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  • 1
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    Methylation increases sodium transport into A6 apical membrane vesicles: possible mode of aldosterone action (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-08-17
    Description: When isolated apical membrane vesicles prepared from cultured A6 epithelia were incubated in vitro with the methyl donor S-adenosylmethionine, the control rate of amiloride-inhibitable sodium transport was doubled. The methylation inhibitors 3-deazaadenosine and S-adenosyl homocysteine returned the S-adenosyl-methionine-stimulated sodium transport to control levels. Neither these agents nor adenosine affected sodium transport into control vesicles. In vesicles incubated with S-adenosyl-[3H-methyl]methionine, both membrane phospholipids and proteins were labeled, and this labeling was inhibited by deazaadenosine. In vesicles prepared from A6 cells treated with aldosterone, sodium transport was twice the control value and S-adenosylmethionine did not cause any further stimulation of transport. In those vesicles, both lipid and protein methylation were increased. These results suggest that methylation, which increases the rate of amiloride-sensitive sodium transport is involved in the action of aldosterone at the apical membrane level in epithelia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sariban-Sohraby, S -- Burg, M -- Wiesmann, W P -- Chiang, P K -- Johnson, J P -- New York, N.Y. -- Science. 1984 Aug 17;225(4663):745-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6463652" target="_blank"〉PubMed〈/a〉
    Keywords: Aldosterone/*physiology ; Amiloride/pharmacology ; Amphibians ; Animals ; Biological Transport, Active/drug effects ; Cell Line ; Cell Membrane/drug effects/*metabolism ; Kidney/metabolism ; Methylation ; S-Adenosylhomocysteine/pharmacology ; S-Adenosylmethionine/pharmacology ; Sodium/*metabolism ; Tubercidin/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Sex pheromone of the tsetse fly: isolation, identification, and synthesis of contact aphrodisiacs (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-08-25
    Description: Sex pheromones isolated from the cuticle of the female tsetse fly, Glossina morsitans morsitans Westwood, release mating behavior in the male fly at ultrashort range or upon contact with baited decoys. Three active components were identified as 15,19-dimethylheptatriacontane, 17,21-dimethylheptatriacontane, and 15,19,23-trimethylheptatriacontane. Chemical and biological comparisons show that the natural and synthetic compounds are identical.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carlson, D A -- Langley, P A -- Huyton, P -- New York, N.Y. -- Science. 1978 Aug 25;201(4357):750-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/675256" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dose-Response Relationship, Drug ; Female ; Male ; Pheromones/*isolation & purification ; Sex Attractants/chemical synthesis/*isolation & purification/pharmacology ; Sexual Behavior, Animal/drug effects ; Tsetse Flies/*analysis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Chicken gizzard: relation between calcium-activated phosphorylation and contraction (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-05-04
    Description: Of the proteins in mechanically disrupted chicken gizzard fibers (no functional sarcolemma) only the 20,000-dalton light chains of myosin underwent large Ca2+-and Sr2+-dependent changes in phosphorylation. Phosphorylation closely corresponded with the Ca2+- and Sr2+-activated tensions. Adenosine 5'-O (3'-thiotriphosphate) only in the presence of Ca2+ induced irreversible Ca2+-insensitive activation of tension and thiophosphorylation of the 20,000-dalton light chains, and blocked incorporation of 32P from [gamma-32P]adenosine triphosphate into the myosin light chains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoar, P E -- Kerrick, W G -- Cassidy, P S -- New York, N.Y. -- Science. 1979 May 4;204(4392):503-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/432654" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*pharmacology ; Chickens ; Gizzard/*physiology ; In Vitro Techniques ; Molecular Weight ; Muscle Contraction/*drug effects ; Muscle, Smooth/*physiology ; Myosins/*metabolism ; Phosphorylation ; Protein Kinases/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Inosine may be an endogenous ligand for benzodiazepine receptors on cultured spinal neurons (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-08-17
    Description: Mouse spinal neurons grown in tissue culture were used to study the membrane effects of the benzodiazepine flurazepam and the naturally occurring purine nucleoside inosine, which competes for benzodiazepine receptor sites in the central nervous system. Application of inosine elicited two types of transmitter-like membrane effects: a rapidly desensitizing excitatory response and a nondesensitizing inhibitory response. Flurazepam produced a similar excitatory response which showed cross-desensitization with the purine excitation. Flurazepam also blocked the inhibitory inosine response. The results provide electrophysiological evidence that an endogenous purine can activate two different conductances on spinal neurons and that flurazepam can activate one of the conductances and antagonize the other.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacDonald, J F -- Barker, J L -- Paul, S M -- Marangos, P J -- Skolnick, P -- New York, N.Y. -- Science. 1979 Aug 17;205(4407):715-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/37602" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Benzodiazepines/*metabolism ; Cells, Cultured ; Electric Conductivity ; Flurazepam/antagonists & inhibitors ; Inosine/*metabolism/pharmacology ; Ligands ; Mice ; Neurotransmitter Agents/metabolism ; Receptors, Drug/*metabolism ; Receptors, Neurotransmitter/metabolism ; Spinal Cord/*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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  • 5
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    Neurochemical and behavioral evidence for a selective presynaptic dopamine receptor agonist (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-12-05
    Description: A new dopamine analog, 6,7-dihydroxy-2-dimethylaminotetralin (TL-99), was compared to apomorphine in three tests of dopaminergic function in the central nervous system. The tests, performed on rats, included production of changes in locomotor activity (involving both presynaptic and postsynaptic receptors), inhibition of dopa accumulation (quantifying presynaptic receptor activity), and the rotation model (quantifying postsynaptic receptor activation). Apomorphine was efficacious at both presynaptic and postsynaptic receptors, whereas TL-99 was much more efficacious at the presynaptic receptor. This result indicates not only that differences exist between presynaptic and postsynaptic dopamine receptors, but also that these differences may be exploited in the design of selective dopamine agonists.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goodale, D P -- Rusterholz, D B -- Long, J P -- Flynn, J R -- Walsh, B -- Cannon, J G -- Lee, T -- GM 12675/GM/NIGMS NIH HHS/ -- GM-22365/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1980 Dec 5;210(4474):1141-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7444443" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apomorphine/pharmacology ; Behavior, Animal/drug effects ; Brain/*drug effects ; Levodopa/metabolism ; Motor Activity/drug effects ; Naphthols ; Rats ; Receptors, Dopamine/*drug effects ; Synaptic Membranes/*drug effects ; *Tetrahydronaphthalenes
