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Journal of the American Chemical Society|February 18, 2014
The role of stable α-synuclein oligomers in the molecular events underlying amyloid formationNikolai Lorenzen, Søren Bang Nielsen, Alexander K Buell, et al.Nature Communications|August 17, 2024
α-Synuclein oligomers form by secondary nucleationCatherine K Xu, Georg Meisl, Ewa A Andrzejewska, et al.Brain Communications|August 16, 2021
Soluble amyloid beta-containing aggregates are present throughout the brain at early stages of Alzheimer's diseaseDimitrios I Sideris, John S H Danial, Derya Emin, et al.Chemical Society Reviews|July 8, 2020
Half a century of amyloids: past, present and futurePu Chun Ke, Ruhong Zhou, Louise C Serpell, et al.Cell|May 29, 2012
Direct observation of the interconversion of normal and toxic forms of α-synucleinNunilo Cremades, Samuel I A Cohen, Emma Deas, et al.Acta Neuropathologica Communications|July 28, 2019
Soluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer's disease progressionSuman De, Daniel R Whiten, Francesco S Ruggeri, et al.Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences|March 27, 2013
Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2Li-Qiong Xu, Si Wu, Alexander K Buell, et al.Chembiochem : a European Journal of Chemical Biology|November 6, 2022
The Chromatin Regulator HMGA1a Undergoes Phase Separation in the NucleusHongjia Zhu, Masako Narita, Jerelle A Joseph, et al.Chemical Science|May 17, 2024
Molecular mechanism of α-synuclein aggregation on lipid membranes revealedAlexander J Dear, Xiangyu Teng, Sarah R Ball, et al.Nature Chemical Biology|March 20, 2024
Design of amyloidogenic peptide trapsDanny D Sahtoe, Ewa A Andrzejewska, Hannah L Han, et al.Pageof 47