| A new era for understanding amyloid structures and disease MG Iadanza, MP Jackson, EW Hewitt, NA Ranson, SE Radford Nature reviews Molecular cell biology 19 (12), 755-773, 2018 | 992 | 2018 |
| Three-dimensional electron crystallography of protein microcrystals D Shi, BL Nannenga, MG Iadanza, T Gonen Elife 2, e01345, 2013 | 448 | 2013 |
| Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM MG Iadanza, AJ Higgins, B Schiffrin, AN Calabrese, DJ Brockwell, ... Nature communications 7 (1), 12865, 2016 | 214 | 2016 |
| Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE G Wisedchaisri, MS Park, MG Iadanza, H Zheng, T Gonen Nature communications 5 (1), 4521, 2014 | 155 | 2014 |
| Variations on negative stain electron microscopy methods: tools for tackling challenging systems CA Scarff, MJG Fuller, RF Thompson, MG Iadaza Journal of visualized experiments: JoVE, 57199, 2018 | 154 | 2018 |
| The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism MG Iadanza, R Silvers, J Boardman, HI Smith, TK Karamanos, ... Nature Communications 9 (1), 4517, 2018 | 145 | 2018 |
| pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers KW Tipping, TK Karamanos, T Jakhria, MG Iadanza, SC Goodchild, ... Proceedings of the National Academy of Sciences 112 (18), 5691-5696, 2015 | 133 | 2015 |
| Engineering the surface properties of a human monoclonal antibody prevents self-association and rapid clearance in vivo CL Dobson, PWA Devine, JJ Phillips, DR Higazi, C Lloyd, B Popovic, ... Scientific reports 6 (1), 38644, 2016 | 131 | 2016 |
| The structure of purified kinetochores reveals multiple microtubule-attachment sites S Gonen, B Akiyoshi, MG Iadanza, D Shi, N Duggan, S Biggins, T Gonen Nature structural & molecular biology 19 (9), 925-929, 2012 | 108 | 2012 |
| Collection, pre-processing and on-the-fly analysis of data for high-resolution, single-particle cryo-electron microscopy RF Thompson, MG Iadanza, EL Hesketh, S Rawson, NA Ranson Nature protocols 14 (1), 100-118, 2019 | 104 | 2019 |
| A cryo-EM grid preparation device for time-resolved structural studies D Kontziampasis, DP Klebl, MG Iadanza, CA Scarff, F Kopf, F Sobott, ... IUCrJ 6 (6), 1024-1031, 2019 | 101 | 2019 |
| Fibril structures of diabetes-related amylin variants reveal a basis for surface-templated assembly R Gallardo, MG Iadanza, Y Xu, GR Heath, R Foster, SE Radford, ... Nature structural & molecular biology 27 (11), 1048-1056, 2020 | 92 | 2020 |
| Biologically active peptidomimetic macrocycles HM Nash, R Kapeller-Libermann, TK Sawyer, N Kawahata, V Guerlavais, ... US Patent App. 12/420,816, 2009 | 86 | 2009 |
| Methods for preparing purified polypeptide compositions HM Nash, M Iadanza, C Leitheiser, N Kawahata US Patent 9,206,223, 2015 | 69 | 2015 |
| Biologically active peptidomimetic macrocycles HM Nash, R Kapeller-Libermann, TK Sawyer, N Kawahata, V Guerlavais, ... US Patent App. 13/570,146, 2013 | 56 | 2013 |
| Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs MG Iadanza, B Schiffrin, P White, MA Watson, JE Horne, AJ Higgins, ... Communications Biology 3 (1), 766, 2020 | 45 | 2020 |
| Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane MJ Byrne, MG Iadanza, MA Perez, DP Maskell, RM George, EL Hesketh, ... Nature communications 12 (1), 2791, 2021 | 44 | 2021 |
| Methods to account for movement and flexibility in cryo-EM data processing S Rawson, MG Iadanza, NA Ranson, SP Muench Methods 100, 35-41, 2016 | 44 | 2016 |
| Biologically active peptidomimetic macrocycles HM Nash, R Kapeller-Libermann, TK Sawyer, N Kawahata, V Guerlavais, ... US Patent App. 14/156,350, 2014 | 43 | 2014 |
| Overview of electron crystallography of membrane proteins: crystallization and screening strategies using negative stain electron microscopy BL Nannenga, MG Iadanza, BS Vollmar, T Gonen Current protocols in protein science 72 (1), 17.15. 1-17.15. 11, 2013 | 38 | 2013 |
Neil A RansonAstbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University ofZweryfikowany adres z leeds.ac.uk