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A novel innate defense mechanism of cell lysis involves the coordinated oligomerization of a defensin by interaction with the membrane lipid, phosphatidylinositol 4,5-bisphosphate.

A disease-associated polymorphism in a related protein that regulates neurotransmitter release reveals that antiviral protein IFITM3 forms oligomers to rigidify membranes and inhibit virus fusion with cells.

Multimodal spectroscopy (smFRET, EPR, SAXS, and SANS) and integrative structural modeling reveal large-scale domain rearrangements in human guanylate binding protein 1 (hGBP1) that are driving forces for the formation of oligomers that enable its biological function in innate immune defense.

Canonical centriole duplication is much less prone to errors than de novo synthesis of centrioles, but neither depends on self-oligomerization of the centriole protein SAS-6.

Calcium-binding synaptotagmins are involved in ring oligomer formation, which allows synaptotagmins to synchronize neurotransmitter release to Ca²⁺ influx.

In vitro and in cellulo characterization of oligomerization by the cytoplasmic Wnt effector dishevelled and its partner Axin provide new mechanistic principles for Wnt/β-catenin signaling.

A biallelic missense mutation in the highly conserved, neuron-specific kinase CAMK2A abrogates holoenzyme assembly and causes a new inherited neurodevelopmental disease.

A combined NMR and kinetic study demonstrates how the dynamic transition of a molecular chaperone between different oligomerization states can modulate its activity by altering the binding kinetics and energetics of non-native proteins.

APOBEC3G, an anti-viral protein with the capability to inhibit HiV-1 infectivity, binds single stranded DNA in multiple physical conformations, enabling complex interactions that allow APOBEC3G to perform multiple diverse functions.

The first reconstitution of an unconventional secretory mechanism uncovered the molecular mechanism by which Fibroblast Growth Factor 2 is secreted from mammalian cells.