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  • Articles  (29)
  • Kinetics  (27)
  • Models, Molecular
  • 2005-2009
  • 1975-1979  (29)
  • 1978  (29)
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  • Articles  (29)
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Keywords
Publisher
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  • 2005-2009
  • 1975-1979  (29)
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Journal
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  • 1
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    Light stimulates tyrosine hydroxylase activity and dopamine synthesis in retinal amacrine neurons (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-11-24
    Description: Retinal dopamine-containing amacrine neurons are rapidly activated by light, as shown by an increase in the rate of dopamine formation in vivo and a concomitant increase in the activity of tyrosine hydroxylase, measured in vitro with a subsaturating concentration of pteridine cofactor. Activation of tyrosine hydroxylase also occurs when isolated eyes from rats killed in the dark are exposed to a strobe light. Studies of amacrine neurons should provide basic data about the biochemical processing of visual information, as well as the physiological presynaptic regulatory mechanisms of dopamine-containing neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Iuvone, P M -- Galli, C L -- Garrison-Gund, C K -- Neff, N H -- New York, N.Y. -- Science. 1978 Nov 24;202(4370):901-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/30997" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Circadian Rhythm ; Dopamine/*biosynthesis ; Enzyme Activation/radiation effects ; Kinetics ; *Light ; Male ; Neurons/metabolism ; Rats ; Retina/cytology/enzymology/*metabolism ; Tyrosine 3-Monooxygenase/*biosynthesis
    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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    Rapid changes in brain benzodiazepine receptors after experimental seizures (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-11-24
    Description: Seizures induced in the rat by electroshock or by injections of pentylenetetrazol increase the specific binding of diazepam to putative receptor sites in cerebral cortical membranes. The enhancement of diazepam binding results from a rapid increase in the number of available binding sites rather than a change in receptor affinity. The postictal increase in cortical benzodiazepine receptors suggests that the cerebral cortex might be more sensitive to the anticonvulsant effects of the benzodiazepines after seizures. This observation may be related to the mechanism of action of these drugs in the treatment of recurrent seizures such as status epilepticus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paul, S M -- Skolnick, P -- New York, N.Y. -- Science. 1978 Nov 24;202(4370):892-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/715447" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anoxia/metabolism ; Binding Sites ; Brain/*metabolism ; Cerebral Cortex/metabolism ; Diazepam/*metabolism ; Electroshock ; Kinetics ; Male ; Pentylenetetrazole ; Rats ; Receptors, Drug/*metabolism ; Seizures/*metabolism ; Synaptosomes/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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  • 3
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    S-adenosylhomocysteine hydrolase is an adenosine-binding protein: a target for adenosine toxicity (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-11-17
    Description: When adenosine deaminase activity is inhibited, low concentrations of adenosine are toxic to human lymphoblast mutants that are unable to convert adenosine to intracellular nucleotides. In order to identify the mediator of this cytotoxicity, we searched for a cytoplasmic protein capable of binding adenosine with high affinity. Such a protein was identified in extracts of human lymphoblasts and placenta as the enzyme S-adenosylhomocysteine hydrolase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hershfield, M S -- Krodich, N M -- New York, N.Y. -- Science. 1978 Nov 17;202(4369):757-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/715439" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/*metabolism ; Adenosine Deaminase/*deficiency ; Carrier Proteins/*metabolism ; Female ; Humans ; Hydrolases/*metabolism ; Kinetics ; Lymphocytes/metabolism ; Nucleoside Deaminases/*deficiency ; Placenta/metabolism ; Pregnancy ; S-Adenosylhomocysteine/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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    Entry of insulin into human cultured lymphocytes: electron microscope autoradiographic analysis (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-11-17
