Shi's team has made another breakthrough in Alzheimer's research

, the research team, led by Professor Shi Igong of The University of West Lake University and Professor Shi Igong of the Center for Structural Biology and Innovation of Tsinghua University's School of Life, published two articles in the journal Nature, revealing the high-resolution frozen electroscopic structure of the human body γ-secretase in combination with the substrate Notch and amyloid prebiogen protein (APP) respectively. The structural changes that occur after two different substrates, γ-secretion enzymes, and bio-chemical studies of the function of these changes provide a cognitive basis for understanding the molecular mechanisms of γ-secretase-specific identification and cutting of substrates, thus providing important structural information for the study of specific drug design related to cancer and Alzheimer's disease.
According to the co-authors of these two long articles, postdoctoral students Yang Guangguang and Zhou Rui, if the substrate Notch or APP is likened to a rope, the role of γ-secretase is to cut this rope into a section. If the cut produces abnormalities, or if the small pieces of the cut are wrapped together, it may lead to disease. PS1 γ scissors in the part of the secretion enzyme.
there is no doubt that the development of drugs that specifically inhibit app processing without affecting Notch processing is of great value for targeted treatments for Alzheimer's disease without causing side effects. Currently, the team is studying the γ-secretion enzymes and specific inhibitors in the hope of providing more basic information for drug development. (Source: People's Daily Zhao Yongxin)
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