Benjamin G. Davis

This study reveals a covalent mechanism in a bifunctional glycosyltransferase for hexosyl transfer and reports a novel self-priming function for polymerization.

This paper develops a nanopore-based method to deconvolute glycosaminoglycan structures at single-molecule resolution, achieving high precision in detecting sulfate groups and stereochemistry.

This study uses cryo-CLEM to reveal the molecular structure of PML bodies, identifying columnar trinucleosome assemblies and a porous interior that may facilitate chromatin partitioning.

This paper develops a high-throughput method to discover a novel photochemical reaction for editing protein side chains and using it to probe protein function through combined photochemical and photophysical approaches.

The paper introduces Di-Gluebodies, covalently-dimerized nanobodies, to improve cryo-EM structure determination of small proteins by providing rigidity and modularity.

This paper introduces FIRESCAPE, a radiolabeling method to study extracellular histone H3 clearance and effects, revealing distinct behaviors compared to intact nucleosomes.

Seedless calculates NMR pulses on-the-fly to improve signal-to-noise by compensating for RF inhomogeneity and chemical shift effects.

The paper uses live-cell 3D-SIM and genetic-code expansion to reveal the polygonal web architecture of RVFV NSs filaments in infected nuclei.

The paper identifies lipoamide as a small molecule that dissolves stress granules and improves outcomes in ALS models by modulating redox-sensitive proteins.

This paper introduces a method to track neurodegeneration biomarkers using PET imaging with isosteric protein mimics, revealing spinal fluid dynamics and neuronal loss mechanisms.

The paper develops a method to efficiently remove over-labelled peptides in proteomics samples, improving identification rates and quantitation precision.

This study investigates how penicillin G forms immunogenic adducts on proteins and elicits specific antibody responses in mice, revealing clonal dominance and limited cross-reactivity with other beta-lactam antibiotics.

This paper describes a light-mediated method for stereoretentive post-translational protein editing that generates site-selectively edited proteins with full stereochemistry retention.