👤 Xiying Li

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Also published as: A Li, Ai-Jun Li, Ai-Qin Li, Ailing Li, Aimin Li, Aixin Li, Alexander H Li, Alexander Li, Amy Li, An-Qi Li, AnHai Li, Anan Li, Andrew C Li, Ang Li, Anna Fen-Yau Li, Annie Li, Anqi Li, Anyao Li, Ao Li, Aowen Li, Aoxi Li, Audrey Li, Bai-Qiang Li, Baichuan Li, Baiqiang Li, Baixing Li, Baizhou Li, Bang-Yan Li, Bao Li, Bao-Shan Li, Baoguang Li, Baoguo Li, Baohong Li, Baohua Li, Baolin Li, Baoqi Li, Baoqing Li, Baosheng Li, Baoting Li, Bei Li, Bei-Bei Li, Beibei Li, Beixu Li, Ben Li, Ben-Shang Li, Benyi Li, Biao Li, Bichun Li, Bin Li, Bin-Kui Li, Binbin Li, Bing Li, Bing-Heng Li, Bing-Hui Li, Bing-Mei Li, Bingbing Li, Binghu Li, Binghua Li, Bingjie Li, Bingjue Li, Bingkun Li, Binglan Li, Bingong Li, Bingshan Li, Bingsheng Li, Bingsong Li, Bingxin Li, Binjun Li, Binkui Li, Binru Li, Binxing Li, Biyu Li, Bizhi Li, Bo Li, BoWen Li, Bohao Li, Bohua Li, Bolun Li, Boru Li, Botao Li, Boxuan Li, Boya Li, Boyang Li, Bugao Li, C H Li, C Li, C X Li, C Y Li, Caesar Z Li, Cai Li, Cai-Hong Li, Caihong Li, Caili Li, Caixia Li, Caiyu Li, Caiyun Li, Can Li, Cang Li, Caolong Li, Chang Li, Chang-Da Li, Chang-Ping Li, Chang-Sheng Li, Chang-Yan Li, Chang-hai Li, Changcheng Li, Changgui Li, Changhong Li, Changhui Li, Changjiang Li, Changkai Li, Changqing Li, Changwei Li, Changxian Li, Changyan Li, Changyu Li, Changzheng Li, Chanjuan Li, Chanyuan Li, Chao Bo Li, Chao Li, Chaochen Li, Chaojie Li, Chaonan Li, Chaoqian Li, Chaowei Li, Chaoying Li, Chen Li, Chen-Chen Li, Chen-Lu Li, Chen-Xi Li, Chenfeng Li, Cheng Li, Cheng-Lin Li, Cheng-Tian Li, Cheng-Wei Li, Chengbin Li, Chengcheng Li, Chenghao Li, Chenghong Li, Chengjian Li, Chengjun Li, Chenglan Li, Chenglong Li, Chengnan Li, Chengping Li, Chengqian Li, Chengquan Li, Chengsi Li, Chenguang Li, Chengwen Li, Chengxin Li, Chengyun Li, Chenhao Li, Chenjie Li, Chenli Li, Chenlin Li, Chenlong Li, Chenlu Li, Chenmeng Li, Chenrui Li, Chensheng Li, Chenwen Li, Chenxi Li, Chenxiao Li, Chenxin Li, Chenxuan Li, Chenyang Li, Chenyao Li, Chenyu Li, Cheung Li, Chi-Ming Li, Chi-Yuan Li, Chia Li, Chia-Yang Li, Chien-Feng Li, Chien-Hsiu Li, Chien-Te Li, Chih-Chi Li, Chitao Li, Chiyang Li, Chong Li, Chongyang Li, Chongyi Li, Chris Li, Chu-Qiao Li, Chuan F Li, Chuan Li, Chuan-Hai Li, Chuan-Yun Li, Chuanbao Li, Chuanfang Li, Chuang Li, Chuangpeng Li, Chuanning Li, Chuanyin Li, Chumei Li, Chun Li, Chun-Bo Li, Chun-Lai Li, Chun-Mei Li, Chun-Quan Li, Chun-Xiao Li, Chun-Xu Li, Chung-Hao Li, Chung-I Li, Chunhong Li, Chunhui Li, Chunjie Li, Chunjun Li, Chunlan Li, Chunlian Li, Chunliang Li, Chunlin Li, Chunmei Li, Chunmiao Li, Chunqing Li, Chunqiong Li, Chunshan Li, Chunsheng