Michael P. Andreas

This paper introduces a permeable protein nanocage, QtEnc, enabling rapid and efficient cytosolic protein delivery through post-assembly cargo loading and pH-triggered release.

This study identifies a two-component Family 2B encapsulin shell that compartmentalizes geosmin synthase, showing its role in enzyme activity and stability through cargo loading peptides and pore conformation changes.

This paper introduces a directed evolution strategy for multimeric proteins using gene duplication to enable the selection of diverse high-performing variants.

The paper characterizes a two-component encapsulin from Streptomyces lydicus, showing differential assembly and mixed shell formation with irregular tiling.

The paper characterizes a DyP encapsulin from enterobacteria, showing its structural features, stability under harsh conditions, and catalytic activity preference at low pH.

The paper redefines the function of EshA as a protein shell encapsulating 2-MIB synthase, showing it is a cargo-loaded nanocompartment for secondary metabolite biosynthesis.

This paper introduces a pore-engineered enzyme nanoreactor platform based on encapsulins to improve catalytic activity and substrate range.

The paper shows that a single point mutation in a virus-like capsid can drive the formation of tetrahedral structures instead of the typical icosahedral symmetry.

This study investigates how pore structure affects stability and molecular flux in engineered protein cages through design, structural analysis, and simulations.

This study engineers a protein nanocage that can reversibly disassemble and reassemble under physiological conditions, enabling controlled cargo encapsulation.