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
Templating S100A9 amyloids on Aβ fibrillar surfaces revealed by charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses
– Chemical science
(2020)
11,
7031
(doi: 10.1039/c9sc05905a)
Identification of on- And off-pathway oligomers in amyloid fibril formation
– Chemical science
(2020)
11,
6236
(doi: 10.1039/c9sc06501f)
Continuous population-level monitoring of SARS-CoV-2 seroprevalence in a large metropolitan region
(2020)
2020.05.31.20118554
(doi: 10.1101/2020.05.31.20118554)
Templating S100A9 amyloids on Aβ fibrillar surfaces revealed by charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses
(2020)
2020.05.26.116400
(doi: 10.1101/2020.05.26.116400)
Ultrastructural evidence for self-replication of alzheimer-associated Aβ42 amyloid along the sides of fibrils
– Proceedings of the National Academy of Sciences of the United States of America
(2020)
117,
11265
(doi: 10.1073/pnas.1918481117)
Kinetic diversity of amyloid oligomers.
– Proceedings of the National Academy of Sciences of the United States of America
(2020)
117,
12087
(doi: 10.1073/pnas.1922267117)
Author Correction: Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide (Nature Chemistry, (2020), 12, 5, (445-451), 10.1038/s41557-020-0452-1)
– Nature chemistry
(2020)
12,
497
(doi: 10.1038/s41557-020-0468-6)
Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide
– Nature Chemistry
(2020)
12,
445
(doi: 10.1038/s41557-020-0452-1)
The Influence of Pathogenic Mutations in α-Synuclein on Biophysical and Structural Characteristics of Amyloid Fibrils
– ACS nano
(2020)
14,
5213
(doi: 10.1021/acsnano.9b09676)
Effects of sedimentation, microgravity, hydrodynamic mixing and air–water interface on α-synuclein amyloid formation
– Chem Sci
(2020)
11,
3687
(doi: 10.1039/d0sc00281j)
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