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  • Structure-Activity Relationship  (5)
  • American Association for the Advancement of Science (AAAS)  (5)
  • Periodicals Archive Online (PAO)
  • 1980-1984  (5)
  • 1940-1944
  • 1981  (5)
  • 1957
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (5)
  • Periodicals Archive Online (PAO)
Years
  • 1980-1984  (5)
  • 1940-1944
Year
  • 1
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    GABA analogues activate channels of different duration on cultured mouse spinal neurons (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-04-17
    Description: Voltage-clamp recordings from mouse spinal neurons grown in culture were used to study the membrane current fluctuations induced by 12 substances structurally similar to gamma-aminobutyric acid (GABA). Fluctuation analysis provided estimates of the electrical properties of the elementary events underlying these responses. Estimates of the mean conductance of channels activated by all of the substances except glycine did not differ significantly from that estimated for GABA, whereas mean durations of agonist-activated channels all differed significantly from that found for GABA. The results indicate that all of the substances tested except glycine activate channels of similar conductance but of different durations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barker, J L -- Mathers, D A -- New York, N.Y. -- Science. 1981 Apr 17;212(4492):358-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6259733" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/drug effects ; Ion Channels/*drug effects ; Membrane Potentials/drug effects ; Mice ; Neurons/drug effects ; Receptors, Cell Surface/metabolism ; Receptors, GABA-A ; Spinal Nerves/*drug effects ; Structure-Activity Relationship ; Time Factors ; gamma-Aminobutyric Acid/*analogs & derivatives/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Rational approaches to chemotherapy: antisickling agents (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-08-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klotz, I M -- Haney, D N -- King, L C -- New York, N.Y. -- Science. 1981 Aug 14;213(4509):724-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256275" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/*drug therapy ; Aspirin/analogs & derivatives/therapeutic use ; Chemical Phenomena ; Chemistry ; *Hemoglobin, Sickle ; Humans ; Protein Binding/drug effects ; Protein Conformation ; Salicylates/*therapeutic use ; Solubility ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Didemnins: antiviral and antitumor depsipeptides from a caribbean tunicate (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-05-22
    Description: Extracts of samples of a Caribbean tunicate (ascidian, sea squirt) of the family Didemnidae inhibit in vitro at low concentrations the growth of DNA and RNA viruses as well as L1210 leukemic cells. The active compounds isolated from the tunicate, didemnins A, B, and C, are depsipeptides, and didemnin B (a derivative of didemnin A) is the component active at the lowest concentration in inhibiting viral replication in vitro and P388 leukemia in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rinehart, K L Jr -- Gloer, J B -- Hughes, R G Jr -- Renis, H E -- McGovren, J P -- Swynenberg, E B -- Stringfellow, D A -- Kuentzel, S L -- Li, L H -- AI 04769/AI/NIAID NIH HHS/ -- GM 27029/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1981 May 22;212(4497):933-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7233187" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibiotics, Antineoplastic/*isolation & purification ; Antiviral Agents/*isolation & purification ; *Depsipeptides ; Leukemia, Experimental/*drug therapy ; Peptides, Cyclic/*isolation & purification/therapeutic use ; Structure-Activity Relationship ; Urochordata/*analysis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Heart imaging with cationic complexes of technetium (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-10-02
    Description: The cationic technetium-99 complex trans-[99TC(dmpe)2Cl2]+, where dmpe is bis(1,2-dimethylphosphino)ethane or (CH3)2P-CH2-P(CH3)2, has been prepared and characterized by single-crystal, x-ray structural analysis. The technetium-99m analog, trans-(99mTc(dmpe) 2Cl2]+, has also been prepared and shown to yield excellent gamma-ray images of the heart. The purposeful design, characterization, and synthesis of this technetium-99m radiopharmaceutical represents a striking application of fundamental inorganic chemistry to a problem in applied nuclear medicine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deutsch, E -- Bushong, W -- Glavan, K A -- Elder, R C -- Sodd, V J -- Scholz, K L -- Fortman, D L -- Lukes, S J -- HL-21276/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1981 Oct 2;214(4516):85-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6897930" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cations, Monovalent ; Dogs ; Heart/*radionuclide imaging ; *Organotechnetium Compounds ; *Phosphines ; Structure-Activity Relationship ; *Technetium
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    Pineal N-acetyltransferase is inactivated by disulfide-containing peptides: insulin is the most potent (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-07-31
    Description: Pineal N-acetyltransferase can be inactivated in broken cell preparations by cystamine through a mechanism of thiol-disulfide exchange. Some, but not all, disulfide-containing peptides can inactivate this enzyme; the most potent inactivator is insulin. These findings suggest that a disulfide-containing peptide with high reactivity toward N-acetyltransferase may participate in the intracellular regulation of this enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Namboodiri, M A -- Favilla, J T -- Klein, D C -- New York, N.Y. -- Science. 1981 Jul 31;213(4507):571-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7017937" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/*antagonists & inhibitors ; Animals ; Disulfides/pharmacology ; Dithiothreitol/pharmacology ; Hormones/pharmacology ; Hydrogen-Ion Concentration ; Insulin/*pharmacology ; Kinetics ; Male ; Peptides/*pharmacology ; Pineal Gland/*enzymology ; Rats ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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