stf-083010 and Neoplasms

Accumulation of unfolded or misfolded proteins in the endoplasmic reticulum (ER) leads to ER stress, which is characteristic of cells with high level of secretory activity and implicated in a variety of disease conditions. In response to ER stress, the cell elicits an adaptive process called the unfolded protein response (UPR) to support cellular homeostasis and survival. However, prolonged and unsolvable ER stress also induces apoptosis. As the most conserved signaling branch of the UPR, the IRE1α-XBP1 pathway plays important roles in both physiological and pathological settings and its activity has profound effects on disease progression and prognosis. Recently, modulating this pathway with small molecule compounds has been demonstrated as a promising approach for disease therapy. In this review, we summarize a list of current investigational compounds targeting this pathway and their therapeutic features for treating human diseases.

Topics: Aldehydes; Animals; Apoptosis; Cell Survival; Coumarins; Disease Models, Animal; Disease Progression; DNA-Binding Proteins; Drug Design; Drug Discovery; Endoplasmic Reticulum; Endoplasmic Reticulum Stress; Endoribonucleases; Homeostasis; Humans; Mice; Neoplasms; Neurodegenerative Diseases; Prognosis; Protein Folding; Protein Serine-Threonine Kinases; Quercetin; Regulatory Factor X Transcription Factors; Signal Transduction; Sulfonamides; Thiophenes; Toyocamycin; Transcription Factors; Unfolded Protein Response; X-Box Binding Protein 1