782):1385-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3787250" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division ; Cell Line ; *Cell Transformation, Neoplastic/drug effects/radiation effects ; Clone Cells ; Mice ; Mice, Inbred C3H ; Phenotype ; Tetradecanoylphorbol Acetate/pharmacology ; *Ultraviolet Rays
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-04-04
    Description: Goat antibodies to idiotypes (anti-idiotypic antibodies; Ab2) that recognize an idiotype associated with the combining site of a BALB/c mouse IgG2a monoclonal antibody (Ab1) to human gastric carcinoma were used to immunize BALB/c mice and rabbits. A monoclonal anti-anti-idiotypic antibody (Ab3) of IgG1 isotype was obtained after immunization of mice. The Ab3 and the Ab1 showed identical binding specificities and bound with similar avidities to the same tumor antigen. The induction of Ab1-like Ab3 by Ab2 was not restricted to mice, since Ab3 could also be induced in rabbits. Both the mouse- and the rabbit-derived Ab3 bound the same gastrointestinal cancer-associated antigen as Ab1. These findings indicate that Ab2 induced the formation of antigen-specific Ab3, probably because it bears the internal image of the tumor-associated antigen. This Ab2 may therefore have potential for modulating the immune response of cancer patients to their tumors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herlyn, D -- Ross, A H -- Koprowski, H -- CA-10815/CA/NCI NIH HHS/ -- CA-21124/CA/NCI NIH HHS/ -- CA-33490/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 4;232(4746):100-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3952496" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibodies ; Antibodies, Monoclonal ; Antigen-Antibody Complex ; Antigens, Neoplasm/*immunology ; Female ; Goats/immunology ; Humans ; Immunoglobulin Idiotypes/*immunology ; Mice ; Mice, Inbred BALB C/immunology ; Neoplasms/immunology ; Rabbits/immunology
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-12-19
    Description: Thyroid hormones stimulate the rate of cell division by poorly understood mechanisms. The possibility that thyroid hormones increase cell growth by stimulating secretion of a growth factor was investigated. Thyroid hormones are nearly an absolute requirement for the division of GH4C1 rat pituitary tumor cells plated at low density. Conditioned media from cells grown with or without L-triiodothyronine (T3) were treated with an ion exchange resin to remove T3 and were tested for ability to stimulate the division of GH4C1 cells. Conditioned medium from T3-treated cells was as active as thyroid hormone at promoting GH4C1 cell growth but did not elicit other thyroid hormone responses, induction of growth hormone, and down-regulation of thyrotropin-releasing hormone receptors, as effectively as T3 did. A substance or substances associated with T3-induced growth stimulatory activity migrated at high molecular weight at neutral pH and was different from known growth-promoting hormones induced by T3. The results demonstrate that thyroid hormones stimulate the division of GH4C1 pituitary cells by stimulating the secretion of an autocrine growth factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hinkle, P M -- Kinsella, P A -- AM 32847/AM/NIADDK NIH HHS/ -- AM/NS 00827/AM/NIADDK NIH HHS/ -- CA 11198/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Dec 19;234(4783):1549-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3097825" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division ; Cell Line ; Epidermal Growth Factor/metabolism ; Growth Hormone/metabolism ; Growth Substances/*secretion ; Nerve Growth Factors/metabolism ; Pituitary Neoplasms/*metabolism/pathology ; Rats ; Thyrotropin-Releasing Hormone/metabolism ; Triiodothyronine/*pharmacology
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  • 45
    Publication Date: 1986-05-30
    Description: Glutamate decarboxylase (GAD; E.C. 4.1.1.15) converts glutamate to gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the vertebrate central nervous system. This report describes the isolation of a GAD complementary DNA clone by immunological screening of a lambda gt-11 brain complementary DNA expression library. The fusion protein produced by this clone catalyzes the conversion of glutamate to GABA and carbon dioxide, confirming its identity as GAD. Antibodies to beta-galactosidase remove GAD enzymatic activity from solution, showing that this activity is associated with the fusion protein. In immunoblotting experiments all three available antisera to GAD reacted with the fusion polypeptide and with two major polypeptides (molecular size, 60,000 and 66,000 daltons) in brain extracts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaufman, D L -- McGinnis, J F -- Krieger, N R -- Tobin, A J -- HD05615/HD/NICHD NIH HHS/ -- NS20356/NS/NINDS NIH HHS/ -- NS22256/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 May 30;232(4754):1138-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3518061" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*enzymology ; Cloning, Molecular ; DNA/genetics ; Escherichia coli/metabolism ; Glutamate Decarboxylase/biosynthesis/genetics/*metabolism ; Humans ; Mice ; Rats ; Recombinant Proteins/biosynthesis/metabolism ; gamma-Aminobutyric Acid/*biosynthesis
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  • 46
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-09-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kohler, G -- New York, N.Y. -- Science. 1986 Sep 19;233(4770):1281-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3092353" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/*biosynthesis/genetics/immunology ; *Antibody Diversity ; Antibody Specificity ; Cell Fusion ; Hybridomas ; Immunoglobulin Heavy Chains/immunology ; Immunoglobulin Light Chains/immunology ; Immunoglobulin Variable Region/immunology ; Immunoglobulin kappa-Chains/immunology ; Immunoglobulin mu-Chains/immunology ; Mice ; Mice, Inbred BALB C ; Mutation
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  • 47
    Publication Date: 1986-01-10
    Description: To characterize the precursor of mammalian thyrotropin-releasing hormone (TRH), a rat hypothalamic lambda gt11 library was screened with an antiserum directed against a synthetic peptide representing a portion of the rat TRH prohormone. The nucleotide sequence of the immunopositive complementary DNA encoded a protein with a molecular weight of 29,247. This protein contained five copies of the sequence Gln-His-Pro-Gly flanked by paired basic amino acids and could therefore generate five TRH molecules. In addition, potential cleavage sites in the TRH precursor could produce other non-TRH peptides, which may be secreted. In situ hybridization to rat brain sections demonstrated that the pre-proTRH complementary DNA detected neurons concentrated in the parvocellular division of the paraventricular nucleus, the same location as cells detected by immunohistochemistry. These findings indicate that mammalian TRH arises by posttranslational processing of a larger precursor protein. The ability of the TRH prohormone to generate multiple copies of the bioactive peptide may be an important mechanism in the amplification of hormone production.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lechan, R M -- Wu, P -- Jackson, I M -- Wolf, H -- Cooperman, S -- Mandel, G -- Goodman, R H -- AM 34540/AM/NIADDK NIH HHS/ -- CA 37370/CA/NCI NIH HHS/ -- P30 AM 39428/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 10;231(4734):159-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3079917" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/*physiology ; DNA/genetics ; Hypothalamus/physiology ; Molecular Weight ; Protein Precursors/genetics/*physiology ; Pyrrolidonecarboxylic Acid/analogs & derivatives ; Rats ; Rats, Inbred Strains ; Thyrotropin-Releasing Hormone/genetics/*physiology
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  • 48
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-04-25
    Description: The acoustic startle response in rats shows both short-term habituation, which recovers in seconds or minutes, and long-term habituation, which is effectively permanent. Lesions of the cerebellar vermis significantly attenuated long-term habituation without affecting the short-term process or altering initial response levels. In this response system the cerebellar vermis is part of an essential circuit for long-term habituation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leaton, R N -- Supple, W F Jr -- New York, N.Y. -- Science. 1986 Apr 25;232(4749):513-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3961494" target="_blank"〉PubMed〈/a〉
    Keywords: Acoustic Stimulation ; Animals ; Auditory Pathways/anatomy & histology/physiology ; Cerebellum/anatomy & histology/*physiology ; Habituation, Psychophysiologic/*physiology ; Male ; Rats ; Reflex, Startle/*physiology ; Reticular Formation/analysis/physiology
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  • 49
    Publication Date: 1986-02-07
    Description: In mammals different isoforms of myosin heavy chain are encoded by the members of a multigene family. The expression of each gene of this family is regulated in a tissue- and developmental stage-specific manner as well as by hormonal and various pathological stimuli. In this study the molecular basis of isoform switches induced in myosin heavy chain by thyroid hormone was investigated. The expression of the myosin heavy chain gene family was analyzed in seven different muscles of adult rats subjected to hypo- or hyperthyroidism with complementary DNA probes specific for six different myosin heavy chain genes. The results demonstrate that all six genes are responsive to thyroid hormone. More interestingly, the same myosin heavy chain gene can be regulated by thyroid hormone in highly different modes, even in opposite directions, depending on the tissue in which it is expressed. Furthermore, the skeletal embryonic and neonatal myosin heavy chain genes, so far considered specific to these two developmental stages, can be reinduced by hypothyroidism in specific adult muscles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Izumo, S -- Nadal-Ginard, B -- Mahdavi, V -- New York, N.Y. -- Science. 1986 Feb 7;231(4738):597-600.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3945800" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Diaphragm/drug effects/growth & development/metabolism ; Genes/*drug effects ; Heart/drug effects/growth & development ; Hyperthyroidism/metabolism ; Hypothyroidism/metabolism ; Male ; Muscle Development ; Muscles/drug effects/metabolism ; Myocardium/metabolism ; Myosins/*genetics ; Rats ; Thyroid Hormones/*pharmacology
