👤 Shurong Yang

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Also published as: A Yang, A-Li Yang, Acong Yang, Ai-Lun Yang, Aige Yang, Airong Yang, Aiting Yang, Aizhen Yang, Albert C Yang, Alex J T Yang, An-Qi Yang, Andrew Yang, Angang Yang, Angela Wei Hong Yang, Anni Yang, Aram Yang, B Yang, Baigao Yang, Baixia Yang, Bangjia Yang, Bao Yang, Baofeng Yang, Baoli Yang, Baoxin Yang, Baoxue Yang, Bei Yang, Beibei Yang, Biao Yang, Bin Q Yang, Bin Yang, Bing Xiang Yang, Bing Yang, Bingyu Yang, Bo Yang, Bohui Yang, Boo-Keun Yang, Bowen Yang, Boya Yang, Burton B Yang, Byoung Chul Yang, Caimei Yang, Caixia Yang, Caixian Yang, Caixin Yang, Can Yang, Canchai Yang, Ce Yang, Celi Yang, Chan Mo Yang, Chan-Mo Yang, Chang Yang, Chang-Hao Yang, Changheng Yang, Changqing Yang, Changsheng Yang, Changwei Yang, Changyun Yang, Chanjuan Yang, Chao Yang, Chao-Yuh Yang, Chaobo Yang, Chaofei Yang, Chaogang Yang, Chaojie Yang, Chaolong Yang, Chaoping Yang, Chaoqin Yang, Chaoqun Yang, Chaowu Yang, Chaoyun Yang, Chaozhe Yang, Chen Die Yang, Chen Yang, Cheng Yang, Cheng-Gang Yang, Chengfang Yang, Chenghao Yang, Chengkai Yang, Chengkun Yang, Chengran Yang, Chenguang Yang, Chengyingjie Yang, Chengzhang Yang, Chensi Yang, Chensu Yang, Chenxi Yang, Chenyu Yang, Chenzi Yang, Chi Yang, Chia-Wei Yang, Chieh-Hsin Yang, Chien-Wen Yang, Chih-Hao Yang, Chih-Min Yang, Chih-Yu Yang, Chihyu Yang, Ching-Fen Yang, Ching-Wen Yang, Chongmeng Yang, Chuan He Yang, Chuan Yang, Chuanbin Yang, Chuang Yang, Chuanli Yang, Chuhu Yang, Chun Yang, Chun-Chun Yang, Chun-Mao Yang, Chun-Seok Yang, Chunbaixue Yang, Chung-Hsiang Yang, Chung-Shi Yang, Chung-Yi Yang, Chunhua Yang, Chunhui Yang, Chunjie Yang, Chunjun Yang, Chunlei Yang, Chunli Yang, Chunmao Yang, Chunping Yang, Chunqing Yang, Chunru Yang, Chunxiao Yang, Chunyan Yang, Chunyu Yang, Congyi Yang, Cui Yang, Cuiwei Yang, Cunming Yang, Dai-Qin Yang, Dan Yang, Dan-Dan Yang, Dan-Hui Yang, Dandan Yang, Danlu Yang, Danrong Yang, Danzhou Yang, Dapeng Yang, De-Hua Yang, De-Zhai Yang, Decao Yang, Defu Yang, Deguang Yang, Dehao Yang, Dehua Yang, Dejun Yang, Deli Yang, Dengfa Yang, Deok Chun Yang, Deshuang Yang, Di Yang, Dianqiang Yang, Ding Yang, Ding-I Yang, Diya Yang, Diyuan Yang, Dong Yang, Dong-Hua Yang, Dongfeng Yang, Dongjie Yang, Dongliang Yang, Dongmei Yang, Dongren Yang, Dongshan Yang, Dongwei Yang, Dongwen Yang, DuJiang Yang, Eddy S Yang, Edwin Yang, Ei-Wen Yang, Emily Yang, Enlu Yang, Enzhi Yang, Eric Yang, Eryan Yang, Ethan Yang, Eunho Yang, Fajun Yang, Fan Yang, Fang Yang, Fang-Ji Yang, Fang-Kun Yang, Fei Yang, Feilong Yang, Feiran Yang, Feixiang Yang, Fen Yang, Feng Yang, Feng-Ming Yang, Feng-Yun Yang, Fengjie Yang, Fengjiu Yang, Fengjuan Yang, Fenglian Yang, Fengling Yang, Fengping Yang, Fengying Yang, Fengyong Yang, Fu Yang, Fude Yang, Fuhe Yang, Fuhuang Yang, Fumin Yang, Fuquan Yang, Furong Yang, Fuxia Yang, Fuyao Yang, G Y Yang, G Yang, Gan Yang, Gang Yang, Gangyi Yang, Gao Yang, Gaohong Yang, Gaoxiang Yang, Ge Yang, Gong Yang, Gong-Li Yang, Grace H Y Yang, Guan Yang, Guang Yang, Guangdong Yang, Guangli Yang, Guangwei Yang, Guangyan Yang, Guanlin Yang, Gui-Zhi Yang, Guigang Yang, Guitao Yang, Guo Yang, Guo-Can Yang, Guobin Yang, Guofen Yang, Guojun Yang, Guokun Yang, Guoli Yang, Guomei Yang, Guoping Yang, Guoqi Yang, Guosheng Yang, Guotao Yang, Guowang Yang, Guowei Yang, H X Yang, H Yang, Hai Yang, Hai-Chun Yang, Haibo Yang, Haihong Yang, Haikun Yang, Hailei Yang, Hailing Yang, Haiming Yang, Haiping Yang, Haiqiang Yang, Haitao Yang, Haixia Yang, Haiyan Yang, Haiying Yang, Han Yang, Hanchen Yang, Handong Yang, Hang Yang, Hannah Yang, Hanseul Yang, Hanteng Yang, Hao Yang, Hao-Jan Yang, HaoXiang Yang, Haojie Yang, Haolan Yang, Haoqing Yang, Haoran Yang, Haoyu Yang, Harrison Hao Yang, Hee Joo Yang, Heng Yang, Hengwen Yang, Henry Yang, Heqi Yang, Heyi Yang, Heyun Yang, Hoe-Saeng Yang, Hong Yang, Hong-Fa Yang, Hong-Li Yang, HongMei Yang, Hongbing Yang, Hongbo Yang, Hongfa Yang, Honghong Yang, Hongjie Yang, Hongjun Yang, Hongli Yang, Hongling Yang, Hongqun Yang, Hongxia Yang, Hongxin Yang, Hongyan Yang, Hongyu Yang, Hongyuan Yang, Hongyue Yang, Howard H Yang, Howard Yang, Hsin-Chou Yang, Hsin-Jung Yang, Hsin-Sheng Yang, Hua Yang, Hua-Yuan Yang, Huabing Yang, Huafang Yang, Huaijie Yang, Huan Yang, Huanhuan Yang, Huanjie Yang, Huanming Yang, Huansheng Yang, Huanyi Yang, Huarong Yang, Huaxiao Yang, Huazhao Yang, Hui Yang, Hui-Ju Yang, Hui-Li Yang, Hui-Ting Yang, Hui-Yu Yang, Hui-Yun Yang, Huifang Yang, Huihui Yang, Huijia Yang, Huijie Yang, Huiping Yang, Huiran Yang, Huixia Yang, Huiyu Yang, Hung-Chih Yang, Hwai-I Yang, Hye Jeong Yang, Hyerim Yang, Hyun Suk Yang, Hyun-Sik Yang, Ill Yang, Ivana V Yang, J S Yang, J Yang, James Y Yang, Jaw-Ji Yang, Jee Sun Yang, Jenny J Yang, Jerry Yang, Ji Hye Yang, Ji Yang, Ji Yeong Yang, Ji-chun Yang, Jia Yang, Jia-Ling Yang, Jia-Ying Yang, Jiahong Yang, Jiahui Yang, Jiajia Yang, Jiakai Yang, Jiali Yang, Jialiang Yang, Jian Yang, Jian-Bo Yang, Jian-Jun Yang, Jian-Ming Yang, Jian-Ye Yang, JianHua Yang, JianJun Yang, Jianbo Yang, Jiang-Min Yang, Jiang-Yan Yang, Jianing Yang, Jianke Yang, Jianli Yang, Jianlou Yang, Jianmin Yang, Jianming Yang, Jianqi Yang, Jianwei Yang, Jianyu Yang, Jiao Yang, Jiarui Yang, Jiawei Yang, Jiaxin Yang, Jiayan Yang, Jiayi Yang, Jiaying Yang, Jiayue Yang, Jichun Yang, Jie Yang, Jie-Cheng Yang, Jie-Hong Yang, Jie-Kai Yang, Jiefeng Yang, Jiehong Yang, Jieping Yang, Jiexiang Yang, Jihong Yang, Jimin Yang, Jin Yang, Jin-Jian Yang, Jin-Kui Yang, Jin-gang Yang, Jin-ju Yang, Jinan Yang, Jinfeng Yang, Jing Yang, Jing-Quan Yang, Jing-Yu Yang, Jingang Yang, Jingfeng Yang, Jinggang Yang, Jinghua Yang, Jinghui Yang, Jingjing Yang, Jingmin Yang, Jingping Yang, Jingran Yang, Jingshi Yang, Jingwen Yang, Jingya Yang, Jingyan Yang, Jingyao Yang, Jingye Yang, Jingyu Yang, Jingyun Yang, Jingze Yang, Jinhua Yang, Jinhui Yang, Jinjian Yang, Jinpeng Yang, Jinru Yang, Jinshan Yang, Jinsong Yang, Jinsung Yang, Jinwen Yang, Jinzhao Yang, Jiong Yang, Ju Dong Yang, Ju Young Yang, Juan Yang, Juesheng Yang, Jumei Yang, Jun J Yang, Jun Yang, Jun-Hua Yang, Jun-Xia Yang, Jun-Xing Yang, Junbo Yang, Jung Dug Yang, Jung Wook Yang, Jung-Ho Yang, Junhan Yang, Junjie Yang, Junlin Yang, Junlu Yang, Junping Yang, Juntao Yang, Junyao Yang, Junyi Yang, Kai Yang, Kai-Chien Yang, Kai-Chun Yang, Kaidi Yang, Kaifeng Yang, Kaijie Yang, Kaili Yang, Kailin Yang, Kaiwen Yang, Kang Yang, Kang Yi Yang, Kangning Yang, Karen Yang, Ke Yang, Keming Yang, Keping Yang, Kexin Yang, Kuang-Yao Yang, Kui Yang, Kun Yang, Kunao Yang, Kunqi Yang, Kunyu Yang, Kuo Tai Yang, L Yang, Lamei Yang, Lan Yang, Le Yang, Lei Yang, Lexin Yang, Leyi Yang, Li Chun Yang, Li Yang, Li-Kun Yang, Li-Qin Yang, Li-li Yang, LiMan Yang, Lian-he Yang, Liang Yang, Liang-Yo Yang, Liangbin Yang, Liangle Yang, Liangliang Yang, Lichao Yang, Lichuan Yang, Licong Yang, Liehao Yang, Lihong Yang, Lihua Yang, Lihuizi Yang, Lijia Yang, Lijie Yang, Lijuan Yang, Lijun Yang, Lili Yang, Lin Sheng Yang, Lin Yang, Lina Yang, Ling Ling Yang, Ling Yang, Lingfeng Yang, Lingling Yang, Lingzhi Yang, Linlin Yang, Linnan Yang, Linqing Yang, Linquan Yang, Lipeng Yang, Liping Yang, Liting Yang, Liu Yang, Liu-Kun Yang, LiuMing Yang, Liuliu Yang, Liwei Yang, Lixian Yang, Lixue Yang, Long In Yang, Long Yang, Long-Yan Yang, Longbao Yang, Longjun Yang, Longyan Yang, Lu M Yang, Lu Yang, Lu-Hui Yang, Lu-Kun Yang, Lu-Qin Yang, Luda Yang, Man Yang, Manqing Yang, Maojie Yang, Maoquan Yang, Mei Yang, Meichan Yang, Meihua Yang, Meili Yang, Meiting Yang, Meixiang Yang, Meiying Yang, Meng Yang, Menghan Yang, Menghua Yang, Mengjie Yang, Mengli Yang, Mengliu Yang, Mengmeng Yang, Mengsu Yang, Mengwei Yang, Mengying Yang, Miaomiao Yang, Mickey Yang, Min Hee Yang, Min Yang, Mina Yang, Ming Yang, Ming-Hui Yang, Ming-Yan Yang, Minghui Yang, Mingjia Yang, Mingjie Yang, Mingjun Yang, Mingli Yang, Mingqian Yang, Mingshi Yang, Mingyan Yang, Mingyu Yang, Minyi Yang, Misun Yang, Mu Yang, Muh-Hwa Yang, Na Yang, Nan Yang, Nana Yang, Nanfei Yang, Neil V Yang, Ni Yang, Ning Yang, Ningjie Yang, Ningli Yang, Pan Yang, Pan-Chyr Yang, Paul