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Impact of GM1 on Membrane-Mediated Aggregation/Oligomerization of β-Amyloid: Unifying View
M. Cebecauer, M. Hof, M. Amaro,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, přehledy
NLK
Cell Press Free Archives
od 1960-01-01 do Před 1 rokem
Free Medical Journals
od 1960 do Před 1 rokem
Freely Accessible Science Journals
od 1960 do Před 12 měsíci
PubMed Central
od 1960 do Před 1 rokem
Europe PubMed Central
od 1960 do Před 1 rokem
Open Access Digital Library
od 1960-09-01
Elsevier Open Access Journals
od 1960-09-01 do 2018-02-06
Elsevier Open Archive Journals
od 1960-09-01 do Před 1 rokem
- MeSH
- amyloidní beta-protein chemie metabolismus MeSH
- G(M1) gangliosid chemie metabolismus MeSH
- lidé MeSH
- mozek metabolismus MeSH
- patologická konformace proteinů metabolismus MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- přehledy MeSH
In this perspective we summarize current knowledge of the effect of monosialoganglioside GM1 on the membrane-mediated aggregation of the β-amyloid (Aβ) peptide. GM1 has been suggested to be actively involved in the development of Alzheimer's disease due to its ability to seed the aggregation of Aβ. However, GM1 is known to be neuroprotective against Aβ-induced toxicity. Here we suggest that the two scenarios are not mutually exclusive but rather complementary, and might depend on the organization of GM1 in membranes. Improving our understanding of the molecular details behind the role of gangliosides in neurodegenerative amyloidoses might help in developing disease-modifying treatments.
Citace poskytuje Crossref.org
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- $a Cebecauer, Marek $u Department of Biophysical Chemistry, J. Heyrovský Institute of Physical Chemistry of the Czech Academy of Sciences, v.v.i., Prague, Czech Republic.
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- $a In this perspective we summarize current knowledge of the effect of monosialoganglioside GM1 on the membrane-mediated aggregation of the β-amyloid (Aβ) peptide. GM1 has been suggested to be actively involved in the development of Alzheimer's disease due to its ability to seed the aggregation of Aβ. However, GM1 is known to be neuroprotective against Aβ-induced toxicity. Here we suggest that the two scenarios are not mutually exclusive but rather complementary, and might depend on the organization of GM1 in membranes. Improving our understanding of the molecular details behind the role of gangliosides in neurodegenerative amyloidoses might help in developing disease-modifying treatments.
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- $a Amaro, Mariana $u Department of Biophysical Chemistry, J. Heyrovský Institute of Physical Chemistry of the Czech Academy of Sciences, v.v.i., Prague, Czech Republic. Electronic address: amaro@jh-inst.cas.cz.
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