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
Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication.
Proc Natl Acad Sci U S A
(2017)
114
6444
(doi: 10.1073/pnas.1700407114)
Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants
Chemical Science
(2017)
8
4352
(doi: 10.1039/c7sc00215g)
Physical principles of filamentous protein self-assembly kinetics.
Journal of physics. Condensed matter : an Institute of Physics journal
(2017)
29
153002
(doi: 10.1088/1361-648X/aa5f10)
Correction for Perni et al., A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity.
Proc Natl Acad Sci U S A
(2017)
114
E2543
(doi: 10.1073/pnas.1701964114)
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity
Proceedings of the National Academy of Sciences
(2017)
114
e1009
(doi: 10.1073/pnas.1610586114)
Attenuating the Toxicity of Amyloid-Beta Aggregation with Specific Species
Biophysical Journal
(2017)
112
494A
(doi: 10.1016/j.bpj.2016.11.2673)
Secondary nucleation of monomers on fibril surface dominates $\alpha$-synuclein aggregation and provides autocatalytic amyloid amplification
Quarterly reviews of biophysics
(2017)
50
e6
(doi: 10.1017/S0033583516000172)
β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces
Sci Rep
(2016)
6
36010
(doi: 10.1038/srep36010)
Physical determinants of the self-replication of protein fibrils.
Nature physics
(2016)
12
874
(doi: 10.1038/NPHYS3828)
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