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Biochemistry|February 16, 2006
A systematic study of the effect of physiological factors on beta2-microglobulin amyloid formation at neutral pHSarah L Myers, Susan Jones, Thomas R Jahn, et al.Nature Chemical Biology|August 30, 2011
Ligand binding to distinct states diverts aggregation of an amyloid-forming proteinLucy A Woods, Geoffrey W Platt, Andrew L Hellewell, et al.Biophysical Journal|August 13, 2013
Aggregation modulators interfere with membrane interactions of β2-microglobulin fibrilsTania Sheynis, Anat Friediger, Wei-Feng Xue, et al.Journal of Neurochemistry|August 11, 2020
Monitoring alpha-synuclein oligomerization and aggregation using bimolecular fluorescence complementation assays: What you see is not always what you getBryan Frey, Abdelrahman AlOkda, Matthew P Jackson, et al.Proceedings of the National Academy of Sciences of the United States of America|November 28, 2012
Direct three-dimensional visualization of membrane disruption by amyloid fibrilsLilia Milanesi, Tania Sheynis, Wei-Feng Xue, et al.Proceedings of the National Academy of Sciences of the United States of America|April 23, 2015
pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomersKevin W Tipping, Theodoros K Karamanos, Toral Jakhria, et al.Plos One|August 8, 2014
β2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pHSophia C Goodchild, Tania Sheynis, Rebecca Thompson, et al.Chemmedchem|January 26, 2012
Synthesis and evaluation of 1-amino-6-halo-β-carbolines as antimalarial and antiprion agentsMark J Thompson, Jennifer C Louth, Susan M Little, et al.Protein Science : a Publication of the Protein Society|February 9, 2018
A peptide-display protein scaffold to facilitate single molecule force studies of aggregation-prone peptidesCiaran P A Doherty, Lydia M Young, Theodoros K Karamanos, et al.The Journal of Biological Chemistry|April 14, 2018
Conformational flexibility within the nascent polypeptide-associated complex enables its interactions with structurally diverse client proteinsEsther M Martin, Matthew P Jackson, Martin Gamerdinger, et al.Pageof 5