Area of research
Molecular Biology · Physiology
Research interest
Our research interests are primarily focused on the investigation of the structures and properties of biological molecules, especially proteins, and their relationship to biological evolution and disease. We have particular interest in the fundamental science underlying disorders such as Alzheimer's and Parkinson's disease. In addition, however, we have recently become involved in the novel utilisation of biological molecules in materials science and nanotechnology.
Structure–Toxicity Relationship in Intermediate Fibrils from α-Synuclein Condensates
N-Terminal Acetylation of α-Synuclein Slows down Its Aggregation Process and Alters the Morphology of the Resulting Aggregates
The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells.
Systematic Activity Maturation of a Single-Domain Antibody with Non-canonical Amino Acids through Chemical Mutagenesis
Two human metabolites rescue a C. elegans model of Alzheimer's disease via a cytosolic unfolded protein response.
Cytosolic aggregation of mitochondrial proteins disrupts cellular homeostasis by stimulating the aggregation of other proteins
Publisher Correction: Two human metabolites rescue a C. elegans model of Alzheimer's disease via a cytosolic unfolded protein response.
Half a century of amyloids: past, present and future
Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide
Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies.
Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease.
ThX – a next-generation probe for the early detection of amyloid aggregates
The N-terminal Acetylation of α-Synuclein Changes the Affinity for Lipid Membranes but not the Structural Properties of the Bound State.
Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism.
Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation.
Biophysical studies of protein misfolding and aggregation in <i>in vivo</i> models of Alzheimer's and Parkinson's diseases - ERRATUM.
Biophysical studies of protein misfolding and aggregation in <i>in vivo</i> models of Alzheimer's and Parkinson's diseases.
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms.
Secondary nucleation and elongation occur at different sites on Alzheimer’s amyloid-β aggregates
Defining α-synuclein species responsible for Parkinson’s disease phenotypes in mice
Secondary nucleation and elongation occur at different sites on Alzheimer's amyloid-β aggregates.
Human pregnancy zone protein stabilizes misfolded proteins including preeclampsia- and Alzheimer’s-associated amyloid beta peptide
The metastability of the proteome of spinal motor neurons underlies their selective vulnerability in ALS
Identifying A- and P-site locations on ribosome-protected mRNA fragments using Integer Programming.
Bacterial production and direct functional screening of expanded molecular libraries for discovering inhibitors of protein aggregation.
Using Tetracysteine-Tagged TDP-43 with a Biarsenical Dye To Monitor Real-Time Trafficking in a Cell Model of Amyotrophic Lateral Sclerosis
Probing the dynamic stalk region of the ribosome using solution NMR.
Small molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer’s disease
ThX – A next-generation probe for the early detection of amyloid aggregates
The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity