The hypoxia-inducible factor HIF drives transcription of the gene cyp-36A1, which encodes a cytochrome P450 enzyme that acts via a putative intercellular signal to regulate the nuclear receptor NHR-46 and consequently stress resistance and behavior.

Type II nuclear receptors do not always compete for a limiting pool of their obligate partner RXRa.

A homopolymer-sphere model is shown to accurately reproduce the interactions that underpin selective gating of macromolecular transport into and out of the cell nucleus.

Metabolic activity of the methionine/S-adenosylmethionine cycle is sensed and transcriptionally regulated by a nuclear hormone receptor in Caenorhabditis elegans in order to maintain metabolic homeostasis in a tightly controlled regime.

NR4A is a broadly conserved transcription factor that is required for concordance of patterning information and anatomy at both ends of the planarian anterior-posterior axis.

Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.

Synthetic PPARγ ligands push and cobind with natural endogenous ligands, instead of compete and displace, which synergistically affects the structure and function of PPARγ.

The nuclear export receptor Crm1 cooperatively binds its HIV Rev-RRE cargo as a dimer using a species-specific interface that supports viral replication by enhancing nuclear export of HIV RNA.

T-cell receptor signaling actively regulates gating of the nuclear pore complex (NPC) in T cells by inducing translocation of protein kinase C-θ to the NPC to promote the sumoylation of RanGAP1.

Mecp2 expression is cell cycle-dependent and negatively regulates quiescence exit.