A. K. Buell

This study improves a DNA polymerase's ability to incorporate modified nucleotides through combinatorial mutagenesis, resulting in a 20-fold efficiency gain.

This study uses mass photometry to detect and quantify nanoscale α-synuclein phase separation, revealing its occurrence under a wider range of conditions than previously thought.

The paper improves a DNA polymerase's efficiency for unnatural nucleotide incorporation by identifying two key mutations through machine learning and mechanistic analysis.

This study shows that all tested patient-derived immunoglobulin light chains have comparable amyloidogenic potential, with proteolytic cleavage being a key determinant of in vivo aggregation.

This study uses molecular dynamics simulations to show that the Aβ42 monomer adopts a fibril-like conformation in solution, suggesting a potential role in amyloid aggregation.

The paper engineers a monomer-binding protein that inhibits α-synuclein fibril proliferation in vitro and in vivo, showing it reduces aggregates and related pathologies.

This study investigates how α-Synuclein interacts with membrane surfaces and how these interactions influence its aggregation into amyloid fibrils.