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  • Macmillan Magazines Ltd.  (2)
  • Wiley-Blackwell  (1)
  • 1995-1999  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Alzheimer's disease The ins and outs of amyloid- β (1997)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 389 (1997), S. 677-678 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The devastating consequences of Alzheimer's disease — marked by extracellular senile plaques with fibrils of amyloid-β peptide (Aβ) and intraneuronal tangles of polymerized tau protein — are experienced by more and more elderly people in the Western world. The latest step ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/39479
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Spongiform encephalopathies Tracking turncoat prion proteins (1997)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 388 (1997), S. 228-229 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The persistent fear that bovine spongiform encephalopathy (BSE, or ‘mad cow’ disease) has crossed species barriers into humans and other animals has increased the pressure on scientists to come up with a molecular explanation for infectivity. Two in vitro experiments, one assaying the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/388228a0
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    A synthetic substrate assay for the gamma-secretase of the β-A4 amyloid of alzheimer's disease (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 1 (1995), S. 132-139 
    Details
    ISSN: 1075-2617
    Keywords: βA4 amyloid peptide ; radiometric assay ; transmembrane peptide ; reverse-phase TLC ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: γ-secretase, the endoprotease which releases the C-terminus of βA4 amyloid peptide, cleaves within the hydrophobic transmembrane domain of the amyloid precursor protein. In order to obtain a substrate for γ-secretase, a dodecapeptide which spans the cleavage site was synthesized, labelled with 125-iodine and conjugated to an agarose gel. A radiometric solid-phase assay was developed using this immobilized substrate. Peptide products were separated by reverse-phase HPLC and TLC to allow characterization of the cleavage site(s).
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.310010205
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    Paper (German National Licenses)
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