Edward H. Egelman

The paper investigates the structural basis of endopilus assembly, stability, and functional specificity in bacterial type II secretion systems using comparative analysis of two pathogens.

The paper identifies a novel MYO7A isoform, MYO7A-N, and shows its distinct expression and function in outer hair cells, contributing to hearing sensitivity and cochlear frequency resolution.

This study investigates how interhelical interactions guide the assembly of collagen mimetic peptides into D-periodic fibrils, nanotubes, and nanosheets.

This study reveals the structural basis for IFI16's inflammasome-independent functions through cryo-EM and computational analysis of its unique filament assembly.

This study identifies donor strand complementation and calcium ion coordination as key drivers of chaperone-free cannulae polymerization in archaea.

The paper reports the cryo-EM structure of the H-pilus, revealing its cyclic pilin subunit and explaining its role in conjugation.

The paper determines the structure of ARF6 protein lattice on tubulated membranes, revealing its role in vesicle fission and how GAP proteins interact with it.

The paper identifies F-ENA as a widespread family of endospore appendages in Firmicutes using cryo-EM, revealing their structure and role in spore clustering.

The paper designs collagenous assemblies using a peptide self-assembly system and solves their structure with cryo-EM, revealing a non-twisting triple helix conformation that differs from the canonical right-handed triple helix.

This study explores the sequence-structure relationship in collagen-like peptides, designing new peptides that form diverse quaternary structures beyond triple helices.

This study shows that Salmonella effector SipA stabilizes F-actin through a unique binding mechanism, similar to inorganic phosphate and phalloidin, enhancing toxin effects while avoiding host detection.

The paper determines the 4.0 Å resolution structure of CFA/I pili and confirms the role of proline 13 in structural stability using optical tweezers.