Yang, Peichang Yang, Peiran Yang, Peiyan Yang, Peiying Yang, Peiyuan Yang, Peizeng Yang, Peng Yang, Peng-Fei Yang, PengXiang Yang, Pengfei Yang, Penghui Yang, Pengwei Yang, Pengyu Yang, Phillip C Yang, Pin Yang, Ping Yang, Ping-Fen Yang, Pinghong Yang, Pu Yang, Q H Yang, Q Yang, Qi Yang, Qi-En Yang, Qian Yang, Qian-Jiao Yang, Qian-Li Yang, QianKun Yang, Qiang Yang, Qianhong Yang, Qianqian Yang, Qianru Yang, Qiaoli Yang, Qiaorong Yang, Qiaoyuan Yang, Qifan Yang, Qifeng Yang, Qiman Yang, Qimeng Yang, Qiming Yang, Qin Yang, Qinbo Yang, Qing Yang, Qing-Cheng Yang, Qingcheng Yang, Qinghu Yang, Qingkai Yang, Qinglin Yang, Qingling Yang, Qingmo Yang, Qingqing Yang, Qingtao Yang, Qingwu Yang, Qingya Yang, Qingyan Yang, Qingyi Yang, Qingyu Yang, Qingyuan Yang, Qiong Yang, Qiu Yang, Qiu-Yan Yang, Qiuhua Yang, Qiuhui Yang, Qiulan Yang, Qiuli Yang, Qiuxia Yang, Qiwei Yang, Qiwen Yang, Quan Yang, Quanjun Yang, Quanli Yang, Qun-Fang Yang, R Yang, Ran Yang, Ren-Zhi Yang, Renchi Yang, Renhua Yang, Renjun Yang, Renqiang Yang, Renzhi Yang, Ri-Yao Yang, Richard K Yang, Robert Yang, Rong Yang, Rongrong Yang, Rongxi Yang, Rongyuan Yang, Rongze Yang, Rui Xu Yang, Rui Yang, Rui-Xu Yang, Rui-Yi Yang, Ruicheng Yang, Ruifang Yang, Ruihua Yang, Ruilan Yang, Ruili Yang, Ruiqin Yang, Ruirui Yang, Ruiwei Yang, Rulai Yang, Ruming Yang, Run Yang, Runjun Yang, Runxu Yang, Runyu Yang, Runzhou Yang, Ruocong Yang, Ruoyun Yang, Ruyu Yang, S J Yang, Se-Ran Yang, Sen Yang, Senwen Yang, Seung Yun Yang, Seung-Jo Yang, Seung-Ok Yang, Shan Yang, Shangchen Yang, Shanghua Yang, Shangwen Yang, Shanzheng Yang, Shao-Hua Yang, Shaobin Yang, Shaohua Yang, Shaoling Yang, Shaoqi Yang, Shaoqing Yang, Sheng Sheng Yang, Sheng Yang, Sheng-Huei Yang, Sheng-Qian Yang, Sheng-Wu Yang, ShengHui Yang, Shenglin Yang, Shengnan Yang, Shengqian Yang, Shengyong Yang, Shengzhuang Yang, Shenhui Yang, Shi-Ming Yang, Shiaw-Der Yang, Shifeng Yang, Shigao Yang, Shijie Yang, Shiming Yang, Shipeng Yang, Shiping Yang, Shiu-Ju Yang, Shiyi Yang, Shizhong Yang, Shizhuo Yang, Shu Yang, ShuSheng Yang, Shuai Yang, Shuaibing Yang, Shuaini Yang, Shuang Yang, Shuangshuang Yang, Shucai Yang, Shufang Yang, Shuhua Yang, Shujuan Yang, Shujun Yang, Shulan Yang, Shulin Yang, Shuming Yang, Shun-Fa Yang, Shuo Yang, Shuofei Yang, Shuping Yang, Shuqi Yang, Shuquan Yang, Shushen Yang, Shuye Yang, Shuyu Yang, Si Yang, Si-Fu Yang, Sibao Yang, Sibo Yang, Sichong Yang, Sihui Yang, Sijia Yang, Siqi Yang, Sirui Yang, Sisi Yang, Sitao Yang, Siwen Yang, Siyi Yang, Siyu Yang, Sizhen Yang, Sizhu Yang, Song Yang, Song-na Yang, Songpeng Yang, Songye Yang, Soo Hyun Yang, Su Yang, Su-Geun Yang, Suhong Yang, Sujae Yang, Sujuan Yang, Suk-Kyun Yang, Sun Kyung Yang, Suwol Yang, Suxia Yang, Suyi Yang, Suyu Yang, Tai-Hui Yang, Tailai Yang, Tao Yang, Tengyun Yang, Thomas P Yang, Ti Yang, Tian Yang, Tianbao Yang, Tianfeng Yang, Tianjie Yang, Tianmin Yang, Tianpeng Yang, Tianqiong Yang, Tiantian Yang, Tianxin Yang, Tianyou Yang, Tianyu Yang, Tianze Yang, Tianzhong Yang, Ting Yang, Ting-Xian Yang, Tingting Yang, Tingyu Yang, Tong Yang, Tong Yi Yang, Tong-Xin Yang, Tonglin Yang, Tongren Yang, Tuanmin Yang, Ueng-Cheng Yang, W Yang, Wan-Chen Yang, Wan-Jung Yang, Wang Yang, Wannian Yang, Wei Qiang Yang, Wei Yang, Wei-Fa Yang, Wei-Xin Yang, Weidong Yang, Weiguang Yang, Weihan Yang, Weijian Yang, Weili Yang, Weimin Yang, Weiran Yang, Weiwei Yang, Weixian Yang, Weizhong Yang, Wen Yang, Wen Z Yang, Wen-Bin Yang, Wen-Chin Yang, Wen-He Yang, Wen-Hsuan Yang, Wen-Ming Yang, Wen-Wen Yang, Wen-Xiao Yang, WenKai Yang, Wenbo Yang, Wenchao Yang, Wending Yang, Wenfei Yang, Wenhong Yang, Wenhua Yang, Wenhui Yang, Wenjian Yang, Wenjie Yang, Wenjing Yang, Wenjuan Yang, Wenjun Yang, Wenli Yang, Wenlin Yang, Wenming Yang, Wenqin Yang, Wenshan Yang, Wentao Yang, Wenwen Yang, Wenwu Yang, Wenxin Yang, Wenxing Yang, Wenying Yang, Wenzhi Yang, Wenzhu Yang, William Yang, Woong-Suk Yang, Wu Yang, Wu-de Yang, X Yang, X-J Yang, Xi Yang, Xi-You Yang, Xia Yang, Xian Yang, Xiang Yang, Xiang-Hong Yang, Xiang-Jun Yang, Xianggui Yang, Xianghong Yang, Xiangliang Yang, Xiangling Yang, Xiangqiong Yang, Xiangxiang Yang, Xiangyu Yang, Xiao Yang, Xiao-Dong Yang, Xiao-Fang Yang, Xiao-Hong Yang, Xiao-Jie Yang, Xiao-Juan Yang, Xiao-Meng Yang, Xiao-Ming Yang, Xiao-Qian Yang, Xiao-Yan Yang, Xiao-Ying Yang, Xiao-Yu Yang, Xiao-guang Yang, XiaoYan Yang, Xiaoao Yang, Xiaobin Yang, Xiaobo Yang, Xiaochen Yang, Xiaodan Yang, Xiaodi Yang, Xiaodong Yang, Xiaofei Yang, Xiaofeng Yang, Xiaohao Yang, Xiaohe Yang, Xiaohong R Yang, Xiaohong Yang, Xiaohuang Yang, Xiaohui Yang, Xiaojian Yang, Xiaojie Yang, Xiaojing Yang, Xiaojuan Yang, Xiaojun Yang, Xiaoli Yang, Xiaolu Yang, Xiaomeng Yang, Xiaoming Yang, Xiaonan Yang, Xiaoping Yang, Xiaoqian Yang, Xiaoqin Yang, Xiaoqun Yang, Xiaorong Yang, Xiaoshan Yang, Xiaoshi Yang, Xiaosong Yang, Xiaotian Yang, Xiaotong Yang, Xiaowei Yang, Xiaowen Yang, Xiaoxiao Yang, Xiaoxin Yang, Xiaoxu Yang, Xiaoyao Yang, Xiaoyi Yang, Xiaoyong Yang, Xiaoyu Yang, Xiaoyun Yang, Xiaozhen Yang, Xifei Yang, Xiling Yang, Ximan Yang, Xin Yang, Xin-He Yang, Xin-Yu Yang, Xin-Zhuang Yang, Xing Yang, Xinghai Yang, Xinglong Yang, Xingmao Yang, Xingming Yang, Xingsheng Yang, Xingyu Yang, Xingyue Yang, Xingzhi Yang, Xinjing Yang, Xinming Yang, Xinpu Yang, Xinwang Yang, Xinxin Yang, Xinyan Yang, Xinyi Yang, Xinyu Yang, Xinyue Yang, Xiong Ling Yang, Xiru Yang, Xitong Yang, Xiu Hong Yang, Xiuhua Yang, Xiulin Yang, Xiuna Yang, Xiuqin Yang, Xiurong Yang, Xiuwei Yang, Xiwen Yang, Xiyue Yang, Xu Yang, Xuan Yang, Xue Yang, Xue-Feng Yang, Xue-Ping Yang, Xuecheng Yang, Xuehan Yang, Xuejing Yang, Xuejun Yang, Xueli Yang, Xuena Yang, Xueping Yang, Xuesong Yang, Xuhan Yang, Xuhui Yang, Xuping Yang, Xuyang Yang, Y C Yang, Y F Yang, Y L Yang, Y P Yang, Y Q Yang, Y Yang, Y-T Yang, Ya Yang, Ya-Chen Yang, Yadong Yang, Yafang Yang, Yajie Yang, Yalan Yang, Yali Yang, Yaming Yang, Yan Yang, Yan-Bei Yang, Yan-Ling Yang, Yanan Yang, Yanfang Yang, Yang Yang, Yangfan Yang, Yangyang Yang, Yanhui Yang, Yanjianxiong Yang, Yanling Yang, Yanmei Yang, Yanmin Yang, Yanping Yang, Yanru Yang, Yanting Yang, Yanyan Yang, Yanzhen Yang, Yaorui Yang, Yaping Yang, Yaqi Yang, Yaxi Yang, Ye Yang, Yefa Yang, Yefeng Yang, Yeqing Yang, Yexin Yang, Yi Yang, Yi-Chieh Yang, Yi-Fang Yang, Yi-Feng Yang, Yi-Liang Yang, Yi-Ping Yang, Yi-ning Yang, Yibing Yang, Yichen Yang, Yidong Yang, Yifan Yang, Yifang Yang, Yifei Yang, Yifeng Yang, Yihe Yang, Yijie Yang, Yilian Yang, Yimei Yang, Yimin Yang, Yiming Yang, Yimu Yang, Yin-Rong Yang, Yinfeng Yang, Ying Yang, Ying-Hua Yang, Ying-Ying Yang, Yingdi Yang, Yingjun Yang, Yingqing Yang, Yingrui Yang, Yingxia Yang, Yingyu Yang, Yinhua Yang, Yining Yang, Yinxi Yang, Yiping Yang, Yiting Yang, Yiyi Yang, Yiying Yang, Yong Yang, Yong-Yu Yang, Yongfeng Yang, Yongguang Yang, Yonghong Yang, Yonghui Yang, Yongjia Yang, Yongjie Yang, Yongkang Yang, Yongqiang Yang, Yongsan Yang, Yongxin Yang, Yongxing Yang, Yongzhong Yang, Yoon La Yang, Yoon Mee Yang, Youhua Yang, YoungSoon Yang, Yu Yang, Yu-Fan Yang, Yu-Feng Yang, Yu-Jie Yang, Yu-Shi Yang, Yu-Tao Yang, Yu-Ting Yang, Yuan Yang, Yuan-Han Yang, Yuan-Jian Yang, Yuanhao Yang, Yuanjin Yang, Yuanquan Yang, Yuanrong Yang, Yuanying Yang, Yuanzhang Yang, Yuanzhi Yang, Yuchen Yang, Yucheng Yang, Yue Yang, Yueh-Ning Yang, Yuejin Yang, Yuexiang Yang, Yueze Yang, Yufan Yang, Yuhan Yang, Yuhang Yang, Yuhua Yang, Yujie Yang, Yujing Yang, Yulin Yang, Yuling Yang, Yulong Yang, Yun Yang, YunKai Yang, Yunfan Yang, Yung-Li Yang, Yunhai Yang, Yunlong Yang, Yunmei Yang, Yunwen Yang, Yunyun Yang, Yunzhao Yang, Yupeng Yang, Yuqi Yang, Yuta Yang, Yutao Yang, Yuting Yang, Yutong Yang, Yuwei Yang, Yuxi Yang, Yuxing Yang, Yuxiu Yang, Yuyan Yang, Yuyao Yang, Yuying Yang, Z Yang, Zaibin Yang, Zaiming Yang, Zaiqing Yang, Zanhao Yang, Ze Yang, Zemin Yang, Zeng-Ming Yang, Zengqiang Yang, Zengqiao Yang, Zeyu Yang, Zhang Yang, Zhangping Yang, Zhanyi Yang, Zhao Yang, Zhao-Na Yang, Zhaojie Yang, Zhaoli Yang, Zhaoxin Yang, Zhaoyang Yang, Zhaoyi Yang, Zhehan Yang, Zheming Yang, Zhen Yang, Zheng Yang, Zheng-Fei Yang, Zheng-lin Yang, Zhenglin Yang, Zhengqian Yang, Zhengtao Yang, Zhenguo Yang, Zhengyan Yang, Zhengzheng Yang, Zhengzhong Yang, Zhenhua Yang, Zhenjun Yang, Zhenmei Yang, Zhenqi Yang, Zhenrong Yang, Zhenwei Yang, Zhenxing Yang, Zhenyun Yang, Zhenzhen Yang, Zheyu Yang, Zhi Yang, Zhi-Can Yang, Zhi-Hong Yang, Zhi-Jun Yang, Zhi-Min Yang, Zhi-Ming Yang, Zhi-Rui Yang, Zhibo Yang, Zhichao Yang, Zhifen Yang, Zhigang Yang, Zhihang Yang, Zhihong Yang, Zhikuan Yang, Zhikun Yang, Zhimin Yang, Zhiming Yang, Zhiqiang Yang, Zhitao Yang, Zhiwei Yang, Zhixin Yang, Zhiyan Yang, Zhiyong Yang, Zhiyou Yang, Zhiyuan Yang, Zhongan Yang, Zhongfang Yang, Zhonghua Yang, Zhonghui Yang, Zhongli Yang, Zhongshu Yang, Zhongzhou Yang, Zhou Yang, Zhuliang Yang, Zhuo Yang, Zhuoya Yang, Zhuoyu Yang, Zi F Yang, Zi Yang, Zi-Han Yang, Zi-Wei Yang, Zicong Yang, Zifeng Yang, Zihan Yang, Ziheng Yang, Zijiang Yang, Zishan Yang, Zixia Yang, Zixuan Yang, Ziying Yang, Ziyou Yang, Ziyu Yang, Zong-de Yang, Zongfang Yang, Zongyu Yang, Zunxian Yang, Zuozhen Yang
