Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy.

By K. Conway, Seung Jae Lee, J. Rochet, T. T. Ding, Robin E. Williamson, P. Lansbury. Proceedings of the National Academy of Sciences of the United States of America, 2000

1,612 citations recorded by the source corpus.

Subfields: Neurology

View Paper: https://www.semanticscholar.org/paper/55d4d365c601ec7c605e1ebd5bca282d2153e1d5

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Neurology

Citations in the corpus

Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution (2003, background): “In particular, a number of reports concerning Aβ peptides, α synuclein and transthyretin indicate that these early aggregates are the most toxic species [18, 76, 77, 78, 79, 80]; in addition, the presence of such species has also been reported for huntingtin [44], and possibly the androgen receptor ”
α‐Synuclein implicated in Parkinson's disease is present in extracellular biological fluids, including human plasma (2003, background): “oligomerization, have been identified in the gene encoding α-syn (3, 4).”
Different Species of α-Synuclein Oligomers Induce Calcium Influx and Seeding (2007, background): “In vitro studies revealed that -syn aggregation is a nucleation-dependent process that occurs in a process ranging from monomer via oligomers to fibrils (Wood et al., 1999; Conway et al., 2000).”
In vivo demonstration that α-synuclein oligomers are toxic (2011, background): “Discussion It has been proposed that prefibrillar oligomers, as opposed to mature fibrils, may represent the toxic species in PD (21, 32).”
Sensitivity of secondary structure propensities to sequence differences between α‐ and γ‐synuclein: Implications for fibrillation (2006, background): “…protein is implied except in the case of mouse a-synuclein. bFibrillation propensity rank is based upon relative fibrillation propensities given in Conway et al. (1998, 2000), Rochet et al. (2000), Uversky et al. (2002), and Greenbaum et al. (2005). cCalculated by averaging GOR4 helix predictions…”
Secondary Structure of α-Synuclein Oligomers: Characterization by Raman and Atomic Force Microscopy (2006, background): “than the mature fibrils, could be pathogenic.(5,8,12) Thus, there are distinct steps in the aggregation process where intervention might be able to prevent or reverse the formation of oligomers and/or fibrils.”