Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein.

By C. Bertoncini, Young-Sang Jung, W. Hoyer, C. Griesinger, T. Jovin, M. Zweckstetter. Proceedings of the National Academy of Sciences of the United States of America, 2005

763 citations recorded by the source corpus.

Subfields: Neurology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/8a840b91caf98dc29f365b89fe2b666a58b29f1f

Citations in the corpus

• Developing a molecular dynamics force field for both folded and disordered protein states (2018, neutral): “The benchmark includes the disordered proteins ACTR (21), drkN SH3 (22), α -synuclein (23), the N TAIL domain of the measles virus nucleoprotein (24), A β 40 (25), the ParE2-associated antitoxin PaaA2 (26), the proliferating cell nuclear antigen-associated factor p15 PAF (27), the cyclin-dependent…”
• Structural Polymorphism of 441-Residue Tau at Single Residue Resolution (2009, neutral): “Moreover, using NMR dipolar couplings a reduced mobility in regions that harbour many proline residues had been previously observed in the Cterminal tails of a- and b-synuclein [53,54].”
• Α-synuclein misfolding and Parkinson's disease. (2012, neutral): “and the region in the vicinity of residue 120 also interacted with the N terminus in the vicinity of residue 20 [46].”