Browse our latest Biochemistry and Chemical Biology articles

Structure-guided biochemistry defines how the coupling between nucleic acid substrate binding and ATPase activity is used by a molecular switch to load ring-shaped motor proteins onto single-stranded DNA.

Two proteins called Sec17 and Sec18 may have a larger role in membrane fusion than is commonly assumed in textbook models.

Activation of the sarcoplasmic reticulum calcium pump and enhancement of cellular calcium homeostasis by dwarf open reading frame reveal how this small membrane protein opposes phospholamban inhibitory function in cardiac muscle.

An immunofluorescent analysis of 465 protein kinases revealed a substantial role of liquid-liquid phase separation in kinase localization and identified new kinase localizations to mitochondria and other organelles.

Hoxa3 and Hoxa11 translation inhibitory elements block cap-dependent translation by using upstream open reading frames with distinct modes of action.

Analysis of neo-splicetope-specific T cell responses strongly questions the idea that in vitro proteasome-catalyzed peptide splicing reaction simulates the in vivo situation with the same high fidelity as the in vitro generation of non-spliced epitopes.

Spliced peptides present on tumor cells can help to mount an immune response, but algorithms offer limited help in predicting which ones actually exist and perform this role in vivo.

The first-in-class cell-permeant fluorescent probe provides direct and visual evidence of SARM1 activation in axonal degeneration and identified the first covalent, allosteric inhibitor of SARM1 acting on the NAD-binding pocket in the ARM domain.

Sec18(NSF) and Sec17(αSNAP) provide a parallel pathway to fusion that is independent of energy from SNARE zippering.

Laterally associating specific ESCRT-III subunits can replace one another with simple modifications, providing insights into the design principles of ESCRT-III heteropolymerization.