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  • Molecular Sequence Data
  • Temperature
  • American Association for the Advancement of Science (AAAS)  (5)
  • Springer Nature
  • 2000-2004
  • 1995-1999
  • 1980-1984  (5)
  • 1940-1944
  • 1982  (5)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (5)
  • Springer Nature
Years
  • 2000-2004
  • 1995-1999
  • 1980-1984  (5)
  • 1940-1944
Year
  • 1
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    Epidermis of human skin: pyroelectric and piezoelectric sensor layer (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-05-28
    Description: The epidermis of live human skin has a permanent electric dipole moment perpendicular to its surface. Voltage responses to a rapid change of temperature are pyroeletric, while voltage responses to pressure pulses are piezoelectric in nature. The time course of the responses depends on dX/dt (X, temperature or pressure). The epidermal surface can react to all physical environmental influences to which nonbiological pyroelectric materials are known to respond. Epidermal voltage signals can be perceived through the intraepidermal and the superficial dermal nervous network. The pyroelectric and piezoelectric properties are also measurable on dead, dry skin samples.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Athenstaedt, H -- Claussen, H -- Schaper, D -- New York, N.Y. -- Science. 1982 May 28;216(4549):1018-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6177041" target="_blank"〉PubMed〈/a〉
    Keywords: Biomechanical Phenomena ; Electrophysiology ; Epidermis/*physiology ; Humans ; Keratins/physiology ; Temperature
    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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    Phagocyte impotence caused by an invasive bacterial adenylate cyclase (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-09-03
    Description: For unknown reasons, humans infected with the bacterium Bordetella pertussis are exceptionally vulnerable to secondary infections. Bordetella species elaborate a soluble, heat-stable, and highly active adenylate cyclase. This enzyme is internalized by phagocytic cells and catalyzes the unregulated formation of adenosine 3',5'-monophosphate (cyclic AMP), thereby disrupting normal cellular function. This unusual phenomenon may explain Bordetella-induced aphylaxis and may prove to be useful for investigating a variety of cyclic AMP-governed processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Confer, D L -- Eaton, J W -- 5T32H- L07062/PHS HHS/ -- New York, N.Y. -- Science. 1982 Sep 3;217(4563):948-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6287574" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/*metabolism ; Animals ; Bordetella pertussis/*enzymology ; Cells, Cultured ; Cyclic AMP/biosynthesis ; Humans ; Macrophages/physiology ; Neutrophils/physiology ; Phagocytes/*physiology ; Rabbits ; Superoxides/metabolism ; Temperature
    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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    Physiological basis for swimming endurance differences between LDH-B genotypes of Fundulus heteroclitus (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-05-28
    Description: Adenosine triphosphate levels in erythrocytes are correlated with LDH-B genotype in Fundulus heteroclitus. Adenosine triphosphate is the fish's allosteric modifier of hemoglobin oxygen affinity. Since oxygen delivery to muscle affects swimming performance, fish of each homozygous LDH-B phenotype were swum to exhaustion at 10 degrees or 25 degrees C to determine whether in vitro differences attributed to the LDH-B allelic isozymes were manifest in vivo. At 10 degrees C, the critical swimming speed of the LDH-BaBa phenotype was 3.6 body lengths per second, whereas that of the LDH-BbBb phenotype was 4.3 body lengths per second. At 25 degrees C there were no differences between LDH-B phenotypes in erythrocyte adenosine triphosphate levels, blood oxygen affinity, or swimming performance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DiMichele, L -- Powers, D A -- 1-F32-GMO7889-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 May 28;216(4549):1014-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7079747" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/blood ; Animals ; Fishes/*physiology ; Gene Frequency ; Isoenzymes ; Killifishes/*physiology ; L-Lactate Dehydrogenase/genetics/*physiology ; Oxygen/blood ; *Physical Exertion ; Swimming ; Temperature
    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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    Serotonin and octopamine in the nematode Caenorhabditis elegans (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-05-28
    Description: The biogenic amines serotonin and octopamine are present in the nematode Caenorhabditis elegans. Serotonin, detected histochemically in whole mounts, is localized in two pharyngeal neurons that appear to be neurosecretory. Octopamine, identified radioenzymatically in crude extracts, probably is also localized in a few neurons. Exogenous serotonin and octopamine elicit specific and opposite behavioral responses in Caenorhabditis elegans, suggesting that these compounds function physiologically as antagonists.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horvitz, H R -- Chalfie, M -- Trent, C -- Sulston, J E -- Evans, P D -- GM07287/GM/NIGMS NIH HHS/ -- GM24663/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 May 28;216(4549):1012-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6805073" target="_blank"〉PubMed〈/a〉
    Keywords: Age Factors ; Animals ; Behavior, Animal/physiology ; Caenorhabditis/*physiology ; Female ; Octopamine/*physiology ; Ovulation/drug effects ; Serotonin/*physiology ; Temperature
    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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    DNA conformation, dynamics, and interactions in solution (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-05-07
    Description: The conformation and dynamics of the d(CGCGAATTCGCG) duplex, its analogs containing mismatched base pairs and helix interruptions, and its complexes with actinomycin and Netropsin, bound separately and simultaneously, have been investigated by nuclear magnetic resonance spectroscopy in aqueous solution. Structural information has been deduced from chemical shift and nuclear Overhauser effect parameters, while the kinetics have been probed from line width and saturation recovery experiments on proton and phosphorus markers at the individual base pair level. These studies lead to an improved understanding of the role of nucleic acid sequence on the structure, flexibility, and conformational interconversions in the duplex state. The nuclear magnetic resonance measurements readily identify helix modification and antibiotic binding sites on the nucleic acid and estimate the extent to which the observed conformational and dynamic perturbations are transmitted to adjacent base pair regions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patel, D J -- Pardi, A -- Itakura, K -- New York, N.Y. -- Science. 1982 May 7;216(4546):581-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6280281" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Dna ; Dactinomycin ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Motion ; Netropsin ; *Nucleic Acid Conformation ; Oligodeoxyribonucleotides ; Protons ; Structure-Activity Relationship ; Temperature
    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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