Browse our latest Biochemistry and Chemical Biology articles

A newly discovered pathway suggests histone proteins H3 and H4 are imported into the nucleus as individual units rather than joined together as heterodimers as was previously thought.

Transcriptional activity is characterized for five steroid receptors complexed with multiple ligands and it is shown that the extent of transcriptional activation in complexes is accurately described by conformational shifts in computationally-generated ensembles.

The motility of three different kinesin-dynein pairs were analyzed and found to be strikingly similar, suggesting that bidirectional transport is not regulated by motor type, but rather by scaffold, adapter, and regulatory proteins.

The repair of oxidatively damaged proteins by the newly discovered activity in YjbI is important for the adaptation of Bacillus subtilis to oxidative environments.

Imaging studies of connexin-coupled networks of colorectal cancer cells reveal that cells carrying a genetic defect in an essential metabolic pathway can be rescued by diffusive exchange with neighboring wild-type cells via gap junctions, particularly Cx26, thereby evading negative selection.

Organellar lipidomics and lipid reporter studies in intact cells reveal how disease-relevant mutations in a sphingolipid biosynthetic enzyme cause a wide-ranging perturbation of lipid distributions and membrane properties along the secretory pathway.

A large-scale phylogenetic inference of the ribonucleotide reductase family reveals a new distinct clade with implications on how nature adapted to environmental changes.

Site-specific phosphorylation of the A-kinase anchoring protein 12 (AKAP12) in hepatic stellate cells modulates its scaffolding function and promotes liver fibrosis.

Unbiased proteomics and molecular analysis revealed a new role for S6K1 in regulating DNA repair through the orchestrated phosphorylation of CDK1 and MSH6. The findings may explain why RPS6KB1 gene amplification contributed to breast cancer drug resistance.

Unique sequence feature requirements for the plasmid centromere pSM19035-parS for ParA_pSM-ATPase activation byribbon-helix-helix-ParB_pSM, a non-CTPase centromere-binding protein, evince complex interaction gymnastics among the three reaction components necessary for plasmid partition, which is distinct from ParABS-systems involving helix-turn-helix-ParB-CTPases.