Li, Chunting Li, Chunxia Li, Chunxiao Li, Chunxing Li, Chunxue Li, Chunya Li, Chunyan Li, Chunyi Li, Chunying Li, Chunyu Li, Chunzhu Li, Chuzhong Li, Cien Li, Cong Li, Congcong Li, Congfa Li, Conghui Li, Congjiao Li, Conglin Li, Congxin Li, Congye Li, Cui Li, Cui-lan Li, Cuicui Li, Cuiguang Li, Cuilan Li, Cuiling Li, Cun Li, Cunxi Li, Cyril Li, D C Li, Da Li, Da-Hong Li, Da-Jin Li, Da-Lei Li, Da-wei Li, DaZhuang Li, Dacheng Li, Dai Li, Daiyue Li, Dalei Li, Dali Li, Dalin Li, Dan C Li, Dan Li, Dan-Dan Li, Dan-Ni Li, Dandan Li, Daniel Tian Li, Danjie Li, Danni Li, Danxi Li, Danyang Li, Daoyuan Li, Dapei Li, Dawei Li, Dayong Li, Dazhi Li, De-Jun Li, De-Tao Li, Dechao Li, Defa Li, Defeng Li, Defu Li, Dehai Li, Deheng Li, Dehua Li, Dejun Li, Demin Li, Deming Li, Dengfeng Li, Dengke Li, Dengxiong Li, Deqiang Li, Desen Li, Desheng Li, Dexiong Li, Deyu Li, Dezhi Li, Di Li, Di-Jie Li, Dianjie Li, Dijie Li, Ding Li, Ding Yang Li, Ding-Biao Li, Ding-Jian Li, Dingchen Li, Dingshan Li, Diyan Li, Dong Li, Dong Sheng Li, Dong-Jie Li, Dong-Ling Li, Dong-Run Li, Dong-Yun Li, Dong-fei Li, Dongbiao Li, Dongdong Li, Dongfang Li, Dongfeng Li, Donghe Li, Donghua Li, Dongliang Li, Dongmei Li, Dongmin Li, Dongnan Li, Dongtao Li, Dongyang Li, Dongye Li, Duan Li, Duanbin Li, Duanxiang Li, Dujuan Li, Duo Li, Duoyun Li, Ellen Li, En Li, En-Min Li, Enhao Li, Enhong Li, Enxiao Li, F Li, Fa-Hong Li, Fa-Hui Li, Fadi Li, Fan Li, Fang Li, Fangqi Li, Fangyan Li, Fangyong Li, Fangyuan Li, Fangzhou Li, Fei Li, Fei-Lin Li, Fei-feng Li, Feifei Li, Feilong Li, Fen Li, Feng Li, Feng-Feng Li, Fengfeng Li, Fengjuan Li, Fengli Li, Fengqi Li, Fengqiao Li, Fengqing Li, Fengxia Li, Fengxiang Li, Fengyi Li, Fengyuan Li, Fu-Rong Li, Fugen Li, Fuhai Li, Fujun Li, Fulun Li, Fuping Li, Fusheng Li, Fuyu Li, Fuyuan Li, G Li, G-P Li, Gaijie Li, Gaizhen Li, Gaizhi Li, Gan Li, Gang Li, Ganggang Li, Gao-Fei Li, Gaoyuan Li, Ge Li, Gen Li, Gen-Lin Li, Gerard Li, Gong-Hua Li, Gongda Li, Guanbin Li, Guandu Li, Guang Li, Guang Y Li, Guang-Li Li, Guang-Xi Li, Guangda Li, Guangdi Li, Guanghua Li, Guanghui Li, Guangjin Li, Guangli Li, Guanglu Li, Guanglve Li, Guangming Li, Guangping Li, Guangpu Li, Guangqiang Li, Guangquan Li, Guangwen Li, Guangxi Li, Guangxiao Li, Guangyan Li, Guangzhao Li, Guangzhen Li, Guannan Li, Guanqiao Li, Guanyu Li, Gui Lin Li, Gui-Bo Li, Gui-Hua Li, Gui-Rong Li, Gui-xing Li, Guigang Li, Guihua Li, Guilan Li, Guisen Li, Guixia Li, Guixin Li, Guiyang Li, Guiying Li, Guiyuan Li, Guo Li, Guo-Chun Li, Guo-Jian Li, Guo-Li Li, Guo-Ping Li, Guo-Qiang Li, Guobin Li, Guoge Li, Guohong Li, Guohua Li, Guohui Li, Guojin Li, Guojun Li, Guoli Li, Guoping Li, Guoqin Li, Guoqing Li, Guowei