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  • *Biological Evolution
  • Models, Molecular
  • American Association for the Advancement of Science (AAAS)  (7)
  • MDPI Publishing
  • 2005-2009
  • 1995-1999
  • 1980-1984  (7)
  • 1984  (7)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (7)
  • MDPI Publishing
Years
  • 2005-2009
  • 1995-1999
  • 1980-1984  (7)
Year
  • 1
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-11-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gould, S J -- New York, N.Y. -- Science. 1984 Nov 23;226(4677):994-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6505682" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Mathematics ; *Models, Genetic ; Selection, Genetic ; *Time
    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: 1984-08-24
    Description: Malaria parasites can be grouped evolutionarily by analysis of DNA composition and genome arrangement. Those that vary widely with regard to host range, morphology, and biological characteristics fit into only a small number of distinctive groups. The DNA of the human parasite Plasmodium falciparum fits into a group that includes rodent and avian malarias and is unlike the DNA of other primate malaria parasites. The DNA of Plasmodium vivax, which is also a human parasite, fits into a distinctly different group that includes Plasmodium cynomolgi, a parasite of monkeys. The evolutionary lines suggested here appear to be consistent with similarities seen among malaria parasites with regard to gene sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCutchan, T F -- Dame, J B -- Miller, L H -- Barnwell, J -- New York, N.Y. -- Science. 1984 Aug 24;225(4664):808-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6382604" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Base Sequence ; *Biological Evolution ; DNA/*analysis ; Deoxycytidine/analysis ; Deoxyguanosine/analysis ; Nucleic Acid Hybridization ; Plasmodium/*classification/genetics ; Plasmodium berghei/classification/genetics ; Plasmodium falciparum/classification/genetics ; Plasmodium vivax/classification/genetics ; Species Specificity
    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: 1984-09-14
    Description: X-ray diffraction studies of crystals from samples of bimolane synthesized in China and in the United States showed that the crystals consist of the related compound ICRF-154. Analysis of the results of biological tests did not show any significant differences between the anticancer activity of bimolane and ICRF-154. It appears that the anticancer activity of bimolane is due to ICRF-154.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Camerman, N -- Hempel, A -- Camerman, A -- CA 15879/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Sep 14;225(4667):1165-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6474171" target="_blank"〉PubMed〈/a〉
    Keywords: Antineoplastic Agents/*pharmacology ; Models, Molecular ; *Piperazines ; *Razoxane/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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  • 4
    Publication Date: 1984-01-27
    Description: The genetic relationships among molecularly cloned prototype viruses representing all of the major oncovirus genera were investigated by molecular hybridization and nucleotide sequence analysis. One of the major progenitors of the pol genes of such viruses gives rise to mammalian type C viruses and another gives rise to type A, B, D, and avian type C oncoviruses. Evidence of unusual patterns of homology among the env genes of mammalian type C and D oncoviruses illustrates that genetic interactions between their progenitors contributed to the evolution of oncoviruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chiu, I M -- Callahan, R -- Tronick, S R -- Schlom, J -- Aaronson, S A -- New York, N.Y. -- Science. 1984 Jan 27;223(4634):364-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6197754" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Avian Sarcoma Viruses/genetics ; Base Sequence ; *Biological Evolution ; Cloning, Molecular ; DNA Restriction Enzymes ; *Genes, Viral ; Nucleic Acid Heteroduplexes ; Nucleic Acid Hybridization ; RNA-Directed DNA Polymerase/*genetics/metabolism ; Recombination, Genetic ; Retroviridae/classification/*genetics ; Viral Envelope Proteins/genetics
    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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-04-27
    Description: Proteolytic enzymes have many physiological functions, ranging from generalized protein digestion to more specific regulated processes such as the activation of zymogens, blood coagulation and the lysis of fibrin clots, the release of hormones and pharmacologically active peptides from precursor proteins, and the transport of secretory proteins across membranes. They are present in all forms of living organisms. Comparisons of amino acid sequences, three-dimensional structures, and enzymatic reaction mechanisms of proteases indicate that there are distinct families of these proteins. Changes in molecular structure and function have accompanied the evolution of proteolytic enzymes and their inhibitors, each having relatively simple roles in primitive organisms and more diverse and more complex functions in higher organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neurath, H -- GM-15731/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):350-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6369538" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; *Biological Evolution ; Blood Coagulation ; Chemistry, Physical ; Enzyme Activation ; Enzyme Precursors/metabolism ; Genes ; Humans ; Mutation ; *Peptide Hydrolases/analysis/genetics/metabolism ; Peptides/metabolism ; Physicochemical Phenomena ; Protease Inhibitors/analysis/metabolism ; Protein Conformation ; Protein Sorting Signals ; Substrate Specificity
    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
    Publication Date: 1984-11-23
    Description: X-ray analysis of the free-acid crystal form of the coenzyme nicotinamide adenine dinucleotide (NAD+) revealed a conformational difference between the free NAD+ molecule and one bound in enzymes or complexed to Li+ ions. The pyrophosphate group showed asymmetry in the phosphate-oxygen bonds of the phosphate-oxygen-phosphate link; this bond at the nicotinamide side of the link is longer than that at the adenosine side by 0.04 angstrom. The crystal structure showed a novel intermolecular stacking of adenine and water molecules on opposite sides of nicotinamide that gives rise to a nicotinamide sandwich.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parthasarathy, R -- Fridey, S M -- GM-24864/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 23;226(4677):969-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6239374" target="_blank"〉PubMed〈/a〉
    Keywords: Alcohol Dehydrogenase ; Alcohol Oxidoreductases/metabolism ; Animals ; Geobacillus stearothermophilus/enzymology ; Glyceraldehyde-3-Phosphate Dehydrogenases/metabolism ; L-Lactate Dehydrogenase/metabolism ; Liver/enzymology ; Malate Dehydrogenase/metabolism ; Models, Molecular ; Molecular Conformation ; *NAD/metabolism ; Nephropidae ; Niacinamide ; Protein Binding ; 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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  • 7
    Publication Date: 1984-09-14
    Description: The molecular structure of triostin A, a cyclic octadepsipeptide antibiotic, has been solved complexed to a DNA double helical fragment with the sequence CGTACG (C, cytosine; G, guanine; T, thymine; A, adenine). The two planar quinoxaline rings of triostin A bis intercalate on the minor groove of the DNA double helix surrounding the CG base pairs at either end. The alanine residues form hydrogen bonds to the guanines. Base stacking in the DNA is perturbed, and the major binding interaction involves a large number of van der Waals contacts between the peptides and the nucleic acid. The adenine residues in the center are in the syn conformation and are paired to thymine through Hoogsteen base pairing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, A H -- Ughetto, G -- Quigley, G J -- Hakoshima, T -- van der Marel, G A -- van Boom, J H -- Rich, A -- New York, N.Y. -- Science. 1984 Sep 14;225(4667):1115-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6474168" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallization ; DNA/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; Protein Conformation ; Quinoxalines/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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