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Ying Shan on Muck Rack

Ying Shan

As seen in: Nature, Wiley Online Library, PLOS ONE, Frontiers, heart, MDPI, Taylor & Francis Online, Arthritis Research & Therapy, JAMA (The Journal of the American Medical Association), BioRxiv and
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Articles

USP21-mediated deubiquitylation stimulates NuMA recruitment to the cell cortex to promote mitotic spindle orientation

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By Mingzheng Hu, Huixian Ma, Jinqiong Wang, Lin Li, Difei Wang, Hanxiao Yin, Mulin Yang, Feifei Qi, Ying Shan, Huijie Zhao, Jinmin Gao, Dengwen Li, Min Liu, Jun L Zhou, Runa Wang, Zhenqi Yu
| Nature Verified
Abstract Proper orientation of the mitotic spindle is critical for a wide range of biological processes. However, the molecular mechanisms that regulate the formation of the spindle orientation machinery remain incompletely understood. In this study, we identify an essential role for ubiquitin-specific peptidase 21 (USP21)-mediated deubiquitylation in the control of spindle orientation.
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A pilot study of the effect of norepinephrine dose on left ventricular-arterial coupling in patients with septic shock

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By Xueqing Wang, Xuwei Lin, Yingxin Lin, Bin Huang, Qing Feng, Ying Shan, Lei Huang, Yunyin Xu
| Nature Verified
Abstract Left ventricular-arterial (V-A) coupling is a key determinant of cardiovascular performance, which integrates intrinsic myocardial contractility with ventricular afterload. Septic shock frequently disrupts this coupling, and norepinephrine (NE) may worsen it in some scenarios.
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LINC-AC092535.5 regulates MICAL2 mRNA level to inhibit p53-mediated ferroptosis in nasopharyngeal carcinoma

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By Siyu Zhang, Wenyue Chen, Ji Yang, Zhen Ge, Yan Kong, Lili Bao, Ying Shan, Zhiyuan Yang, Wenhui Chen, Si Hui Pan, Yiwen You, Qicheng Zhang, Haiou Yan
| Nature Verified
Abstract Ferroptosis is a form of iron-dependent programmed cell death (PCD) that, once activated, inhibits tumor progression. However, the specific mechanisms influencing ferroptosis in nasopharyngeal carcinoma (NPC) are limited and warrant further investigation. This study proposes that MICAL2 not only influences the nuclear translocation of p53 but also facilitates the ubiquitination of p53 by recruiting the E3 ubiquitination ligase MDM2, leading to its degradation.
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