Browse our latest Biochemistry and Chemical Biology articles

The malaria parasite uses an enzyme called GDPD to absorb choline, an important nutrient, from the bloodstream and this is essential for the parasite to survive inside the red blood cell.

Cryo-EM structure and functional analyses show that human iron exporter ferroportin (Fpn) can bind and transport calcium ions and the transport activity is reduced when the concentration of ferrous ions is high.

Comparision of current and fluorescent kinetics from P2X7 receptor mutants labeled with the fluorescent amino acid ANAP suggests that the characteristic P2X7 current facilitation involves changes in channel gating rather than interactions or conformational changes of its intracellular ballast domain.

An evolutionarily conserved protein sequence present in diverse species like yeast, frogs, chickens, and humans binds a well-known template for microtubule nucleation, the gamma-tubulin ring complex, activating and enhancing its ability to nucleate microtubules, even under low tubulin concentrations.

Hypoxic accumulation of squalene, the substrate of squalene monooxygenase, triggers its proteasomal truncation to a constitutively active variant that preserves downstream sterol synthesis.

New cryoEM structures reveal how small bacteriophage proteins suppress bacterial immunity.

The modelled structure of a membrane protein supports the hypothesis that it has a new fold with a channel that allows a chemical group to cross the membrane to decorate surface structures.

Dominant mutations in Arl3, linked to inherited retinal dystrophy, disrupt the active Arl3-GTP ciliary gradient and cause a defect in rod photoreceptor nuclear migration that can be rescued by elevating ciliary Arl3 activity or reducing aberrant non-ciliary Arl3 activity.

The dimer destabilizers cause a dimer-to-monomer equilibrium shift favoring the human thymidylate synthase monomer more degradable by the proteasome, thus breaking the long-standing link between inhibition and enhanced expression of the protein to fight cancer drug resistance.

A common genomic deletion in various human cancers disrupts mitochondrial protein homeostasis in a way that might be targeted by existing drugs.