Jonathan N. Pruneda

This study shows HOIL1 ubiquitinates LGP2 to activate MDA5 and induce IFN responses, highlighting a mechanism distinct from RIG-I sensing.

This study shows that isopeptidase and esterase activities of deubiquitinases have distinct catalytic requirements, with cysteine not strictly needed for esterase activity.

This study identifies a novel E3 ligase secreted by Pseudomonas aeruginosa that regulates virulence through ubiquitin modification.

The paper identifies UFMylation as an antibacterial pathway using proximity biotinylation and mass spectrometry, showing it targets intracellular Shigella and Salmonella.

This paper develops a single-domain antibody specific for M1-linked ubiquitin chains, enabling their detection and analysis across multiple applications.

This paper identifies OspC2 and OspC3 as Shigella effectors that specifically target Caspase-5 and Caspase-4, respectively, through their PCS domains, revealing evolutionary adaptations in host and pathogen interactions.

The paper identifies RNF114 as an E3 ligase that extends K11 polyubiquitin on MARUbylated sites, revealing a novel mechanism of Ub-ADPr recognition and polyubiquitylation.

This paper discovers a new dual post-translational modification, MARUbylation, where PARP10 is mono-ADP-ribosylated and ubiquitylated on Glu/Asp residues, leading to proteasomal degradation.

The paper correlates allelic strengths of UBA5 variants in vivo and in vitro, classifying them into mild, intermediate, and severe based on functional assays.

The paper shows that an 'invisible' conformation of ubiquitin enhances its phosphorylation by PINK1 through a dynamic equilibrium involving the Ser65 loop.