Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation
By Alexander K. Buell, Céline Galvagnion, Ricardo Gaspar, E. Sparr, Michele Vendruscolo, Tuomas P. J. Knowles, S. Linse, Christopher M. Dobson. Proceedings of the National Academy of Sciences of the United States of America, 2014
658 citations recorded by the source corpus.
Subfields: Biomaterials, Neurology, Physiology
View Paper: https://www.semanticscholar.org/paper/6a34d4084547fda703dd13ce344e7b13cb224548
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Biomaterials
In Neurology
In Physiology
- Christopher M. Dobson
- Fabrizio Chiti
- Michele Vendruscolo
- Tuomas P. J. Knowles
- F. Hartl
- E. K. Kim
- E. Choi
Citations in the corpus
- Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, background): “Very high quality kinetic data have now been obtained and analyzed for a range of protein systems in vitro, notably Aβ42 (163), Aβ40 (164), αs (165), polyQ-containing peptides (166), and Ure2p (167).”