Li, Guoxi Li, Guoxiang Li, Guoxing Li, Guoyan Li, Guoyin Li, H J Li, H Li, H-F Li, H-H Li, H-J Li, Hai Li, Hai-Yun Li, Haibin Li, Haibo Li, Haifeng Li, Haihong Li, Haihua Li, Haijun Li, Hailong Li, Haimin Li, Haiming Li, Hainan Li, Haipeng Li, Hairong Li, Haitao Li, Haitong Li, Haixia Li, Haiyan Li, Haiyang Li, Haiying Li, Haiyu Li, Han Li, Han-Bing Li, Han-Bo Li, Han-Ni Li, Han-Ru Li, Han-Wei Li, Hanbin Li, Hanbing Li, Hanbo Li, Handong Li, Hang Li, Hangwen Li, Hanjun Li, Hankun Li, Hanlu Li, Hanmei Li, Hanqi Li, Hanqin Li, Hansen Li, Hanting Li, Hanxiao Li, Hanxue Li, Hao Li, Hao-Fei Li, Haojing Li, Haolong Li, Haomiao Li, Haoqi Li, Haoran Li, Haotong Li, Haoxian Li, Haoyu Li, Haying Li, He Li, He-Zhen Li, Hecheng Li, Hegen Li, Hehua Li, Heng Li, Heng-Zhen Li, Hengguo Li, Hengtong Li, Hengyu Li, Hening Li, Hewei Li, Hexin Li, Heying Li, Hong Li, Hong-Chun Li, Hong-Lan Li, Hong-Lian Li, Hong-Mei Li, Hong-Tao Li, Hong-Wen Li, Hong-Yan Li, Hong-Yu Li, Hong-Zheng Li, Hongbo Li, Hongchang Li, Hongde Li, Honggang Li, Hongguo Li, Honghua Li, Honghui Li, Hongjia Li, Hongjiang Li, Hongjuan Li, Honglei Li, Hongli Li, Honglian Li, Hongliang Li, Honglin Li, Hongling Li, Honglong Li, Hongmei Li, Hongmin Li, Hongming Li, Hongqin Li, Hongquan Li, Hongru Li, Hongsen Li, Hongwei Li, Hongxia Li, Hongxin Li, Hongxing Li, Hongxue Li, Hongyan Li, Hongye Li, Hongyi Li, Hongyu Li, Hongyun Li, Hongzhe K Li, Hongzheng Li, Hongzhi Li, Hsiao-Fen Li, Hsiao-Hui Li, Hsin-Hua Li, Hsin-Yun Li, Hu Li, Hua Li, Hua-Zhong Li, Huabin Li, Huafang Li, Huafu Li, Huaixing Li, Huaiyuan Li, Hualian Li, Hualing Li, Huamao Li, Huan Li, Huanan Li, Huang Li, Huangbao Li, Huangyuan Li, Huanhuan Li, Huanjun Li, Huanqing Li, Huanqiu Li, Huaping Li, Huashun Li, Huawei Li, Huayao Li, Huayin Li, Huaying Li, Hui Li, Hui-Jun Li, Hui-Long Li, Hui-Ping Li, Huibo Li, Huifang Li, Huifeng Li, Huihuang Li, Huihui Li, Huijie Li, Huijuan Li, Huijun Li, Huilan Li, Huili Li, Huiliang Li, Huilin Li, Huilong Li, Huimin Li, Huiping Li, Huiqin Li, Huiqing Li, Huiqiong Li, Huiting Li, Huixia Li, Huixue Li, Huiying Li, Huiyou Li, Huiyuan Li, Huizi Li, Hujie Li, Hulun Li, Hung Li, Hung-Yuan Li, Ivan Li, J Li, J T Li, Jason Li, Jen-Ming Li, Jenny J Li, Ji Li, Ji Xia Li, Ji-Cheng Li, Ji-Feng Li, Ji-Liang Li, Ji-Lin Li, Ji-Min Li, Jia Li, Jia Li Li, Jia-Da Li, Jia-Huan Li, Jia-Peng Li, Jia-Ru Li, Jia-Xin Li, Jiabei Li, Jiachen Li, Jiacheng Li, Jiafang Li, Jiafei Li, Jiahao Li, Jiahui Li, Jiajia Li, Jiajie Li, Jiajing Li, Jiajun Li, Jiajv Li, Jiali Li, Jialin Li, Jialing Li, Jialun Li, Jiaming Li, Jian Li, Jian'an Li, Jian-Jun Li, Jian-Mei Li, Jian-Qiang Li, Jian-Shuang Li, Jianan Li, Jianang Li, Jianbin Li, Jianbo Li, Jianchun