articles
Wu Yao, Peiyan Yang, Yuanmeng Qi +6 more · 2020 · The Science of the total environment · Elsevier · added 2026-04-24
Silicosis, a severe and irreversible form of pulmonary fibrosis (PF) caused by long-term exposure to dust particles in production environments, is the biggest occupational health concern in China and Show more
Silicosis, a severe and irreversible form of pulmonary fibrosis (PF) caused by long-term exposure to dust particles in production environments, is the biggest occupational health concern in China and most low-income countries. The transdifferentiation of pulmonary fibroblasts is the terminal event in silicosis, and specific transcription factors (TFs) play a crucial role in this condition. However, the relationship between TF-mediated regulation and silicosis remains unknown. We performed a transcriptomic analysis to elucidate this relationship, and our results revealed that two TFs, EGR2 and BHLHE40, were upregulated and five, i.e., TBX2, NR1H3 (LXRα), NR2F1, PPARG (PPARγ), and EPAS1, were downregulated in activated fibroblasts. Notably, PPARγ and LXRα expression was also decreased in an experimental mouse model of silicosis. The mechanism underlying these changes may involve TGF-β1 secretion from silica-exposed alveolar macrophages, causing PPARγ and LXRα downregulation, which in turn would result in aberrant α-SMA transcription. Our results suggest that LXRα is a potential target for the prevention of silicosis and PF. Show less
no PDF DOI: 10.1016/j.scitotenv.2020.141531
NR1H3
Yueyuan Xiao, Haizhen Wang, Chang Wang +7 more · 2020 · Cell cycle (Georgetown, Tex.) · Taylor & Francis · added 2026-04-24
Psoriasis is an immune-mediated chronic inflammatory skin disease. Keratinocyte hyperproliferation has been regarded as a significant event in psoriasis pathogenesis. Considering the vital role of miR Show more
Psoriasis is an immune-mediated chronic inflammatory skin disease. Keratinocyte hyperproliferation has been regarded as a significant event in psoriasis pathogenesis. Considering the vital role of miRNA-mediated mRNA repression in psoriasis pathogenesis, in the present study, we attempted to investigate the mechanism of keratinocyte overproliferation from the point of miRNA-mRNA regulation. Both online microarray expression profiles and experimental results indicated that the expression of LXR-α and PPAR-γ was downregulated in psoriasis lesion skin. LXR-α or PPAR-γ overexpression alone was sufficient to inhibit keratinocyte proliferation, decrease KRT5 and KRT14 protein levels and increase KRT1 and KRT10 protein levels. miR-203 negatively regulated LXR-α and PPAR-γ expression through direct targeting. miR-203 inhibition exerted the opposite effects to LXR-α or PPAR-γ overexpression on HaCaT cells. More importantly, LXR-α or PPAR-γ overexpression could markedly remarkably attenuate the effects of miR-203 overexpression in keratinocytes, indicating that miR-203 promotes keratinocyte proliferation by targeting LXR-α and PPAR-γ. In conclusion, the miR-203-LXR-α/PPAR-γ axis modulates the proliferation of keratinocytes and might be a novel target for psoriasis treatment, which needs further in vivo investigation. Show less
no PDF DOI: 10.1080/15384101.2020.1783934
NR1H3
Haitao Wang, Haifeng Zhu, Xiaodong Yang · 2020 · Immunopharmacology and immunotoxicology · Taylor & Francis · added 2026-04-24
Osteoarthritis (OA) is the most common joint disease that characterized by the degradation of articular cartilage. In this study, we aimed to investigate the anti-inflammatory activity of dioscin on I Show more
Osteoarthritis (OA) is the most common joint disease that characterized by the degradation of articular cartilage. In this study, we aimed to investigate the anti-inflammatory activity of dioscin on IL-1β-stimulated human osteoarthritis chondrocytes. The production of PGE2 and NO was measured in this study. MMP1 and MMP3 were detected by ELISA. The expression of LXRα and NF-κB were tested by western blot analysis. Treatment of dioscin suppressed the production of PGE2 and NO, as well as the expression of COX-2 and iNOS (their key regulatory genes). Dioscin also attenuated the secretion of MMP1 and MMP3. Furthermore, dioscin inhibited the phosphorylation of NF-κB p65 and IκBα induced by IL-1β. The degradation of IκBα induced by IL-1β was also suppressed by dioscin. Dioscin increased the expression of LXRα and pretreatment of GGPP, the LXRα inhibitor, blocked the anti-inflammatory effects of dioscin. In conclusion, this study indicated that dioscin-mediated anti-inflammatory effect may be involved in the activation of LXRα. Show less
no PDF DOI: 10.1080/08923973.2020.1775248
NR1H3
Feizhou Huang, Huaizheng Liu, Zhao Lei +5 more · 2020 · Journal of cellular physiology · Wiley · added 2026-04-24
Nonalcoholic fatty liver disease (NAFLD) is regarded as a threat to public health; however, the pathologic mechanism of NAFLD is not fully understood. We attempted to identify abnormally expressed lon Show more
Nonalcoholic fatty liver disease (NAFLD) is regarded as a threat to public health; however, the pathologic mechanism of NAFLD is not fully understood. We attempted to identify abnormally expressed long noncoding RNA (lncRNAs) and messenger RNA that may affect the occurrence and development of NAFLD in this study. The expression of differentially expressed lncRNAs in NAFLD was determined in oleic acid (OA)-treated L02 cells, and the functions of CCAT1 in lipid droplet formation were evaluated in vitro. Differentially expressed genes (DEGs) were analyzed by microarray analysis, and DEGs related to CCTA1 were selected and verified by weighted correlation network analysis. The dynamic effects of LXRα and CCTA1 on lipid droplet formation and predicted binding was examined. The binding between miR-631 and CCAT1 and LXRα was verified. The dynamic effects of miR-613 inhibition and CCTA1 silencing on lipid droplet formation were examined. The expression and correlations of miR-631, CCAT1, and LXRα were determined in tissue samples. As the results show, CCAT1 was induced by OA and upregulated in NAFLD clinical samples. CCAT1 silencing significantly suppressed lipid droplet accumulation in vitro. LXRα was positively correlated with CCAT1. By inhibiting miR-613, CCAT1 increased the transcription of LXRα and promoted LXRα expression. The expression of LXRα was significantly increased in NAFLD tissues and was positively correlated with CCAT1. In conclusion, CCAT1 increases LXRα transcription by serving as a competing endogenous RNA for miR-613 in an LXRE-dependent manner, thereby promoting lipid droplet formation and NAFLD. CCAT1 and LXRα might be potent targets for NAFLD treatment. Show less
no PDF DOI: 10.1002/jcp.29795
NR1H3
Jianjiao Wang, Zhi Liang, Kunlong Li +5 more · 2020 · Journal of natural products · ACS Publications · added 2026-04-24
Seven unusual new ene-yne hydroquinones (
no PDF DOI: 10.1021/acs.jnatprod.0c00050
NR1H3

NAD

Xiaojing Wei, Ru Jia, Zhao Yang +4 more · 2020 · FEBS letters · Wiley · added 2026-04-24
The nicotinamide adenine dinucleotide (NAD
