Browse our latest Biochemistry and Chemical Biology articles

A branch to the protein prenylation pathway has been previously overlooked.

Cell biological, biochemical and structural studies reveal the mechanistic roles of two new mitochondrial iron-sulfur protein assembly factors, explaining the patho-biochemical defects of affected patients.

Mitochondrial proteins Nfu1 and BolA3 mediate the transfer of preformed [4Fe-4S] clusters within the mitochondria to recipient proteins to shield clusters from oxidative damage during transfer.

A new stress granule assembly mechanism has implications for other RNP granules and pathological aggregates.

Encapsulin-associated ferritin proteins form metal-dependent decamers that are active as ferroxidase enzymes, but require encapsulation to form an iron store.

Epigenetic modifications to DNA can regulate E3 ubiquitin ligase activity in human cells.

Measuring the equilibrium dimerization of a polytopic membrane protein in lipid bilayers forms the basis of a new system for studying the physical forces that stabilize membrane protein association in membranes.

The protease γ-secretase generates amyloid-beta peptides using a mechanism that is driven by the stabilization of an enzyme-substrate scisson complex.

Peptidase activity of DDI2 is required to activate Nrf1 in order to enable proteasome recovery in response to proteasome inhibition.