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  • 50
    Publication Date: 1986-04-25
    Description: Anterior pituitaries from the dwarf mouse strain "little" did not release growth hormone or accumulate adenosine 3',5'-monophosphate (cyclic AMP) in response to human and rat growth hormone-releasing factor (GRF). Dibutyryl cyclic AMP, as well as the adenylate cyclase stimulators forskolin and cholera toxin, markedly stimulated growth hormone (GH) release. The basis of the GH deficiency in the little mouse may therefore be a defect in an early stage of GRF-stimulated GH release related either to receptor binding or to the function of the hormone-receptor complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jansson, J O -- Downs, T R -- Beamer, W G -- Frohman, L A -- AM 17947/AM/NIADDK NIH HHS/ -- AM 30667/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 25;232(4749):511-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3008329" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Colforsin/pharmacology ; Cyclic AMP/analysis ; Dwarfism, Pituitary/*physiopathology ; Female ; Growth Hormone-Releasing Hormone/metabolism/pharmacology/physiology/secretion ; Humans ; Mice ; Mice, Inbred C57BL ; Mice, Mutant Strains/*physiology ; Pituitary Gland, Anterior/analysis/drug effects/physiopathology/secretion ; Receptors, Cell Surface/metabolism/*physiology ; *Receptors, Neuropeptide ; *Receptors, Pituitary Hormone-Regulating Hormone
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  • 51
    Publication Date: 1986-10-03
    Description: The cyclosporines are a family of cyclic endecapeptides that cause a profound suppression of primary immune stimulation both in vitro and in vivo. Recently, the regulatory protein calmodulin (CaM) has been implicated as a target for cyclosporin A (CsA) binding. This study utilized two less-active isomers of CsA to evaluate the specificity and biological significance of CaM binding. The three cyclosporines exhibited equivalent in vitro binding to CaM, regardless of immunosuppressive activity. Furthermore, CaM-dependent enzyme systems were inhibited equally by active and inactive cyclosporines, but only at concentrations 100 times those necessary to block lymphocyte activation. Thus the exquisite immunosuppressive stereospecificity displayed by cyclosporine isomers is not reflected in the binding to and inhibition of CaM, suggesting that inhibition of CaM-dependent processes is not sufficient to explain the immunosuppressive activity of CsA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉LeGrue, S J -- Turner, R -- Weisbrodt, N -- Dedman, J R -- GM29323/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Oct 3;234(4772):68-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3749892" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calmodulin/antagonists & inhibitors/metabolism/*physiology ; *Cyclosporine ; Cyclosporins/metabolism/*pharmacology ; Immune Tolerance/*drug effects ; Lymphocyte Activation/drug effects ; Mice ; Muscle Contraction/drug effects ; Muscle, Smooth/drug effects ; Stereoisomerism ; Sulfonamides/pharmacology ; Trifluoperazine/pharmacology
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  • 52
    Publication Date: 1986-07-18
    Description: Addition of mouse interferon-alpha/beta (IFN) to confluent, quiescent BALB/c 3T3 (clone A31) mouse fibroblasts resulted in a block or delay in serum-induced activation of the cell cycle. It was necessary to add IFN within 6 hours after serum stimulation to inhibit nuclear labeling with [3H]thymidine. This is consistent with the time required for platelet-derived growth factor (PDGF) to induce cells to become competent to respond to additional growth factors present in platelet-poor plasma. Simultaneous addition of IFN with PDGF inhibited the PDGF-induced synthesis of a 29-kilodalton and a 35-kilodalton protein that normally occurs within 1 hour after PDGF addition. IFN also suppressed the general increase in protein synthesis that occurs by the fifth hour after PDGF addition. These results show that IFN antagonizes the action of PDGF, thereby interfering with the activation of Go cells for G1 traverse and S-phase entry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, S L -- Kikuchi, T -- Pledger, W J -- Tamm, I -- CA 18213/CA/NCI NIH HHS/ -- CA 18608/CA/NCI NIH HHS/ -- CA 42713/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Jul 18;233(4761):356-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3726533" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood ; Cell Cycle/*drug effects ; Electrophoresis, Polyacrylamide Gel ; Interferon Type I/*pharmacology ; Interphase ; Mice ; Mice, Inbred BALB C ; Molecular Weight ; Platelet-Derived Growth Factor/pharmacology ; Protein Biosynthesis ; Time Factors
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  • 53
    Publication Date: 1986-01-10
    Description: In rat hippocampal pyramidal cells tested in situ by iontophoresis of several neurotransmitters, ethanol significantly enhanced excitatory responses to acetylcholine and inhibitory responses to somatostatin-14 but had no statistically significant effect on excitatory responses to glutamate or inhibitory responses to gamma-aminobutyric acid or, in preliminary tests, to norepinephrine or serotonin. The effects of ethanol on responses to acetylcholine and somatostatin-14 may provide insight into synaptic mechanisms underlying the behavioral consequences of ethanol intoxication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mancillas, J R -- Siggins, G R -- Bloom, F E -- AA-06420/AA/NIAAA NIH HHS/ -- AM-26741/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 10;231(4734):161-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2867600" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/*pharmacology ; Action Potentials/drug effects ; Animals ; Ethanol/*pharmacology ; Goldfish ; Hippocampus/*drug effects ; Male ; Neurons/drug effects/physiology ; Norepinephrine/pharmacology ; Rats ; Rats, Inbred Strains ; Serotonin/pharmacology ; Somatostatin/*pharmacology ; Synaptic Membranes/drug effects ; gamma-Aminobutyric Acid/pharmacology
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  • 54
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-10-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1986 Oct 31;234(4776):543-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3532323" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Epidermal Growth Factor ; History, 20th Century ; Italy ; Mice ; *Nerve Growth Factors ; *Nobel Prize ; United States
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  • 55
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-05-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1986 May 16;232(4752):824-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3085217" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Deaminase/deficiency/genetics ; Animals ; Bone Marrow ; Genetic Diseases, Inborn/genetics/*therapy ; *Genetic Engineering ; Genetic Vectors ; Haplorhini ; Humans ; Mice
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  • 56
    Publication Date: 1986-12-12
    Description: The hypogonadal (hpg) mouse lacks a complete gonadotropin-releasing hormone (GnRH) gene and consequently cannot reproduce. Introduction of an intact GnRH gene into the genome of these mutant mice resulted in complete reversal of the hypogonadal phenotype. Transgenic hpg/hpg homozygotes of both sexes were capable of mating and producing offspring. Pituitary and serum concentrations of luteinizing hormone, follicle-stimulating hormone, and prolactin were restored to those of normal animals. Immunocytochemistry and in situ hybridization showed that GnRH expression was restored in the appropriate hypothalamic neurons of the transgenic hpg animals, an indication of neural-specific expression of the introduced gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mason, A J -- Pitts, S L -- Nikolics, K -- Szonyi, E -- Wilcox, J N -- Seeburg, P H -- Stewart, T A -- New York, N.Y. -- Science. 1986 Dec 12;234(4782):1372-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3097822" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Follicle Stimulating Hormone/blood ; Gene Expression Regulation ; *Genetic Engineering ; Gonadotropin-Releasing Hormone/genetics ; Histocytochemistry ; Hypogonadism/*genetics ; Hypothalamus/analysis/cytology ; Infertility/genetics/*therapy ; Luteinizing Hormone/blood ; Male ; Mice ; Mutation ; Neurons/analysis ; Phenotype ; Prolactin/blood ; Tissue Distribution
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  • 57
    Publication Date: 1986-12-12
    Description: One characteristic of the immune response during hepatitis B virus (HBV) infection in humans is the vigorous production and subsequent persistence of antibodies of immunoglobulin (Ig) classes M and G to the nucleocapsid antigen (HBcAg). In this study HBcAg was shown to be similarly immunogenic in mice. When injected into athymic (nude) B10.BR and athymic BALB/c mice, HBcAg induced IgM and IgG class antibodies to HBc in spite of the absence of T cells in nude mice. In euthymic mice, HBcAg efficiently stimulated T-cell proliferation in vitro and helper T-cell function in vivo. The dual functions of HBcAg as a T-cell-independent and a T-cell-dependent antigen may explain its enhanced immunogenicity. Denaturation of HBcAg yields a nonparticulate antigen designated HBeAg; when HBeAg was used as the immunogen, antibody production required helper T-cell function. Although HBcAg and HBeAg are serologically distinct, they are structurally related, and in these experiments were highly cross-reactive at the T-cell level. These results suggest that the elevated levels of IgM antibodies to HBc and the enhanced immunogenicity of HBcAg during HBV infection in humans reflect the ability of HBcAg to directly activate B cells to produce antibodies to HBc in the presence or absence of HBcAg- or HBeAg-sensitized T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milich, D R -- McLachlan, A -- AI00585/AI/NIAID NIH HHS/ -- AI20720/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1986 Dec 12;234(4782):1398-401.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3491425" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Capsid/*immunology ; Cross Reactions ; Hepatitis B Core Antigens/analysis ; Hepatitis B e Antigens/analysis ; Hepatitis B virus/*immunology ; Immunization ; Mice ; Mice, Inbred BALB C ; T-Lymphocytes/*immunology ; Viral Core Proteins/*immunology
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  • 58
