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The nuclear exosome cofactors Mpp6 and Rrp47 can stimulate exoribonuclease activities of the nuclear RNA exosome and recruit the Mtr4 helicase to promote helicase dependent RNA decay.

ARH3 is an enzyme that hydrolyses serine ADP-ribosylation, a recently uncovered post-translational protein modification.

Hypervariable regions of mtDNA contribute to transcriptional regulation by serving as sites for TFAM binding and looping.

Interactions between serines and molecules of ADP-ribose play an important role in signaling that the DNA in a cell has been damaged and needs to be repaired.

A flip of the dimer asymmetry following the first ATP hydrolysis provides a mechanistic model for client remodeling by the mitochondrial Hsp90, TRAP1.

The SHIP2 inositol phosphatase is an important upstream regulator of the Akt signaling pathway, which requires a catalytic core formed by the phosphatase domain tightly packed to a C2 domain for its function.

The emergence of complementary electrostatic potentials after the prokaryotic-to-eukaryotic split drives physical and functional cooperation between canonical class A and class B J-proteins to boost protein disaggregation.

The structures of photosystem II, with the water-oxidizing Mn4CaO5-cluster fully removed and in an intermediate assembly state, show that photoassembly is facilitated by perfectly pre-arranged protein ligands of the five metal ions.

Agonist and antagonist peptides of the corticotropin-releasing factor receptor type 1 adopt different folds and stabilize distinct conformations of the receptor transmembrane domain, which involves tilting of helices VI and VII around conserved glycine hinges.

Sec17 (αSNAP) and Sec18 (NSF) are shown to act twice, to promote fusion per se and to recycle SNAREs after fusion.