Attenuated T2 relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large … K Pervushin, R Riek, G Wider, K Wüthrich Proceedings of the National Academy of Sciences 94 (23), 12366-12371, 1997 | 3095 | 1997 |
3D structure of Alzheimer's amyloid-β (1–42) fibrils T Lührs, C Ritter, M Adrian, D Riek-Loher, B Bohrmann, H Döbeli, ... Proceedings of the National Academy of Sciences 102 (48), 17342-17347, 2005 | 2421 | 2005 |
In vivo demonstration that α-synuclein oligomers are toxic B Winner, R Jappelli, SK Maji, PA Desplats, L Boyer, S Aigner, C Hetzer, ... Proceedings of the National Academy of Sciences 108 (10), 4194-4199, 2011 | 1708 | 2011 |
NMR structure of the mouse prion protein domain PrP (121–231) R Riek, S Hornemann, G Wider, M Billeter, R Glockshuber, K Wüthrich Nature 382 (6587), 180-182, 1996 | 1639 | 1996 |
NMR solution structure of the human prion protein R Zahn, A Liu, T Lührs, R Riek, C von Schroetter, F López García, ... Proceedings of the National Academy of Sciences 97 (1), 145-150, 2000 | 1391 | 2000 |
Functional amyloids as natural storage of peptide hormones in pituitary secretory granules SK Maji, MH Perrin, MR Sawaya, S Jessberger, K Vadodaria, ... Science 325 (5938), 328-332, 2009 | 1123 | 2009 |
Amyloid fibrils of the HET-s (218–289) prion form a β solenoid with a triangular hydrophobic core C Wasmer, A Lange, H Van Melckebeke, AB Siemer, R Riek, BH Meier Science 319 (5869), 1523-1526, 2008 | 1099 | 2008 |
NMR characterization of the full-length recombinant murine prion protein, mPrP (23–231) R Riek, S Hornemann, G Wider, R Glockshuber, K Wüthrich FEBS letters 413 (2), 282-288, 1997 | 970 | 1997 |
Identifying the amylome, proteins capable of forming amyloid-like fibrils L Goldschmidt, PK Teng, R Riek, D Eisenberg Proceedings of the National Academy of Sciences 107 (8), 3487-3492, 2010 | 892 | 2010 |
Atomic-resolution structure of a disease-relevant Aβ (1–42) amyloid fibril MA Wälti, F Ravotti, H Arai, CG Glabe, JS Wall, A Böckmann, P Güntert, ... Proceedings of the National Academy of Sciences 113 (34), E4976-E4984, 2016 | 836 | 2016 |
Prion (PrPSc)-specific epitope defined by a monoclonal antibody C Korth, B Stierli, P Streit, M Moser, O Schaller, R Fischer, ... Nature 390 (6655), 74-77, 1997 | 792 | 1997 |
The fold of α-synuclein fibrils M Vilar, HT Chou, T Lührs, SK Maji, D Riek-Loher, R Verel, G Manning, ... Proceedings of the National Academy of Sciences 105 (25), 8637-8642, 2008 | 676 | 2008 |
Biology of amyloid: structure, function, and regulation J Greenwald, R Riek Structure 18 (10), 1244-1260, 2010 | 668 | 2010 |
Quantitative mass imaging of single biological macromolecules G Young, N Hundt, D Cole, A Fineberg, J Andrecka, A Tyler, A Olerinyova, ... Science 360 (6387), 423-427, 2018 | 560 | 2018 |
Cryo-EM structure of alpha-synuclein fibrils R Guerrero-Ferreira, NMI Taylor, D Mona, P Ringler, ME Lauer, R Riek, ... elife 7, e36402, 2018 | 546 | 2018 |
NMR structure of the bovine prion protein F López García, R Zahn, R Riek, K Wüthrich Proceedings of the National Academy of Sciences 97 (15), 8334-8339, 2000 | 542 | 2000 |
α-Synuclein aggregation nucleates through liquid–liquid phase separation S Ray, N Singh, R Kumar, K Patel, S Pandey, D Datta, J Mahato, ... Nature chemistry 12 (8), 705-716, 2020 | 523 | 2020 |
Correlation of structural elements and infectivity of the HET-s prion C Ritter, ML Maddelein, AB Siemer, T Lührs, M Ernst, BH Meier, SJ Saupe, ... Nature 435 (7043), 844-848, 2005 | 523 | 2005 |
The activities of amyloids from a structural perspective R Riek, DS Eisenberg Nature 539 (7628), 227-235, 2016 | 467 | 2016 |
Half a century of amyloids: past, present and future PC Ke, R Zhou, LC Serpell, R Riek, TPJ Knowles, HA Lashuel, E Gazit, ... Chemical Society Reviews 49 (15), 5473-5509, 2020 | 429 | 2020 |