The INM protein LAP1B, an activator of Torsin ATPases, is a chromatin-binding factor that erroneously persists on mitotic chromatin if Torsin functionality is compromised, inducing chromosome segregation defects and binucleation.
Sean R Cuddy, Austin R Schinlever ... Anna R Cliffe
Herpes simplex virus reactivates from a latent infection when neurons become hyperexcitable in response to an inflammatory cytokine known to be released during fever and stress.
Sofya A Kasatskaya, Kristin Ladell ... Dmitriy M Chudakov
Functional subsets of helper CD4+ T cells carry TCR repertoires with distinct features that are reproducible across donors and are partially acquired at the level of thymic selection.
Holger Dannenberg, Hallie Lazaro ... Michael E Hasselmo
Spatial accuracy of grid cell firing correlates with the slope of the local field potential theta frequency vs. running speed relationship and integrates velocity signals over past time.
A widespread family of chaperones functions to stabilize membrane protein effectors by mimicking transmembrane helical environments and promotes effector export by the bacterial type VI secretion system.
Loss of hepatic Cdk1 leads to oxidative stress, increased fatty acids in blood, and hyperinsulinemia, which resulted in insulin resistance and hepatic steatosis, similar as in diabetes.
Kristen L Wells, Corey N Miller ... Lars M Steinmetz
Combination of experimental mouse models with single-cell RNA-sequencing creates a detailed map of medullary thymic epithelial cell development and identifies a transit-amplifying population as the immediate precursor to Aire-expressing mTECs.
Pierre-Louis Bazin, Anneke Alkemade ... Birte U Forstmann
An open-source software tool enables the anatomical parcellation of an unprecedented number of subcortical structures in magnetic resonance images of the human brain, automatically and in individual subjects.
Benjamin M Adams, Nathan P Canniff ... Daniel N Hebert
Natural substrates of the central endoplasmic reticulum quality control glycoprotein sensors UDP-glucose:glycoproteinglucosyltransferase (UGGT)1 and UGGT2 were identified using a glycoproteomics approach and the role for their modification was explored.