Release date: 2017-10-13 Recently, many articles by Chinese scholars have appeared frequently in the same issue of top academic journals. In July of this year, there were six Chinese scholars on the same day, and in the past September, four research papers from the Chinese scholars' group were published on the same day. Today, Nature once again published five articles from Chinese scholars on the same day, continuing the good momentum in recent months. 1. Dr. Jiang Youxing / Dr. Bai Xiaochen's research group Structure of mammalian endolysosomal TRPML1 channel in nanodiscs Dr. Jiang Youxing Dr. Bai Xiaochen TRPML1 is a cation channel located on the endosomal and lysosomal membranes and is ubiquitously expressed in mammalian cells. If it undergoes an inactivating mutation, it can lead to severe lysosomal storage disease. Using the cryo-electron microscopy technique of the Nobel Prize in Chemistry, Professor Jiang Youxing from the University of Texas Southwestern Medical Center and Professor Bai Xiaochen jointly obtained the structure of the mouse TRPML1 channel in nanodiscs. Structural analysis revealed that phosphatidylinositol-3,5-diphosphate binds to the N-terminus of the channel protein, while the helix-turn-helix region of the S2 and S3 regions may be coupled to the ligand. In addition, this structure also found the potential role of the S4 and S5 region linkages for the mechanism of action of the TRPML channel. Paper address: http://#affil-auth 2. Dr. Li Xiaotong's research group Human TRPML1 channel structures in open and closed conformations This issue of Nature published two papers on TRPML1 online. The second one is also from the University of Texas Southwestern Medical Center. One of the principals is Professor Li Xiaochun. Professor Li, Professor of the Nobel Prize in Physiology or Medicine at Rockefeller University, is also a co-author of the post-doctoral post of Professor Li. In this study, the researchers published a full-length cryo-electron microscopic structure of the human TRPML1 protein. It is worth mentioning that this team also obtained the structure of the channel protein "closed" and "opened". The researchers point out that these structures reveal the regulatory mechanisms of TRPML channel proteins and are expected to lead to new insights into the treatment of lysosomal storage diseases caused by TRPML1 mutations. Paper address: http://#affil-auth 3. Dr. Liu Yitao's research group Establishment of mouse expanded potential stem cells Conventional stem cells fall into two categories - embryonic stem cells and induced pluripotent stem cells. In theory, they can differentiate into a variety of cell types, but previous studies have shown that these two types of cells can differentiate into a limited number of cells - there are still some cells that cannot be obtained from these two types of stem cells. A team of professors from the Wellcome Trust Sanger Institute in the UK developed a new technology. They developed mouse expanded potential stem cells, which are very close to the original cell properties of the embryo and can form any cell type. Professor Liu Taotao also believes that this technology is expected to be applied to other mammals, including humans. Paper address: http://#affil-auth 4. Dr. Shao Feng's research group Ubiquitination and degradation of GBPs by a Shigella effector to suppress host defence The GBP protein mediates cellular autonomic antimicrobial defense mechanisms. In this study, Professor Shao Feng from the Beijing Institute of Life Sciences found that a microorganism called Shigella flexneri can induce rapid degradation of human GBP1 protein after infection. Further research found that a molecule called IpaH9.8 played a key role in it. This molecule directly targets the human GBP1 protein and is ubiquitinated at the Lys-48 site. In fact, this molecule can target multiple GBP proteins, affecting the defense mechanisms of the antimicrobial. This finding helps us better understand the GBP protein-mediated immunity. Paper address: Http:// 5. Dr. Jin Billy Li's research group Dynamic landscape and regulation of RNA editing in mammals The transition from adenosine to inosine (A-to-I) is a common and conserved RNA editing tool mediated by ADAR enzymes. This editing can change specific nucleotides in RNA and increase the diversity of the transcriptome. Although the researchers have found multiple editing sites, the degree of editing of most of the sites, and how these editors regulate biological processes, remains an unsolved mystery. In this article, the team of Professor Jin Billy Li of Stanford University analyzed the editing of the 8551 human sample. They found that ADAR1 is primarily responsible for repeat sites, while ADAR2 is primarily responsible for non-repetitive sites. Interestingly, ADAR3, which has no catalytic activity, also acts as a suppressor. The researchers pointed out that their findings brought new insights into the A-to-I transition. Source: Academic Jingwei 10000Hz High Frequency LiDAR Module 10000 Hz is one of our 2021 new solutions products,which can be widely used in drone postioning, car anti-collision, intelligent traffic monitoring etc. with high accuracy. We support customized service of different frequency(100hz,200hz,300hz,400hz,1000hz,5000hz,10000hz etc.), you can choose the suitable design. 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