Regulation of the endoplasmic reticulum chaperone BiP by calcium.

Molecular details of how the iron–sulfur cluster cofactor of a bacterial global iron regulatory protein simultaneously senses iron and O₂ are revealed by mass spectrometry and spectroscopy.

The sequence of neural and physiological processes underlying action-stopping has been delineated.

An iron-sensitive gene cluster encodes proteins that co-localize with phytotransferrin endosomes and are involved in key intracellular iron transformation and trafficking processes in a model marine diatom.

Client protein-driven reversal of endoplasmic reticulum chaperone (BiP) mediated-repression is revealed as a principal component of the regulation of the unfolded protein response transducer IRE1 in cells.

An alternative iron storage system based on a 9.6 megadalton microbial protein compartment is able to sequester and store large amounts of iron.

Analysis of the atypical tryptophan biosynthetic operon of Chlamydia trachomatis revealed the simultaneous regulation of transcriptional initiation and termination by an iron-dependent repressor, expanding known regulatory mechanisms of this pathway.

In vivo studies reveal that mitochondrial Complex I deficiencies induce iron misregulation and liver iron overload that may contribute to neurodegeneration in mitochondrial disease mice, and that iron restriction is effective in reducing disease progression.

An ECF-type transporter serves as broad-spectrum heme iron scavenger and allows an opportunistic pathogen to use multiple eukaryotic hemoproteins to overcome nutritional iron-limitation.

AMPylation of BiP allosterically interferes with stimulation of its ATPase activity by J-proteins that is required for high affinity substrate binding.