Brian A. Kelch

This study identifies the molecular mechanism by which LIMD1 recruits LATS1/2 to adherens junctions through LIM domains and an N-terminal IDR, mediated by a conserved LATS-LATCH motif.

This study investigates how the two active sites of SARS-CoV-2 Mpro communicate and cooperate in catalysis using enzymatic assays, crystal structures, and engineered mutations.

The paper determines the structure of the portal vertex and neck complex in the hyperthermophilic phage Oshimavirus, revealing a pressure-sensitive mechanism for terminating DNA packaging and triggering tail attachment.

This study identifies SARM1 as an ADP-ribosyl transferase that auto-MARylates, regulating its activity and subcellular localization in axon degeneration.

The paper presents structures of the yeast clamp loader RFC and shows PCNA facilitates nucleotide exchange by promoting ADP release through subunit separation.

This study compares the clamp loader mechanism in bacteria and eukaryotes, revealing structural and functional differences in clamp opening and p/t-junction binding.

This study shows that the Copia retrotransposon protein influences synaptic plasticity in Drosophila by antagonizing the Arc homolog, suggesting transposons play an essential role in cellular processes.

The paper identifies a second PCNA mutation, C148S, causing PARD, showing both variants have thermo-stability defects leading to reduced chromatin-bound PCNA and temperature-dependent phenotypes.

The paper presents the first atomic-resolution structure of a viral DNA packaging motor and describes its mechanism through molecular dynamics simulations.