Li, Jiandong Li, Jianfang Li, Jianfeng Li, Jiang Li, Jiangan Li, Jiangbo Li, Jiangchao Li, Jiangfeng Li, Jianglin Li, Jianglong Li, Jiangtao Li, Jiangui Li, Jianguo Li, Jiangxia Li, Jiangya Li, Jianhai Li, Jianhua Li, Jiani Li, Jianing Li, Jianliang Li, Jianlin Li, Jianmin Li, Jiannan Li, Jianping Li, Jianrong Li, Jianrui Li, Jiansheng Li, Jianshuang Li, Jianwei Li, Jianxin Li, Jianxiong Li, Jianye Li, Jianyi Li, Jianyong Li, Jianyu Li, Jianzhong Li, Jiao Li, Jiao-Jiao Li, Jiaomei Li, Jiaping Li, Jiaqi Li, Jiawei Li, Jiaxi Li, Jiaxin Li, Jiaxuan Li, Jiayan Li, Jiayang Li, Jiayi Li, Jiaying Li, Jiayu Li, Jiayuan Li, Jiazhou Li, Jicheng Li, Jie Li, Jie-Pin Li, Jie-Shou Li, Jiehan Li, Jiejia Li, Jiejie Li, Jiejing Li, Jieming Li, Jiequn Li, Jieshou Li, Jiexi Li, Jiexin Li, Jiezhen Li, Jifang Li, Jihua Li, Jin Li, Jin-Jiang Li, Jin-Liang Li, Jin-Long Li, Jin-Mei Li, Jin-Ping Li, Jin-Qiu Li, Jin-Wei Li, Jin-Xiu Li, Jinchen Li, Jinfang Li, Jinfeng Li, Jing Li, Jing-Jing Li, Jing-Ming Li, Jing-Yao Li, Jing-Yi Li, Jing-gao Li, Jingcheng Li, Jingchun Li, Jingfeng Li, Jinghao Li, Jinghui Li, Jingjing Li, Jingke Li, Jinglin Li, Jingmei Li, Jingming Li, Jingping Li, Jingqi Li, Jingshang Li, Jingshu Li, Jingtong Li, Jingui Li, Jingwen Li, Jingxia Li, Jingxiang Li, Jingxin Li, Jingya Li, Jingyi Li, Jingyong Li, Jingyu Li, Jingyun Li, Jinhua Li, Jinhui Li, Jinjie Li, Jinku Li, Jinlan Li, Jinliang Li, Jinlin Li, Jinman Li, Jinming Li, Jinping Li, Jinsong Li, Jinwei Li, Jinxia Li, Jinxin Li, Jinzhi Li, Jiong Li, Jiong-Ming Li, Jipeng Li, Jiqing Li, Jisen Li, Jisheng Li, Jiuke Li, Jiuyi Li, Jiwei Li, Jiwen Li, Jixi Li, Jixuan Li, Jiyang Li, Jiyuan Li, John Zhong Li, Jonathan Z Li, Joyce Li, Ju-Rong Li, Juan Li, Juan-Juan Li, Juanjuan Li, Juanling Li, Juanni Li, Jufang Li, Julia Li, Jun Li, Jun Z Li, Jun-Cheng Li, Jun-Jie Li, Jun-Ling Li, Jun-Ru Li, Jun-Yan Li, Jun-Ying Li, JunBo Li, Junfeng Li, Junhong Li, Junhui Li, Junjie Li, Junjun Li, Junming Li, Junping Li, Junqin Li, Junru Li, Junsheng Li, Juntong Li, Junxian Li, Junxin Li, Junxu Li, Junya Li, Junyi Li, Junying Li, Justin Li, Jutang Li, Juxue Li, K-L Li, Ka Li, Ka Wan Li, Kai Li, Kai-Wen Li, Kaibin Li, Kaibo Li, Kaifeng Li, Kailong Li, Kaimi Li, Kainan Li, Kaiwei Li, Kaixin Li, Kaiyi Li, Kaiyuan Li, Kang Li, Kangli Li, Kangyuan Li, Karen Li, Kathy H Li, Kawah Li, Ke Li, KeZhong Li, Keanning Li, Kecheng Li, Kechun Li, Keguo Li, Kejuan Li, Keke Li, Kening Li, Kenli Li, Kenneth Kai Wang Li, Keqing Li, Keshen Li, Keying Li, Keyuan Li, Kezhen Li, Kongdong Li, Kuan Li, Kui Li, Kuiliang Li, Kun Li, Kun-Peng Li, Kun-Ping Li, Kun-Xin Li, Kunlin Li, Kunlong Li, Kunlun Li, Kunpeng Li, L I Li, L K Li, L Li, L P