The unfolded protein response (UPR) is a protective mechanism against endoplasmic reticulum (ER) stress that induces a series of signal transduction pathways to eliminate misfolded proteins. The UPR mechanism is highly conserved in fungi, higher organisms, plants and mammals. The UPR pathway is activated to stabilize ER functions when there are too many unfolded proteins or misfolded proteins in the ER. However, stress continues when ER proteins are stimulated by toxic substances that affect the balance of the UPR pathway, which causes changes in the structure and function of the ER and other organelles. These ultimately disrupt homeostasis in the body and cause pathological reactions that can be fatal. The UPR mechanism has clear effects on stabilizing the protein-folding environment. Dysfunction or disruption of the UPR mechanism is associated with numerous disorders, including neurodegenerative diseases, loss of control of protein secretion, cerebral ischemia and epilepsy, neuropsychiatric diseases, eye diseases, skin diseases, metabolic and inflammatory diseases, atherosclerosis, and heart disease. Thus, characterization of UPR function and its dysfunction has significant importance and has broad application prospects, which make research into the UPR a research hotspot.

展开的蛋白质反应（UPR）是针对内质网（ER）应激的保护机制，该机制诱导一系列信号转导途径以消除错误折叠的蛋白质。UPR机制在真菌，高等生物，植物和哺乳动物中高度保守。当ER中存在太多未折叠的蛋白质或错误折叠的蛋白质时，UPR途径被激活以稳定ER功能。但是，当有毒物质刺激内质网蛋白时，压力会持续，这会影响UPR途径的平衡，从而导致内质网和其他细胞器的结构和功能发生变化。这些最终会破坏体内的体内平衡，并导致可能致命的病理反应。UPR机制对稳定蛋白质折叠环境具有明显的作用。UPR机制的功能障碍或破坏与许多疾病有关，包括神经退行性疾病，失去蛋白分泌控制，脑缺血和癫痫，神经精神疾病，眼病，皮肤病，代谢和炎性疾病，动脉粥样硬化和心脏病。因此，表征UPR功能及其功能异常具有重要的意义，具有广阔的应用前景，这使得对UPR的研究成为研究热点。