Cryo-EM reveals that an unexpected domain separation in the zona pellucida module of uromodulin is required for its assembly to filamentous homopolymers that promote pathogen clearance in urinary tract infections.

The electroconvulsive therapy induced electric field magnitude and laterality is related to volumetric increases in cortical and subcortical structures, but the association with clinical outcomes remains elusive.

Cryo-EM structure of monomeric human Frizzled5 was determined with a universal fiducial antibody at 3.7 Å overall resolution, which supports a simple Fzd/LRP6 heterodimerization mechanism of canonical Wnt/β-catenin signaling.

An ECF-type transporter serves as broad-spectrum heme iron scavenger and allows an opportunistic pathogen to use multiple eukaryotic hemoproteins to overcome nutritional iron-limitation.

Replication origins are established throughout the genome with the exception of transcribed genes, and the local chromatin composition likely modulates the density of ORC and MCM as well as origin activation.

Structure-function characterization of the EMC's cytoplasmic, transmembrane, and lumenal domains reveal features critical for terminal helix insertion and a specialized role for the lumenal domain in polytopic membrane protein biogenesis.

The identification of the insulin binding site 2 by high resolution cryo-EM analysis.

Cryo-EM studies reveal structural basis for the activation, auto-inhibition and regulation of RET receptor tyrosine kinase.

Nascent regulatory peptides tune the translation rate through a continuous, dynamic reshaping of the functional center of the ribosome.

Structural and biochemical analysis of an abundant and conserved protein complex called EMC shows how it is likely to insert nascent membrane proteins into the endoplasmic reticulum membrane.