
Research Associate
Publications
Single-molecule imaging reveals that small amyloid-β1-42 oligomers interact with the cellular prion protein (PrP(C)).
– ChemBioChem
(2014)
15,
2515
(doi: 10.1002/cbic.201402377)
A high‐resolution structure of the EF‐hand domain of human polycystin‐2
– Protein science : a publication of the Protein Society
(2014)
23,
1301
(doi: 10.1002/pro.2513)
Structural interactions between inhibitor and substrate docking sites give insight into mechanisms of human PS1 complexes
– Structure
(2014)
22,
125
(doi: 10.1016/j.str.2013.09.018)
Structural Interactions between Inhibitor and Substrate Docking Sites Give Insight into Mechanisms of Human PS1 Complexes
– Structure (London, England : 1993)
(2013)
22,
125
(doi: 10.1016/j.str.2013.09.018)
Interactome Analyses of Mature γ-Secretase Complexes Reveal Distinct Molecular Environments of Presenilin (PS) Paralogs and Preferential Binding of Signal Peptide Peptidase to PS2
– Journal of Biological Chemistry
(2013)
288,
15352
(doi: 10.1074/jbc.M112.441840)
Single Molecule Characterization of the Interactions between Amyloid‑β Peptides and the Membranes of Hippocampal Cells
– J Am Chem Soc
(2013)
135,
1491
(doi: 10.1021/ja3103567)
Vigilin interacts with signal peptide peptidase
– Proteome Sci
(2012)
10,
33
(doi: 10.1186/1477-5956-10-33)
Investigating the Interaction Between Characterized Amyloid-Beta Oligomers and the Prion Protein Receptor in Live Cells
– Biophysical Journal
(2012)
102,
243a
(doi: 10.1016/j.bpj.2011.11.1339)
Receptor protein tyrosine phosphatases are novel components of a polycystin complex
– Biochimica et Biophysica Acta - Molecular Basis of Disease
(2011)
1812,
1225
(doi: 10.1016/j.bbadis.2010.11.006)
Single molecule imaging of amyloid-peptide and the prion protein receptor on neurons
– EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2011)
40,
151
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