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-09-19
    Description: Prenatal exposure to alcohol produces many developmental defects of the central nervous system, such as microcephaly, mental retardation, motor dysfunction, and cognitive deficiencies. Therefore, the generation of neurons in the cerebral cortex was examined in the offspring of female rats fed a diet containing ethanol. Prenatal exposure to ethanol delayed and extended the period during which cortical neurons were generated, reduced the number of neurons in the nature cortex with the same time of origin, and altered the distribution of neurons generated on a particular day. Thus, the proliferation and migration of cortical neurons are profoundly affected by in utero exposure to ethanol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, M W -- AA 06916/AA/NIAAA NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 19;233(4770):1308-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3749878" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cerebral Cortex/*drug effects/embryology ; Ethanol/*pharmacology ; Female ; Gestational Age ; Humans ; Motor Cortex/drug effects/embryology ; Neurons/*drug effects/embryology ; Pregnancy ; Rats
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  • 59
    Publication Date: 1986-07-11
    Description: The mechanism by which sex steroids rapidly modulate the excitability of neurons was investigated by intracellular recording of neurons in rat medial amygdala brain slices. Brief hyperpolarization and increased potassium conductance were produced by 17 beta-estradiol. This effect persisted after elimination of synaptic input and after suppression of protein synthesis. Thus, 17 beta-estradiol directly changes the ionic conductance of the postsynaptic membrane of medial amygdala neurons. In addition, a greater proportion of the neurons from females than from males responded to 17 beta-estradiol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nabekura, J -- Oomura, Y -- Minami, T -- Mizuno, Y -- Fukuda, A -- New York, N.Y. -- Science. 1986 Jul 11;233(4760):226-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3726531" target="_blank"〉PubMed〈/a〉
    Keywords: Amygdala/cytology/*drug effects ; Animals ; Cycloheximide/pharmacology ; Dactinomycin/pharmacology ; Estradiol/*pharmacology ; Female ; Male ; Membrane Potentials/drug effects ; Neurons/drug effects/physiology ; Rats ; Rats, Inbred Strains
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  • 60
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-05-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nelson, T -- Lucignani, G -- Sokoloff, L -- New York, N.Y. -- Science. 1986 May 9;232(4751):776-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3008340" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*metabolism ; Brain Chemistry ; Deoxy Sugars/*metabolism ; Deoxyglucose/*metabolism ; Glucose-6-Phosphatase/metabolism ; *Glucose-6-Phosphate/*analogs & derivatives ; Glucosephosphates/analysis ; *Magnetic Resonance Spectroscopy ; Rats
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  • 61
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-08-01
    Description: Plasmacytoma (PCT) cell lines dependent for proliferation and survival on a factor elaborated by the murine macrophage cell line, P388D1, were established in vitro. Adherent peritoneal cells induced by pristane produced 50-fold greater amounts of this activity in vitro than did resident cells. The molecules responsible for plasmacytoma growth were distinct from a number of characterized factors including interleukin-1, -2, and -3, macrophage colony-stimulating factor, B-cell stimulatory factor-1, B-cell growth factor II, epidermal growth factor, transforming growth factor-beta, and gamma- and beta-interferon, none of which were able to support the growth of the factor-dependent PCT cell lines. These results suggest that PCT growth factor may be a novel factor that has not been previously characterized and, further, that its production is associated with the pristane-induced, chronic peritoneal inflammatory response that precedes plasmacytoma formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nordan, R P -- Potter, M -- New York, N.Y. -- Science. 1986 Aug 1;233(4763):566-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3726549" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Division/drug effects ; Cell Line ; *Cell Survival/drug effects ; Growth Substances/*isolation & purification/pharmacology/physiology ; Humans ; In Vitro Techniques ; Macrophages/*physiology ; Mice ; Plasmacytoma/*physiopathology
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  • 62
    Publication Date: 1986-03-28
    Description: Transgenic mice were generated with pRSV-CAT, a chimeric gene construct containing the long terminal repeat of Rous sarcoma virus (RSV) linked to the bacterial gene encoding chloramphenicol acetyltransferase (CAT). CAT expression, detected in adult animals of five independent strains, was preferentially directed to organs rich in tendon, bone, and muscle. This pattern reflects the disease specificity of the intact virus and suggests that the tissue tropism of RSV is determined at least in part by the presence of endogenous tissue-specific factors that can promote expression of genetic information linked to the long terminal repeat. In two of the mouse strains, insertion of the pRSV-CAT DNA resulted in developmental abnormalities. One of these strains was characterized by a dominant trait of embryonic lethality, the other by a recessive trait of fused toes in all four feet.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Overbeek, P A -- Lai, S P -- Van Quill, K R -- Westphal, H -- New York, N.Y. -- Science. 1986 Mar 28;231(4745):1574-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3006249" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/genetics ; Age Factors ; Animals ; Avian Sarcoma Viruses/*genetics ; Chloramphenicol O-Acetyltransferase ; DNA, Viral/*genetics ; Gene Expression Regulation ; Genes, Regulator ; Limb Deformities, Congenital ; Mice ; Repetitive Sequences, Nucleic Acid ; Tissue Distribution ; Transcription, Genetic ; Transfection
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  • 63
    Publication Date: 1986-07-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paul, S M -- Schwartz, R D -- Creveling, C R -- Hollingsworth, E B -- Daly, J W -- Skolnick, P -- New York, N.Y. -- Science. 1986 Jul 11;233(4760):228-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014649" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport ; Brain/*metabolism ; Cell Membrane/metabolism/*physiology ; Chick Embryo ; Chlorides/*metabolism ; Guinea Pigs ; Mice ; Rats ; Receptors, GABA-A/metabolism/*physiology ; Synaptosomes/metabolism
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  • 64
    Publication Date: 1986-05-16
    Description: Interleukin-1 (IL-1) is a product of mononuclear phagocytes that mediates changes characteristic of the response to inflammation or tissue injury (the acute-phase response). One of two structurally and functionally homologous major histocompatibility complex (MHC) class III genes encodes a positive acute-phase protein, complement factor B. The closely linked complement C2 gene is not affected during the acute-phase response. Purified human IL-1, pH 7.0, and recombinant-generated murine IL-1, pH 5.0, increased the expression of factor B and other positive acute-phase proteins in human hepatoma cells but decreased the expression of albumin, a negative acute-phase reactant. Furthermore, in a murine fibroblast L-cell line transfected with cosmid DNA bearing the human C2 and factor B genes, IL-1 mediated a reversible dose- and time-dependent increase in factor B expression in the transfected cells. Expression of the C2 gene was not affected by IL-1. The effect of IL-1 on factor B expression involves a mechanism acting at a pre-translational level as demonstrated by an increase in specific messenger RNA content and a corresponding increase in biosynthesis and secretion of factor B. The structural basis and mechanism for selective and independent regulation of these genes provides insight into the molecular control of the inflammatory response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perlmutter, D H -- Goldberger, G -- Dinarello, C A -- Mizel, S B -- Colten, H R -- AI20032/AI/NIAID NIH HHS/ -- GM33293/GM/NIGMS NIH HHS/ -- HD17461/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 May 16;232(4752):850-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3010455" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carcinoma, Hepatocellular/metabolism ; Electrophoresis, Polyacrylamide Gel ; Fibroblasts/metabolism ; Gene Expression Regulation/drug effects ; Humans ; Interleukin-1/*pharmacology ; Liver Neoplasms/metabolism ; Major Histocompatibility Complex/*drug effects ; Mice
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  • 65
    Publication Date: 1986-10-10
    Description: Biological and serological assays have been used to define four subregions for the I region of the major histocompatibility complex (MHC) in the order I-A, I-B, I-J, and I-E. The I-J subregion presumably encodes the I-J polypeptide of the elusive T-cell suppressor factors. Restriction enzyme site polymorphisms and DNA sequence analyses of the I region from four recombinant mouse strains were used to localize the putative I-B and I-J subregions to a 1.0-kilobase (kb) region within the E beta gene. Sequencing this region from E beta clones derived from the two mouse strains: B10.A(3R), I-Jb and B10.A(5R), I-Jk initially used to define the I-J subregion revealed that these regions are identical, hence the distinct I-Jb and I-Jk molecules cannot be encoded by this DNA. In addition, the DNA sequence data also refute the earlier mapping of the I-B subregion. Analysis of the DNA sequences of three parental and four I region recombinants reveals that the recombinant events in three of the recombinant strains occurred within a 1-kb region of DNA, supporting the proposition that a hotspot for recombination exists in the I region. The only striking feature of this hotspot is a tetramer repeat (AGGC)n that shows 80 percent homology to the minisatellite sequence which may facilitate recombination in human chromosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kobori, J A -- Strauss, E -- Minard, K -- Hood, L -- New York, N.Y. -- Science. 1986 Oct 10;234(4773):173-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3018929" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA Restriction Enzymes ; Genes, MHC Class II ; *Major Histocompatibility Complex ; Mice ; *Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; Suppressor Factors, Immunologic/genetics