no PDF DOI: 10.1002/1873-3468.13779
NR1H3
Ting Li, Shu-Mei Hu, Xiao-Yan Pang +9 more · 2020 · Journal of cellular and molecular medicine · Blackwell Publishing · added 2026-04-24
Recent studies have demonstrated that commercially available lipid-lowering drugs cause various side effects; therefore, searching for anti-hyperlipidaemic compounds with lower toxicity is a research Show more
Recent studies have demonstrated that commercially available lipid-lowering drugs cause various side effects; therefore, searching for anti-hyperlipidaemic compounds with lower toxicity is a research hotspot. This study was designed to investigate whether the marine-derived compound, 5-hydroxy-3-methoxy-5-methyl-4-butylfuran-2(5H)-one, has an anti-hyperlipidaemic activity, and the potential underlying mechanism in vitro. Results showed that the furanone had weaker cytotoxicity compared to positive control drugs. In RAW 264.7 cells, the furanone significantly lowered ox-LDL-induced lipid accumulation (~50%), and its triglyceride (TG)-lowering effect was greater than that of liver X receptor (LXR) agonist T0901317. In addition, it significantly elevated the protein levels of peroxisome proliferator-activated receptors (PPARα) and ATP-binding cassette (ABC) transporters, which could be partially inhibited by LXR antagonists, GSK2033 and SR9243. In HepG2 cells, it significantly decreased oleic acid-induced lipid accumulation, enhanced the protein levels of low-density lipoprotein receptor (LDLR), ABCG5, ABCG8 and PPARα, and reduced the expression of sterol regulatory element-binding protein 2 (~32%). PPARα antagonists, GW6471 and MK886, could significantly inhibit the furanone-induced lipid-lowering effect. Furthermore, the furanone showed a significantly lower activity on the activation of the expression of lipogenic genes compared to T0901317. Taken together, the furanone exhibited a weak cytotoxicity but had powerful TC- and TG-lowering effects most likely through targeting LXRα and PPARα, respectively. These findings indicate that the furanone has a potential application for the treatment of dyslipidaemia. Show less
no PDF DOI: 10.1111/jcmm.15012
NR1H3
Yu Chen, Yi-Fan Zhao, Jing Yang +6 more · 2020 · Food & function · Royal Society of Chemistry · added 2026-04-24
Selenium (Se) is an essential trace element for living organisms and plays diverse biological roles. Endometritis is a common reproductive disorder in dairy cows, causing huge economic losses. In this Show more
Selenium (Se) is an essential trace element for living organisms and plays diverse biological roles. Endometritis is a common reproductive disorder in dairy cows, causing huge economic losses. In this study, we explored the effects of Se on lipopolysaccharide (LPS)-induced endometritis in mice and expounded its underlying mechanism of action. We validated the anti-inflammatory effects of Se in vivo by establishing a mouse model of endometriosis induced by LPS. Se significantly reversed the LPS-induced uterine histopathological changes, MPO activity and inflammatory cytokine levels in vivo. Simultaneously, TLR4 and its downstream signaling pathways, lipid rafts and cholesterol levels in the tissues were also attenuated by Se under LPS stimulation. In addition, the molecular mechanism of the Se anti-inflammatory effect was clarified in mouse endometrial epithelial cells. Se inhibited TLR4-mediated NF-κB and IRF3 signal transduction pathways to reduce the production of inflammatory factors. We found that Se promoted the consumption of cholesterol to suppress the lipid rafts coming into being and inhibited the TLR4 positioning to the lipid raft to prevent the inflammatory response caused by LPS. Meanwhile, Se activated the LxRα-ABCA1 pathway to cause the outflow of cholesterol in cells. The anti-inflammatory effect of Se was disrupted by silencing LxRα. In conclusion, Se exerted anti-inflammatory effects most likely by the LxRα-ABCA1 pathway activation, which inhibited lipid rafts by depleting cholesterol and ultimately impeded the migration of TLR4 to lipid rafts. Show less
no PDF DOI: 10.1039/c9fo02415h
NR1H3
Pingshi Gao, Lei Wang, Nanfei Yang +5 more · 2020 · Environment international · Elsevier · added 2026-04-24
Bisphenol A (BPA) and its replacement analog, bisphenol S (BPS), have been proposed as environmental obesogen to disrupt the lipid metabolism through regulating peroxisome proliferator-activated recep Show more
Bisphenol A (BPA) and its replacement analog, bisphenol S (BPS), have been proposed as environmental obesogen to disrupt the lipid metabolism through regulating peroxisome proliferator-activated receptor gamma (PPARγ) receptor. However, there is a dearth of information on whether this biological effect can occur in human macrophage, a cell type which closely interacts with adipocytes and hepatocytes to control lipid metabolism. Here, we for the first time investigate the activity of BPA and BPS on PPARγ pathway in human macrophages. The results demonstrated that BPA and BPS served as activators of PPARγ in human macrophage cell line, and significantly induced the expression of lipid metabolism-related genes, including fatty acid binding protein 4 (FABP4), cluster of differentiation 36 (CD36) and nuclear receptor subfamily 1 group H member 3 (NR Show less
no PDF DOI: 10.1016/j.envint.2019.105328
NR1H3
Guan Yang, Luc Van Kaer · 2020 · Cell death & disease · Nature · added 2026-04-24
no PDF DOI: 10.1038/s41419-020-2568-z
PIK3C3
Pan Yang, Ruirui Song, Ning Li +7 more · 2020 · Environmental toxicology · Wiley · added 2026-04-24
Increased deposition of silica dust in pulmonary interstitial tissues leads to silicosis, in which autophagy plays a defensive role in silica dust-associated stress response and cell death. Our previo Show more
Increased deposition of silica dust in pulmonary interstitial tissues leads to silicosis, in which autophagy plays a defensive role in silica dust-associated stress response and cell death. Our previous studies revealed that silica dust exposure contributed to autophagy in pulmonary macrophages in vivo, while the specific regulatory mechanism is still unclear. This study aimed to figure out the regulatory mechanism as well as the role of autophagy in the pathogenesis of experimental silicosis. We used 3-methyladenine (3-MA) and ABT-737 to suppress the expression of phosphatidylinositol 3-kinase catalytic subunit type 3 (PIK3C3) and B cell leukemia/lymphoma 2 (Bcl-2), two critical initiators of autophagy, and detected and evaluated the autophagy in NR8383 cells with or without silica dust exposure. We found that exposure of silica dust increased autophagy in NR8383 cells and elevated the expression of Beclin1 and PIK3C3, but it reduced the expression of Bcl-2. The relationship among Beclin1, PIK3C3, and Bcl-2 were then investigated using immunoprecipitation analysis, and we found that suppression of PIK3C3 and/or Bcl-2 using 3-MA and/or ABT-737 could alter the autophagy induced by silica dust in NR8383 cells, and the complexes of Beclin1/PIK3C3 and Beclin1/Bcl-2 were both downregulated, which may be that inhibition of PIK3C3 and Bcl-2 altered the affinity of Beclin1 with PIK3C3 and Bcl-2 and lead to the silence of PIK3C3 signaling. These findings indicate that silica dust exposure induces autophagy via changing the connectivity of Beclin1 from Bcl-2 to PIK3C3. Show less
no PDF DOI: 10.1002/tox.22910
PIK3C3
Cefan Zhou, Xuehong Qian, Miao Hu +12 more · 2020 · Autophagy · Taylor & Francis · added 2026-04-24
Macroautophagy/autophagy plays key roles in development, oncogenesis, and cardiovascular and metabolic diseases. Autophagy-specific class III phosphatidylinositol 3-kinase complex I (PtdIns3K-C1) is e Show more
