Risultati scientifici

Single molecule experiments emphasize GM1 as a key player of the different cytotoxicity of structurally distinct Aβ1-42 oligomers

Anno: 2015

Autori: Calamai M., Evangelisti E., Cascella R., Parenti N., Cecchi C., Stefani M., Pavone F.

Affiliazione autori: European Laboratory for Non-linear Spectroscopy (LENS), University of Florence, Florence, Italy 50019, National Institute of Optics, National Research Council of Italy (CNR), Largo Fermi 6, 50125, Florence, Italy; Dipartimento di Scienze Biomediche Sperimentali e Clinche “Mario Serio”- Università degli Studi di Firenze, 50134, Florence, Italy; Centro Interuniversitario per lo Studio delle Malattie Neurodegenerative (CIMN), 50134, Florence, Italy

Abstract: It is well established that cytotoxic Aß oligomers are the key factor that triggers the initial tissue and cell modifications eventually culminating in the development of Alzheimer

Giornale/Rivista: BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

Volume: 1858 (2)      Da Pagina: 386  A: 392

Maggiori informazioni: We thank the Italian Ministry for Education, University and Research in the framework of the Flagship Project NANOMAX, the European Community\’s Seventh Framework Programme [FP7 2007-2013, LASERLABEUROPE GA 284464] and the Fondazione Cassa di Risparmio di Pistoia e Pescia [project no. 2014.0251].
Parole chiavi: Amyloid beta protein[1-42]; Ganglioside GM1; Oligomer; Amyloid beta protein; Amyloid beta-protein (1-42); Ganglioside GM1; Peptide fragment, Article; Biotinylation; Cell viability; Cellular distribution; Controlled study; Cytotoxicity; human; Human cell; Lipid raft; Membrane binding; Molecular interaction; Neuroblastoma cell; Priority journal; Pprotein expression; Protein localization; Cell membrane; Chemistry; metabolism; protein multimerization; tumor cell line, Amyloid beta-Peptides; Cell Line, Tumor; G(M1) Ganglioside; Humans; Membrane Microdomains; Peptide Fragments; Protein Multimerization; Alzheimer’s disease
DOI: 10.1016/j.bbamem.2015.12.009

Citazioni: 15
dati da “WEB OF SCIENCE” (of Thomson Reuters) aggiornati al: 2021-09-19
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