Research Associate
Publications
Super-resolution imaging reveals α-synuclein seeded aggregation in SH-SY5Y cells.
– Communications biology
(2021)
4,
613
(doi: 10.1038/s42003-021-02126-w)
α-Synuclein strains target distinct brain regions and cell types.
– Nature neuroscience
(2019)
23,
21
(doi: 10.1038/s41593-019-0541-x)
Direct observation of prion protein oligomer formation reveals an aggregation mechanism with multiple conformationally distinct species.
– Chem Sci
(2019)
10,
4588
(doi: 10.1039/c8sc05627g)
Filamentous Aggregates Are Fragmented by the Proteasome Holoenzyme
– Cell Rep
(2019)
26,
2140
(doi: 10.1016/j.celrep.2019.01.096)
Mapping Surface Hydrophobicity of α-Synuclein Oligomers at the Nanoscale
– Nano Lett
(2018)
18,
7494
(doi: 10.1021/acs.nanolett.8b02916)
Direct Observation of Murine Prion Protein Replication in Vitro
– J Am Chem Soc
(2018)
140,
14789
(doi: 10.1021/jacs.8b08311)
Arachidonic acid mediates the formation of abundant alpha-helical multimers of alpha-synuclein.
– Scientific reports
(2016)
6,
33928
(doi: 10.1038/srep33928)
Revealing structural changes of prion protein during conversion from α-helical monomer to β-oligomers by means of ESR and nanochannel encapsulation.
– ACS Chemical Biology
(2014)
10,
493
(doi: 10.1021/cb500765e)
Slow spontaneous α-to-β structural conversion in a non-denaturing neutral condition reveals the intrinsically disordered property of the disulfide-reduced recombinant mouse prion protein.
– Prion
(2012)
6,
489
(doi: 10.4161/pri.22217)