Macroautophagy/autophagy plays key roles in development, oncogenesis, and cardiovascular and metabolic diseases. Autophagy-specific class III phosphatidylinositol 3-kinase complex I (PtdIns3K-C1) is essential for autophagosome formation. However, the regulation of this complex formation requires further investigation. Here, we discovered that STYK1 (serine/threonine/tyrosine kinase 1), a member of the receptor tyrosine kinases (RTKs) family, is a new upstream regulator of autophagy. We discovered that STYK1 facilitated autophagosome formation in human cells and zebrafish, which was characterized by elevated LC3-II and lowered SQSTM1/p62 levels and increased puncta formation by several marker proteins, such as ATG14, WIPI1, and ZFYVE1. Moreover, we observed that STYK1 directly binds to the PtdIns3K-C1 complex as a homodimer. The binding with this complex was promoted by Tyr191 phosphorylation, by means of which the kinase activity of STYK1 was elevated. We also demonstrated that STYK1 elevated the serine phosphorylation of BECN1, thereby decreasing the interaction between BECN1 and BCL2. Furthermore, we found that STYK1 preferentially facilitated the assembly of the PtdIns3K-C1 complex and was required for PtdIns3K-C1 complex kinase activity. Taken together, our findings provide new insights into autophagy induction and reveal evidence of novel crosstalk between the components of RTK signaling and autophagy. Show less
no PDF DOI: 10.1080/15548627.2019.1687212
PIK3C3
Xiangli Bai, XiaoYan Yang, Xiong Jia +15 more · 2020 · Autophagy · Taylor & Francis · added 2026-04-24
Diabetes is a recognized high-risk factor for the development of atherosclerosis, in which macroautophagy/autophagy is emerging to play essential roles. The retention of low-density lipoprotein (LDL) Show more
Diabetes is a recognized high-risk factor for the development of atherosclerosis, in which macroautophagy/autophagy is emerging to play essential roles. The retention of low-density lipoprotein (LDL) particles in subendothelial space following transcytosis across the endothelium is the initial step of atherosclerosis. Here, we identified that high glucose could promote atherosclerosis by stimulating transcytosis of LDL. By inhibiting AMPK-MTOR-PIK3C3 pathway, high glucose suppresses the CAV-CAVIN-LC3B-mediated autophagic degradation of CAV1; therefore, more CAV1 is accumulated in the cytosol and utilized to form more caveolae in the cell membrane and facilitates the LDL transcytosis across endothelial cells. For a proof of concept, higher levels of lipids were accumulated in the subendothelial space of umbilical venous walls from pregnant women with gestational diabetes mellitus (GDM), compared to those of pregnant women without GDM. Our results reveal that high glucose stimulates LDL transcytosis by a novel CAV1-CAVIN1-LC3B signaling-mediated autophagic degradation pathway. 3-MA: 3-methyladenine; ACTB: actin beta; AMPK: AMP-activated protein kinase; Bafi: bafilomycin A Show less
no PDF DOI: 10.1080/15548627.2019.1659613
PIK3C3
Kejia Liu, Chu Guo, Yimin Lao +5 more · 2020 · Autophagy · Taylor & Francis · added 2026-04-24
The roles of SUMOylation and the related enzymes in autophagic regulation are unclear. Based on our previous studies that identified the SUMO2/3-specific peptidase SENP3 as an oxidative stress-respons Show more
The roles of SUMOylation and the related enzymes in autophagic regulation are unclear. Based on our previous studies that identified the SUMO2/3-specific peptidase SENP3 as an oxidative stress-responsive molecule, we investigated the correlation between SUMOylation and macroautophagy/autophagy. We found that AL: autolysosome; AP: autophagosome; ATG: autophagy related; ATG14: autophagy related 14; BECN1: beclin 1, autophagy related; cKO: conditional knockout; co-IP: co-immunoprecipitation; CQ: chloroquine; EBSS: Earle's balanced salt solution; GFP: green fluorescent protein; MAP1LC3/LC3: microtubule-associated protein 1 light chain 3; MTOR: mechanistic target of rapamycin kinase; NAC: N-acetyl-L-cysteine; PIK3C3: phosphatidylinositol 3-kinase catalytic subunit type 3; PTM: post-translational modification; RFP: red fluorescent protein; ROS: reactive oxygen species; RUBCN/rubicon: RUN domain and cysteine-rich domain containing, BECN1-interacting protein; SENP3: SUMO specific peptidase 3; shRNA: small hairpin RNA; siRNA: small interfering RNA; SQSTM1: sequestosome 1; SUMO: small ubiquitin-like modifier; UVRAG: UV radiation resistance associated gene. Show less
no PDF DOI: 10.1080/15548627.2019.1647944
PIK3C3
Bo Yang, Qinghong Xue, Jiaona Guo +8 more · 2020 · Autophagy · Taylor & Francis · added 2026-04-24
Macroautophagy/autophagy is an essential cellular response in the fight against intracellular pathogens. Although some viruses can escape from or utilize autophagy to ensure their own replication, the Show more
Macroautophagy/autophagy is an essential cellular response in the fight against intracellular pathogens. Although some viruses can escape from or utilize autophagy to ensure their own replication, the responses of autophagy pathways to viral invasion remain poorly documented. Here, we show that peste des petits ruminants virus (PPRV) infection induces successive autophagic signalling in host cells via distinct and uncoupled molecular pathways. Immediately upon invasion, PPRV induced a first transient wave of autophagy via a mechanism involving the cellular pathogen receptor NECTIN4 and an AKT-MTOR-dependent pathway. Autophagic detection showed that early PPRV infection not only increased the amounts of autophagosomes and LC3-II but also downregulated the phosphorylation of AKT-MTOR. Subsequently, we found that the binding of viral protein H to NECTIN4 ultimately induced a wave of autophagy and inactivated the AKT-MTOR pathway, which is a critical step for the control of infection. Soon after infection, new autophagic signalling was initiated that required viral replication and protein expression. Interestingly, expression of IRGM and HSPA1A was significantly upregulated following PPRV replication. Strikingly, knockdown of IRGM and HSPA1A expression using small interfering RNAs impaired the PPRV-induced second autophagic wave and viral particle production. Moreover, IRGM-interacting PPRV-C and HSPA1A-interacting PPRV-N expression was sufficient to induce autophagy through an IRGM-HSPA1A-dependent pathway. Importantly, syncytia formation could facilitate sustained autophagy and the replication of PPRV. Overall, our work reveals distinct molecular pathways underlying the induction of self-beneficial sustained autophagy by attenuated PPRV, which will contribute to improving the use of vaccines for therapy. Show less
no PDF DOI: 10.1080/15548627.2019.1643184
PIK3C3
Xiao-Wei Zhang, Ji-Chao Zhou, Dian Peng +14 more · 2020 · Autophagy · Taylor & Francis · added 2026-04-24
Impaired macroautophagy/autophagy is involved in the pathogenesis of hepatic fibrosis. However, how aberrant autophagy promotes fibrosis is far from understood. Here, we aimed to define a previously u Show more
Impaired macroautophagy/autophagy is involved in the pathogenesis of hepatic fibrosis. However, how aberrant autophagy promotes fibrosis is far from understood. Here, we aimed to define a previously unrevealed pro-fibrotic mechanism for the stress protein TRIB3 (tribbles pseudokinase 3)-mediated autophagy dysfunction. Human fibrotic liver tissues were obtained from patients with cirrhosis who underwent an open surgical repair process. The functional implications of TRIB3 were evaluated in mouse models of hepatic fibrosis induced by bile duct ligation (BDL) or thioacetamide (TAA) injection. Human fibrotic liver tissues expressed higher levels of TRIB3 and selective autophagic receptor SQSTM1/p62 (sequestosome 1) than nonfibrotic tissues and the elevated expression of TRIB3 and SQSTM1 was positively correlated in the fibrotic tissues. Silencing Show less
no PDF DOI: 10.1080/15548627.2019.1635383
PIK3C3
Rong Qiao, Feifei Di, Jun Wang +7 more · 2020 · Cancer management and research · added 2026-04-24
Early detection is essential to improve the survival and life quality of lung cancer (LC) patients. Changes of peripheral blood DNA methylation could be associated with malignancy but were mostly stud Show more
