John L. Rubinstein

The paper determines the Cryo-EM structure of the Arabidopsis thaliana V-type ATPase, revealing its catalytic cycle and organelle-specific interactions with TLDc proteins.

This paper determines the structure and dynamics of the non-canonical inflammasome using biophysical methods, showing it is heterogeneous and primed for rapid substrate cleavage.

The paper identifies an unusual [3Fe-4S] cluster in EtfD from Mycobacterium smegmatis and shows its role in linking β-oxidation to proton pumping in the electron transport chain.

This paper determines the structure of the mycobacterial LCC complex using cryo-EM, revealing substrate specificity mechanisms and interactions with MSMEG_0435-0436.

This study identifies PRRC2A, PRRC2B, and PRRC2C as stress granule proteins that regulate translation by interacting with the eIF3 complex and 48S PIC factors.

This paper designs potent small protein inhibitors of C. difficile toxin B using deep learning and Rosetta, showing high affinity and stability for potential clinical use.

The paper determines cryo-EM structures of CpaF in different conformations and proposes a rotary mechanism of catalysis for Tad pilus assembly and disassembly.

The paper determines the structure of mycobacterial NDH-2 bound to an inhibitor using cryo-EM, revealing structural features that could guide inhibitor design.

The paper uses cryo-EM to show that malate-quinone oxidoreductase associates with the CIII2CIV2 supercomplex in mycobacteria, linking Krebs cycle and respiration.

The paper determines the structure of the Pfs230:Pfs48/45 complex bound to transmission-blocking antibodies, revealing molecular interactions and epitopes that inform vaccine development.

The paper determines the structure of yeast RAVE bound to a partial V1 complex using cryo-EM, revealing its role in facilitating V1-VO reassociation.

Vesicle Picker automatically identifies vesicles and selects particle locations in cryo-EM micrographs, improving efficiency for membrane protein complex analysis.

This paper identifies the V1H subunit of V-ATPase as a regulator of ATG16L1 recruitment in response to pH gradient disruption, linking V-ATPase function to autophagy activation.

The paper determines the high-resolution structure of V-ATPase in native synaptic vesicles using cryo-EM, revealing interactions with cholesterol and synaptophysin.

This study reveals the structural basis of Plasmodium vivax inhibition by antibodies targeting the CSP repeats through molecular dynamics simulations and crystal structure analysis of inhibitory monoclonal antibodies.

The paper describes a multimerization platform that transforms antibodies into potent, broad-spectrum neutralizers against SARS-CoV-2.

The paper identifies SEMA6A and SEMA6B as receptors for C. sordellii lethal toxin and shows how mutations can switch receptor specificity between related toxins.