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  • 66
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-11-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G -- New York, N.Y. -- Science. 1986 Nov 28;234(4780):1076-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3775376" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; H-Y Antigen/genetics ; Humans ; Lizards ; Male ; Mice ; *Sex Determination Analysis ; *Y Chromosome
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  • 67
    Publication Date: 1986-01-10
    Description: Antibodies were raised in mice immunized with several recombinant and synthetic peptides of the circumsporozoite protein of Plasmodium falciparum. The antibodies were evaluated for protective activity in a human hepatocyte culture system. They exerted their protective effect against the parasite at three points: sporozoite attachment to the hepatocyte surface, entry, and subsequent intracellular development. Inhibition of attachment and entry were found to be related to the antibody titer against the authentic circumsporozoite protein on the sporozoite surface, especially when peptides were administered with alum or complete Freund's adjuvant. Even when invasion was not totally inhibited, the presence of abnormal trophozoites and a frequent inhibition of schizont development in long-term cultures suggested continued activity of antibodies at the intracellular level after sporozoite penetration had been completed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mazier, D -- Mellouk, S -- Beaudoin, R L -- Texier, B -- Druilhe, P -- Hockmeyer, W -- Trosper, J -- Paul, C -- Charoenvit, Y -- Young, J -- New York, N.Y. -- Science. 1986 Jan 10;231(4734):156-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3510455" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/*immunology ; Antigens, Protozoan/*immunology ; Fluorescent Antibody Technique ; Humans ; In Vitro Techniques ; Liver/cytology/parasitology ; Mice ; Peptides/immunology ; Plasmodium falciparum/*immunology ; Recombinant Proteins/immunology
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  • 68
    Publication Date: 1986-11-28
    Description: The bombesin-like peptides are potent mitogens for Swiss 3T3 fibroblasts, human bronchial epithelial cells, and cells isolated from small cell carcinoma of the lung. The mechanism of signal transduction in the proliferative response to bombesin was investigated by studying the effect of Bordetella pertussis toxin on bombesin-stimulated mitogenesis. At nanomolar concentrations, bombesin increased levels of c-myc messenger RNA and stimulated DNA synthesis in Swiss 3T3 cells. Treatment of the cells with pertussis toxin (5 nanograms per milliliter) completely blocked bombesin-enhanced c-myc expression and eliminated bombesin-stimulated DNA synthesis. This treatment had essentially no effect on the mitogenic responses to either platelet-derived growth factor or phorbol 12,13-dibutyrate. These results suggest that the mitogenic actions of bombesin-like growth factors are mediated through a pertussis toxin-sensitive guanine nucleotide-binding protein. Furthermore they indicate that bombesin-like growth factors act through pathways that are different from those activated by platelet-derived growth factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Letterio, J J -- Coughlin, S R -- Williams, L T -- R01 HL 32898/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Nov 28;234(4780):1117-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3465038" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bombesin/*pharmacology ; Cells, Cultured ; DNA, Neoplasm/*biosynthesis ; Humans ; Mice ; Oncogenes/*drug effects ; *Pertussis Toxin ; Phorbol 12,13-Dibutyrate ; Phorbol Esters/pharmacology ; Platelet-Derived Growth Factor/pharmacology ; Virulence Factors, Bordetella/*pharmacology
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  • 69
    Publication Date: 1986-03-14
    Description: Human malignant melanoma cells express specific chondroitin sulfate proteoglycans (mel-CSPG) on the surface, both in vivo and in vitro. Melanocytes in normal skin show no detectable mel-CSPG but can be induced to express the antigen when cultured in the presence of cholera toxin and the tumor promoter 12-O-tetradecanoylphorbol-13-acetate. Most other cell types do not express mel-CSPG either in vivo or in vitro. A study was designed to examine regulatory signals controlling mel-CSPG expression. The gene encoding mel-CSPG was mapped to human chromosome 15, and this chromosome was introduced into rodent cells derived from distinct differentiation lineages. Three types of mel-CSPG--expressing hybrids were found: (i) hybrids derived from human melanomas; (ii) hybrids derived from human cells that do not express mel-CSPG; and (iii) hybrids derived from human cells expressing mel-CSPG that are antigen-negative but that are induced to express mel-CSPG when cultured on extracellular matrix instead of plastic surfaces. Thus, mel-CSPG expression can be controlled both through intrinsic signals, provided by the differentiation program of the rodent fusion partner, and through extrinsic signals, provided by specific cell-matrix interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rettig, W J -- Real, F X -- Spengler, B A -- Biedler, J L -- Old, L J -- CA-08748/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Mar 14;231(4743):1281-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3633135" target="_blank"〉PubMed〈/a〉
    Keywords: Aggrecans ; Animals ; Antibodies, Monoclonal ; Cell Line ; Cholera Toxin/pharmacology ; Chromosome Mapping ; Chromosomes, Human, 13-15 ; Cricetinae ; Cricetulus ; *Extracellular Matrix Proteins ; Gene Expression Regulation/drug effects ; Glycoproteins/*biosynthesis/genetics ; Humans ; Hybrid Cells/drug effects/*metabolism ; Lectins, C-Type ; Lymphocytes/metabolism ; Melanocytes/drug effects/metabolism ; Melanoma/*metabolism ; Mice ; Neoplasm Proteins/*biosynthesis/genetics ; Neuroblastoma/metabolism ; *Proteoglycans ; Rats ; Tetradecanoylphorbol Acetate/pharmacology
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  • 70
    Publication Date: 1986-07-25
    Description: Bovine papillomavirus (BPV-1) contains two independent transforming genes that have been mapped to the E5 and E6 open reading frames (ORF's). The E5 transforming protein was identified by means of an antiserum against a synthetic peptide corresponding to the 20 COOH-terminal amino acids of the E5 ORF. The E5 polypeptide is the smallest viral transforming protein yet characterized; it had an apparent size of 7 kilodaltons. The transforming polypeptide is encoded entirely within the second half of the E5 ORF and its predicted amino acid composition is very unusual; 68% of the amino acids are strongly hydrophobic and 34% are leucine. Cell fractionation studies localized this polypeptide predominantly to cellular membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schlegel, R -- Wade-Glass, M -- Rabson, M S -- Yang, Y C -- New York, N.Y. -- Science. 1986 Jul 25;233(4762):464-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014660" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bovine papillomavirus 1/*genetics ; Cell Line ; Cell Transformation, Viral ; *Genes, Viral ; Mice ; Oncogene Proteins, Viral/*genetics ; Papillomaviridae/*genetics
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  • 71
    Publication Date: 1986-06-13
    Description: Tissue welding is a potentially important biomedical application of laser technology. The structural alterations basic to this phenomenon were studied in experimental repair of lesions of the rat carotid artery and sciatic nerve. A modified neodymiumdoped yttrium-aluminum-garnet laser operating at a wavelength of 1.319 micrometers was used in conjunction with conventional suture techniques. Histological and fine-structural analysis revealed a homogenizing change in collagen with interdigitation of altered individual fibrils that appeared to be the structural basis of the welding effect.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schober, R -- Ulrich, F -- Sander, T -- Durselen, H -- Hessel, S -- New York, N.Y. -- Science. 1986 Jun 13;232(4756):1421-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3715454" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carotid Arteries/*radiation effects ; *Collagen ; Dose-Response Relationship, Radiation ; Extracellular Matrix/radiation effects ; *Lasers ; Rats ; Sciatic Nerve/*radiation effects
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  • 72
    Publication Date: 1986-02-07
    Description: In the adult castrated male rat, exposure to inescapable, intermittent electroshocks inhibited the pulsatile pattern of luteinizing hormone release and markedly lowered its plasma concentrations. The central administration of the corticotropin-releasing factor (CRF) antagonist alpha-helical ovine CRF residues 9 to 41 reversed the inhibitory action of stress. Neither its peripheral injection, nor the intraventricular injection of the inactive CRF analog des-Glu to Arg ovine CRF was effective. These results suggest that endogenous CRF may mediate some deleterious effects of noxious stimuli on reproduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rivier, C -- Rivier, J -- Vale, W -- AA03504/AA/NIAAA NIH HHS/ -- AM26741/AM/NIADDK NIH HHS/ -- HD13527/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1986 Feb 7;231(4738):607-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3003907" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenocorticotropic Hormone/physiology ; Animals ; Corticotropin-Releasing Hormone/pharmacology/*physiology ; Electroshock ; Female ; Humans ; Luteinizing Hormone/blood ; Male ; Orchiectomy ; Rats ; *Reproduction/drug effects ; Stress, Psychological/*physiopathology
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  • 73
    Publication Date: 1986-02-21
    Description: A 4-week assay for screening tumor promoters of bladder cancer has been developed in which increased agglutinability of isolated rat bladder cells with concanavalin A is used as an indicator. On the basis of this assay system, L-isoleucine and L-leucine were suspected of being possible tumor promoters. Results of 40- to 60-week carcinogenesis experiments in which N-butyl-N-(4-hydroxybutyl)nitrosamine was used as an initiator demonstrate that L-isoleucine and L-leucine promote bladder cancer in rats. This finding may be relevant to the high incidence of human bladder cancer in Western countries, where the diet is rich in protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nishio, Y -- Kakizoe, T -- Ohtani, M -- Sato, S -- Sugimura, T -- Fukushima, S -- New York, N.Y. -- Science. 1986 Feb 21;231(4740):843-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3945812" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Carcinogens ; Carcinoma/*chemically induced ; *Isoleucine ; *Leucine ; Papilloma/*chemically induced ; Precancerous Conditions/*chemically induced ; Rats ; Rats, Inbred F344 ; Urinary Bladder Neoplasms/*chemically induced
