Publications
Expanding the solvent chemical space for self-assembly of dipeptide nanostructures.
ACS Nano
(2014)
2
1243
(doi: 10.1021/nn404237f)
Determination of Primary Nucleation Mechanisms of α-Synuclein Amyloid Aggregation
BIOPHYSICAL JOURNAL
(2014)
106
267A
Direct Observation of Heterogeneous Amyloid Fibril Growth Kinetics via Two-Color Super-Resolution Microscopy
Nano Lett
(2013)
14
339
(doi: 10.1021/nl4041093)
Three-dimensional domain swapping and supramolecular protein assembly: Insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase
Acta crystallographica. Section D, Biological crystallography
(2013)
69
2116
(doi: 10.1107/S0907444913020507)
Nanobodies raised against monomeric α-synuclein distinguish between fibrils at different maturation stages
Journal of Molecular Biology
(2013)
425
2397
(doi: 10.1016/j.jmb.2013.01.040)
A Label‐Free, Quantitative Assay of Amyloid Fibril Growth Based on Intrinsic Fluorescence
Chembiochem
(2013)
14
846
(doi: 10.1002/cbic.201300103)
Electrostatic effects in filamentous protein aggregation
Biophys J
(2013)
104
1116
(doi: 10.1016/j.bpj.2013.01.031)
A Rationally Designed Six-Residue Swap Generates Comparability in the Aggregation Behavior of α-Synuclein and β-Synuclein
Biochemistry
(2012)
51
8771
(doi: 10.1021/bi300558q)
Detailed analysis of the energy barriers for amyloid fibril growth.
Angewandte Chemie International Edition
(2012)
51
5247
(doi: 10.1002/anie.201108040)
Measuring the Kinetics of Amyloid Fibril Elongation Using Quartz Crystal Microbalances
Methods Mol Biol
(2012)
849
101
(doi: 10.1007/978-1-61779-551-0_8)
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