Rate My Professor Regina Murphy

Murphy's research specialized in protein misfolding and aggregation associated with neurodegenerative disorders like Alzheimer’s and Huntington’s diseases. Her investigations encompassed amyloid fibrillar aggregates of cross-beta sheet structure, beta-amyloid (Aβ) aggregation mechanisms, transthyretin (TTR)'s role in regulating Aβ aggregation and toxicity, heterotypic interactions in amyloid regulatory networks, self-association of polyglutamine-containing peptides, and the role of water and dehydration in fibril assembly. She also studied aggregation of polyasparagine peptides. Murphy's influential publications include "Solvent effects on self-assembly of beta-amyloid peptide" (1995, 389 citations), "A mathematical model of the kinetics of β-amyloid fibril growth from the denatured state" (2001, 349 citations), "A strategy for designing inhibitors of β-amyloid toxicity" (1996, 314 citations), "Correlation of β-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes" (2000, 313 citations), and "Recognition sequence design for peptidyl modulators of β-amyloid aggregation and toxicity" (1999, 303 citations). Her work has had substantial impact in biophysical chemistry and biomedical engineering, reflected in her affiliations and mentorship of graduate students emphasizing rigorous scientific inquiry. Murphy received honors such as the Chancellor’s Distinguished Teaching Award, Fellowship in the American Institute for Medical and Biological Engineering, and the Vilas Faculty Mid-Career Investigator Award.