Early detection is essential to improve the survival and life quality of lung cancer (LC) patients. Changes of peripheral blood DNA methylation could be associated with malignancy but were mostly studied in Caucasians. Here, in a Chinese population, we performed mass spectrometry assays to investigate the association between very early stage LC and methylation levels of RAPSN in the peripheral blood by a case-control cohort using of 221 LC patients (93.2% LC at stage I) and 285 unrelated cancer free control individuals. The odds ratios (ORs) of all CpG sites were evaluated for their risk to LC using inter-quartile analyses by logistic regression. In general, we observed an association between very early LC and decreased methylation of RAPSN_CpG₁.15 and RAPSN_CpG₃.4 (referring to Q4, OR range from 1.64 to 1.81, Our study reveals an association between RAPSN hypomethylation in peripheral blood and LC and suggests the occurrence of altered blood-based methylation at the early stage of cancer. Show less
no PDF DOI: 10.2147/CMAR.S275321
RAPSN
Yuhan Yang, Hequn Jiang, Wanxin Li +9 more · 2020 · Aging · Impact Journals · added 2026-04-24
Colorectal cancer (CRC) is the third most common type of cancer worldwide. Metastasis and chemoresistance are regarded as the two leading causes of treatment failure and high mortality in CRC. Forkhea Show more
Colorectal cancer (CRC) is the third most common type of cancer worldwide. Metastasis and chemoresistance are regarded as the two leading causes of treatment failure and high mortality in CRC. Forkhead Box M1 (FOXM1) has been involved in malignant behaviors of cancer. However, the role and mechanism of FOXM1 in simultaneously regulating metastasis and chemoresistance of CRC remain poorly understood. Here, we found that FOXM1 was overexpressed in oxaliplatin- and vincristine-resistant CRC cells (HCT-8/L-OHP and HCT-8/VCR) with enhanced metastatic potential, compared with HCT-8 cells. FOXM1 overexpression increased migration, invasion and drug-resistance to oxaliplatin and vincristine in HCT-8 cells, while FOXM1 knockdown using shFOXM1 impaired metastasis and drug-resistance in HCT-8/L-OHP and HCT-8/VCR cells. Moreover, FOXM1 up-regulated Snail to trigger epithelial-mesenchymal transition-like molecular changes and multidrug-resistance protein P-gp expression, while silencing Snail inhibited FOXM1-induced metastasis and drug-resistance. We further identified that disheveled-2 (DVL2) was crucial for FOXM1-induced Snail expression, metastasis and chemoresistance. Furthermore, FOXM1 bound to DVL2, and enhanced nuclear translocation of DVL2 and DVL2-mediated transcriptional activity of Wnt/β-catenin known to induce Snail expression. In conclusion, FOXM1/DVL2/Snail axis triggered aggressiveness of CRC. Blocking FOXM1/DVL2/Snail pathway simultaneously inhibited metastasis and chemoresistance in CRC cells, providing a new strategy for successful CRC treatment. Show less
no PDF DOI: 10.18632/aging.202300
SNAI1
Huating Wu, Dawei Xie, Yingxia Yang +3 more · 2020 · Technology in cancer research & treatment · SAGE Publications · added 2026-04-24
Ultrasound-targeted microbubble destruction (UTMD) has been found to be an effective method for delivering microRNAs (miRNAs, miRs). The current study is aimed at discovering the potential anti-cancer Show more
Ultrasound-targeted microbubble destruction (UTMD) has been found to be an effective method for delivering microRNAs (miRNAs, miRs). The current study is aimed at discovering the potential anti-cancer effects of UTMD-mediated miR-206 on HCC. In our study, the expressions of miR-206 and peptidyl-prolyl MiR-206 expression was downregulated while PPIB expression was upregulated in HCC, and PPIB was recognized as a target gene of miR-206 in HCC tissues. UTMD-mediated miR-206 inhibited HCC cell migration and invasion while promoting apoptosis via regulating the expressions of proteins related to apoptosis, migration, and invasion by targeting PPIB. Our results suggested that the delivery of UTMD-mediated miR-206 could be a potential therapeutic method for HCC treatment, given its effects on inhibiting cell migration and invasion and promoting cell apoptosis. Show less
no PDF DOI: 10.1177/1533033820959355
SNAI1
Li Li, Ruihong Zhang, Hailei Yang +4 more · 2020 · FEBS open bio · Wiley · added 2026-04-24
Growth differentiation factor 15 (GDF15), a member of the transforming growth factor β (TGF-β) superfamily, is a prognostic biomarker of cervical cancer. In addition, GDF15 has been reported to enhanc Show more
Growth differentiation factor 15 (GDF15), a member of the transforming growth factor β (TGF-β) superfamily, is a prognostic biomarker of cervical cancer. In addition, GDF15 has been reported to enhance the migration of colorectal cancer cells and liver cancer stem-like cells. However, the mechanism by which GDF15 promotes cervical cancer cell migration is not completely understood. Here, we report that GDF15 expression is enhanced in cervical cancer tissues, as well as in cultured cervical cancer cells. ShGDF15 transfection markedly inhibited expression of Vimentin, N-cadherin and Snail1, and resulted in up-regulation of E-cadherin expression in HT-3 and HeLa cells. Moreover, knockdown of GDF15 suppressed wound healing rate and reduced the number of invasive cells. Furthermore, knockdown of GDF15 significantly suppressed the expression of phosphorylated Smad2 and Smad3. The addition of TGF-β1 partially abolished the inhibitory effects of GDF15 knockdown on the migration and invasion of cervical cancer cells. In summary, we report here that GDF15 knockdown inhibits migration and invasion of cervical cancer cells in vitro through the TGF-β/Smad2/3/Snail1 pathway. Show less
no PDF DOI: 10.1002/2211-5463.13013
SNAI1
Wenli Qian, Qi Li, Xinglong Wu +11 more · 2020 · Oncogene · Nature · added 2026-04-24
Snail is a master inducer of epithelial-mesenchymal transition (EMT) and metastasis, however, Snail protein is labile and is quickly degraded through the predominate ubiquitination-mediated proteasome Show more
Snail is a master inducer of epithelial-mesenchymal transition (EMT) and metastasis, however, Snail protein is labile and is quickly degraded through the predominate ubiquitination-mediated proteasome pathway. Deubiquitinases (DUBs) can counteract the Snail degradation process to maintain high level of Snail protein in cancer cells. In this study, we screened a cDNA library containing 79 DUBs, and discovered that a panel of DUBs consisting of USP13, USP28, USP29, USP37, OTUD6A, and DUB3 can markedly stabilize Snail protein, with USP29 displaying the strongest activity to prevent Snail degradation. Mechanistically, USP29 enhances the interaction of Snail and SCP1, resulting in simultaneous dephosphorylation and deubiquitination of Snail and thereafter cooperative prevention of Snail degradation. Biologically, ectopic expression of USP29 promotes gastric cancer cell migration, and depletion of Snail abolishes USP29-mediated cell migration; and USP29 can be induced by major EMT and metastatic inducing factors such as TGFβ, TNFα, and hypoxia. More importantly, high expression levels of Snail, USP29, and SCP1 are associated with poor survival and prognosis. Collectively, these data indicate that Snail is a crucial substrate for USP29 to promote cell migration and USP29/SCP1 complex may be new therapeutic targets to treat metastatic cancer. Show less
no PDF DOI: 10.1038/s41388-020-01471-0
SNAI1
Deheng Li, Liangdong Li, Wentao Yang +6 more · 2020 · Annals of translational medicine · added 2026-04-24
Breast cancer (BC) is one of the most lethal malignant tumors and the leading cause of cancer-related death worldwide. Although early diagnostic techniques for BC have been well developed, 40% of case Show more
