Xiang Chen on Muck Rack

Xiang Chen

Dallas
As seen in: Arthritis & Rheumatology, British Journal of Cancer, Color Research & Application, Journal of Environmental Quality, Nature, Wiley, Wiley Online Library, PLOS, PLOS ONE, ScienceDirect and
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Articles

A molten salt metal-air electrolyzer for recycling superalloy

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By Xiang Chen, Shiyu Wang, Beilei Zhang, Yanyang Guo, Zishuai Hu, Xin Qu, MengYi Tang, Lei Guo, Kaifa Du, Yuan Sun, Dihua Wang, Huayi Yin
| Nature Verified
Abstract Recovering critical strategic metals from superalloy scraps is indispensable to sustaining the materials supply chain. However, the excellent physicochemical properties of superalloy make them difficult to dissolve and separate, thereby hindering their recycling and reutilization. Here, we design a molten salt metal–air electrolyzer (MMAE) that synergistically oxidizes and pulverizes scraps, which generates oxide powders that can be easily dissolved and separated for all element recovery.
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TranDep: a transcriptomics atlas of depression

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By Xiaogang Zhong, Siwen Gui, Dongfang Wang, Yong He, Xiang Chen, Yue Chen, Xiaopeng Chen, Yanyi Jiang, Yikun Ren, Hanping Zhang, Qiuxiang Tan, Wei Wang, Philipp Khaitovich, Juncai Pu, Yiyun Liu, Peng Xie, Renjie Qiao
| Nature Verified
Abstract Depression is a severe mental illness that poses substantial burdens on public health. Given that depression research is still challenged by its multifaceted pathogenesis, depicting the depression associated genetic regulatory networks is essential for understanding its mechanism, optimizing diagnosis, and developing targeted therapies. However, a comprehensive panoramic view of transcriptional alterations in depression remains lacking.
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Sweetening the bonds: how O-GlcNAcylation modulates cell adhesion

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By Shi-Sheng Zhou, YUE WANG, Bei Chen, Zhi-wei Xu, Xiang Chen, Wen-hui Lou, Guo-hong Qiao, Zi-jun Wei, Yu-qin Hu, Qi-jie Zhao
| Nature Verified
Abstract O-GlcNAcylation is a dynamic, reversible post-translational modification that attaches N-acetylglucosamine (GlcNAc) to the serine or threonine residues of intracellular proteins. Catalysed by O-GlcNAc transferase and removed by O-GlcNAcase, this modification acts as a key nutrient and stress sensor. Although cell adhesion is fundamental to tissue architecture and mechanotransduction, emerging evidence has shown that O-GlcNAcylation profoundly orchestrates these processes.
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