Monomer-dependent secondary nucleation in amyloid formation
Author:
Funder
ERC
Swedish Research Council (VR)
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology,Biophysics
Link
http://link.springer.com/article/10.1007/s12551-017-0289-z/fulltext.html
Reference73 articles.
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2. Abelein A, Jarvet J, Barth A, Gräslund A, Danielsson J (2016) Ionic strength modulation of the free energy landscape of Aβ40 peptide fibril formation. J Am Chem Soc 138:6893–6902. doi: 10.1021/jacs.6b04511
3. Anfinsen CB (1973) Principles that govern the folding of protein chains. Science 181:223–230
4. Antzutkin ON, Balbach JJ, Leapman RD, Rizzo NW, Reed J, Tycko R (2000) Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer’s beta-amyloid fibrils. Proc Natl Acad Sci USA 97:13045–13050. doi: 10.1073/pnas.230315097
5. Anwar J, Khan S, Lindfors L (2015) Secondary crystal nucleation: nuclei breeding factory uncovered. Angew Chem Int Ed Engl 54:14681–14684. doi: 10.1002/anie.201501216
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