- Works count
- 602
- Citation count
- 26,695
- H-index
- 83
- i10-index
- 358
Research interests
Publications
Half a century of amyloids: past, present and future
Chemical Society Reviews · 2020 · https://doi.org/10.1039/c9cs00199a
Functional Amyloids
Cold Spring Harbor Perspectives in Biology · 2019 · https://doi.org/10.1101/cshperspect.a033860
α‐synuclein oligomers and fibrils: a spectrum of species, a spectrum of toxicities
Journal of Neurochemistry · 2019 · https://doi.org/10.1111/jnc.14808
ThT 101: a primer on the use of thioflavin T to investigate amyloid formation
Amyloid · 2017 · https://doi.org/10.1080/13506129.2017.1304905
Biosurfactants and surfactants interacting with membranes and proteins: Same but different?
Biochimica et Biophysica Acta (BBA) - Biomembranes · 2016 · https://doi.org/10.1016/j.bbamem.2016.09.024
How Epigallocatechin Gallate Can Inhibit α-Synuclein Oligomer Toxicity in Vitro
Journal of Biological Chemistry · 2014 · https://doi.org/10.1074/jbc.m114.554667
The Role of Stable α-Synuclein Oligomers in the Molecular Events Underlying Amyloid Formation
Journal of the American Chemical Society · 2014 · https://doi.org/10.1021/ja411577t
The Antimicrobial Mechanism of Action of Epsilon-Poly- l -Lysine
Applied and Environmental Microbiology · 2014 · https://doi.org/10.1128/aem.02204-14
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
Proceedings of the National Academy of Sciences · 2013 · https://doi.org/10.1073/pnas.1218402110
Protein–surfactant interactions: A tale of many states
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · 2011 · https://doi.org/10.1016/j.bbapap.2011.03.003
Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation
Proceedings of the National Academy of Sciences · 2011 · https://doi.org/10.1073/pnas.1013225108
Functional amyloid in Pseudomonas
Molecular Microbiology · 2010 · https://doi.org/10.1111/j.1365-2958.2010.07269.x
Unique Identification of Supramolecular Structures in Amyloid Fibrils by Solid‐State NMR Spectroscopy
Angewandte Chemie International Edition · 2009 · https://doi.org/10.1002/anie.200804198
p25α Relocalizes in Oligodendroglia from Myelin to Cytoplasmic Inclusions in Multiple System Atrophy
American Journal Of Pathology · 2007 · https://doi.org/10.2353/ajpath.2007.070201
Amyloid adhesins are abundant in natural biofilms
Environmental Microbiology · 2007 · https://doi.org/10.1111/j.1462-2920.2007.01418.x
Aggregation and fibrillation of bovine serum albumin
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · 2007 · https://doi.org/10.1016/j.bbapap.2007.06.008
Protein drug stability: a formulation challenge
Nature Reviews Drug Discovery · 2005 · https://doi.org/10.1038/nrd1695
The Changing Face of Glucagon Fibrillation: Structural Polymorphism and Conformational Imprinting
Journal of Molecular Biology · 2005 · https://doi.org/10.1016/j.jmb.2005.09.100
Protein Unfolding in Detergents: Effect of Micelle Structure, Ionic Strength, pH, and Temperature
Biophysical Journal · 2002 · https://doi.org/10.1016/s0006-3495(02)73982-9
The Major Birch Allergen, Bet v 1, Shows Affinity for a Broad Spectrum of Physiological Ligands
Journal of Biological Chemistry · 2002 · https://doi.org/10.1074/jbc.m202065200
Structure of the Transition State for Folding of a Protein Derived from Experiment and Simulation
Journal of Molecular Biology · 1996 · https://doi.org/10.1006/jmbi.1996.0173
The Structure of the Transition State for Folding of Chymotrypsin Inhibitor 2 Analysed by Protein Engineering Methods: Evidence for a Nucleation-condensation Mechanism for Protein Folding
Journal of Molecular Biology · 1995 · https://doi.org/10.1006/jmbi.1995.0616
Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.
Proceedings of the National Academy of Sciences · 1994 · https://doi.org/10.1073/pnas.91.22.10422
Current projects
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