    Description: Electron microscope autoradiographs were prepared of IM-9 human cultured lymphocytes incubated with iodine-125-labeled insulin. With the use of [125I]insulin and Ilford L-4 emulsion, the technique had a resolution half-distance of approximately 0.085 micrometer. Autoradiographs revealed a time-dependent entry of insulin into the cell interior that was maximal after 30 minutes of incubation. At this time point nearly 40 percent of the [125I]insulin was in the interior of the cell at a distance 1 micrometer or greater from the plasma membrane. Grain distribution and volume density analyses revealed that the intracellular insulin was concentrated in the endoplasmic reticulum and nuclear membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldfine, I D -- Jones, A L -- Hradek, G T -- Wong, K Y -- Mooney, J S -- New York, N.Y. -- Science. 1978 Nov 17;202(4369):760-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/715440" target="_blank"〉PubMed〈/a〉
    Keywords: Autoradiography ; Biological Transport ; Cell Nucleus/metabolism ; Cells, Cultured ; Endoplasmic Reticulum/metabolism ; Humans ; Insulin/*metabolism ; Kinetics ; Lymphocytes/*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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    Slow axonal transport of neurofilament proteins: impairment of beta,beta'-iminodipropionitrile administration (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-11-10
    Description: beta,beta'-Iminodipropionitrile (IDPN) administration prevented normal slow axonal transport of [35S]methionine- or [3H]leucine-labeled proteins in rat sciatic motor axons. Ultrastructural and electrophoretic studies showed that the neurofilament triplet proteins in particular were retained within the initial 5 millimeters of the axons, resulting in neurofilament-filled axonal swellings. Fast anterograde and retrograde axonal transport were not affected. The IDPN thus selectively impaired slow axonal transport. The neurofibrillary pathology in this model is the result of the defective slow transport of neurofilaments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Griffin, J W -- Hoffman, P N -- Clark, A W -- Carroll, P T -- Price, D L -- New York, N.Y. -- Science. 1978 Nov 10;202(4368):633-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/81524" target="_blank"〉PubMed〈/a〉
    Keywords: Axonal Transport/*drug effects ; Kinetics ; Molecular Weight ; Nerve Tissue Proteins/*metabolism ; Neurofibrils/metabolism/ultrastructure ; Nitriles/*pharmacology/toxicity ; Sciatic Nerve/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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  • 6
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    Sickling rates of human AS red cells infected in vitro with Plasmodium falciparum malaria (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-11-10
    Description: The kinetics of sickling of malaria-infected red cells from humans with sickle cell trait were studied in vitro in an attempt to obtain direct experimental evidence for a selective advantage of the hemoglobin S heterozygote in a malarious region. The sickling rates of cells infected with Plasmodium falciparum and of non-infected cells were studied both in the total absence of oxygen (by dithionite addition) and at several different concentrations of oxyhemoglobin which might obtain in vivo. In all cases, red cells containing small plasmodium parasite forms (ring forms) sickled approximately eight times as readily as uninfected cells. Cells containing large parasitic forms (trophozoites and schizonts) appeared to sickle less readily than uninfected cells, by light microscopy criteria, but electron micrographs demonstrated the presence of polymerized deoxyhemoglobin S with a high frequency. It is concluded that enhanced sickling of plasmodium-infected AS cells may be one mechanism whereby the hemoglobin S polymorphism is balanced in favor of the heterozygote.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roth, E F Jr -- Friedman, M -- Ueda, Y -- Tellez, I -- Trager, W -- Nagel, R L -- New York, N.Y. -- Science. 1978 Nov 10;202(4368):650-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/360396" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/*parasitology ; Erythrocytes, Abnormal/*parasitology ; Heterozygote ; Humans ; Kinetics ; Malaria/*blood ; Plasmodium falciparum ; Sickle Cell Trait/parasitology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Presynaptic alpha-receptor subsensitivity after long-term antidepressant treatment (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-10-20
    Description: After 3 weeks of twice-daily administration of desipramine to rats, the frequency-response curve for field stimulation of adrenergic neurons in isolated left atrial strips was shifted markedly to the left and the efflux of [3H]norepinephrine was enhanced greatly. After 1 day of treatment, only slight shifts in the frequency-response curve and small increases in [3H]norepinephrine efflux occurred although inhibition of [3H]norepinephrine uptake was already maximal, and phenoxybenzamine caused a further shift to the left in the frequency-response curve similar to that which occurred after 3 weeks of desipramine treatment alone. A gradual decrease in the sensitivity of the presynaptic alpha receptor would explain the delay in the onset of the linical effect of the tricyclic antidepressants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crews, F T -- Smith, C B -- New York, N.Y. -- Science. 1978 Oct 20;202(4365):322-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/211589" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Desipramine/*pharmacology ; In Vitro Techniques ; Kinetics ; Neuromuscular Junction/drug effects ; Norepinephrine/*metabolism/pharmacology ; Phenoxybenzamine/pharmacology ; Rats ; Receptors, Adrenergic/*drug effects ; Receptors, Adrenergic, alpha/*drug effects ; Receptors, Adrenergic, beta/drug effects ; Synaptic Membranes/drug effects ; Synaptic Transmission/*drug effects ; Time Factors
