Viral evolution can lead to mutations that render specific glycosylation sites dispensable for folding and for supporting the protein's function, allowing changes in the shield, and in the immunogenic profile.

Endothelial cells from separate cardiac lineages start off in distinct transcriptional states, but over the course of development converge into transcriptional and functional states which are unrelated to lineage and which are conserved between mouse and human.

Human red blood cells from healthy donors display marked biophysical and genetic variation that impacts the growth of Plasmodium falciparum malaria parasites, outside of known disease alleles.

Genetic analysis identifies an enzyme of the malaria parasite that is required to seal its host red blood cell membrane upon invasion, a key requirement of this important intracellular pathogen.

Super-resolution microscopy and single particle tracking analysis of Piezo1 in red blood cells demonstrate its ability to sense membrane curvature, consistent with a force-through-membrane mechanism of channel mechanosensation in these cells.

In red blood cells, the Piezo1 protein is responsible for sensing mechanical forces and volume regulation.

Red blood cells infected by the malaria parasite Plasmodium falciparum are destroyed by human natural killer cells in the presence of antibodies from people who have acquired clinical immunity to malaria.

The person-specific adjusted HbA_1c addresses non-glycaemic variation in laboratory HbA_1c due to red blood cell lifespan differences, potentially providing a better marker to predict diabetes complications and guide glycaemic management.

Accessible cholesterol levels in human red blood cells were found to be stable within individuals but vary >10-fold among individuals and this variability may contribute to differences in cholesterol trafficking among tissues.

Cryo-electron tomography of close-to-native rod outer segments resolves connectors between disks and a scaffold at the disk rim enforcing the high membrane curvature of the unique long-range organization in these rhodopsin-rich light-sensitive subcellular organelles.