Structural and biochemical characterization of the protease domain of an ABC transporter demonstrates the basis for recognition of substrate leader peptides.
Cryo-EM structure of a peptidase-containing ABC transporter in complex with its protein substrate reveals a mechanism of coupling substrate cleavage to translocation.
The strength of TCR signalling determines the rate at which cells initiate a tightly coordinated signalling programme, without altering its organization.
ER-stress sensing mechanism of the unfolded protein response sensor/transducer IRE1 is conserved from yeast to mammals, where in mammals, unfolded protein binding to IRE1's ER lumenal domain is coupled to its oligomerization and activation through an allosteric conformational change.
We reveal TAPBPR is a peptide exchange catalyst which restricts the peptide repertoire presented by MHC I on cells, a finding which has important implications for all aspects of immune recognition.
The combination of in vitro investigations, the zebrafish screening model and rodent experiments offered a unique approach to optimizing nanoparticles modified with Hepatitis B virus-derived peptides to specifically target hepatocytes.
An enrichable cross-linker with optional isotope labeling quadruples the number of cross-linked peptides identified from high-complexity samples, enhancing proteome-wide analysis of protein-protein interactions and protein conformational changes by mass spectrometry.
Theoretical analysis and in vitro reconstitution of a biological reaction-diffusion system identify key functional motifs as well as underlying principles and enable rebuilding pattern formation in a modular fashion.
ATR protects stem cell genomes by activating a transcriptional response mediated by totipotency genes, conferring trophoblast differentiation potential, the derepression of which in somatic cells might favour cancer features emergence.
