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 …

The endoplasmic reticulum (ER) is an important site for protein folding and maturation in
eukaryotes. The cellular requirement to synthesize proteins within the ER is matched by its …

The secretory capacity of a cell is constantly challenged by physiological demands and
pathological perturbations. To adjust and match the protein-folding capacity of the …

The spliced form of X-box binding protein 1 (XBP1s) is an active transcription factor that
plays a vital role in the unfolded protein response (UPR). Under endoplasmic reticulum (ER) …

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

Most of the secreted and plasma membrane proteins are synthesized on membrane-bound
ribosomes on the endoplasmic reticulum (ER). They require engagement of ER-resident …

Selective autophagy of organelles is critical for cellular differentiation, homeostasis, and
organismal health. Autophagy of the ER (ER-phagy) is implicated in human neuropathy but …

Protein-folding stress at the endoplasmic reticulum (ER) is a salient feature of specialized
secretory cells and is also involved in the pathogenesis of many human diseases. ER stress …

The endoplasmic reticulum (ER) is a critical organelle for protein synthesis, folding and
modification, and lipid synthesis and calcium storage. Dysregulation of ER functions leads to …

Secretory and transmembrane proteins enter the endoplasmic reticulum (ER) as unfolded
proteins and exit as either folded proteins in transit to their target organelles or as misfolded …