Confocal fluorescence anisotropy and FRAP imaging of α-synuclein amyloid aggregates in living cells

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We assessed the intracellular association states of the Parkinson's disease related protein α-synuclein (AS) in living cells by transfection with a functional recombinant mutant protein (AS-C4) bearing a tetracysteine tag binding the fluorogenic biarsenical ligands FlAsH and ReAsH, The aggregat...

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Detalles Bibliográficos
Autores principales: Roberti, M.J., Jovin, T.M., Jares-Erijman, E.
Formato: Artículo publishedVersion
Publicado: 2011
Materias:
alpha synuclein
amyloid
cysteine
FIAsH ligand
ligand
membrane protein
monomer
REAsH ligand
recombinant mutant protein
recombinant protein
tetracysteine
unclassified drug
fluorescent dye
hybrid protein
anisotropy
article
brightness
chemical structure
confocal fluorescence anisotropy
controlled study
diffusion coefficient
fluorescence microscopy
fluorescence recovery after photobleaching
genetic transfection
human
human cell
human tissue
in situ hybridization
molecular density
molecular dynamics
Parkinson disease
protein aggregation
protein structure
quantitative analysis
translation regulation
algorithm
chemistry
confocal microscopy
fluorescence
fluorescence polarization
genetics
kinetics
metabolism
methodology
mutation
single cell analysis
tumor cell line
Algorithms
alpha-Synuclein
Amyloid
Cell Line, Tumor
Cysteine
Fluorescence
Fluorescence Polarization
Fluorescence Recovery After Photobleaching
Fluorescent Dyes
Humans
Kinetics
Microscopy, Confocal
Mutation
Recombinant Fusion Proteins
Single-Cell Analysis
Transfection
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_19326203_v6_n8_p_Roberti
https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_19326203_v6_n8_p_Roberti_oai
Aporte de:
Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires

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