title: Physiological and pathological properties of alpha-synuclein.
abstract: alpha-Synuclein belongs to a small group of natively unfolded proteins that can transiently bind to lipid membranes and acquire a partial alpha-helical conformation. Under certain pathogenic conditions, alpha-synuclein aggregates to form oligomers and insoluble fibrils with increased ss-sheet configuration. Although genetic mutations and multiplications of the gene have been found in familial cases, the mechanism by which this protein aggregates in sporadic cases of Parkinson's disease, dementia with Lewy bodies and multisystem atrophy is not fully understood. Here we review the function of alpha-synuclein and recent insight into the mechanisms by which it aggregates.
authors.affiliation: Cambridge Centre for Brain Repair and Department of Clinical Neuroscience Forvie Site, Robinson Way, Cambridge CB2 2PY, United Kingdom.
authors.forename: G K
authors.initials: GK
authors.lastname: Tofaris
authors.forename: M G
authors.initials: MG
authors.lastname: Spillantini
mesh_terms: D006801:Humans; D016631:Lewy Bodies / Q000378:metabolism; D010300:Parkinson Disease / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D051844:alpha-Synuclein / Q000737:chemistry / Q000235:genetics / Q000502:physiology*
chemical_list: D051844:alpha-Synuclein