Li, L-Y Li, Lai K Li, Laiqing Li, Lamei Li, Lan Li, Lan-Juan Li, Lan-Lan Li, Lanfang Li, Lang Li, Lanjuan Li, Lanlan Li, Lanzhou Li, Le Li, Le-Le Li, Le-Ying Li, Lei Li, Leilei Li, Leipeng Li, Letai Li, Leyao Li, Li Li, Li-Min Li, Li-Na Li, Lian Li, Lianbing Li, Liang Li, Liangdong Li, Liangji Li, Liangkui Li, Liangqian Li, Lianhong Li, Lianjian Li, Lianyong Li, Liao-Yuan Li, Lieyou Li, Liguo Li, Lihong Li, Lihua Li, Lijia Li, Lijuan Li, Lijun Li, Lili Li, Liliang Li, Liling Li, Liming Li, Lin Li, Lin-Feng Li, Linchuan Li, Linfeng Li, Ling Li, Ling-Jie Li, Ling-Ling Li, Ling-Zhi Li, Lingjiang Li, Lingjie Li, Lingjun Li, Lingling Li, Lingxi Li, Lingyan Li, Lingyi Li, Lingzhi Li, Linhong Li, Linke Li, Linlin Li, Linqi Li, Linqing Li, Linsheng Li, Linting Li, Linxin Li, Linyan Li, Linying Li, Lipeng Li, Liping Li, Liqin Li, Liqun Li, Lirong Li, Lisha Li, Litao Li, Liuzheng Li, Liwei Li, Lixi Li, Lixia Li, Lixiang Li, Liyan Li, Long Li, Long Shan Li, Long-Yan Li, Longhui Li, Longxuan Li, Longyu Li, Lu Li, Lu-Yun Li, Lucia M Li, Lucy Li, Luhan Li, Lujiao Li, Lujie Li, Lulu Li, Luquan Li, Luxuan Li, Luyao Li, Luying Li, M D Li, M Li, M V Li, M-J Li, Man Li, Man-Xiang Li, Man-Zhi Li, Mangmang Li, Manjiang Li, Manna Li, Manru Li, Manxia Li, Mao Li, Maogui Li, Maolin Li, Maoquan Li, Maosheng Li, Marilyn Li, Mei Li, Mei-Lan Li, Mei-Ya Li, Mei-Zhen Li, Meifang Li, Meifen Li, Meijia Li, Meilan Li, Meiqing Li, Meitao Li, Meiting Li, Meiyan Li, Meiying Li, Meiyue Li, Meizi Li, Melody M H Li, Meng Li, Meng-Hua Li, Meng-Jun Li, Meng-Meng Li, Meng-Miao Li, Meng-Yang Li, Meng-Yao Li, Meng-Yue Li, MengGe Li, Mengfan Li, Menghua Li, Mengjiao Li, Mengjuan Li, Mengling Li, Menglu Li, Mengmeng Li, Mengqing Li, Mengqiu Li, Mengsen Li, Mengshi Li, Mengxi Li, Mengxia Li, Mengxuan Li, Mengyang Li, Mengyao Li, Mengying Li, Mengyuan Li, Mengyun Li, Mengze Li, Mi Li, Mian Li, Miao Li, Miao X Li, Miaoxin Li, Michelle Li, Mimi Li, Min Li, Min-Dian Li, Min-Rui Li, Min-jun Li, Minerva X Li, Ming D Li, Ming Li, Ming V Li, Ming Xing Li, Ming Zhou Li, Ming-Han Li, Ming-Hao Li, Ming-Jiang Li, Ming-Kai Li, Ming-Qing Li, Ming-Wei Li, Ming-Xing Li, Ming-Yang Li, Mingdan Li, Mingfang Li, Mingfei Li, Minghao Li, Minghua Li, Minghui Li, Mingjiang Li, Mingjie Li, Mingjun Li, Mingke Li, Mingkun Li, Mingli Li, Minglong Li, Minglun Li, Mingna Li, Mingqiang Li, Mingquan Li, Mingrui Li, Mingwei Li, Mingxi Li, Mingxia Li, Mingxing Li, Mingxu Li, Mingxuan Li, Mingyang Li, Mingyao Li, Mingyue Li, Mingzhe Li, Mingzhou Li, Minhui Li, Minle Li, Minmin Li, Minqi Li, Minyue Li, Minze Li, Minzhe Li, Miyang Li, Mo Li, Mohan Li, Monica M Li, Moyi Li, Mufan Li, Mulin Jun Li, Muzi Li, N Li, Na Li, Naishi Li, Nan