
Research Associate
Publications
Single-MOLECULE IMAGING REVEALS THAT SMALL AMYLOID-β1-42 oligomers interact with the cellular prion protein (PrPC)
– Chembiochem : a European journal of chemical biology
(2014)
15,
2515
(doi: 10.1002/cbic.201402377)
A high‐resolution structure of the EF‐hand domain of human polycystin‐2
– Protein Science
(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.
– J Biol Chem
(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 science
(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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