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  • 74
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-07-18
    Description: Protein kinase C, an enzyme that is activated by the receptor-mediated hydrolysis of inositol phospholipids, relays information in the form of a variety of extracellular signals across the membrane to regulate many Ca2+-dependent processes. At an early phase of cellular responses, the enzyme appears to have a dual effect, providing positive forward as well as negative feedback controls over various steps of its own and other signaling pathways, such as the receptors that are coupled to inositol phospholipid hydrolysis and those of some growth factors. In biological systems, a positive signal is frequently followed by immediate negative feedback regulation. Such a novel role of this protein kinase system seems to give a logical basis for clarifying the biochemical mechanism of signal transduction, and to add a new dimension essential to our understanding of cell-to-cell communication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nishizuka, Y -- New York, N.Y. -- Science. 1986 Jul 18;233(4761):305-12.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014651" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Animals ; Blood Platelets/metabolism ; Calcimycin/pharmacology ; Calcium-Transporting ATPases/metabolism ; Carrier Proteins/metabolism ; *Cation Transport Proteins ; Cell Membrane/physiology ; Cyclic AMP/metabolism ; Diglycerides/metabolism ; Electric Conductivity ; Enzyme Activation ; Fluorescent Antibody Technique ; Isoenzymes/metabolism ; Models, Biological ; Phosphatidylinositols/*metabolism ; Potassium/metabolism ; Protein Kinase C/*metabolism ; Purkinje Cells/enzymology ; Rats ; Serotonin/blood ; Sodium/metabolism ; Sodium-Hydrogen Antiporter ; Tetradecanoylphorbol Acetate/pharmacology ; Time Factors
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  • 75
    Publication Date: 1986-06-13
    Description: Almost all B cells in autoimmune mice with the viable motheaten (mev) mutation express the Ly-1 cell surface antigen, which marks a minor population of B cells constituting a separate lineage in normal mice. Immunoglobulins primarily of the M and G3 classes, which in both normal and mev mice contain high levels of lambda light chain, are produced in excess in mev mice. These and other observations suggest that the development of B cells that express Ly-1 is regulated independently from the development of B cells that do not express Ly-1. B cells bearing the Ly-1 surface antigen may play specialized roles in the normal immune system and in autoimmunity by regulating other B cells via lymphokines, by producing antibodies to self and certain foreign antigens, and by preferentially secreting immunoglobulin M and immunoglobulin G3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sidman, C L -- Shultz, L D -- Hardy, R R -- Hayakawa, K -- Herzenberg, L A -- AI-20232/AI/NIAID NIH HHS/ -- CA-20408/CA/NCI NIH HHS/ -- CA-35845/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Jun 13;232(4756):1423-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3487115" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Ly/*immunology ; Autoimmune Diseases/genetics/*immunology ; B-Lymphocytes/classification/*immunology ; Flow Cytometry ; Immunoglobulin D/metabolism ; Immunoglobulin G/metabolism ; Immunoglobulin M/metabolism ; Immunoglobulins/analysis ; Lymph Nodes/cytology ; Mice ; Mice, Mutant Strains/*immunology ; Peritoneal Cavity/cytology ; Spleen/cytology
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  • 76
    Publication Date: 1986-02-14
    Description: While assessing a potential role of adrenal glands in the production of the hitherto unidentified puberty-delaying pheromone of female mice, the urinary volatile profiles of normal and adrenalectomized animals were quantitatively compared. Six components, whose concentrations were depressed after adrenalectomy, were identified: 2-heptanone, trans-5-hepten-2-one, trans-4-hepten-2-one, n-pentyl acetate, cis-2-penten-1-yl acetate, and 2,5-dimethylpyrazine. When these laboratory-synthesized chemicals were added (in their natural concentrations) to either previously inactive urine from adrenalectomized females or plain water, the biological activity was fully restored.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Novotny, M -- Jemiolo, B -- Harvey, S -- Wiesler, D -- Marchlewska-Koj, A -- New York, N.Y. -- Science. 1986 Feb 14;231(4739):722-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3945805" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Glands/*physiology ; Animals ; Female ; Ketones/urine ; Mice ; Ovary/physiology ; Pentanols/urine ; Pheromones/physiology/urine ; Pyrazines/urine ; *Sexual Maturation
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  • 77
    Publication Date: 1986-08-08
    Description: The MH-3 gene, which contains a homeo box that is expressed specifically in the adult testis, was identified and mapped to mouse chromosome 6. By means of in situ hybridization with adult testis sections and Northern blot hybridization with testis RNA from prepuberal mice and from Sl/Sld mutant mice, it was demonstrated that this gene is expressed in male germ cells during late meiosis. In the embryo, MH-3 transcripts were present at day 11.5 post coitum, a stage in mouse development when gonadal differentiation has not yet occurred. The MH-3 gene may have functions in spermatogenesis and embryogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rubin, M R -- Toth, L E -- Patel, M D -- D'Eustachio, P -- Nguyen-Huu, M C -- New York, N.Y. -- Science. 1986 Aug 8;233(4764):663-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3726554" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA/genetics ; Drosophila ; Embryo, Mammalian/*metabolism ; *Embryo, Nonmammalian ; *Genes ; Male ; Mice ; Morphogenesis ; Mutation ; Nucleic Acid Hybridization ; Sequence Homology, Nucleic Acid ; Spermatocytes/*metabolism ; Spermatogenesis
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  • 78
    Publication Date: 1986-09-05
    Description: The oral administration of peptide drugs is well known to be precluded by their digestion in the stomach and small intestine. As a new approach to oral delivery, peptide drugs were coated with polymers cross-linked with azoaromatic groups to form an impervious film to protect orally administered drugs from digestion in the stomach and small intestine. When the azopolymer-coated drug reached the large intestine, the indigenous microflora reduced the azo bonds, broke the cross-links, and degraded the polymer film, thereby releasing the drug into the lumen of the colon for local action or for absorption. The ability of the azopolymer coating to protect and deliver orally administered peptide drugs was demonstrated in rats with the peptide hormones vasopressin and insulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saffran, M -- Kumar, G S -- Savariar, C -- Burnham, J C -- Williams, F -- Neckers, D C -- AI 18710/AI/NIAID NIH HHS/ -- SO-7-RR05700-15/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 5;233(4768):1081-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3526553" target="_blank"〉PubMed〈/a〉
    Keywords: Administration, Oral ; Animals ; Azo Compounds ; Blood Glucose/metabolism ; Diabetes Mellitus, Experimental/drug therapy ; Enterobacteriaceae/metabolism ; Insulin/*administration & dosage ; Lypressin/administration & dosage ; Peptides/*administration & dosage ; Polymers ; Rats ; *Tablets, Enteric-Coated
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  • 79
    Publication Date: 1986-08-01
    Description: Transforming growth factor-beta (TGF-beta) is a multifunctional peptide that controls proliferation, differentiation, and other functions in many cell types. Many cells synthesize TGF-beta and essentially all of them have specific receptors for this peptide. TGF-beta regulates the actions of many other peptide growth factors and determines a positive or negative direction of their effects. Its marked ability to enhance formation of connective tissue in vivo suggests several therapeutic applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sporn, M B -- Roberts, A B -- Wakefield, L M -- Assoian, R K -- New York, N.Y. -- Science. 1986 Aug 1;233(4763):532-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3487831" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division/drug effects ; Epidermal Growth Factor/metabolism ; Genes ; Humans ; Peptides/genetics/metabolism/pharmacology/*physiology ; Platelet-Derived Growth Factor/pharmacology ; Rats ; Transforming Growth Factors
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  • 80
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-06-27
    Description: Recent studies of animals with complex nervous systems, including humans and other primates, have improved our understanding of how the brain accomplishes learning and memory. Major themes of recent work include the locus of memory storage, the taxonomy of memory, the distinction between declarative and procedural knowledge, and the question of how memory changes with time, that is, the concepts of forgetting and consolidation. An important recent advance is the development of an animal model of human amnesia in the monkey. The animal model, together with newly available neuropathological information from a well-studied human patient, has permitted the identification of brain structures and connections involved in memory functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Squire, L R -- MH24600/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1986 Jun 27;232(4758):1612-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3086978" target="_blank"〉PubMed〈/a〉
    Keywords: Alcohol Amnestic Disorder/physiopathology ; Amnesia/physiopathology ; Amnesia, Retrograde/physiopathology ; Amygdala/physiology ; Animals ; Brain/physiology/physiopathology ; Electroconvulsive Therapy ; Haplorhini ; Hippocampus/physiology ; Humans ; Learning/physiology ; Memory/*physiology ; Memory Disorders/physiopathology ; Memory, Short-Term/physiology ; Mice ; Models, Neurological ; Retention (Psychology)/physiology
