| On the lag phase in amyloid fibril formation P Arosio, TPJ Knowles, S Linse Physical Chemistry Chemical Physics 17, 7606-7618, 2015 | 860 | 2015 |
| Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology G Wei, Z Su, NP Reynolds, P Arosio, IW Hamley, E Gazit, R Mezzenga Chemical Society Reviews 46 (15), 4661-4708, 2017 | 852 | 2017 |
| Molecular mechanisms of protein aggregation from global fitting of kinetic models. G Meisl, JB Kirkegaard, P Arosio, TCT Michaels, M Vendruscolo, ... Nature Protocols 11 (2), 252-272, 2016 | 751 | 2016 |
| A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers SIA Cohen, P Arosio, J Presto, F Kurudenkandy, H Roshan Biverstal, ... Nature structural & molecular biology 22 (3), 207-213, 2015 | 446 | 2015 |
| Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide TCT Michaels, A Šarić, S Curk, K Bernfur, P Arosio, G Meisl, AJ Dear, ... Nature chemistry 12 (5), 445-451, 2020 | 315 | 2020 |
| The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation N Lorenzen, SB Nielsen, AK Buell, JD Kaspersen, P Arosio, BS Vad, ... Journal of the American Chemical Society 136 (10), 3859-3868, 2014 | 272 | 2014 |
| Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation P Arosio, TCT Michaels, S Linse, C Månsson, C Emanuelsson, J Presto, ... Nature communications 7 (1), 10948, 2016 | 257 | 2016 |
| Chemical kinetics for drug discovery to combat protein aggregation diseases P Arosio, M Vendruscolo, CM Dobson, TPJ Knowles Trends in pharmacological sciences 35 (3), 127-135, 2014 | 247 | 2014 |
| An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer’s disease J Habchi, P Arosio, M Perni, AR Costa, M Yagi-Utsumi, P Joshi, S Chia, ... Science advances 2 (2), e1501244, 2016 | 232 | 2016 |
| Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer’s disease J Habchi, S Chia, R Limbocker, B Mannini, M Ahn, M Perni, O Hansson, ... Proceedings of the National Academy of Sciences 114 (2), E200-E208, 2017 | 225 | 2017 |
| The S/T-rich motif in the DNAJB6 chaperone delays polyglutamine aggregation and the onset of disease in a mouse model V Kakkar, C Månsson, EP de Mattos, S Bergink, M van Der Zwaag, ... Molecular cell 62 (2), 272-283, 2016 | 185 | 2016 |
| Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method FA Aprile, P Sormanni, M Perni, P Arosio, S Linse, TPJ Knowles, ... Science advances 3 (6), e1700488, 2017 | 158 | 2017 |
| Secondary nucleation and elongation occur at different sites on Alzheimer’s amyloid-β aggregates T Scheidt, U Łapińska, JR Kumita, DR Whiten, D Klenerman, MR Wilson, ... Science Advances 5 (4), eaau3112, 2019 | 153 | 2019 |
| Quantification of the concentration of Aβ42 propagons during the lag phase by an amyloid chain reaction assay P Arosio, R Cukalevski, B Frohm, TPJ Knowles, S Linse Journal of the American Chemical Society 136 (1), 219-225, 2014 | 151 | 2014 |
| Microfluidic diffusion analysis of the sizes and interactions of proteins under native solution conditions P Arosio, T Mueller, L Rajah, EV Yates, FA Aprile, Y Zhang, SIA Cohen, ... ACS Nano 10, 333-341, 2016 | 134 | 2016 |
| Machine learning for biologics: opportunities for protein engineering, developability, and formulation H Narayanan, F Dingfelder, A Butté, N Lorenzen, M Sokolov, P Arosio Trends in pharmacological sciences 42 (3), 151-165, 2021 | 127 | 2021 |
| Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation C Månsson, P Arosio, R Hussein, HH Kampinga, RM Hashem, ... Journal of Biological Chemistry 289 (45), 31066-31076, 2014 | 122 | 2014 |
| Aggregation mechanism of an IgG2 and two IgG1 monoclonal antibodies at low pH: from oligomers to larger aggregates P Arosio, S Rima, M Morbidelli Pharmaceutical research 30, 641-654, 2013 | 121 | 2013 |
| Aggregation stability of a monoclonal antibody during downstream processing P Arosio, G Barolo, T Müller-Späth, H Wu, M Morbidelli Pharmaceutical research 28, 1884-1894, 2011 | 113 | 2011 |
| Scalable production and isolation of extracellular vesicles: available sources and lessons from current industrial bioprocesses C Paganini, U Capasso Palmiero, G Pocsfalvi, N Touzet, A Bongiovanni, ... Biotechnology Journal 14 (10), 1800528, 2019 | 109 | 2019 |
Tuomas KnowlesProfessor of Physical Chemistry and Biophysics, University of CambridgeПодтвержден адрес электронной почты в домене cam.ac.uk
