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(GM1) Ganglioside Inhibits beta-Amyloid Oligomerization Induced bySphingomyelin

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F16%3A00088531" target="_blank" >RIV/00216224:14740/16:00088531 - isvavai.cz</a>

  • Result on the web

    <a href="http://onlinelibrary.wiley.com/doi/10.1002/anie.201603178/abstract" target="_blank" >http://onlinelibrary.wiley.com/doi/10.1002/anie.201603178/abstract</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/anie.201603178" target="_blank" >10.1002/anie.201603178</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    (GM1) Ganglioside Inhibits beta-Amyloid Oligomerization Induced bySphingomyelin

  • Original language description

    beta-Amyloid (A beta) oligomers are neurotoxic and implicated in Alzheimer's disease. Neuronal plasma membranes may mediate formation of A beta oligomers in vivo. Membrane components sphingomyelin and GM(1) have been shown to promote aggregation of A beta; however, these studies were performed under extreme, non-physiological conditions. We demonstrate that physiological levels of GM(1), organized in nanodomains do not seed oligomerization of A beta(40) monomers. We show that sphingomyelin triggers oligomerization of A beta(40) and that GM(1) is counteractive thus preventing oligomerization. We propose a molecular explanation that is supported by all-atom molecular dynamics simulations. The preventive role of GM(1) in the oligomerization of A beta(40) suggests that decreasing levels of GM(1) in the brain, for example, due to aging, could reduce protection against A beta oligomerization and contribute to the onset of Alzheimer's disease.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2016

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Angewandte Chemie International Edition

  • ISSN

    1433-7851

  • e-ISSN

  • Volume of the periodical

    55

  • Issue of the periodical within the volume

    32

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    5

  • Pages from-to

    9411-9415

  • UT code for WoS article

    000383371800055

  • EID of the result in the Scopus database