Alpha-synuclein pore forming activity upon membrane association (Articolo in rivista)

Type
Label
  • Alpha-synuclein pore forming activity upon membrane association (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.bbamem.2012.07.007 (literal)
Alternative label
  • Tosatto L; Andrighetti AO; Plotegher N; Antonini V; Tessari I; Ricci L; Bubacco; Dalla Serra M (2012)
    Alpha-synuclein pore forming activity upon membrane association
    in Biochimica et biophysica acta. Biomembranes; Elsevier, Amsterdam (Paesi Bassi)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Tosatto L; Andrighetti AO; Plotegher N; Antonini V; Tessari I; Ricci L; Bubacco; Dalla Serra M (literal)
Pagina inizio
  • 2876 (literal)
Pagina fine
  • 2883 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.sciencedirect.com/science/article/pii/S0005273612002398 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 1818 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 11 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biofisica, Consiglio Nazionale delle Ricerche & Fondazione Bruno Kessler, Trento, Italy; Department of Physics, University of Trento, Trento, Italy; Department of Biology, University of Padova, Padova, Italy (literal)
Titolo
  • Alpha-synuclein pore forming activity upon membrane association (literal)
Abstract
  • Alpha-synuclein is a natively unfolded protein widely expressed in neurons at the presynaptic level. It is linked to Parkinson's disease by two lines of evidence: amyloid fibrils of the protein accumulate in patients' brains and three genetic mutants cause autosomal dominant forms of the disease. The biological role of the protein and the mechanisms involved in the etiopathogenesis of Parkinson's disease are still unknown. Membrane binding causes the formation of an amphipathic alpha-helix, which lies on the surface without crossing the bilayer. Recent observations however reported that the application of a voltage induces a pore-like activity of alpha-synuclein. This study aims to characterize the pore forming activity of the protein starting from its monomeric form. In particular, experiments with planar lipid membranes allowed recording of conductance activity bursts with a defined and reproducible fingerprint. Additional experiments with deletion mutants and covalently bound alpha-synuclein dimers were performed to understand both pore assembly and stoichiometry. The information acquired allowed formulation of a model for pore formation at different conductance levels. (literal)
Editore
Prodotto di
Autore CNR
Insieme di parole chiave

Incoming links:


Prodotto
Autore CNR di
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
Editore di
Insieme di parole chiave di
data.CNR.it