Andreas Plückthun

This paper develops a retargeted adenovirus system to produce IgA antibodies and CD47 blockers in tumors, enhancing innate immune responses and reducing tumor volume in mice.

This study determines the structure of higher-order gephyrin oligomers using cryo-EM, revealing how its flexible linker regulates receptor binding and oligomerization.

This paper develops a dArmRP that selectively shields the KRAS4B hypervariable region, blocking prenylation and reducing membrane localization without affecting other KRAS isoforms.

This study compares extracellular vesicles (EVs) and mechanically induced vesicles (MVs) for membrane protein structure determination, finding that MVs provide better structural representation of HER2 in native environments.

This study shows that RSV forms condensates by pre-assembling replication centers within viral particles, explaining infection heterogeneity and enabling efficient replication without requiring pre-existing condensates.

This study uses T-DARPins to inhibit TBXT in chordoma cells, revealing its regulome and identifying therapeutic vulnerabilities, including sensitivity to JAK2 inhibitors.

This paper develops a genome-replicating high-capacity adenoviral vector that enhances transgene expression without causing host cell death.

This paper develops a modular adapter system to target dendritic cells with adenoviral vectors, enhancing tumor vaccination by improving DC transduction and co-delivering cytokines.

This study investigates the role of SV isoforms of the staphylococcal phage φ2638A endolysin during infection, showing they form heterodimers with the full-length endolysin to enhance lytic activity.

This study develops DARPin-based tools to study gephyrin and inhibitory synapses, revealing new interactors and binding modes.

The paper shows that Dpp/BMP morphogen dispersal is not strictly required for overall wing patterning and growth in Drosophila, challenging a long-standing dogma.

The paper proposes an atomistic structural model of a Ras-Raf signalosome based on molecular dynamics simulations, mutagenesis, electron microscopy, and cell-based experiments.

This paper describes the engineering of ubiquibodies (uAbs) that degrade all forms of endogenous ERK1/2 protein kinase in multiple cell lines.

The paper introduces a computational method for designing rigid protein assemblies through three-body fusion and validates it experimentally with mass spectrometry and cryo-EM.

The paper reports cryo-EM structures of a GPCR-G protein complex in lipid nanodiscs, revealing structural insights into G protein activation without stabilizing agents.