Biophysical properties and cellular toxicity of covalent crosslinked oligomers of α-synuclein formed by photoinduced side-chain tyrosyl radicals

Alpha-synuclein (αS), a 140 amino acid presynaptic protein, is the major component of the fibrillar aggregates (Lewy bodies) observed in dopaminergic neurons of patients affected by Parkinson's disease. It is currently believed that noncovalent oligomeric forms of αS, arising as intermediates i...

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Detalles Bibliográficos
Autores principales:	Borsarelli, C.D., Falomir-Lockhart, L.J., Ostatná, V., Fauerbach, J.A., Hsiao, H.-H., Urlaub, H., Paleček, E., Jares-Erijman, E.A., Jovin, T.M.
Formato:	JOUR
Materias:	Neurodegeneration Oxidative stress Parkinson's disease Photocrosslinking Protein aggregation Protein photooxidation SH-SY5Y alpha synuclein oligomer tris(2,2' bipyridine)ruthenium tyrosine anion exchange chromatography article biophysics controlled study cytotoxicity fluorescence human human cell light absorption light scattering oligomerization photosensitization polyacrylamide gel electrophoresis priority journal steady state Western blotting alpha-Synuclein Ammonium Sulfate Amyloid Cell Line Cell Survival Cross-Linking Reagents Free Radicals Humans Kinetics Organometallic Compounds Oxidative Stress Photochemical Processes Photosensitizing Agents Protein Stability Tyrosine
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_08915849_v53_n4_p1004_Borsarelli
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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