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  • Articles  (12)
  • Binding Sites
  • Mutation
  • American Association for the Advancement of Science (AAAS)  (12)
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  • 1981  (12)
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  • Articles  (12)
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  • American Association for the Advancement of Science (AAAS)  (12)
  • American Chemical Society (ACS)
  • Elsevier
  • Wiley
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  • 2015-2019
  • 2005-2009
  • 1990-1994
  • 1980-1984  (12)
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  • Computer Science  (12)
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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-08-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evans, C H -- Tew, W P -- New York, N.Y. -- Science. 1981 Aug 7;213(4508):653-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256262" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cations ; *Erbium ; Kinetics ; *Magnetics
    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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  • 2
    Publication Date: 1981-04-24
    Description: The chromosomes of the ovarian nurse cells of Drosophila melanogaster fall apart during their cycles of endoreduplication. However, chromosomal synapsis occurs in the pseudonurse cells produced in certain mutant females. The resulting polytene chromosomes undergo developmental changes that are strikingly different from those recorded for the giant chromosomes of the larval salivary gland cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, R C -- Riley, S F -- Cassidy, J D -- White, P E -- Paik, Y K -- New York, N.Y. -- Science. 1981 Apr 24;212(4493):441-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6782674" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromatin/ultrastructure ; Chromosome Inversion ; Chromosomes/*ultrastructure ; DNA Replication ; Drosophila melanogaster/*genetics ; Female ; Heterochromatin/ultrastructure ; Mutation ; Ovarian Neoplasms/genetics/veterinary ; Ovary/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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  • 3
    Publication Date: 1981-10-23
    Description: The complete nucleotide sequence of a mammalian transforming retrovirus. Moloney murine sarcoma virus, has been determined. MSV, recombinant virus derived of helper viral and cellular sequences, possesses termini resembling prokaryotic transposable elements. The viral genome has the coding capacity for the Moloney murine leukemia virus gag gene product and contains large deletions in pol and env genes. A large open reading frame encompassing its cell-derived sequences codes for its putative transforming protein. The nature of some of the important domains in the viral genome has been established, and their structure is discussed in relation to their function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reddy, E P -- Smith, M J -- Aaronson, S A -- New York, N.Y. -- Science. 1981 Oct 23;214(4519):445-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6170110" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Viral/genetics ; Base Sequence ; Binding Sites ; Cell Transformation, Viral ; DNA, Viral/*genetics ; Defective Viruses/genetics ; Gene Products, gag ; *Genes, Viral ; Moloney murine leukemia virus/*genetics ; RNA, Transfer/genetics ; RNA-Directed DNA Polymerase/genetics ; Repetitive Sequences, Nucleic Acid ; Sarcoma Viruses, Murine/*genetics ; Transcription, Genetic ; Viral Proteins/genetics
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 1981-05-01
    Description: The kinetic patterns of DNA synthesis in wild-type (RAD+) and rad 52 mutants of yeast, which exhibit high levels of synchrony during meiosis, are comparable. However, RAD 52 mutants accumulate single-strand breaks in parental DNA during the DNA synthesis period. Thus, the product of the RAD 52 gene has a role in meiotic DNA metabolism, as well as in the repair of DNA damage during mitotic growth. The observed breaks may be unresolved recombination intermediates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Resnick, M A -- Kasimos, J N -- Game, J C -- Braun, R J -- Roth, R M -- 5 R01 GM17317-11/GM/NIGMS NIH HHS/ -- S07-RR07027/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1981 May 1;212(4494):543-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7010606" target="_blank"〉PubMed〈/a〉
    Keywords: *DNA Repair ; DNA, Fungal/genetics ; DNA, Single-Stranded/genetics ; Genes ; *Meiosis ; Molecular Weight ; Mutation ; *Recombination, Genetic ; Saccharomyces cerevisiae/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 1981-01-02
    Description: Fischer 344 male rats were treated with cyclophosphamide (10 milligrams per kilogram of body weight) for 5 weeks and subsequently mated to females previously treated with saline or cyclophosphamide. The F1 progeny of the cyclophosphamide-treated males exhibited behavior deficits when compared to controls. These data could indicate a chemically induced genetic effect manifested by behavioral alterations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adams, P M -- Fabricant, J D -- Legator, M S -- New York, N.Y. -- Science. 1981 Jan 2;211(4477):80-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7444453" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avoidance Learning ; Behavior, Animal/*physiology ; Cyclophosphamide/*pharmacology ; Female ; Locomotion ; Male ; Motor Activity ; Mutation ; Rats ; Spermatogenesis/*drug effects
