M. S. Dickinson

Broadly neutralizing antibodies against emerging delta-coronaviruses

The paper isolates two human monoclonal antibodies that broadly neutralize PDCoV variants and identifies their mechanism of action.

Light-sensitive phosphorylation regulates enzyme activity and filament assembly of human IMPDH1 retinal splice variants

This paper shows phosphorylation at S477 regulates IMPDH1 filament assembly and activity, modulating GTP synthesis in retinal cells.

Blueprinting expandable nanomaterials with standardized protein building blocks

This paper introduces standardized protein building blocks and geometric design principles to create expandable protein nanomaterials, validated through X-ray crystallography and electron microscopy.

GBP2 aggregates LPS and activates the caspase-4 inflammasome independent of the bacterial encapsulation factor GBP1

This paper shows GBP2 can trigger pyroptosis by aggregating free LPS and activating caspase-4, independent of GBP1's bacterial binding function.

Structure and dynamics of the essential endogenous mycobacterial polyketide synthasePks13

This paper determines the structure and dynamics of the mycobacterial polyketide synthase Pks13 using cryoEM and complementary techniques, revealing intermediate states and substrate binding.

Vicia faba TPC1, a genetically encoded variant of the vacuole Two Pore Channel 1, is hyperexcitable

This paper identifies a hyperexcitable variant of the TPC1 channel in Vicia faba, showing it differs from Arabidopsis in Ca2+ sensitivity and vacuole excitability.

Symmetry reduction in a hyperpolarization-activated homotetrameric ion channel

The paper determines the structure of the hyperpolarization-activated channel AKT1 from Arabidopsis thaliana and shows it undergoes symmetry reduction to regulate electrical activation.

CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.

The paper uses cryo-EM and AlphaFold2 to determine the structure of SARS-CoV-2 Nsp2, revealing its zinc-binding site and potential interactions with host proteins.

Proximity-dependent proteomics of the Chlamydia trachomatis inclusion membrane reveals functional interactions with endoplasmic reticulum exit sites

This study uses proximity-dependent biotinylation to identify inclusion membrane proteins of Chlamydia trachomatis and reveals a novel interaction with endoplasmic reticulum exit sites.