Andrew P. Leis

The paper identifies detergent LMNG as stabilizing a weak FZD-G protein interface, revealing that FZDs inherently weakly couple to G proteins and preferentially signal through DVL.

The paper determines the cryo-EM structure of LRRC15 and identifies the epitope recognized by the antibody samrotamab, revealing a binding mode that preserves signaling surfaces.

This study identifies EGF7 in PfRipr as a critical domain for inhibiting Plasmodium falciparum erythrocyte invasion and provides a basis for vaccine design.

This study identifies a second DNA-binding site in SMCHD1 and shows that DNA binding stimulates its ATPase activity, revealing a mechanism for gene silencing.

The paper identifies a conserved complex formed by PTRAMP, CSS, and Ripr in Plasmodium species that facilitates merozoite invasion of erythrocytes and shows its structural and functional conservation across species.

PartiNet improves particle picking in cryo-EM with a dynamic neural network that adapts to micrograph quality, enhancing efficiency and particle yield without sacrificing accuracy.

This paper presents cryo-EM structures of PORCN with inhibitors, revealing a conserved water-mediated binding mechanism for rational drug design.

This study characterizes MORC2 phosphorylation's role in DNA compaction and chromatin remodelling, showing it regulates ATP hydrolysis and DNA binding.

The paper investigates PINK1's interaction with nucleotides and kinetin, revealing structural changes and binding constraints that affect its activity and mitophagy.