A century-old debate on protein aggregation and neurodegeneration enters the clinic

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Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences (2012, neutral): “It has now widely been accepted that not the ﬁnal ﬁbrillar a -synuclein aggregates but rather oligomeric preﬁbrillar folding intermediates are the major toxic species (reviewed in Lansbury and Lashuel, 2006; Cookson and van der Brug, 2008; and Winklhofer et al , 2008).”
Mutations in UBQLN2 cause dominant X-linked juvenile and adult onset ALS and ALS/dementia (2011, neutral): “Protein aggregates or inclusions have been recognized as a pathological hallmark of several neurodegenerative disorders, such as extra-cellular amyloid-b plaques and intracellular tau neurofibrillary tangles in Alzheimer’s disease, and a -synuclein-containing Lewy bodies in Parkinson’s disease 16 .”
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers (2008, background): “Determining the role of these so-called 'prefibrillar' species in the amyloid-assembly process is of paramount importance, as they have been variously proposed to be responsible for toxicity associated with protein misfolding [ 6 ].”