Partitioning and confinement of GM1 ganglioside induced by amyloid aggregates

FEBS Letters

Volumn 587, Issue 9, 2013, Pages 1385-1391

  Calamai, Martino ^a,b   Pavone, Francesco S ^b,c,d,e  

^a CNR   (Italy)

^b UNIVERSITY OF FLORENCE   (Italy)

^c UNIVERSITY OF FLORENCE   (Italy)

^d ISTITUTO NAZIONALE DI OTTICA   (Italy)

^e International Center of Computational Neurophotonics   (Italy)

Author keywords

Keywords GM1 A 1 42 Amylin Single particle tracking Lateral diffusion

Indexed keywords

AMYLIN; AMYLOID BETA PROTEIN[1-42]; GANGLIOSIDE GM1; GEPHYRIN; GLYCINE RECEPTOR; OLIGOMER;

ANTIBODY LABELING; ARTICLE; BINDING AFFINITY; CELL MEMBRANE; CONTROLLED STUDY; HUMAN; HUMAN CELL; NEUROBLASTOMA CELL; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION;

AMYLOID BETA-PEPTIDES; ANIMALS; BIOLOGICAL TRANSPORT; CELL LINE, TUMOR; CELL SURVIVAL; DIFFUSION; G(M1) GANGLIOSIDE; HUMANS; ISLET AMYLOID POLYPEPTIDE; MEMBRANE MICRODOMAINS; PEPTIDE FRAGMENTS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; TIME FACTORS;

EID: 84876472619     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.03.014     Document Type: Article

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