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  • 1990-1994  (525)
  • 1975-1979  (162)
  • 1970-1974  (141)
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  • 1
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    Template supercoiling by a chimera of yeast GAL4 protein and phage T7 RNA polymerase (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-14
    Description: Fusion of the DNA-binding domain of yeast GAL4 protein to the amino terminus of bacteriophage T7 RNA polymerase yields a chimera that retains the characteristics of its components. The presence of the GAL4 peptide allows the chimeric enzyme to anchor itself on the DNA template, and this anchoring in turn drives the formation of a supercoiled DNA loop, in linear or circular templates, when RNA synthesis at the polymerase site forces a translocation of the DNA relative to the site. Nonspecific interaction between the chimeric enzyme and DNA appears to be sufficient to effect supercoiling during transcription. Transcription by the chimeric polymerase is strictly dependent on the presence of a T7 promoter; thus it provides a tool in vitro and in vivo for specifically supercoiling DNA segments containing T7 promoter sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ostrander, E A -- Benedetti, P -- Wang, J C -- GM24544/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 14;249(4974):1261-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2399463" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA, Superhelical/*metabolism ; DNA-Binding Proteins/*physiology ; DNA-Directed RNA Polymerases/*physiology ; Fungal Proteins/*metabolism ; Macromolecular Substances ; Molecular Sequence Data ; Promoter Regions, Genetic/physiology ; Recombinant Fusion Proteins/metabolism ; *Saccharomyces cerevisiae Proteins ; T-Phages/*enzymology ; Transcription Factors/physiology ; Transcription, Genetic/*physiology ; Viral Proteins
    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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    Design, activity, and 2.8 A crystal structure of a C2 symmetric inhibitor complexed to HIV-1 protease (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-03
    Description: A two-fold (C2) symmetric inhibitor of the protease of human immunodeficiency virus type-1 (HIV-1) has been designed on the basis of the three-dimensional symmetry of the enzyme active site. The symmetric molecule inhibited both protease activity and acute HIV-1 infection in vitro, was at least 10,000-fold more potent against HIV-1 protease than against related enzymes, and appeared to be stable to degradative enzymes. The 2.8 angstrom crystal structure of the inhibitor-enzyme complex demonstrated that the inhibitor binds to the enzyme in a highly symmetric fashion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erickson, J -- Neidhart, D J -- VanDrie, J -- Kempf, D J -- Wang, X C -- Norbeck, D W -- Plattner, J J -- Rittenhouse, J W -- Turon, M -- Wideburg, N -- AI 27220/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):527-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Computer-Assisted Molecular Design, Abbott Laboratories, Abbott Park, IL 60064.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2200122" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Drug Design ; Endopeptidases/*metabolism ; Gene Products, pol/*metabolism ; HIV Protease ; HIV-1/*enzymology ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Protease Inhibitors/*pharmacology ; Protein Conformation ; Sugar Alcohols/*pharmacology ; Valine/*analogs & derivatives/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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  • 3
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    Knotting of a DNA chain during ring closure (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-04-23
    Description: The formation of knotted species on random ring closure of two DNAs that are 5.6 kilobase pairs (kbp) and 8.6 kbp in length was measured, and these data were used to calculate the effective DNA helix diameter as a function of sodium ion and magnesium ion concentration. In the presence of more than 50 mM magnesium ion, interactions between DNA segments appear to be attractive rather than repulsive. The free energy of formation of relaxed trefoil and figure-eight DNA knots and of supercoiled trefoil DNA knots was also evaluated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shaw, S Y -- Wang, J C -- New York, N.Y. -- Science. 1993 Apr 23;260(5107):533-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Harvard University, Department of Biochemistry and Molecular Biology, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8475384" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/*chemistry/metabolism ; DNA, Circular/*chemistry/metabolism ; DNA, Single-Stranded/chemistry ; DNA, Superhelical/*chemistry/metabolism ; Magnesium/pharmacology ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Probability ; Sodium Chloride/pharmacology ; Thermodynamics
    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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    Uncertainties in carbon dioxide radiative forcing in atmospheric general circulation models (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-19
    Description: Global warming caused by an increase in the concentrations of greenhouse gases, is the direct result of greenhouse gas-induced radiative forcing. When a doubling of atmospheric carbon dioxide is considered, this forcing differed substantially among 15 atmospheric general circulation models. Although there are several potential causes, the largest contributor was the carbon dioxide radiation parameterizations of the models.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cess, R D -- Zhang, M H -- Potter, G L -- Barker, H W -- Colman, R A -- Dazlich, D A -- Del Genio, A D -- Esch, M -- Fraser, J R -- Galin, V -- Gates, W L -- Hack, J J -- Ingram, W J -- Kiehl, J T -- Lacis, A A -- Le Treut, H -- Li, Z X -- Liang, X Z -- Mahfouf, J F -- McAvaney, B J -- Meleshko, V P -- Morcrette, J J -- Randall, D A -- Roeckner, E -- Royer, J F -- Sokolov, A P -- Sporyshev, P V -- Taylor, K E -- Wang, W C -- Wetherald, R T -- New York, N.Y. -- Science. 1993 Nov 19;262(5137):1252-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17772648" 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
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  • 5
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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
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  • 6
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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
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  • 7
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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
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  • 8
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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
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  • 9
    Electronic Resource
    Electronic Resource
    Approximate molecular orbital theory for positrons and positronium atoms bound to molecules (1976)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 80 (1976), S. 2507-2518 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j100563a016
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  • 10
    Electronic Resource
    Electronic Resource
    C-12 substituted prostaglandins: synthesis and biological evaluation of (.+-.)-12-hydroxyprostaglandin F2.alpha. methyl ester (1978)
    s.l. : American Chemical Society
    The @journal of organic chemistry 43 (1978), S. 4178-4182 
    Details
    ISSN: 1520-6904
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jo00415a042
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