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  • Calcitriol/analogs & derivatives/pharmacology  (1)
  • Key words. Amyloid; amyloidosis; fibrils; protofilaments; Alzheimer's disease; spongiform encephalopathies; fibre diffraction; cross-β conformation.  (1)
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  • 1
    Publication Date: 1982-07-30
    Description: As shown previously, laying hens given 1,25-dihydroxyvitamin D3 as their sole source of vitamin D produce fertile eggs having normal shells, but only 35 to 55 percent of the embryos are normal. Giving these hens additional 25-hydroxyvitamin D3, 24,25-dihydroxyvitamin D3, or 24,24-difluoro-25-hydroxyvitamin D3 at 1.25 nanomoles per day resulted in 90 to 100 percent normal embryos, and hence, hatchability. Since 24,24-difluoro-25-hydroxyvitamin D3 cannot be 24-hydroxylated, 24-hydroxylation is not required for this function of 25-hydroxyvitamin D3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ameenuddin, S -- Sunde, M -- DeLuca, H F -- Ikekawa, N -- Kobayashi, Y -- New York, N.Y. -- Science. 1982 Jul 30;217(4558):451-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6979782" target="_blank"〉PubMed〈/a〉
    Keywords: 24,25-Dihydroxyvitamin D 3 ; Animal Feed ; Animals ; Calcifediol ; Calcitriol/analogs & derivatives/pharmacology ; Chick Embryo/*growth & development ; Chickens/metabolism ; Dihydroxycholecalciferols/pharmacology ; Female ; Hydroxycholecalciferols/*metabolism/pharmacology ; Hydroxylation
    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
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 53 (1997), S. 871-887 
    ISSN: 1420-9071
    Keywords: Key words. Amyloid; amyloidosis; fibrils; protofilaments; Alzheimer's disease; spongiform encephalopathies; fibre diffraction; cross-β conformation.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Amyloidoses are diseases, including some currently prominent such as Alzheimer's disease, bovine spongiform encephalophaty (BSE) and Type II diabetes, in which soluble proteins are deposited in a specific, highly stable, fibrillar form. The amyloid fibrils are made up of protofilaments whose molecular structure is composed of pairs of β-sheets in a helical form that allows them to be continuously hydrogen-bonded along the length of the fibril. The observation that similar fibrils are generated from different proteins indicates that fibril formation is accompanied by structural conversion. The transmissible spongiform encephalopathies, such as BSE and kuru, involve an infectious agent identified with the prion protein. The properties of the agent are more consistent with prion amyloid than the protein itself, suggesting infectivity in these diseases is equivalent to the 'seeding' of amyloid fibrils at a new site.
    Type of Medium: Electronic Resource
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