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  • 6
    Publication Date: 1981-07-31
    Description: Membrane binding of ethanol, anesthetics, and hydrophobic molecules in brain synaptosomes and liver mitochondria from rats is conspicuously reduced after long-term consumption of ethanol. The membranes are resistant to structural disordering by both ethanol and halothane. Tolerance, cross-tolerance, and dependence in chronic alcoholics may in part result from membrane alterations that inhibit the binding of ethanol and other drugs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rottenberg, H -- Waring, A -- Rubin, E -- AA3442/AA/NIAAA NIH HHS/ -- GM 28173/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1981 Jul 31;213(4507):583-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6264608" target="_blank"〉PubMed〈/a〉
    Keywords: Alcoholism/*metabolism ; Binding Sites ; Brain/*metabolism ; Cell Membrane/drug effects/metabolism/ultrastructure ; Drug Tolerance ; Electron Spin Resonance Spectroscopy ; Ethanol/*pharmacology ; Halothane/pharmacology ; Humans ; Intracellular Membranes/drug effects/metabolism/ultrastructure ; Mitochondria, Liver/*metabolism ; Spin Labels ; Synaptosomes/*metabolism/ultrastructure
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-04-24
    Description: Five ICR-170--induced mutations at the His4 locus in yeast are +1 G.C (G, guanine; C, cytosine) additions in DNA regions that contain multiple G.C base pairs. These mutations represents both nonsuppressible and suppressible alleles. All externally, suppressible frameshift mutations occur in glycine and proline codons to produce the four-base codons GGGU (U, uracil), GGGG, and CCCU. This implies that suppression of these four-base codons in yeast, as in bacteria, involves a four-base anticodon or its functional equivalent. Two identical four-base codons (CCCU) at widely separate regions with His4 are not suppressed equally.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Donahue, T F -- Farabaugh, P J -- Fink, G R -- New York, N.Y. -- Science. 1981 Apr 24;212(4493):455-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7010605" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Codon ; DNA, Fungal/genetics ; Glycine/*genetics ; Histidine/genetics ; Mutation ; Proline/*genetics ; *RNA, Messenger ; Saccharomyces cerevisiae/*genetics ; *Suppression, Genetic
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-04-24
    Description: A secondary structure model for 16S ribosomal RNA which is based on available chemical, enzymatic, and comparative sequence data shows good agreement between constraints dictated by the model and a wide variety of experimental observations. The four major structural domains created by the base-pairing scheme correspond closely to RNA fragments isolated after nuclease digestion in the presence of bound ribosomal proteins. Functionally important sites appear to be located in unpaired regions and are phylogenetically highly conserved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noller, H F -- Woese, C R -- GM 17129/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1981 Apr 24;212(4493):403-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6163215" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Biological Evolution ; Escherichia coli/ultrastructure ; Hydrogen Bonding ; Nucleic Acid Conformation ; Protein Binding ; *RNA, Bacterial ; *RNA, Ribosomal ; Ribonucleases/metabolism ; Ribosomal Proteins/metabolism ; Ribosomes/*ultrastructure ; Substrate Specificity
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ehrenstein, G -- Huang, L Y -- New York, N.Y. -- Science. 1981 Dec 18;214(4527):1365-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7313696" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Dose-Response Relationship, Drug ; Drug Synergism ; *Drug-Related Side Effects and Adverse Reactions ; Models, Biological ; Receptors, Drug/*drug effects
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    Electronic ISSN: 1095-9203
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-04-24
    Description: The affinity of the amino terminal tetrapeptide of the beta chain of fibrin, Gly-His-Arg-Pro, for fibrinogen dramatically increases in the presence of 2 millimolar calcium ion. In contrast, there is no significant increase in the affinity of peptides beginning with the amino terminal sequence of the fibrin alpha chain, Gly-Pro-Arg, in the presence of calcium ions, although the number of binding sites increases. In the latter case, the increased number of sites is due to the alpha chain analogs binding to the site ordinarily occupied by the beta chain analogs. These results indicate that structures at the amino terminus of the fibrin beta chain play a more important role in fibrin polymerization when calcium ions are present.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Laudano, A P -- Doolittle, R F -- AM-07233/AM/NIADDK NIH HHS/ -- HE-18, 576/PHS HHS/ -- New York, N.Y. -- Science. 1981 Apr 24;212(4493):457-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7209542" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Calcium/*pharmacology ; Fibrin/*metabolism ; Fibrinogen/*metabolism ; Humans ; Peptide Fragments/metabolism ; Protein Binding/drug effects
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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