University of Otago discovers key kinases involved in the development of many diseases

Recently, in a research report published in the international magazine PNAS, researchers from institutions such as the University of Otago discovered key factors involved in the occurrence of various diseases, such as Parkinson's disease, gastric cancer, and melanoma. In the article, researchers studied a protein called Apoptosis Signal-regulating kinase 1 (ASK1). Like other kinases, ASK1 plays a key signaling protein that can control Cell behavior in multiple ways.

Kinases "tag" proteins that they want to turn off/on, controlling cell division, death, movement, or any other cellular biological process. Researcher Dr. Peter Mace said that ASK1 plays an important role in controlling cell response to injury, and it can promote cells to perform a programmed cell death process that is beneficial to the body. In this study, researchers determined by crystallography. The molecular structure of ASK1 was also better understood by performing biochemical experiments on the function of the protein.

奥塔哥大学发现参与多种疾病发生的关键激酶

The researchers found that ASK1 has an unexpected structure that helps control the mechanism by which protein expression is turned on, and that the entire family of ASKs may have such characteristics. Researchers on how ASK1 turns on/off protein expression have done a lot of research, and of course this is very important because the level of ASK1 is either too high or too low in patients such as Parkinson's, gastric cancer, and melanoma.

Researcher Mace believes the study can help understand how cells can respond to different threats or encounter different injuries, such as oxidants, which can damage the normal tissues of the body by promoting inflammation. He added that kinases are potential targets for researchers developing new drugs because the kinase has a trough-like structure that binds to specific compounds, but researchers may need to develop better drugs. A deeper understanding of the molecular mechanisms by which these compounds bind to the trough structure.

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