Loren B. Andreas

This study determines the bilayer-bound structure of SARS-CoV-2 E protein in complex with a host PDZ domain, revealing its pentameric oligomer state and structural interactions.

This paper shows that anle138b binds to a cavity in lipidic Aβ fibrils and reduces fibril formation by 75%, suggesting a potential therapeutic mechanism for Alzheimer's disease.

This study identifies two binding sites of the PET tracer MODAG-005 on lipidic α-synuclein fibrils, with the cavity site being more stable and selectively occupied under certain conditions.

The paper investigates the transmembrane signaling mechanism of the CitA histidine kinase using structural biology techniques and shows how structural changes in the sensor domain are transmitted across the membrane.

The paper determines the structure of amyloid-β (Aβ40) fibrils bound to lipids using cryo-EM, showing lipid binding and potential relevance to Alzheimer's disease pathogenesis.

The paper presents six atomic structures of α-synuclein fibrils in the presence of phospholipids, revealing how phospholipids influence fibril morphology and lipid interactions.