A combined chemical genetics, proximity labeling, and ADP-ribose site mapping approach shows that PARP-7 mono-ADP-ribosylates immune-relevant proteins on cysteine amino acids.

Global gene expression analysis unravels the underlying mechanisms for distinct crude oil induced defects in Atlantic haddock eggs and larvae.

PARP-7 is a mono(ADP-ribosyl) transferase that directs an extensive ADP-ribosylated proteome to control microtubule stability, and regulate ovarian cancer cell growth and motility.

A combination of NMR, fluorescence, and molecular dynamics simulations reveals the recognition mechanism for the intrinsically disordered regulator of protein kinase A, highlighting the enzyme's nuclear export process.

Inter-molecular cross-seeding between phenol-soluble modulins facilitates rapid and efficient self-assembly in Staphylococcus aureus biofilms revealing a complex molecular interplay between distinct phenol-soluble modulins orchestrating functional amyloid formation.

A theoretical basis for the spatial regulation of protein aggregation shows how aggregates can partition preferentially into intracellular liquid compartments.

The cAMP-dependent protein kinase A controls the switch from actively sprouting new blood vessel formation to vessel quiescence by reducing endothelial autophagy through phosphorylation-mediated destabilisation of ATG16L1.

Applying bioorthogonal chemistry to the zebrafish/Mycobacterium marinum model of tuberculosis reveals that the virulence lipid PDIM must spread into epithelial cells in order for mycobacteria to establish infection.

Solution NMR provides structural and kinetic information about oligomers on pathway to amyloid fibrils that are precisely structured but not cytotoxic.