Lucy A. Woods

Advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assembly☆

S. Radford, A. Ashcroft, L. A. Woods, 2013, Biochimica et biophysica acta.

Ligand binding to distinct states diverts aggregation of an amyloid-forming protein

S. Radford, S. Homans, A. Ashcroft, 2011, Nature chemical biology.

Expanding the Repertoire of Amyloid Polymorphs by Co-polymerization of Related Protein Precursors*

S. Radford, R. Griffin, P. Stockley, 2013, The Journal of Biological Chemistry.

Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assembly.

S. Radford, A. Ashcroft, David P. Smith, 2011, Biophysical journal.

N‐terminal acetylation of α‐synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer

J. Baum, A. Ashcroft, G. M. Moriarty, 2012, Protein science : a publication of the Protein Society.

Identification of a New Zinc Binding Chemotype by Fragment Screening.

T. Peat, B. Ren, O. Dolezal, 2017, Journal of medicinal chemistry.

Native State Mass Spectrometry, Surface Plasmon Resonance, and X-ray Crystallography Correlate Strongly as a Fragment Screening Combination.

T. Peat, B. Ren, O. Dolezal, 2016, Journal of medicinal chemistry.