    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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  • 8
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    Tumor-promoting phorbol esters inhibit binding of epidermal growth factor to cellular receptors (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-10-20
    Description: Tumor-promoting phorbol esters and related plant macrocyclic diterpenes inhibit the binding of epidermal growth factor to its receptors on HeLa cells. This effect shows marked structural specificity and correlates with other biological effects of these compounds on mouse skin and in cell culture systems. The active compounds inhibited binding of 125I-labeled epidermal growth factor with a 50 per-cent effective dose in the range of 10(-8) to 10(-9) M. Inhibition appears to be due to a decrease in the number of available epidermal growth factor receptors rather than a change in receptor affinity. These results suggest that certain biologic effects of tumor promoters may result from alterations in the function of cell surface receptors involved in growth regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, L S -- Weinstein, I B -- New York, N.Y. -- Science. 1978 Oct 20;202(4365):313-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/308698" target="_blank"〉PubMed〈/a〉
    Keywords: Binding, Competitive ; Cell Membrane/metabolism ; Epidermal Growth Factor/*metabolism ; HeLa Cells ; Kinetics ; Peptides/*metabolism ; Phorbol Esters/*metabolism/pharmacology ; Phorbols/*metabolism ; Receptors, Drug/drug effects/*metabolism ; Tetradecanoylphorbol Acetate/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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  • 9
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    Cocaine plasma concentration: relation to physiological and subjective effects in humans (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-10-13
    Description: Volunteer subjects with previous histories of cocaine use were administered cocaine hydrochloride intravenously or intranasally. There was a positive relationship between peak plasma concentration, physiological and subjective responses, and dose administered. The rate of cocaine disappearance after intravenous administration paralleled the drop in physiological and subjective drug effects. After intranasal administration, blood levels remained elevated for a considerably longer period.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Javaid, J I -- Fischman, M W -- Schuster, C R -- Dekirmenjian, H -- Davis, J M -- New York, N.Y. -- Science. 1978 Oct 13;202(4364):227-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/694530" target="_blank"〉PubMed〈/a〉
    Keywords: Administration, Intranasal ; Cocaine/administration & dosage/*blood/*pharmacology ; Dose-Response Relationship, Drug ; Euphoria/*drug effects ; Heart Rate/drug effects ; Humans ; Injections, Intravenous ; Kinetics ; Metabolic Clearance Rate
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Molecular conformation of a halogen-free thyroxine analog: 4-Methoxy-3,5,3-trimethyl-L-thyronine N-acetyl ethyl ester (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-09-22
    Description: The molecular conformation of the halogen-free thyroxine analog 4-methoxy-3,5,3'-trimethyl-L-thyronine -n-acetyl ethyl ester has been determined by x-ray diffraction techniques. The unsubstituted parent compound, trimethylthyronine, has significant biological activity in rat thymocyte tests when compared with the thyroid hormone 3,5,3'-triiodo-L-thyronine (T3). Although no activity data are available for the analog studied, it is presumed to be inactive because of the 4-methoxy blocking group. The observed conformation of this structure is similar to that found for the natural hormone T(3). The 3'-methyl group is distal, the overall conformation is cisoid, and the diphenyl ether conformation is twist-skewed. The results of this diffraction study show that methyl substituents are capable of maintaining the thyronine conformation required for hormonal activity; they suggest that iodine enhances hormone-protein binding because of the electronic effects it produces either by alteration of molecular charge distributions or by direct charge-transfer interactions with the serum or nuclear binding proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cody, V -- New York, N.Y. -- Science. 1978 Sep 22;201(4361):1131-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/684433" target="_blank"〉PubMed〈/a〉
    Keywords: Models, Molecular ; Molecular Conformation ; Thyronines/*analogs & derivatives ; X-Ray Diffraction
    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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