Breast cancer (BC) is one of the most lethal malignant tumors and the leading cause of cancer-related death worldwide. Although early diagnostic techniques for BC have been well developed, 40% of cases are still diagnosed at the advanced stage, while for BC patients with distant metastases, the 5-year survival rate is usually lower than 30%. The Snail family, generally regarded as transcriptional repressors, has been indicated to be an essential prognostic factor in malignant tumors. However, limited data exist on public databases concerning the prognostic value of individual Snail family members in BC, especially SNAI3. Data from public databases including cBioPortal for Cancer Genomics, Gene Expression Omnibus, UCSC Xena Browser, and Human Protein Atlas (HPA) were downloaded. Based on the Kaplan¬-Meier plotter platform, correlation of the three members of the Snail family and prognosis in BC were analyzed. Individual Snail family members and their co-expressed genes were respectively enriched on different pathways and biological processes via the functional enrichment analysis (FunRich) tool. High SNAI1 mRNA expression was associated with shorter distant metastasis-free survival (DMFS) in all BC patients regardless of PAM50 subtype. Conversely, high SNAI3 mRNA expression was associated with longer DMFS. Although the presence of SNAI2 expression was significantly associated with DMFS in the whole cohort, no significant correlation was found in patients with luminal A or HER2 subtype. For patients with the most diverse clinicopathological features, high SNAI1 expression was associated with poor survival, with the converse being true for SNAI3. However, the impact on prognosis of patients with different clinicopathological features produced by SNAI2 expression was inconclusive. Furthermore, we discovered that SNAI1 or SNAI2 and their co-expressed genes frequently enriched receptor tyrosine kinase (RTK) signaling and integrin-related pathways which mainly functioned on epithelial-mesenchymal transition and were further involved in several processes of signal transduction and cell communication. Furthermore, as SNAI3, along with its co-expressed genes, enriched immune-related pathways, it may thus play a role in mediating the immune system. Our analysis revealed that SNAI1 mRNA expression may potentially be a negative prognostic factor, whereas SNAI3 mRNA was associated with positive prognosis in BC. Therefore, the assessment of SNAI1 and SNAI3 expression may be valuable for predicting prognosis in BC patients. Show less
no PDF DOI: 10.21037/atm-20-681
SNAI1
Xiaobin Guo, Rui Zhu, Aiping Luo +4 more · 2020 · Journal of experimental & clinical cancer research : CR · BioMed Central · added 2026-04-24
Overexpression of eukaryotic translation initiation factor 3H (EIF3H) predicts cancer progression and poor prognosis, but the mechanism underlying EIF3H as an oncogene remains unclear in esophageal sq Show more
Overexpression of eukaryotic translation initiation factor 3H (EIF3H) predicts cancer progression and poor prognosis, but the mechanism underlying EIF3H as an oncogene remains unclear in esophageal squamous cell carcinoma (ESCC). TCGA database and the immunohistochemistry (IHC) staining of ESCC samples were used and determined the upregulation of EIF3H in ESCC. CCK8 assay, colony formation assay and transwell assay were performed to examine the ability of cell proliferation and mobility in KYSE150 and KYSE510 cell lines with EIF3H overexpression or knockdown. Xenograft and tail-vein lung metastatic mouse models of KYSE150 cells with or without EIF3H knockdown were also used to confirm the function of EIF3H on tumor growth and metastasis in vivo. A potential substrate of EIF3H was screened by co-immunoprecipitation assay (co-IP) combined with mass spectrometry in HEK293T cells. Their interaction and co-localization were confirmed using reciprocal co-IP and immunofluorescence staining assay. The function of EIF3H on Snail ubiquitination and stability was demonstrated by the cycloheximide (CHX) pulse-chase assay and ubiquitination assay. The correlation of EIF3H and Snail in clinical ESCC samples was verified by IHC. We found that EIF3H is significantly upregulated in esophageal cancer and ectopic expression of EIF3H in ESCC cell lines promotes cell proliferation, colony formation, migration and invasion. Conversely, genetic inhibition of EIF3H represses ESCC tumor growth and metastasis in vitro and in vivo. Moreover, we identified EIF3H as a novel deubiquitinating enzyme of Snail. We demonstrated that EIF3H interacts with and stabilizes Snail through deubiquitination. Therefore, EIF3H could promote Snail-mediated EMT process in ESCC. In clinical ESCC samples, there is also a positive correlation between EIF3H and Snail expression. Our study reveals a critical EIF3H-Snail signaling axis in tumor aggressiveness in ESCC and provides EIF3H as a promising biomarker for ESCC treatment. Show less
no PDF DOI: 10.1186/s13046-020-01678-9
SNAI1
Chenghao Lu, Zheyu Yang, Dingye Yu +2 more · 2020 · Pathology, research and practice · Elsevier · added 2026-04-24
Colorectal cancer (CRC) was one of the most malignant tumors worldwide due to its metastasis. Epithelial-to-mesenchymal transition (EMT) plays an important role in CRC migration, and transforming grow Show more
Colorectal cancer (CRC) was one of the most malignant tumors worldwide due to its metastasis. Epithelial-to-mesenchymal transition (EMT) plays an important role in CRC migration, and transforming growth factor-β (TGF-β) works as a dominating cytokine in CRC EMT process. Here, we originally identified RUNX1 as an important factor among TGF-β induced EMT in CRC. We found that RUNX1 was overexpressed with the treatment of TGF-β, accompanied with enhanced cancer cell migration and EMT which was characterized by up-graded N-Cadherin levels. Vice versa, knockdown of RUNX1 attenuated the migration ability of TGF-β induced CRC cells. In addition, decreased expression of N-Cadherin suggested that EMT was also attenuated after knocking down RUNX1. Similar decrease was observed in EMT regulator snail family transcriptional repressor 1 (SNAI1). And the knockdown effect of RUNX1 cannot be reversed by the addition of TGF-β. Moreover, we observed that RUNX1 expression was higher in CRC tumor tissues than in normal epithelial tissues. The enhanced expression was detected in cancer cell nucleus. These results revealed RUNX1 could regulate colorectal cancer migration via TGF-β signaling pathway, and RUNX1 might serve as a potential target for preventing CRC metastasis. Show less
no PDF DOI: 10.1016/j.prp.2020.153142
SNAI1
Ji-Min Li, Fang Yang, Juan Li +3 more · 2020 · Medical science monitor : international medical journal of experimental and clinical research · added 2026-04-24
BACKGROUND Emerging evidence suggests the involvement of Reelin in chemoresistance in various cancers. However, its function in cisplatin (DDP) sensitivity of non-small cell lung cancer (NSCLC) needs Show more
BACKGROUND Emerging evidence suggests the involvement of Reelin in chemoresistance in various cancers. However, its function in cisplatin (DDP) sensitivity of non-small cell lung cancer (NSCLC) needs to be investigated. MATERIAL AND METHODS Reelin expression in cisplatin-sensitive A549 cells and cisplatin-resistant NSCLC (A549/DDP) cells was analyzed by western blot analysis. qRT-PCR, western blotting, immunofluorescence, CCK-8 assays, Annexin V/propidium iodide apoptosis assay, and Transwell migration assays were carried out to determine the function of Reelin on DDP resistance. RESULTS Reelin was markedly increased in A549/DDP cells relative to A549 cells. Knockdown of Reelin enhanced DDP chemosensitivity of A549/DDP cells, whereas overexpression of Reelin enhanced DDP resistance of A549, H1299, and H460 cells. Reelin induced DDP resistance in NSCLC cells via facilitating epithelial-mesenchymal transition (EMT). Furthermore, Reelin modulated p38/GSK3ß signal transduction and promoted Snail (EMT-associated transcription factor) expression. Suppression of p38/Snail reversed Reelin-induced EMT and resistance of NSCLC cells to DDP. CONCLUSIONS These data indicated that Reelin induces DDP resistance of NSCLC by regulation of the p38/GSK3ß/Snail/EMT signaling pathway and provide evidence that Reelin suppression can be an effective strategy to suppress DDP resistance in NSCLC. Show less
no PDF DOI: 10.12659/MSM.925298
SNAI1