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  • 81
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-05-16
    Description: The adrenergic control of glucose homeostasis is mediated in part through variations in the release of pancreatic hormones. In this study, purified pancreatic A and B cells were used to identify the recognition and messenger units involved in the adrenergic regulation of glucagon and insulin release. Catecholamines induced beta-adrenergic receptor activity in A cells and alpha 2-adrenergic receptor activity in B cells. The two recognition units provoked opposite variations in the production of cellular cyclic adenosine monophosphate, the beta-adrenergic unit enhancing the nucleotide's permissive effect on amino acid-induced glucagon release and the alpha 2-adrenergic unit inhibiting that upon glucose-induced insulin release. In both cell types, catecholamines interact powerfully with the synergistic control of hormone release by nutrient- and (neuro)hormone-driven messenger systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schuit, F C -- Pipeleers, D G -- New York, N.Y. -- Science. 1986 May 16;232(4752):875-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2871625" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic beta-Agonists/pharmacology ; Adrenergic beta-Antagonists/pharmacology ; Animals ; Cyclic AMP/analysis ; Epinephrine/pharmacology ; Glucagon/secretion ; Insulin/secretion ; Islets of Langerhans/analysis/drug effects/*physiology ; Male ; Rats ; Rats, Inbred Strains ; Receptors, Adrenergic, beta/drug effects/*physiology
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  • 82
    Publication Date: 1986-04-11
    Description: Second-passage rat embryo cells were transfected with a neomycin resistance gene and the activated form of the c-Ha-ras I gene, or with these two genes plus the adenovirus type 2 E1a gene. Foci of morphologically transformed cells were observed in both cases; however, the frequency of transformation was at least ten times higher with two oncogenes than with the ras gene alone. All the transformed cell lines gave rise to rapidly growing tumors when injected subcutaneously into nude mice. All but one of the cell lines transformed by the ras oncogene alone formed metastatic nodules in the lungs of animals that had been injected subcutaneously with transformed cells. When transformed cells were injected intravenously, all the ras single-gene transformants gave rise to many metastatic lung nodules. In contrast, cell lines transformed with ras and E1a did not generate metastases after subcutaneous injection and gave rise to very few metastatic lung nodules after intravenous injection. These data demonstrate that a fully malignant cell with metastatic potential, as measured in an immunodeficient animal, can be obtained from early passage embryo cells by the transfection of the ras oncogene alone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pozzatti, R -- Muschel, R -- Williams, J -- Padmanabhan, R -- Howard, B -- Liotta, L -- Khoury, G -- 3F32CA07245-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 11;232(4747):223-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3456644" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carcinoma/genetics ; Cell Line ; Cell Transformation, Neoplastic/*metabolism ; Cricetinae ; Genetic Engineering ; Mice ; Mice, Nude ; *Oncogenes ; Plasmids ; Rats/embryology ; Rats, Inbred Strains/embryology ; Transfection ; Urinary Bladder Neoplasms/genetics
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  • 83
    Publication Date: 1986-12-05
    Description: Ethanol, at pharmacologically relevant concentrations of 20 to 100 mM, stimulates gamma-aminobutyric (GABA) receptor-mediated uptake of 36Cl-labeled chlorine into isolated brain vesicles. One drug that acts at GABA-benzodiazepine receptors, the imidazobenzodiazepine Ro15-4513, has been found to be a potent antagonist of ethanol-stimulated 36Cl- uptake into brain vesicles, but it fails to antagonize either pentobarbital- or muscimol-stimulated 36Cl- uptake. Pretreatment of rats with Ro15-4513 blocks the anticonflict activity of low doses of ethanol (but not pentobarbital) as well as the behavioral intoxication observed with higher doses of ethanol. The effects of Ro15-4513 in antagonizing ethanol-stimulated 36Cl- uptake and behavior are completely blocked by benzodiazepine receptor antagonists. However, other benzodiazepine receptor inverse agonists fail to antagonize the actions of ethanol in vitro or in vivo, suggesting a novel interaction of Ro15-4513 with the GABA receptor-coupled chloride ion channel complex. The identification of a selective benzodiazepine antagonist of ethanol-stimulated 36Cl- uptake in vitro that blocks the anxiolytic and intoxicating actions of ethanol suggests that many of the neuropharmacologic actions of ethanol may be mediated via central GABA receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Suzdak, P D -- Glowa, J R -- Crawley, J N -- Schwartz, R D -- Skolnick, P -- Paul, S M -- New York, N.Y. -- Science. 1986 Dec 5;234(4781):1243-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3022383" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anxiety/drug effects ; Azides/*pharmacology ; Benzodiazepines/*pharmacology ; Chlorides/metabolism ; Ethanol/*antagonists & inhibitors ; Flumazenil/pharmacology ; Male ; Pyrazoles/pharmacology ; Rats ; Rats, Inbred Strains ; Receptors, GABA-A/drug effects ; Synaptosomes/drug effects
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  • 84
    Publication Date: 1986-06-27
    Description: The posttranslational maturation of a complex precursor polyprotein, human proenkephalin, was assessed by infection of a wide spectrum of cell types with a recombinant vaccinia virus that expressed human proenkephalin. The infected cells rapidly produced both cellular and secreted Met-enkephalin immunoreactivity. Although each cell line could secrete intact proenkephalin, only a mouse pituitary line was capable of processing proenkephalin to mature enkephalin peptides. The quantity of intact proenkephalin secreted from BSC-40 cells (derived from African Green monkey kidney) was sufficient to establish the value of vaccinia virus as a mammalian cell expression vector.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thomas, G -- Herbert, E -- Hruby, D E -- 7 RO1 DA04154-01/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1986 Jun 27;232(4758):1641-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3754979" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cercopithecus aethiops ; Enkephalin, Methionine/biosynthesis ; Enkephalins/*biosynthesis/genetics ; Genetic Vectors ; Humans ; Mice ; Protein Precursors/*biosynthesis/genetics ; Rats ; Recombinant Proteins/*biosynthesis ; Vaccinia virus/*genetics
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  • 85
    Publication Date: 1986-10-24
    Description: Cachectin (tumor necrosis factor), a protein produced in large quantities by endotoxin-activated macrophages, has been implicated as an important mediator of the lethal effect of endotoxin. Recombinant human cachectin was infused into rats in an effort to determine whether cachectin, by itself, can elicit the derangements of host physiology caused by administration of endotoxin. When administered in quantities similar to those produced endogenously in response to endotoxin, cachectin causes hypotension, metabolic acidosis, hemoconcentration, and death within minutes to hours, as a result of respiratory arrest. Hyperglycemia and hyperkalemia were also observed after infusion. At necropsy, diffuse pulmonary inflammation and hemorrhage were apparent on gross and histopathologic examination, along with ischemic and hemorrhagic lesions of the gastrointestinal tract, and acute renal tubular necrosis. Thus, it appears that a single protein mediator (cachectin) is capable of inducing many of the deleterious effects of endotoxin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tracey, K J -- Beutler, B -- Lowry, S F -- Merryweather, J -- Wolpe, S -- Milsark, I W -- Hariri, R J -- Fahey, T J 3rd -- Zentella, A -- Albert, J D -- New York, N.Y. -- Science. 1986 Oct 24;234(4775):470-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3764421" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Glucose/metabolism ; Endotoxins/toxicity ; Female ; Glycoproteins/*toxicity ; Humans ; Potassium/blood ; Rats ; Recombinant Proteins ; Shock/*chemically induced/pathology/physiopathology ; Sodium/blood ; Tumor Necrosis Factor-alpha
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  • 86
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-09-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sun, M -- New York, N.Y. -- Science. 1986 Sep 12;233(4769):1143-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3738527" target="_blank"〉PubMed〈/a〉
    Keywords: Acetamides/*adverse effects ; Animals ; *Government Agencies ; Herbicides/*adverse effects ; Humans ; Neoplasms/chemically induced ; Rats ; United States ; *United States Environmental Protection Agency
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  • 87
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-06-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wehrenberg, W B -- Ehlers, C L -- New York, N.Y. -- Science. 1986 Jun 6;232(4755):1271-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3085220" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arousal/drug effects ; Brain/*drug effects ; Electroencephalography ; Growth Hormone/blood ; Growth Hormone-Releasing Hormone/administration & dosage/*pharmacology ; Injections, Intraventricular ; Motor Activity/drug effects ; Rats
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  • 88
    Publication Date: 1986-10-31