Li, Nan-Nan Li, Nana Li, Nanjun Li, Nanlong Li, Nanxing Li, Nanzhen Li, Ni Li, Nianfu Li, Nianyu Li, Nien Li, Nien-Chen Li, Nien-Chi Li, Ning Li, Ningyan Li, Ningyang Li, Niu Li, Nuomin Li, O Li, P H Li, P Li, Pan Li, Panlong Li, Panyuan Li, Pei Li, Pei-Lin Li, Pei-Qin Li, Pei-Shan Li, Pei-Ying Li, Pei-Zhi Li, PeiQi Li, Peibo Li, Peifen Li, Peifeng Li, Peihong Li, Peihua Li, Peilin Li, Peilong Li, Peining Li, Peipei Li, Peiqin Li, Peiran Li, Peiwu Li, Peixin Li, Peiyu Li, Peiyuan Li, Peiyun Li, Peng Li, Peng Peng Li, Peng-li Li, Pengcui Li, Penghui Li, Pengjie Li, Pengju Li, Pengsong Li, Pengyang Li, Pengyu Li, Pengyun Li, Pik Yi Li, Pilong Li, Pindong Li, Ping Li, Ping'an Li, Pinghua Li, Pingping Li, Pu Li, Pu-Yu Li, Q Li, Qi Li, Qi-Fu Li, Qi-Jing Li, Qian Li, Qian-Qian Li, Qiang Li, Qiang-Ming Li, Qiankun Li, Qianqian Li, Qiao Li, Qiao-Xin Li, Qiaolian Li, Qiaoqiao Li, Qibing Li, Qifang Li, Qihang Li, Qihua Li, Qiji Li, Qijun Li, Qilan Li, Qilong Li, Qin Li, Qiner Li, Qing Li, Qing Run Li, Qing-Chang Li, Qing-Fang Li, Qing-Min Li, Qing-Wei Li, Qingchao Li, Qingfang Li, Qingfeng Li, Qinggang Li, Qinghe Li, Qinghong Li, Qinghua Li, Qingjie Li, Qinglan Li, Qingli Li, Qinglin Li, Qingling Li, Qingqin S Li, Qingrun Li, Qingshang Li, Qingsheng Li, Qingxian Li, Qingyang Li, Qingyu Li, Qingyuan Li, Qingyun Li, Qinqin Li, Qinrui Li, Qintong Li, Qiong Li, Qionghua Li, Qipei Li, Qiqiong Li, Qiu Li, Qiufeng Li, Qiuhong Li, Qiusheng Li, Qiuxuan Li, Qiuya Li, Qiuyan Li, Qiwei Li, Qiyong Li, Qizhai Li, Quan Li, Quan-Zhong Li, Quanpeng Li, Quanshun Li, Quanzhang Li, Qun Li, R H L Li, R Li, Ran Li, Ranchang Li, Ranran Li, Ranwei Li, Ren Li, Ren-Ke Li, Rena Li, Roger Li, Ronald Li, Rong Li, Rong-Bing Li, Ronggui Li, Rongkai Li, Rongling Li, Rongqing Li, Rongsong Li, Rongxia Li, Rongyao Li, Rosa J W Li, Ru Li, Ru-Hao Li, Rui Li, Rui-Fang Li, Rui-Han Li, Rui-Jún Eveline Li, Ruibing Li, Ruidong Li, Ruifang Li, Ruihuan Li, Ruijia Li, Ruijin Li, Ruikai Li, Ruitong Li, Ruiwen Li, Ruixi Li, Ruixia Li, Ruixue Li, Ruiyang Li, Rujia Li, Rulin Li, Rumei Li, Runbing Li, Runwen Li, Runzhao Li, Runzhen Li, Runzhi Li, Ruobing Li, Ruolin Li, Ruonan Li, Ruotai Li, Ruotian Li, Ruotong Li, Ruyi Li, Ruyue Li, S A Li, S E Li, S L Li, S Li, S S Li, S-C Li, Sai Li, Saijuan Li, Sainan Li, San-Feng Li, Sanqiang Li, Senlin Li, Senmao Li, Sha Li, Sha-Sha Li, Shan Li, Shan-Shan Li, Shangjia Li, Shanglai Li, Shangming Li, Shanhang Li, Shanpeng Li, Shanshan Li, Shanyi Li, Shao-Dan Li, Shaobin Li, Shaodan Li, Shaofei Li, Shaoguang Li, Shaojian Li, Shaojing Li, Shaoliang Li, Shaomin Li, Shaoqi Li, Shaoyong Li, Shasha Li, Shawn S C Li, Shawn Shun-Cheng Li, Shen Li, Sheng Li, Sheng-Fu