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Comparison of the nucleic acid sequence of anglerfish and mammalian insulin mRNA's from cloned cDNA's (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-12-19
    Description: Anglerfish (Lophius americanus) insulin complementary DNA was cloned in bacterial plasmids, and its sequence was determined. Fish insulin messenger RNA is larger (1.5 times) than the messenger RNA encoding mammalian (rat and human) insulin, in part because of a larger C peptide (an additional six amino acids or 18 nucleotides in length) but mainly because of increases in the 5' and 3' untranslated regions. Comparison of the fish, rat, and human insulin messenger RNA (from the complementary DNA) reveals that, in addition to the regions coding for the A and B peptides, sequence conservation is limited to a segment within the 5' untranslated region which may be involved in ribosomal binding, two small segments of the signal peptide, and two stretches of sequence in the 3' untranslated region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hobart, P M -- Shen, L P -- Crawford, R -- Pictet, R L -- Rutter, W J -- AM 21344/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1980 Dec 19;210(4476):1360-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001633" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Biological Evolution ; Cloning, Molecular ; Codon ; Fishes/*genetics ; Insulin/*genetics ; Nucleic Acid Conformation ; Proinsulin/genetics ; Protein Biosynthesis ; Protein Precursors/genetics ; RNA, Messenger/*genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Mapping of heavy chain genes for mouse immunoglobulins M and D (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: A single DNA fragment containing both mu and delta immunoglobulin heavy chain genes has been cloned from normal BALB/c mouse liver DNA with a new lambda phage vector Charon 28. The physical distance between the membrane terminal exon of mu and the first domain of delta is 2466 base pairs, with delta on the 3' side of mu. A single transcript could contain a variable region and both mu and delta constant regions. The dual expression of immunoglobulins M and D on spleen B cells may be due to alternate splicing of this transcript.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, C P -- Tucker, P W -- Mushinski, J F -- Blattner, F R -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1348-53.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6774414" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/immunology ; Chromosome Deletion ; *Genes ; Immunoglobulin Constant Regions/genetics ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin delta-Chains/*genetics ; Immunoglobulin mu-Chains/*genetics ; Liver/physiology ; Membrane Proteins/genetics ; Mice ; Myeloma Proteins/genetics ; Plasmids ; RNA, Messenger/genetics ; Recombination, Genetic
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Gap junction development is correlated with insulin content in the pancreatic B cell (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-08-29
    Description: The development of gap junctions between insulin-containing B cells was quantitatively analyzed in islets of Langerhans isolated from rats treated with the sulfonylurea glibenclamid for 1, 2, or 7 days. Glibenclamid treatment was associated with a marked depletion of the insulin content of B cells and with an increase in the number and size of gap junctions between these cells. A significance correlation was found between these two events.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meda, P -- Halban, P -- Perrelet, A -- Renold, A E -- Orci, L -- New York, N.Y. -- Science. 1980 Aug 29;209(4460):1026-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6773144" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Communication/drug effects ; Female ; Freeze Fracturing ; Glyburide/*pharmacology ; Insulin/*metabolism ; Intercellular Junctions/drug effects/*ultrastructure ; Islets of Langerhans/drug effects/metabolism/*ultrastructure ; Rats
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 9
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    Hormone binding alters the conformation of the insulin receptor (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-12-05
    Description: Fat cells or fat cell membranes were briefly subjected to mild proteolysis under conditions where insulin receptors were either free or bound to (125)I-labeled insulin. When receptors were then affinity-labeled to visualize the effects of this treatment, it was observed that receptors that had been occupied by ligand during proteolysis exhibited greater rates of degradation than unoccupied receptors. These results demonstrate that insulin-receptor interaction induces a change in receptor structure that may be related to signal transmission.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pilch, P F -- Czech, M P -- AM 06069/AM/NIADDK NIH HHS/ -- AM 17893/AM/NIADDK NIH HHS/ -- HD 11343/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1980 Dec 5;210(4474):1152-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7003712" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Animals ; Cell Membrane/metabolism ; Insulin/*metabolism ; Male ; Peptide Fragments/analysis ; Protein Binding ; Protein Conformation ; Rats ; Receptor, Insulin/*metabolism ; Trypsin/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 10
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    Magnetic field of a nerve impulse: first measurements (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-04-04
    Description: The magnetic field of the action potential from an isolated frog sciatic nerve was measured by a SQUID magnetometer with a novel room-temperature pickup coil. The 1.2 x 10(-10) tesla field was measured 1.3 millimeters from the nerve with a signal-to-noise ratio of 40 to 1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wikswo, J P -- Barach, J P -- Freeman, J A -- New York, N.Y. -- Science. 1980 Apr 4;208(4439):53-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7361105" target="_blank"〉PubMed〈/a〉
    Keywords: *Action Potentials ; Animals ; Anura ; *Magnetics ; *Neural Conduction ; Sciatic Nerve/physiology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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