    Description: T lymphocytes express on their surface not only a specific receptor for antigen and major histocompatibility complex proteins, but also a number of additional glycoproteins that are thought to play accessory roles in the processes of recognition and signal transduction. L3T4 is one such T-cell surface protein that is expressed on most mouse thymocytes and on mature mouse T cells that recognize class II (Ia) major histocompatibility complex proteins. Such cells are predominantly of the helper/inducer phenotype. In this study, complementary DNA clones encoding L3T4 were isolated and sequenced. The predicted protein sequence shows that L3T4 is a member of the immunoglobulin gene superfamily. It is encoded by a single gene that does not require rearrangement prior to expression. Although the protein has not previously been demonstrated on nonhematopoietic cells, two messenger RNA species specific for L3T4 are found in brain. The minor species comigrates with the L3T4 transcript in T cells, whereas the major species is 1 kilobase smaller.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tourvieille, B -- Gorman, S D -- Field, E H -- Hunkapiller, T -- Parnes, J R -- 1 F32 CA07877-01/CA/NCI NIH HHS/ -- AI11313/AI/NIAID NIH HHS/ -- GM34991/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Oct 31;234(4776):610-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3094146" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Differentiation, T-Lymphocyte ; Antigens, Surface/genetics/*isolation & purification ; Base Sequence ; Brain/*metabolism ; Cloning, Molecular ; DNA/genetics/isolation & purification ; Humans ; Mice ; Mice, Inbred C57BL ; Nucleic Acid Hybridization ; RNA, Messenger/genetics ; Sequence Homology, Nucleic Acid ; T-Lymphocytes/*immunology/metabolism
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  • 89
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-10-17
    Description: Human interferon stimulates a transient two- to threefold increase in the concentration of diacylglycerol and inositol tris-phosphate within 15 to 30 seconds of cell exposure to interferon. Antibodies to interferon inhibit this effect. The stimulation was measurable in isolated cell membranes exposed to interferon. Human alpha and beta, but not gamma, interferon stimulate this increase in cells containing the appropriate interferon receptor. The effect was proportional to the number of interferon receptors. Both the diacylglycerol increase and antiviral effects induced by interferon could be correlated in terms of dose dependence. Thus, a transient diacylglycerol increase is an early event in the interferon-induced transmembrane signaling process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yap, W H -- Teo, T S -- Tan, Y H -- New York, N.Y. -- Science. 1986 Oct 17;234(4774):355-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2429366" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Communication ; Cell Membrane/drug effects ; Diglycerides/analysis ; Dose-Response Relationship, Drug ; Fibroblasts/analysis/drug effects ; Humans ; Inositol 1,4,5-Trisphosphate ; Inositol Phosphates/analysis ; Interferon Type I/pharmacology ; Interferon-gamma/pharmacology ; Interferons/*pharmacology/physiology ; Mice ; Receptors, Immunologic/metabolism ; Receptors, Interferon
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  • 90
    Publication Date: 1986-04-11
    Description: Serum amyloid A protein (SAA) is a precursor for a major component of amyloid fibrils, which, upon deposition, cause secondary amyloidosis in diseases such as rheumatoid arthritis. In mice, SAA is encoded by at least three genes, which show diverse expression during inflammation. Furthermore, in amyloidosis-resistant SJL mice, the gene expression for one SAA isotype, SAA2, is defective, although SAA2 gene expression is normal in amyloidosis-susceptible BALB/c mice. Because only SAA2-derived products deposit in mouse amyloid tissues, the resistance of SJL mice to amyloidosis seems to be due to defective SAA2 gene expression. Thus, the study emphasizes the importance of SAA gene structure in determining susceptibility to amyloidosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamamoto, K -- Shiroo, M -- Migita, S -- New York, N.Y. -- Science. 1986 Apr 11;232(4747):227-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3456645" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid/*genetics ; Amyloidosis/*genetics ; Animals ; DNA/genetics/metabolism ; Genetic Engineering ; Humans ; Mice ; Mice, Inbred BALB C ; Nucleic Acid Hybridization ; Serum Amyloid A Protein/*genetics
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  • 91
    Publication Date: 1986-07-11
    Description: The ninth component of complement (C9) and the pore-forming protein (PFP or perforin) from cytotoxic T lymphocytes polymerize to tubular lesions having an internal diameter of 100 A and 160 A, respectively, when bound to lipid bilayers. Polymerized C9, assembled by slow spontaneous or rapid Zn2+-induced polymerization, and polyperforin, which is assembled only in the presence of Ca2+, constitute large aqueous pores that are stable, nonselective for solutes, and insensitive to changes of membrane potential. Monospecific polyclonal antibodies to purified C9 and PFP show cross-reactivity, suggesting structural homology between the two molecules. The structural and functional homologies between these two killer molecules imply an active role for pore formation during cell lysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Young, J D -- Cohn, Z A -- Podack, E R -- AI070127/AI/NIAID NIH HHS/ -- AI18525/AI/NIAID NIH HHS/ -- CA3019/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Jul 11;233(4760):184-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2425429" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Centrifugation, Isopycnic ; Complement C9/*immunology/physiology ; Cross Reactions ; Humans ; Ion Channels/physiology ; *Membrane Glycoproteins ; Membrane Proteins/*immunology/physiology ; Mice ; Molecular Weight ; Perforin ; Pore Forming Cytotoxic Proteins ; T-Lymphocytes, Cytotoxic/*physiology ; Zinc/physiology
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  • 92
    Publication Date: 1986-05-16
    Description: Genes that are expressed exclusively in cytotoxic T cells should encode proteins that are essential for target cell lysis in cell-mediated immune responses. The sequences of two cytotoxic T lymphocyte-specific complementary DNA's (cDNA's) suggest that the two genes encode serine proteases. A full-length cDNA corresponding to one of the genes was isolated and sequenced. The predicted protein resembles serine proteases in that it includes all the residues that form the catalytic triad of the active site of serine proteases. Moreover, it has sequence characteristics thought to occur only in rat mast cell protease type II. These results are in accord with the view that a protease cascade plays a key role in cytotoxic T-cell activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lobe, C G -- Finlay, B B -- Paranchych, W -- Paetkau, V H -- Bleackley, R C -- New York, N.Y. -- Science. 1986 May 16;232(4752):858-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3518058" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Endopeptidases/*genetics ; Genes ; Mice ; Serine Endopeptidases ; T-Lymphocytes, Cytotoxic/*metabolism
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  • 93
    Publication Date: 1986-11-14
    Description: Interleukin-2 (IL-2) binds to both high- and low-affinity classes of IL-2 receptors on activated T lymphocytes. Only the high-affinity receptors are involved in receptor-mediated endocytosis and normally transduce the mitogenic signals of IL-2; however, the structural features distinguishing the high- and low-affinity receptors are unknown. When 125I-labeled IL-2 was chemically cross-linked to activated human T lymphocytes, two major bands were identified. First, as predicted, a 68- to 72-kilodalton band, consisting of IL-2 (15.5 kilodaltons) cross-linked to the IL-2 receptor (55 kilodaltons), was observed. Second, an unpredicted 85- to 92-kilodalton moiety was detected. This band was not present when IL-2 was cross-linked to transfected C127 cells, which exclusively express low-affinity receptors. The data presented are most consistent with the existence of a 70- to 77-kilodalton glycoprotein subunit (p70) which, upon associating with the 55-kilodalton low-affinity receptor (p55), transforms it into a high-affinity site. It is proposed that p55 and p70 be referred to as the alpha and beta subunits, respectively, of the high-affinity IL-2 receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharon, M -- Klausner, R D -- Cullen, B R -- Chizzonite, R -- Leonard, W J -- New York, N.Y. -- Science. 1986 Nov 14;234(4778):859-63.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3095922" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; *Cross-Linking Reagents ; Humans ; Immunosorbent Techniques ; Interleukin-2/metabolism ; Leukemia, Lymphoid/metabolism ; Lymphocyte Activation ; Mice ; Molecular Weight ; Receptors, Immunologic/*metabolism ; Receptors, Interleukin-2 ; Succinimides ; T-Lymphocytes/metabolism
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  • 94
    Publication Date: 1986-01-24
    Description: Parathyroid hormone-like factors have been found in extracts of tumors associated with humoral hypercalcemia of malignancy, many of which are of squamous epithelial origin. Cultured, nonmalignant human keratinocytes were examined for the production of similar factors. Keratinocyte-conditioned medium from ten cultures stimulated the production of cyclic adenosine monophosphate in clonally derived rat osteosarcoma cells sensitive to parathyroid hormone. Bovine [Nle8,18, Tyr34]PTH-(3-34)NH2, a competitive inhibitor of parathyroid hormone, stopped the adenylate cyclase production stimulated by keratinocyte-conditioned medium, but antisera to parathyroid hormone had no effect on such adenylate cyclase activity. The active component of keratinocyte-conditioned medium has a molecular weight exceeding that of native parathyroid hormone. These characteristics are shared by the parathyroid hormone receptor agonists associated with humoral hypercalcemia of malignancy, which suggests that normal human keratinocytes may produce a factor related to that produced by malignant tumors associated with humoral hypercalcemia of malignancy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Merendino, J J Jr -- Insogna, K L -- Milstone, L M -- Broadus, A E -- Stewart, A F -- AM 30102/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 24;231(4736):388-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2417317" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Animals ; Cattle ; Cells, Cultured ; Cyclic AMP/metabolism ; Epidermis/*cytology/metabolism/physiology ; Humans ; Isoproterenol/pharmacology ; Keratins/*metabolism ; Mice ; Osteosarcoma/metabolism ; Parathyroid Hormone/pharmacology/*physiology ; Peptide Fragments/pharmacology ; Rats ; Teriparatide
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  • 95
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-05-02