Li, Sheng-Jie Li, Sheng-Qing Li, Sheng-Tien Li, Shengbiao Li, Shengbin Li, Shengchao A Li, Shenghao Li, Shengjie Li, Shengli Li, Shengliang Li, Shengsheng Li, Shengwen Li, Shengxian Li, Shengxu Li, Shengze Li, Sherly X Li, Shi Li, Shi-Fang Li, Shi-Guang Li, Shi-Hong Li, Shi-Ying Li, Shibao Li, Shibo Li, Shichao Li, Shigang Li, Shihao Li, Shiheng Li, Shihong Li, Shijie Li, Shijun Li, Shikang Li, Shilan Li, Shili Li, Shiliang Li, Shilin Li, Shilun Li, Shiqi Li, Shiquan Li, Shisheng Li, Shishi Li, Shitao Li, Shiya Li, Shiyan Li, Shiyang Li, Shiyi Li, Shiying Li, Shiyu Li, Shiyue Li, Shiyun Li, Shu Li, Shu-Fang Li, Shu-Fen Li, Shu-Feng Li, Shu-Hong Li, Shu-Qi Li, Shu-Xin Li, Shuai Li, Shuaicheng Li, Shuang Li, Shuang-Ling Li, Shuangding Li, Shuangfei Li, Shuanglong Li, Shuangmei Li, Shuangshuang Li, Shuangxiu Li, Shubo Li, Shude Li, Shufen Li, Shugang Li, Shuguang Li, Shuhao Li, Shuhua Li, Shuhui Li, Shujiao Li, Shujie Li, Shujin Li, Shujing Li, Shulin Li, Shun Li, Shunhua Li, Shunle Li, Shunqin Li, Shunqing Li, Shunwang Li, Shuo Li, Shupeng Li, Shuqiang Li, Shuwei Li, Shuwen Li, Shuying Li, Shuyu D Li, Shuyu Dan Li, Shuyuan Li, Shuyue Li, Si Li, Si-Wei Li, Si-Xing Li, Si-Ying Li, Si-Yuan Li, Sibing Li, Sichen Li, Sichong Li, Side Li, Siguang Li, Sijie Li, Simin Li, Siming Li, Sin-Lun Li, Siqi Li, Sitao Li, Siting Li, Siwen Li, Siyi Li, Siyu Li, Siyue Li, Song Li, Song-Chao Li, Songhan Li, Songlin Li, Songtao Li, Songyu Li, Songyun Li, Stephen Li, Su Li, SuYun Li, Suchun Li, Suheng Li, Suhong Li, Suiyan Li, Sujing Li, Suk-Yee Li, Sumei Li, Sunan Li, Sung-Chou Li, Supeng Li, Suping Li, Suran Li, Suwei Li, Suwen Li, Suyan Li, T Li, Taibo Li, Taiwen Li, Taixu Li, Tao Li, Taoyingnan Li, Teng Li, Tengyan Li, Thomas Li, Tian Li, Tian-Yi Li, Tian-chang Li, Tian-wang Li, Tianchang Li, Tiandong Li, Tianfeng Li, Tiange Li, Tianjiao Li, Tianjun Li, Tianming Li, Tiansen Li, Tiantian Li, Tianxiang Li, Tianyao Li, Tianye Li, Tianyi Li, Tianyou Li, Tie Li, Tiegang Li, Tiehua Li, Tiewei Li, Timmy Li, Ting Li, Tingguang Li, Tinghao Li, Tinghua Li, Tingsong Li, Tingting Li, Tong Li, Tong-Ruei Li, Tongyao Li, Tongzheng Li, Tsai-Kun Li, Tuojian Li, Tuoping Li, Vivian Li, Vivian S W Li, W H Li, W J Li, W Li, W W Li, W Y Li, W-B Li, Wan Jie Li, Wan Li, Wan-Hong Li, Wan-Shan Li, Wan-Xin Li, Wang Li, Wanling Li, Wanni Li, Wanqian Li, Wanru Li, Wanshi Li, Wanshun Li, Wanting Li, Wanwan Li, Wanxin Li, Wanyan Li, Wanyi Li, Wei Li, Wei-Bo Li, Wei-Dong Li, Wei-Jun Li, Wei-Li Li, Wei-Ming Li, Wei-Na Li, Wei-Ping Li, Wei-Qin Li, Wei-Yang Li, Weidong Li, Weifeng Li, Weiguang Li, Weiguo Li, Weihai Li, Weiheng Li, Weihua Li, Weijian Li, Weijie Li, Weijun Li, Weike Li, Weiling Li, Weimin