Channels formed with a mutant prion protein PrP(82-146) homologous to a 7-kDa fragment in diseased brain of GSS patients
Date
2003
Authors
Bahadi, Randa
Farrelly, Peter
Kenna, Bronwyn
Kourie, Joseph
Tagliavini, Fabrizio
Forloni, Gianluigi
Salmona, Mario
Journal Title
Journal ISSN
Volume Title
Publisher
American Physiological Society
Abstract
A major prion protein (PrP) mutant that forms amyloid fibrils in the diseased brain of patients with Gerstmann-Sträussler-Scheinker syndrome (GSS) is a fragment of 7 kDa spanning from residues 81-82 to 144-153 of PrP. Analysis of ionic membrane currents,
Description
Keywords
Keywords: copper ion; ion channel; mutant protein; prion protein; rifampicin; amino acid sequence; article; Gerstmann Straussler Scheinker syndrome; human; lipid bilayer; lipid membrane; membrane current; nerve cell membrane; neurotoxicity; priority journal; sequen Amyloids; Cytotoxic proteins; Membrane-linked pathologies; Neurodegenerative diseases; Prion channels; Prion diseases; Vacuolation
Citation
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Source
American Journal of Physiology - Cell Physiology
Type
Journal article