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Nature Structural & Molecular Biology|October 10, 2020
Author Correction: Fibril structures of diabetes-related amylin variants reveal a basis for surface-templated assemblyRodrigo Gallardo, Matthew G Iadanza, Yong Xu, et al.Nature Communications|October 1, 2016
Lateral opening in the intact β-barrel assembly machinery captured by cryo-EMMatthew G Iadanza, Anna J Higgins, Bob Schiffrin, 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.Nature Communications|October 31, 2018
The structure of a β<sub>2</sub>-microglobulin fibril suggests a molecular basis for its amyloid polymorphismMatthew G Iadanza, Robert Silvers, Joshua Boardman, et al.Iucrj|November 12, 2019
A cryo-EM grid preparation device for time-resolved structural studiesDimitrios Kontziampasis, David P Klebl, Matthew G Iadanza, et al.Nature Communications|May 15, 2021
Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membraneMatthew J Byrne, Matthew G Iadanza, Marcos Arribas Perez, et al.Communications Biology|December 15, 2020
Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscsMatthew G Iadanza, Bob Schiffrin, Paul White, et al.Nature Communications|July 8, 2021
The role of membrane destabilisation and protein dynamics in BAM catalysed OMP foldingPaul White, Samuel F Haysom, Matthew G Iadanza, et al.Scientific Reports|December 21, 2016
Engineering the surface properties of a human monoclonal antibody prevents self-association and rapid clearance in vivoClaire L Dobson, Paul W A Devine, Jonathan J Phillips, et al.Pageof 2