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  • *Biological Evolution
  • Signal Transduction
  • American Association for the Advancement of Science (AAAS)  (6)
  • 1980-1984  (6)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (6)
Years
Year
  • 1
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    Living with water stress: evolution of osmolyte systems (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-09-24
    Description: Striking convergent evolution is found in the properties of the organic osmotic solute (osmolyte) systems observed in bacteria, plants, and animals. Polyhydric alcohols, free amino acids and their derivatives, and combinations of urea and methylamines are the three types of osmolyte systems found in all water-stressed organisms except the halobacteria. The selective advantages of the organic osmolyte systems are, first, a compatibility with macromolecular structure and function at high or variable (or both) osmolyte concentrations, and, second, greatly reduced needs for modifying proteins to function in concentrated intracellular solutions. Osmolyte compatibility is proposed to result from the absence of osmolyte interactions with substrates and cofactors, and the nonperturbing or favorable effects of osmolytes on macromolecular-solvent interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yancey, P H -- Clark, M E -- Hand, S C -- Bowlus, R D -- Somero, G N -- New York, N.Y. -- Science. 1982 Sep 24;217(4566):1214-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7112124" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/physiology ; Animals ; *Biological Evolution ; Biological Transport, Active ; Glycerol/physiology ; Ions/physiology ; Methylamines/physiology ; Molecular Conformation ; Urea/physiology ; Water/physiology ; *Water-Electrolyte Balance
    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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    The evolution of cooperation (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-03-27
    Description: Cooperation in organisms, whether bacteria or primates, has been a difficulty for evolutionary theory since Darwin. On the assumption that interactions between pairs of individuals occur on a probabilistic basis, a model is developed based on the concept of an evolutionarily stable strategy in the context of the Prisoner's Dilemma game. Deductions from the model, and the results of a computer tournament show how cooperation based on reciprocity can get started in an asocial world, can thrive while interacting with a wide range of other strategies, and can resist invasion once fully established. Potential applications include specific aspects of territoriality, mating, and disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Axelrod, R -- Hamilton, W D -- New York, N.Y. -- Science. 1981 Mar 27;211(4489):1390-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7466396" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Cooperative Behavior ; *Game Theory ; Humans ; Mathematics ; Models, Biological ; Selection, Genetic
    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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    Molecular drive (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-12-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dover, G A -- Strachan, T -- Coen, E S -- Brown, S D -- New York, N.Y. -- Science. 1982 Dec 10;218(4577):1069.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7146894" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; DNA/*genetics ; Genes ; Humans
    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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    Heritable true fitness and bright birds: a role for parasites? (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-10-22
    Description: Combination of seven surveys of blood parasites in North American passerines reveals weak, highly significant association over species between incidence of chronic blood infections (five genera of protozoa and one nematode) and striking display (three characters: male "brightness," female "brightness," and male song). This result conforms to a model of sexual selection in which (i) coadaptational cycles of host and parasites generate consistently positive offspring-on-parent regression of fitness, and (ii) animals choose mates for genetic disease resistance by scrutiny of characters whose full expression is dependent on health and vigor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamilton, W D -- Zuk, M -- New York, N.Y. -- Science. 1982 Oct 22;218(4570):384-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7123238" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Animals ; Behavior, Animal/physiology ; *Biological Evolution ; Birds/genetics/*parasitology ; Pigmentation ; Polymorphism, Genetic
    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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    Mouse globin system: a functional and evolutionary analysis (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: Structural and functional analysis of the mouse alpha-globin and beta-globin genes reveals that the globin genes are encoded in discontinous bits of coding information and that each gene locus is much more complex than was originally supposed. Each seems to consist of an array of several authentic genes as well as several apparently inactive pseudogenes. Comparison of the sequences of some of these genes to one another indicates that chromosomal DNA is a dynamic structure. Flanking and intervening sequences change in two ways: quickly, by duplication and extensive insertions and deletions, and slowly, by point mutation. Active coding sequences are usually limited to the slower mode of evolution. In addition to identifying fast and slow modes of evolution, it has also been possible to test the function of several signals that surround these genes and to identify those that appear to play a role in gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leder, P -- Hansen, J N -- Konkel, D -- Leder, A -- Nishioka, Y -- Talkington, C -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1336-42.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7414319" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Biological Evolution ; Genes ; Globins/*genetics ; Mice ; Nucleic Acid Hybridization ; Nucleic Acid Precursors/genetics ; RNA, Messenger/genetics/metabolism
    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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  • 6
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    Lactate dehydrogenases of Atlantic hagfish: physiological and evolutionary implications of a primitive heart isozyme (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-02-15
    Description: Isozymes of lactate dehydrogenase from heart and muscle of Atlantic hagfish show less functional divergence than those from other fishes and higher vertebrates. The enzyme from hagfish heart (B4) displays a higher Michaelis constant for pyruvate and lower substrate inhibition at moderate pyruvate concentrations than heart isozymes from other species. These properties support the hypothesis that the ancestral vertebrate lactate dehydrogenase was a muscle (A4)-type enzyme and also suggest a role for the B4 enzyme in the unusual physiology of hagfish cardiac tissue which functions under sustained hypoxic conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sidell, B D -- Beland, K F -- New York, N.Y. -- Science. 1980 Feb 15;207(4432):769-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7352286" target="_blank"〉PubMed〈/a〉
    Keywords: Anaerobiosis ; Animals ; *Biological Evolution ; Energy Metabolism ; Fishes/genetics/*physiology ; Genes ; Isoenzymes ; Kinetics ; L-Lactate Dehydrogenase/*genetics/metabolism ; Muscles/*enzymology ; Myocardium/enzymology ; Pyruvates/metabolism
    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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