Conformational properties of alpha-synuclein in its free and lipid-associated states.

By D. Eliezer, Esin Kutluay, R. Bussell, G. Browne. Journal of Molecular Biology, 2001

1,096 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/32eb07fae524c153b23a15729ebb5afbf8aab0e4

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Citations in the corpus

Sensitivity of secondary structure propensities to sequence differences between α‐ and γ‐synuclein: Implications for fibrillation (2006, background): “In addition, the a-synuclein 13Ca chemical shifts used here are very similar to those of Eliezer et al. (2001), which were recorded at 10°C (pH 7.4).”
Parkinson's Disease Mechanisms and Models (2003, background): “Parkin, a 465 amino acid protein, contains two RINGthe protein to a stable -helical secondary structure (Davidson et al., 1998; Eliezer et al., 2001), suggesting finger domains separated by an in-between RING (IBR) finger domain at the C terminus and an ubiquitin-likethat membrane binding elicits a…”
Alpha-synuclein and neurodegenerative diseases (2001, background): “Experimental studies have shown that α-synuclein can bind to lipid membranes through its amino-terminal repeats, indicating that it might be a lipid-binding protei”
Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences (2012, positive): “At the N-terminal region it harbours 7 imperfect repeats of 11 amino acids containing a KTKGEV motif which mediate formation of amphipathic a -helices upon membrane binding (Davidson et al , 1998; Eliezer et al , 2001).”
Secondary Structure of α-Synuclein Oligomers: Characterization by Raman and Atomic Force Microscopy (2006, background): “Our previous Raman data of monomeric a-synuclein in aqueous solution suggest that the peptide bonds are distributed in both a-helical and extended b-regions,(13) consistent with the NMR observations of N-terminal residues with a-helical propensity.(14) During a-synuclein fibril formation, the protei”
Helix periodicity, topology, and dynamics of membrane‐associated α‐Synuclein (2005, background): “The membrane-associated structure of aS is divided into an N-terminal membrane-binding region and a C-terminal membrane-free tail in the presence of either SDS micelles or lipid vesicles (Eliezer et al. 2001).”
Intrinsically disordered proteins in human diseases: introducing the D2 concept. (2008, background): “In agreement with this conclusion, a high-resolution NMR analysis of the protein revealed that α-synuclein is largely unfolded in a solution but exhibits a region between residues 6 and 37 with a preference for helical conformation (46).”