Daniel E. Otzen

The paper uses fragment-based methods to explore urethanase active sites and identifies diverse binding modes for polyurethane fragments.

This study uses isothermal titration calorimetry to analyze the thermodynamics of CO2 capture by amino acids and peptides, revealing distinct optimization strategies for carbamate formation.

This paper evaluates DNA-binding dyes for visualizing non-canonical extracellular nucleic acids in biofilms and identifies dyes with specific binding preferences.

This study identifies and characterizes five novel bacterial urethanases capable of degrading polyurethanes, with u15 showing high catalytic efficiency and structural insights for biocatalytic recycling.

This study identifies novel enzymes capable of degrading polyurethane and nylon by screening plastic-degrading bacteria, finding enzymes with improved thermostability and hydrolysis ability.

This study uses single-vesicle tracking to show α-synuclein oligomers form pores through a three-stage process influenced by membrane curvature, charge, lipids, and ligands.

The paper shows microbial amyloids from gut pathogens can trigger microglial hyperactivity and neuroinflammation, contributing to Alzheimer's disease progression.

This study investigates the resilience and charge-dependent fibrillation of Pseudomonas amyloids FapB and FapC, revealing their complex interactions and implications for biofilm persistence and potential applications.

This study shows that the Bri2 BRICHOS domain inhibits α-synuclein oligomer formation and toxicity by suppressing secondary nucleation and binding oligomers, suggesting its potential as a therapeutic target for Parkinson's disease.

This study shows that overexpression of human alpha-synuclein in rats leads to gut microbiome dysbiosis, altered metabolites, and aging-related changes that can be modulated by antibiotics.

This study investigates how alpha-synuclein aggregates affect blood-brain barrier integrity in vitro using co-cultures of brain endothelial cells with neurovascular unit components.

This study identifies penetratin as an inhibitor of α-synuclein aggregation and shows it improves locomotor function in Parkinson's disease mouse models.