Secondary Structure of α-Synuclein Oligomers: Characterization by Raman and Atomic Force Microscopy
By Mihaela M. Apetri, N. Maiti, M. Zagorski, P. Carey, V. Anderson. 2006
268 citations recorded by the source corpus.
Subfields: Neurology
View Paper: https://www.semanticscholar.org/paper/4849e33edb22ecdbf817e5b0a9334983ebe1a407
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In Neurology
Citations in the corpus
- Different Species of α-Synuclein Oligomers Induce Calcium Influx and Seeding (2007, result): “This is consistent with observations of other groups (Conway et al., 2000; Rochet et al., 2000; Volles et al., 2001; Hoyer et al., 2004; Apetri et al., 2006), although these studies were performed with far higher protein concentrations.”
- Α-synuclein misfolding and Parkinson's disease. (2012, background): “found that oligomers formed at the early stages of α-synuclein aggregation are primarily α-helical [81].”
- Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein (2012, methodology): “Structural studies on aS oligomers have also been carried out using FTIR, Raman, CD, and fluorescence spectroscopy (see, e.g., Apetri et al., 2006; Goldberg and Lansbury, 2000; Hong et al., 2008; Nath et al., 2010; Thirunavukkuarasu et al., 2008), which have revealed the formation of various…”
- Toll-like receptor 4 is required for α-synuclein dependent activation of microglia and astroglia (2013, methodology): “Fluorescence emission spectra were immediately recorded at 465–600 nm with excitation at 440 nm as described elsewhere (Apetri et al., 2006).”