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  • Articles  (4)
  • 1975-1979  (4)
  • Computer Science  (4)
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  • Articles  (4)
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  • 1
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    Mount agung eruption provides test of a global climatic perturbation (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-03-10
    Description: The Mount Agung volcanic eruption in 1963 provides the best-documented global radiative perturbation to the earth's atmosphere currently available. Data on stratospheric aerosols produced by this eruption have been used as input to a model for the atmospheric thermal structure. The computed magnitude, sign, and phase lag of the temperature changes in both the stratosphere and the troposphere are in good agreement with observations, providing evidence that the climatic response to a global radiative perturbation is significant, as well as support for the use of theoretical models to predict climatic effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hansen, J E -- Wang, W C -- Lacis, A A -- New York, N.Y. -- Science. 1978 Mar 10;199(4333):1065-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17844417" target="_blank"〉PubMed〈/a〉
    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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    Conformational changes in 16S ribosomal RNA induced by 30S ribosomal subunit proteins from Escherichia coli (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-12-01
    Description: Laser light scattering has been used to evaluate conformational differences between free 16S RNA and several specific protein-16S RNA complexes. Proteins that interact strongly with the 16S RNA early in subunit assembly stabilize the RNA chain against unfolding in 1 mM Mg2+ and actually promote the formation of a more compact teriary structure in 20 mM Mg2+. A vital function of these proteins may therfore consist in altering the configuration of the RNA so that further assembly reactions can take place.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bogdanov, A A -- Zimmermann, R A -- Wang, C C -- Ford, N C Jr -- New York, N.Y. -- Science. 1978 Dec 1;202(4371):999-1001.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/362531" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins ; Diffusion ; Escherichia coli ; Nucleic Acid Conformation ; Protein Binding ; RNA, Bacterial ; *RNA, Ribosomal ; Ribonucleoproteins ; *Ribosomal Proteins ; Ribosomes/*ultrastructure
    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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    Nonhistone proteins HMG1 and HMG2 change the DNA helical structure (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-03-24
    Description: Two chromatin nonhistone proteins (from calf thymus) of the high mobility group, HMG1 and HMG2, reduce the linking number (topological winding number) of a circular DNA if the covalent closure of the DNA is carried out in their presence. This indicates that these proteins can either unwind the double helix, or induce a supercoiling of the DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Javaherian, K -- Liu, J F -- Wang, J C -- New York, N.Y. -- Science. 1978 Mar 24;199(4335):1345-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/628842" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophages ; Chromosomal Proteins, Non-Histone/*pharmacology ; *DNA, Circular ; DNA, Superhelical ; *DNA, Viral ; Nucleic Acid Conformation/drug effects ; Pseudomonas
    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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    Hv(1), a variable-region genetic marker of human immunoglobulin heavy chains (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-04-21
    Description: A new antigenic determinant was discovered with a hemagglutination-inhibition assay system. Designated Hv(1), it is located in the variable region of human immunoglobulin heavy chains of the G, M, and A classes. Pedigree and population analyses suggest that it has an autosomal dominant mode of inheritance. This represents the first description of an allotypic determinant in the variable region of human immunoglobulins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, A C -- Mathur, S -- Pandey, J -- Siegel, F P -- Middaugh, C R -- Litman, G W -- New York, N.Y. -- Science. 1978 Apr 21;200(4339):327-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/416494" target="_blank"〉PubMed〈/a〉
    Keywords: *Binding Sites, Antibody ; Genes ; Hemagglutination Inhibition Tests ; Humans ; Immunoglobulin Fab Fragments/genetics ; Immunoglobulin Fc Fragments/genetics ; Immunoglobulin Heavy Chains/*genetics ; *Immunoglobulin Variable Region ; Pedigree
    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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