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Scientific Reports|March 8, 2019
A method of predicting the in vitro fibril formation propensity of Aβ40 mutants based on their inclusion body levels in E. coliKalyani Sanagavarapu, Elisabeth Nüske, Irem Nasir, et al.Communications Biology|October 12, 2019
Autocatalytic amplification of Alzheimer-associated Aβ42 peptide aggregation in human cerebrospinal fluidRebecca Frankel, Mattias Törnquist, Georg Meisl, et al.Biochemistry|January 5, 2005
Molecular organization in striated domains induced by transmembrane alpha-helical peptides in dipalmitoyl phosphatidylcholine bilayersEmma Sparr, Dragomir N Ganchev, Margot M E Snel, et al.Journal of the American Chemical Society|June 30, 2016
Atomic Resolution Structure of Monomorphic Aβ42 Amyloid FibrilsMichael T Colvin, Robert Silvers, Qing Zhe Ni, et al.The Biochemical Journal|May 3, 2014
Aβ dimers differ from monomers in structural propensity, aggregation paths and population of synaptotoxic assembliesTiernan T O'Malley, Nur Alia Oktaviani, Dainan Zhang, et al.Biochemistry|May 1, 2002
Calcium binding and thermostability of carbohydrate binding module CBM4-2 of Xyn10A from Rhodothermus marinusMaher Abou-Hachem, Eva Nordberg Karlsson, Peter J Simpson, et al.Proceedings of the National Academy of Sciences of the United States of America|May 25, 2013
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanismSamuel I A Cohen, Sara Linse, Leila M Luheshi, et al.Molecular Pharmaceutics|November 14, 2022
Structure-Based Discovery of Small-Molecule Inhibitors of the Autocatalytic Proliferation of α-Synuclein AggregatesSean Chia, Z Faidon Brotzakis, Robert I Horne, et al.Nature Chemistry|March 28, 2018
Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptideSamuel I A Cohen, Risto Cukalevski, Thomas C T Michaels, et al.Science Advances|August 12, 2022
Uncovering the universality of self-replication in protein aggregation and its link to diseaseGeorg Meisl, Catherine K Xu, Jonathan D Taylor, et al.Pageof 35