Research Associate
Education
10/2013 - present University of Cambridge, UK
Doctor of Philosophy (PhD)
10/2011 - 09/2013 Ludwigs-Maximilians-University Munich, Germany
Master of Science Biochemistry
10/2008 - 09/2011 Bielefeld University, Germany
Bachelor of Science Biochemistry
Selected Scholarships
Boehringer Ingelheim Fonds
Bayer Science & Education Foundation
German National Merit Foundation
Publications
An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils
– Elife
(2019)
8,
e46112
(doi: 10.7554/eLife.46112)
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
– Nature communications
(2019)
10,
1541
(doi: 10.1038/s41467-019-09477-3)
Increased Secondary Nucleation Underlies Accelerated Aggregation of the Four-Residue N-Terminally Truncated Aβ42 Species Aβ5-42.
– ACS Chem Neurosci
(2019)
10,
2374
(doi: 10.1021/acschemneuro.8b00676)
Mapping Surface Hydrophobicity of α-Synuclein Oligomers at the Nanoscale.
– Nano letters
(2018)
18,
7494
(doi: 10.1021/acs.nanolett.8b02916)
Quantifying Co-Oligomer Formation by Alpha-Synuclein
– ACS Nano
(2018)
12,
10855
(doi: 10.1021/acsnano.8b03575)
Nanoscopic Characterisation of Individual Endogenous Protein Aggregates in Human Neuronal Cells.
– Chembiochem : a European journal of chemical biology
(2018)
19,
2033
(doi: 10.1002/cbic.201800209)
Multistep Inhibition of α-Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine
– ACS Chem Biol
(2018)
13,
2308
(doi: 10.1021/acschembio.8b00466)
Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic α-Synuclein Oligomers.
– Cell reports
(2018)
23,
3492
(doi: 10.1016/j.celrep.2018.05.074)
Optical Structural Analysis of Individual α‐Synuclein Oligomers
– Angewandte Chemie
(2018)
130,
4980
(doi: 10.1002/ange.201710779)
Hsp70 Inhibits the Nucleation and Elongation of Tau and Sequesters Tau Aggregates with High Affinity.
– ACS Chem Biol
(2018)
13,
636
(doi: 10.1021/acschembio.7b01039)
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