Most of the mRNAs whose translation is resistant to the stress-induced repression of protein synthesis contain upstream open reading frames that are efficiently translated under normal conditions.

Ceapins specifically inhibit ATF6α signaling by preventing its transport to the Golgi during endoplasmic reticulum stress.

Ceapins enable selective pharmacological inhibition of the cytoprotective transcriptional response to endoplasmic reticulum stress through ATF6α without affecting other branches of the unfolded protein response.

A molecular model of the assembled COPI coat, determined by cryo-electron tomography of an in vitro reconstituted budding reaction, reveals details of interactions mediating coat assembly and shows the binding site of ArfGAP2.

Mature axons lose the ability to regenerate because key growth molecules are excluded through changes in vesicle transport, and restoring transport can restore regeneration.

ATF4, the master regulator of transcription during the Integrated Stress Response (ISR), causes global changes in cysteine sulfhydration of proteins and this event causes cellular metabolic reprogramming.

GDE3 is a transmembrane GPI-specific phospholipase C that sheds the urokinase receptor (uPAR) from the cell surface resulting in loss of uPAR function in breast cancer cells and reduced tumor growth.

Inhibiting IRE1α decreases tumor cell proliferation and migration in hepatocellular carcinoma, therefore components of this ER-stress pathway may be therapeutically relevant for liver cancer.