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Biochemical studies in combination with computational modeling and molecular dynamics simulations reveal that the lipid bilayer promotes intramembrane proteolysis by stabilizing the enzyme-substrate complex and the protease active site.

Mg²⁺-dependent JAK1-mediated phosphorylation sensitizes TRPV2 activity and thermo-threshold, which is counterbalanced by PTPN1-mediated dephosphorylation, highlighting a role of phosphorylation homeostasis in setting the basal activity of TRPV2.

Distinct surfaces of an interbacterial competition cell wall toxin mediate interactions with different cellular binding partners, resulting in an inherent evolutionary trade-off across the toxin superfamily.

Determination of a model of mitochondrial protein import elucidated using a high-resolution transport assay and kinetic modelling.

Fluorescently-tagged profilin-1 behaves similar to the tag-free protein in biochemical and cell-based assays.

The human eye lens imports and concentrates within itself a naturally abundant small molecule that inhibits cataract-associated aggregation of an eye lens protein before the aggregates get large enough to scatter light.

Hypertrophic cardiomyopathy-causing mutations in the light chain-binding region of β-cardiac myosin's lever arm appear to disrupt myosin tail-based autoinhibition, while mutations in the pliant region of the lever arm reduce autoinhibition in the presence of actin and impact myosin’s powerstroke.

The cryo-EM structural and functional analyses reveals the lactate dehydrogenase/electron-transferring flavoprotein (Ldh-EtfAB) in its enzymatically active form and the geometry of the confurcating flow of two energetically spitted electrons via 2 FAD and 1 [4Fe-4S] cluster to a central FAD.

The integration of experimental and data mining approaches provides novel insights into deubiquitinating enzymes individually and as a gene family.

Activin class member, activin C, is a canonical TGFβ family member that signals through the type I receptor, action receptor-like kinase 7 and is resistant to follistatin antagonism.