    Description: A novel procedure for saturation mutagenesis of cloned DNA was used to obtain more than 100 single base substitutions within the promoter of the mouse beta-major globin gene. The effects of these promoter substitutions on transcription were determined by transfecting the cloned mutant genes into HeLa cells on plasmids containing an SV40 transcription enhancer, and measuring the levels of correctly initiated beta-globin transcripts after 2 days. Mutations in three regions of the promoter resulted in a significant decrease in the level of transcription: (i) the CACCC box, located between -87 and -95, (ii) the CCAAT box, located between -72 and -77, and (iii) the TATA box, located between -26 and -30 relative to the start site of transcription. In contrast, two different mutations in nucleotides immediately upstream from the CCAAT box resulted in a 3- to 3.5-fold increase in transcription. With two minor exceptions, single base substitutions in all other regions of the promoter had no effect on transcription. These results precisely delineate the cis-acting sequences required for accurate and efficient initiation of beta-globin transcription, and they establish a general approach for the fine structure genetic analysis of eukaryotic regulatory sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Myers, R M -- Tilly, K -- Maniatis, T -- New York, N.Y. -- Science. 1986 May 2;232(4750):613-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3457470" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Genes ; Genetic Engineering ; Globins/biosynthesis/*genetics ; HeLa Cells ; Humans ; Mice ; Mutation ; *Promoter Regions, Genetic ; Transcription, Genetic
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  • 96
    Publication Date: 1986-04-11
    Description: The hypothesis that red-green "color blindness" is caused by alterations in the genes encoding red and green visual pigments has been tested and shown to be correct. Genomic DNA's from 25 males with various red-green color vision deficiencies were analyzed by Southern blot hybridization with the cloned red and green pigment genes as probes. The observed genotypes appear to result from unequal recombination or gene conversion (or both). Together with chromosome mapping experiments, these data identify each of the cloned human visual pigment genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nathans, J -- Piantanida, T P -- Eddy, R L -- Shows, T B -- Hogness, D S -- New York, N.Y. -- Science. 1986 Apr 11;232(4747):203-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3485310" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; Chromosomes, Human ; Color ; *Color Perception/physiology ; Color Vision Defects/genetics ; DNA/genetics/metabolism ; Gene Frequency ; *Genes ; Genetic Variation ; Genotype ; Humans ; Mice ; Nucleic Acid Hybridization ; Retinal Pigments/genetics ; X Chromosome
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  • 97
    Publication Date: 1986-08-29
    Description: Insulin action may involve the intracellular generation of low molecular weight substances that modulate certain key enzymes. The production of two substances that regulate the activity of adenosine 3',5'-monophosphate phosphodiesterase was evaluated in cultured myocytes by incorporation of radiolabeled precursors. Insulin caused the rapid hydrolysis of a chemically undefined membrane glycolipid, resulting in the production of two related complex carbohydrates as well as diacylglycerol. Both the glycolipid precursor and the aqueous products were monitored by labeling with radioactive inositol and glucosamine. Depletion of the labeled precursor and the appearance of labeled water-soluble products and diacylglycerol occurred within 30 seconds after hormone treatment and was followed by rapid resynthesis of the precursor. The aqueous products that were radioactively labeled appeared chromatographically and electrophoretically identical to phosphodiesterase modulating activities produced by insulin from the same cells. The purified radiolabeled and bioactive substances had similar chemical properties. Hydrolysis of the glycolipid precursor and subsequent generation of products could be reproduced by incubation of extracted lipids with a phosphatidylinositol-specific phospholipase C. These studies suggest that insulin stimulates an endogenous, selective phospholipase C activity that hydrolyzes a novel glycolipid, resulting in the generation of a complex carbohydrate-phosphate substance containing inositol and glucosamine that may mediate some of the actions of the hormone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saltiel, A R -- Fox, J A -- Sherline, P -- Cuatrecasas, P -- AM33804/AM/NIADDK NIH HHS/ -- F32 AI07185/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 29;233(4767):967-72.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3016898" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-AMP Phosphodiesterases/*metabolism ; Animals ; Cell Line ; Glucosamine/metabolism ; Glycolipids/*metabolism ; Hydrolysis ; Inositol/metabolism ; Insulin/*pharmacology ; Liver/metabolism ; Mice ; Phosphatidylinositol Diacylglycerol-Lyase ; Phosphoinositide Phospholipase C ; Phosphoric Diester Hydrolases/metabolism ; Staphylococcus aureus/enzymology
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  • 98
    Publication Date: 1986-02-21
    Description: The lymphocyte cell surface receptor for the high endothelial venules (HEV's) of peripheral lymph nodes is specifically recognized by the monoclonal antibody MEL-14. Three independent complementary DNA (cDNA) clones, each of which encodes the protein ubiquitin, were detected by virtue of the expression of the MEL-14 antigenic determinant on cDNA-beta-galactosidase bacterial fusion proteins. The antigenic determinant defined by MEL-14 resides in the carboxyl terminal 13-amino-acid proteolytic peptide of ubiquitin, but is undetected in intact undenatured ubiquitin and other cellular ubiquitinated proteins. Antisera and monoclonal antibodies to ubiquitin determinants bind to the surface of both HEV-receptor positive and negative cell lines. The MEL-14-identified cDNA clones hydridize to RNA transcripts that encode tandemly repeated ubiquitins. Sequence analysis of these polyubiquitin cDNA's does not identify a leader sequence for export to the cell surface. The expression of the MEL-14 epitope of ubiquitin depends upon its local environment. The steady-state levels of expression of the ubiquitin messenger RNA's do not correlate with either the tissue derivation of the RNA or the expression of the lymphocyte HEV receptor. Regulation of the expression of the HEV receptor is not likely to reflect the transcriptional control of ubiquitin genes, but rather to reflect control of the expression of the HEV core polypeptide or its level or form of ubiquitination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉St John, T -- Gallatin, W M -- Siegelman, M -- Smith, H T -- Fried, V A -- Weissman, I L -- AI19512/AI/NIAID NIH HHS/ -- CA 09151/CA/NCI NIH HHS/ -- GM 31461/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Feb 21;231(4740):845-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3003914" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/*immunology ; Antibody Specificity ; Base Sequence ; Cloning, Molecular ; Endothelium/metabolism ; Gene Expression Regulation ; High Mobility Group Proteins/*genetics ; Lymphatic System/metabolism ; Lymphocytes/*physiology ; Mice ; Receptors, Cell Surface/*genetics/immunology/metabolism ; Ubiquitins/*genetics/immunology/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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  • 99
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-07-11
    Description: In studies to determine the biochemical mechanisms responsible for cell proliferation, synchronized T cells were used as a model for cellular growth control. By metabolic and morphologic criteria, it was found that activation of the T-cell antigen receptor rendered the cells responsive to interleukin-2 (IL-2), but did not move them through the cell cycle. Instead, IL-2 stimulated G1 progression to S phase, or lymphocyte "blastic transformation." During IL-2-promoted G1 progression, expression of the cellular proto-oncogene c-myb was induced transiently at six to seven times basal levels, maximal levels occurring at the midpoint of G1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stern, J B -- Smith, K A -- CA 09367/CA/NCI NIH HHS/ -- CA-17643/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jul 11;233(4760):203-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3523754" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Cycle/drug effects ; Cell Division/*drug effects ; Gene Expression Regulation/drug effects ; Humans ; Interleukin-2/*pharmacology ; Mice ; Proto-Oncogene Proteins/biosynthesis ; *Proto-Oncogenes/drug effects ; Receptors, Antigen, T-Cell/drug effects ; T-Lymphocytes/drug effects/*growth & development
    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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  • 100
    Publication Date: 1986-10-31
    Description: The mechanism by which Trypanosoma cruzi, the protozoan parasite that causes Chagas' disease, becomes attached to mammalian cells is not well understood. Fibronectin is thought to participate in the attachment, and in this study the region of fibronectin that interacts with the surface receptors of T. cruzi trypomastigotes was investigated by testing the binding of the amino acid sequence Arg-Gly-Asp-Ser, corresponding to the cell attachment site of fibronectin to T. cruzi trypomastigotes. Peptides with the sequence Arg-Gly-Asp-Ser, but not Arg-Phe-Asp-Ser, Arg-Phe-Asp-Ser-Ala-Ala-Arg-Phe-Asp, Ser-Lys-Pro, Glu-Ser-Gly, or Ala-Lys-Thr-Lys-Pro, bound to the parasite surface and inhibited cell invasion by the pathogen. Monoclonal antibodies to the cell attachment domain of fibronectin also inhibited cell infection by the parasite. The immunization of BALB/c mice with tetanus toxoid-conjugated peptide induced a significant protection against T. cruzi. The data support the notion that the sequence Arg-Gly-Asp-Ser of cell surface fibronectin acts as a recognition site for attachment of the parasites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ouaissi, M A -- Cornette, J -- Afchain, D -- Capron, A -- Gras-Masse, H -- Tartar, A -- New York, N.Y. -- Science. 1986 Oct 31;234(4776):603-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3094145" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Chagas Disease/parasitology/*prevention & control ; Fibronectins/immunology/*physiology ; Mice ; Mice, Inbred BALB C ; Peptides/*therapeutic use ; Trypanocidal Agents/*therapeutic use ; Trypanosoma cruzi/drug effects
    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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