Wei Lv, Mengxi Huan, Wenjie Yang +8 more · 2020 · Biochemical and biophysical research communications · Elsevier · added 2026-04-24
Prostate cancer (PCa) is the second leading cause of cancer-associated mortality in men. Speckle-type pox virus and zinc finger protein (SPOP), the most frequently mutated gene in PCa, functions as a Show more
Prostate cancer (PCa) is the second leading cause of cancer-associated mortality in men. Speckle-type pox virus and zinc finger protein (SPOP), the most frequently mutated gene in PCa, functions as a tumor suppressor via degradation of cancer-promoting substrates. However, its upstream regulation in PCa metastasis remains poorly determined. Here, in a Snail-induced metastatic PCa model, we observed an accelerated degradation of SPOP protein in cells, which is crucial for the PCa migration and activation of the AKT signaling pathway. Mechanistically, we demonstrated that binding to Snail promoted SPOP ubiquitination and degradation. Moreover, the bric-a-brac/tramtrack/broad complex (BTB) domain of SPOP is turned out to be essential for Snail-mediated SPOP degradation. Thus, our findings reveal a post-translational level regulation of SPOP expression that facilitates the metastasis of PCa cells. Show less
no PDF DOI: 10.1016/j.bbrc.2020.05.187
SNAI1
Ting Yang, Wei-Cong Chen, Pei-Cong Shi +7 more · 2020 · Journal of experimental & clinical cancer research : CR · BioMed Central · added 2026-04-24
Long noncoding RNAs (lncRNAs) are considered critical regulators in cancers; however, the clinical significance and mechanisms of MAPKAPK5-AS1 (hereinafter referred to as MK5-AS1) in colorectal cancer Show more
Long noncoding RNAs (lncRNAs) are considered critical regulators in cancers; however, the clinical significance and mechanisms of MAPKAPK5-AS1 (hereinafter referred to as MK5-AS1) in colorectal cancer (CRC) remain mostly unknown. In this study, quantitative real-time PCR (qPCR) and western blotting were utilized to detect the levels of MK5-AS1, let-7f-1-3p and MK5 (MAPK activated protein kinase 5) in CRC tissues and cell lines. The biological functions of MK5-AS1, let-7f-1-3p and MK5 in CRC cells were explored using Cell Counting Kit-8 (CCK8), colony formation and transwell assays. The potential mechanisms of MK5-AS1 were evaluated by RNA pull-down, RNA immunoprecipitation (RIP), dual luciferase reporter assay, chromatin immunoprecipitation (ChIP) and bioinformatics analysis. The effects of MK5-AS1 and MK5 on CRC were investigated by a xenotransplantation model. We confirmed that MK5-AS1 was significantly increased in CRC tissues. Knockdown of MK5-AS1 suppressed cell migration and invasion in vitro and inhibited lung metastasis in mice. Mechanistically, MK5-AS1 regulated SNAI1 expression by sponging let-7f-1-3p and cis-regulated the adjacent gene MK5. Moreover, MK5-AS1 recruited RBM4 and eIF4A1 to promote the translation of MK5. Our study verified that MK5 promoted the phosphorylation of c-Jun, which activated the transcription of SNAI1 by directly binding to its promoter. MK5-AS1 cis-regulated the nearby gene MK5 and acted as a let-7f-1-3p sponge, playing a vital role in CRC tumorigenesis. This study could provide novel insights into molecular therapeutic targets of CRC. Show less
no PDF DOI: 10.1186/s13046-020-01633-8
SNAI1
Lingyu Song, Yan Wang, Yunhuan Zhen +5 more · 2020 · Biotechnology letters · Springer · added 2026-04-24
Cancer metastasis is the primary cause of death in patients diagnosed with colorectal cancer. Piperine, an active nontoxic ingredient in pepper, has potent anti-inflammatory and anti-cancer properties Show more
Cancer metastasis is the primary cause of death in patients diagnosed with colorectal cancer. Piperine, an active nontoxic ingredient in pepper, has potent anti-inflammatory and anti-cancer properties. However, little is known about the anti-migratory and anti-invasive effects of piperine on colorectal cancer. We demonstrated piperine inhibited the migration and invasion of colorectal cancer cells. Then, we found piperine reversed the biomarker expression of epithelial-to-mesenchymal transition (EMT), and suppressed the EMT regulator Snail. Furthermore, signal transducers and activators of transcription 3 (STAT3) was downregulated by piperine. Finally, STAT3 inhibitors were applied to observe the role of STAT3 in colorectal cancer migration, invasion and EMT. Collectively, piperine inhibits colorectal cancer migratory and invasive capacities through STAT3/Snail mediated EMT. Therefore, piperine could be applied as a possible therapeutic regimen for the prevention of colorectal cancer metastasis. Show less
no PDF DOI: 10.1007/s10529-020-02923-z
SNAI1
Guoqing Wan, Jiang Zhu, Xuefeng Gu +7 more · 2020 · British journal of cancer · Nature · added 2026-04-24
Human Schlafen 5 (SLFN5) has been reported to inhibit or promote cell invasion in tumours depending on their origin. However, its role in breast cancer (BRCA) is undetermined. Differential expression Show more
Human Schlafen 5 (SLFN5) has been reported to inhibit or promote cell invasion in tumours depending on their origin. However, its role in breast cancer (BRCA) is undetermined. Differential expression analyses using The Cancer Genome Atlas (TCGA) data, clinical samples and cell lines were performed. Lentiviral knockdown and overexpression experiments were performed to detect changes in cell morphology, molecular markers and invasion. Chromatin immunoprecipitation-sequencing (ChIP-Seq) and luciferase reporter assays were performed to detect the SLFN5-binding motif. TCGA, clinical samples and cell lines showed that SLFN5 expression was negatively correlated with BRCA metastasis. SLFN5 knockdown induced epithelial-mesenchymal transition (EMT) and enhanced invasion in BRCA cell lines. However, overexpression triggered mesenchymal-epithelial transition (MET). SLFN5 inhibited the expression of ZEB1 but not ZEB2, SNAI1, SNAI2, TWIST1 or TWIST2. Knockdown and overexpression of ZEB1 indicated that it was a mediator of the SLFN5-governed phenotype and invasion changes. Moreover, SLFN5 inhibited ZEB1 transcription by directly binding to the SLFN5-binding motif on the ZEB1 promoter, but a SLFN5 C-terminal deletion mutant did not. SLFN5 regulates reversible epithelial and mesenchymal transitions, and inhibits BRCA metastasis by suppression of ZEB1 transcription, suggesting that SLFN5 could be a potential target for BRCA therapy. Show less
no PDF DOI: 10.1038/s41416-020-0873-z
SNAI1
Ji Hye Yang, Nam Hee Kim, Jun Seop Yun +11 more · 2020 · Life science alliance · added 2026-04-24
Despite the importance of mitochondrial fatty acid oxidation (FAO) in cancer metabolism, the biological mechanisms responsible for the FAO in cancer and therapeutic intervention based on catabolic met Show more
Despite the importance of mitochondrial fatty acid oxidation (FAO) in cancer metabolism, the biological mechanisms responsible for the FAO in cancer and therapeutic intervention based on catabolic metabolism are not well defined. In this study, we observe that Snail (SNAI1), a key transcriptional repressor of epithelial-mesenchymal transition, enhances catabolic FAO, allowing pro-survival of breast cancer cells in a starved environment. Mechanistically, Snail suppresses mitochondrial ACC2 (ACACB) by binding to a series of E-boxes located in its proximal promoter, resulting in decreased malonyl-CoA level. Malonyl-CoA being a well-known endogenous inhibitor of fatty acid transporter carnitine palmitoyltransferase 1 (CPT1), the suppression of ACC2 by Snail activates CPT1-dependent FAO, generating ATP and decreasing NADPH consumption. Importantly, combinatorial pharmacologic inhibition of pentose phosphate pathway and FAO with clinically available drugs efficiently reverts Snail-mediated metabolic reprogramming and suppresses in vivo metastatic progression of breast cancer cells. Our observations provide not only a mechanistic link between epithelial-mesenchymal transition and catabolic rewiring but also a novel catabolism-based therapeutic approach for inhibition of cancer progression. Show less
no PDF DOI: 10.26508/lsa.202000683
SNAI1