NMR of α-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation

Mostrar todas las versiones(3)

The aggregation of α-synuclein is characteristic of Parkinson's disease (PD) and other neurodegenerative synucleinopathies. The 140-aa protein is natively unstructured; thus, ligands binding to the monomeric form are of therapeutic interest. Biogenic polyamines promote the aggregation of α-synu...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Fernández, C.O., Hoyer, W., Zweckstetter, M., Jares-Erijman, E.A., Subramaniam, V., Griesinger, C., Jovin, T.M.
Formato: Artículo publishedVersion
Publicado: 2004
Materias:
Amyloid
Fibrillation
Parkinson's disease
Spermine
alpha synuclein
amyloid
polyamine
spermine
article
binding site
carboxy terminal sequence
dissociation constant
ligand binding
molecular dynamics
Parkinson disease
priority journal
protein aggregation
protein folding
alpha-Synuclein
Amino Acid Sequence
Binding Sites
Fluorescent Dyes
Humans
Molecular Sequence Data
Molecular Structure
Nerve Tissue Proteins
Nuclear Magnetic Resonance, Biomolecular
Parkinson Disease
Polyamines
Protein Structure, Secondary
Synucleins
Thiazoles
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_02614189_v23_n10_p2039_Fernandez
https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_02614189_v23_n10_p2039_Fernandez_oai
Aporte de:
Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires

Ejemplares similares

Ejemplares similares