G. Maglia

This study investigates protein translocation through nanopores, finding that blob-like structures form during transport, and identifies conditions for single-file transport.

This paper introduces an engineered electroosmotic flow to transport unfolded proteins across nanopores for non-enzymatic identification and sequencing.

This study designs α-helical peptides that self-assemble into transmembrane barrel pores, effectively killing antibiotic-resistant bacteria with low human cell toxicity.

This paper describes the fabrication of a multi-component nanopore sensor that unfolds, processes, and recognizes single proteins using a 28-component proteasome-nanopore complex.

The paper shows that substrate binding and turnover modulate the affinity landscape of DHFR to enhance catalytic efficiency by inducing allosteric changes and energy-driven conformational switches.

This study develops a continuum model of the nanopore ClyA to simulate ion and water transport, revealing how ionic strength and voltage affect conductance and electro-osmotic flow.

This paper determines the structures of Aβ(1-42) tetramers and octamers in membrane-mimicking environments and identifies a new mechanism of membrane disruption via hydrophilic edge pores.