Andrew C. Kruse

The paper reports the cryoEM structure of the ITG3β1-CD151 complex and shows CD151 promotes ITG3β1 surface export, explaining the epidermolysis bullosa phenotype.

The paper reports cryo-EM structures of GerA, revealing how nutrient binding triggers channel opening through allosteric switches and subunit interactions.

This study shows that G proteins and β-arrestins can directly interact, with Gi family members differing in their association with β-arrestin, and this selectivity is located in the alpha helical domain of Gi.

This study presents cryo-EM structures of RXFP1 bound to relaxin-2 and AZD5462, revealing distinct activation mechanisms for protein and small-molecule agonists.

The paper uses AlphaFold-Multimer to predict nanobody binders to MRGPRX2, demonstrating in silico antibody discovery for a GPCR target.

This paper uses machine learning to predict high-affinity nanobody binders from sparse sequencing data, outperforming deep learning and semi-supervised methods with linear models.

The paper isolates antibodies from a Shigella outbreak in non-human primates, showing some target O-antigen and T3SS proteins, with some antibodies enhancing virulence.

The paper determines the structure of MreC-MreD complex and shows how MreD controls MreC conformation, essential for bacterial cell shape and antibiotic targeting.

The paper develops a large yeast surface display library to identify high-affinity peptide ligands for various protein targets, revealing binding motifs and novel clones.

This paper introduces GTACs, bispecific antibodies that selectively downregulate GPCRs via endocytosis and lysosomal degradation, showing high potency and selectivity for therapeutic targets.

This study shows LpoB transiently binds and activates PBP1b through an allosteric switch, directing PG synthesis to low-density areas and enabling lipoprotein redistribution.

This paper introduces an alignment-free deep generative model for protein design and variant effect prediction, showing improved performance over existing methods in challenging cases.

The paper identifies an activation pathway involving PBP2 that enhances cell wall polymerization and MreB filament formation in E. coli.

The paper investigates how MOP-family flippases recognize and transport lipid-linked oligosaccharides, finding that substrate binding destabilizes the inward-open conformation to promote translocation.