Research Associate
Education
2016 - PhD in Biophysical Chemistry, University of Cambridge
2011 - MSci in Natural Sciences, Chemistry, UNiversity of Cambridge
2010 - Cambridge-MIT Exchange Program, Massachusetts Institute of Technology
Research Interests
Development and application of fundamental biophysical theories to data analysis in a biologically relevant context, Protein Aggregation, Biophysical Chemistry, High Throughput Screening
Selected Publications
- G Meisl, E Hidari, K Allinson, T Rittman, SL DeVos, JS Sanchez, CK Xu, KE Duff, KA Johnson, JB Rowe, BT Hyman, TPJ Knowles and D Klenerman "In vivo rate-determining steps of tau seed accumulation in Alzheimer’s disease", Science Advances 7, eabh1448 (2021)
- G Meisl, T Kurt, I Condado-Morales, C Bett, S Sorce, M Nuvolone, TCT Michaels, D Heinzer, M Avar, SIA Cohen, S Horneman, A Aguzzi, CM Dobson, CJ Sigurdson and TPJ Knowles “Scaling analysis reveals the mechanism and rates of prion replication in vivo”, Nature Structural and Molecular Biology 28, 365 (2021)
- G Meisl, TPJ Knowles, D Klenerman “The molecular processes underpinning prion-like spreading and seed amplification in protein aggregation.” Current Opinion in Neurobiology 61, 58 (2020)
- G Meisl, L Rajah, SAI Cohen, M Pfammatter, A Šarić, E Hellstrand, AK Buell, A Aguzzi, S Linse, M Vendruscolo, CM Dobson and TPJ Knowles, "Scaling behaviour and rate-determining steps in filamentous self-assembly", Chemcial Science (2017)
- G Meisl, X Yang, CM Dobson, S Linse and TPJ Knowles, "Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants", Chemical Science 8, 4352 (2017)
- G Meisl, JB Kirkegaard, P Arosio, M Vendruscolo, CM Dobson, S Linse and TPJ Knowles, “Molecular mechanisms of protein aggregation from global fitting of kinetic models”, Nature Protocols 11, 252 (2016)
- G Meisl, X Yang, E Hellstrand, B Frohm, JB Kirkegaard, SIA Cohen, CM Dobson, S Linse and TPJ Knowles, "Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides.", Proceedings of the National Academy of Sciences, 111, 9384 (2014)
Publications
Direct observation of prion protein oligomer formation reveals an aggregation mechanism with multiple conformationally distinct species.
Chemical science
(2019)
10
4588
(doi: 10.1039/c8sc05627g)
A method of predicting the in vitro fibril formation propensity of Aβ40 mutants based on their inclusion body levels in E. coli.
Scientific reports
(2019)
9
3680
(doi: 10.1038/s41598-019-39216-z)
Increased Secondary Nucleation Underlies Accelerated Aggregation of the Four-Residue N-Terminally Truncated Aβ42 Species Aβ5-42.
ACS chemical neuroscience
(2019)
10
2374
(doi: 10.1021/acschemneuro.8b00676)
Physical Determinants of Amyloid Assembly in Biofilm Formation
Mbio
(2019)
10
10.1128/mbio.02279
(doi: 10.1128/mbio.02279-18)
The presence of autoantibodies against the prion protein is independent of PRNP mutations
PRION
(2019)
13
119
Oligomer Diversity during the Aggregation of the Repeat Region of Tau
ACS Chemical Neuroscience
(2018)
9
3060
(doi: 10.1021/acschemneuro.8b00250)
Direct Observation of Murine Prion Protein Replication in Vitro.
Journal of the American Chemical Society
(2018)
140
14789
(doi: 10.1021/jacs.8b08311)
Extrinsic Amyloid-Binding Dyes for Detection of Individual Protein Aggregates in Solution
Analytical Chemistry
(2018)
90
10385
(doi: 10.1021/acs.analchem.8b02226)
Multistep Inhibition of α-Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine
ACS chemical biology
(2018)
13
2308
(doi: 10.1021/acschembio.8b00466)
Origin of metastable oligomers and their effects on amyloid fibril self-assembly.
Chemical Science
(2018)
9
5937
(doi: 10.1039/c8sc01479e)
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