Neil A Ranson
Neil A Ranson
Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of
Verified email at - Homepage
Cited by
Cited by
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
Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy
S Chen, AM Roseman, AS Hunter, SP Wood, SG Burston, NA Ranson, ...
Nature 371 (6494), 261-264, 1994
ATP-bound states of GroEL captured by cryo-electron microscopy
NA Ranson, GW Farr, AM Roseman, B Gowen, WA Fenton, AL Horwich, ...
Cell 107 (7), 869-879, 2001
An introduction to sample preparation and imaging by cryo-electron microscopy for structural biology
RF Thompson, M Walker, CA Siebert, SP Muench, NA Ranson
Methods 100, 3-15, 2016
Secretin PulD: association with pilot PulS, structure, and ion-conducting channel formation
N Nouwen, N Ranson, H Saibil, B Wolpensinger, A Engel, A Ghazi, ...
Proceedings of the National Academy of Sciences 96 (14), 8173-8177, 1999
Biochemical Journal 333 (2), 233-242, 1998
Multivalent binding of nonnative substrate proteins by the chaperonin GroEL
GW Farr, K Furtak, MB Rowland, NA Ranson, HR Saibil, T Kirchhausen, ...
Cell 100 (5), 561-573, 2000
The origins and consequences of asymmetry in the chaperonin reaction cycle
SG Burston, NA Ranson, AR Clarke
Journal of molecular biology 249 (1), 138-152, 1995
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
Allosteric signaling of ATP hydrolysis in GroEL–GroES complexes
NA Ranson, DK Clare, GW Farr, D Houldershaw, AL Horwich, HR Saibil
Nature structural & molecular biology 13 (2), 147-152, 2006
Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds
NA Ranson, NJ Dunster, SG Burston, AR Clarke
Journal of molecular biology 250 (5), 581-586, 1995
The chaperonin folding machine
HR Saibil, NA Ranson
Trends in biochemical sciences 27 (12), 627-632, 2002
Amyloid structures: much more than just a cross-β fold
R Gallardo, NA Ranson, SE Radford
Current opinion in structural biology 60, 7-16, 2020
The three-dimensional structure of genomic RNA in bacteriophage MS2: implications for assembly
K Toropova, G Basnak, R Twarock, PG Stockley, NA Ranson
Journal of molecular biology 375 (3), 824-836, 2008
Approaches to altering particle distributions in cryo-electron microscopy sample preparation
I Drulyte, RM Johnson, EL Hesketh, DL Hurdiss, CA Scarff, SA Porav, ...
Acta Crystallographica Section D: Structural Biology 74 (6), 560-571, 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
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
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
Packaging signals in single-stranded RNA viruses: nature’s alternative to a purely electrostatic assembly mechanism
PG Stockley, R Twarock, SE Bakker, AM Barker, A Borodavka, ...
Journal of biological physics 39, 277-287, 2013
Direct visualization of the small hydrophobic protein of human respiratory syncytial virus reveals the structural basis for membrane permeability
SD Carter, KC Dent, E Atkins, TL Foster, M Verow, P Gorny, M Harris, ...
FEBS letters 584 (13), 2786-2790, 2010
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