Cellular stress induced by the abnormal accumulation of unfolded or misfolded proteins at
the endoplasmic reticulum (ER) is emerging as a possible driver of human diseases …

Stress induced by accumulation of misfolded proteins in the endoplasmic reticulum is
observed in many physiological and pathological conditions. To cope with endoplasmic …

The endoplasmic-reticulum (ER) stress response constitutes a cellular process that is
triggered by a variety of conditions that disturb folding of proteins in the ER. Eukaryotic cells …

In the last decade, the endoplasmic reticulum (ER) has emerged as a central organelle
regulating the core mitochondrial apoptosis pathway. At the ER membrane, a variety of …

Endoplasmic reticulum (ER) stress is a common feature of several physiological and
pathological conditions affecting the function of the secretory pathway. To restore ER …

The endoplasmic reticulum (ER), mitochondria and lysosomes are physically and/or
functionally linked, establishing close contact sites between these organelles. As a …

Maintenance of endoplasmic reticulum (ER) proteostasis is controlled by a dynamic
signaling network known as the unfolded protein response (UPR). IRE1α is a major UPR …

Anti-apoptotic Bcl-2 contributes to cancer formation and progression by promoting the
survival of altered cells. Hence, it is a prime target for novel specific anti-cancer therapeutics …

Increased demand on the protein folding capacity of the endoplasmic reticulum (ER)
engages an adaptive reaction known as the unfolded protein response (UPR). The UPR …

Cell-death and-survival decisions are critically controlled by intracellular Ca 2+ homeostasis
and dynamics at the level of the endoplasmic reticulum (ER). Inositol 1, 4, 5-trisphosphate …