Li, Weina Li, Weining Li, Weiping Li, Weiqin Li, Weirong Li, Weisong Li, Weiyang Li, Weiye Li, Weiyong Li, Weizu Li, Wen Lan Li, Wen Li, Wen-Chao Li, Wen-Jie Li, Wen-Ting Li, Wen-Wen Li, Wen-Xi Li, Wen-Xing Li, Wen-Ya Li, Wen-Ying Li, Wen-juan Li, Wenbo Li, Wenchao Li, Wende Li, Wendeng Li, Wenfang Li, Wenfeng Li, Wenge Li, Wenguo Li, Wenhao Li, Wenhong Li, Wenhua Li, Wenhui Li, Wenjia Li, Wenjian Li, Wenjie Li, Wenjing Li, Wenjuan Li, Wenjun Li, Wenke Li, Wenlei Li, Wenli Li, Wenlong Li, Wenming Li, Wenqi Li, Wenqiang Li, Wenqing Li, Wenqun Li, Wenrui Li, Wensheng Li, Wentao Li, Wenwen Li, Wenxi Li, Wenxia Li, Wenxiang Li, Wenxin Li, Wenxiu Li, Wenxue Li, Wenyan Li, Wenyang Li, Wenyi Li, Wenying Li, Wenyong Li, Wenyu Li, Wenzhe Li, Wenzhuo Li, Wu-Jun Li, Wuguo Li, Wulan Li, Wuyan Li, X B Li, X L Li, X Li, X Y Li, X-H Li, X-L Li, Xi Li, Xi-Hai Li, Xi-Xi Li, Xia Li, Xian Li, Xiancheng Li, Xiang Li, Xiang-Dong Li, Xiang-Jun Li, Xiang-Ping Li, Xiang-Yu Li, Xiangcheng Li, Xiangchun Li, Xiangdong Li, Xiangfei Li, Xiangjun Li, Xiangling Li, Xianglong Li, Xiangnan Li, Xiangpan Li, Xiangping Li, Xiangqi Li, Xiangrui Li, Xiangwei Li, Xiangyan Li, Xiangyang Li, Xiangyun Li, Xiangzhe Li, Xiankai Li, Xiankun Li, Xianlin Li, Xianlong Li, Xianlu Li, Xianlun Li, Xianrui Li, Xianyong Li, Xiao Li, Xiao-Cheng Li, Xiao-Dong Li, Xiao-Feng Li, Xiao-Gang Li, Xiao-Guang Li, Xiao-Hong Li, Xiao-Hui Li, Xiao-Jiao Li, Xiao-Jing Li, Xiao-Jun Li, Xiao-Kang Li, Xiao-Li Li, Xiao-Lin Li, Xiao-Long Li, Xiao-Min Li, Xiao-Na Li, Xiao-Qiang Li, Xiao-Qin Li, Xiao-Qiu Li, Xiao-Sa Li, Xiao-Tong Li, Xiao-Yao Li, Xiao-Yun Li, Xiao-kun Li, Xiao-mei Li, Xiao-xu Li, Xiao-yu Li, XiaoQiu Li, Xiaobai Li, Xiaobin Li, Xiaobing Li, Xiaobo Li, Xiaochen Li, Xiaochun Li, Xiaocun Li, Xiaodong Li, Xiaofang Li, Xiaofei Li, Xiaofeng Li, Xiaoguang Li, Xiaohan Li, Xiaoheng Li, Xiaohong Li, Xiaohu Li, Xiaohua Li, Xiaohuan Li, Xiaohui Li, Xiaojiao Li, Xiaojiaoyang Li, Xiaojing Li, Xiaoju Li, Xiaojuan Li, Xiaokun Li, Xiaolei Li, Xiaoli Li, Xiaolian Li, Xiaoliang Li, Xiaolin Li, Xiaoling Li, Xiaolong Li, Xiaoman Li, Xiaomei Li, Xiaomeng Li, Xiaomin Li, Xiaoming Li, Xiaona Li, Xiaonan Li, Xiaoning Li, Xiaopeng Li, Xiaoping Li, Xiaoqi Li, Xiaoqiang Li, Xiaoqin Li, Xiaoqing Li, Xiaoqiong Li, Xiaoquan Li, Xiaoran Li, Xiaorong Li, Xiaotian Li, Xiaoting Li, Xiaotong Li, Xiaowei Li, Xiaoxia Li, Xiaoxiao Li, Xiaoxiong Li, Xiaoxuan Li, Xiaoya Li, Xiaoyan Li, Xiaoyao Li, Xiaoyi Li, Xiaoying Li, Xiaoyong Li, Xiaoyu Li, Xiaoyuan Li, Xiaoyun Li, Xiaozhao Li, Xiaozhen Li, Xiaozheng Li, Xiatian Li, Xiawei Li, Xiaxia Li, Xiayu Li, Xidan Li, Xihao Li, Xihe Li, Xijing Li, Xikun Li, Xiliang Li, Ximei Li, Xin Li, Xin-Chang Li, Xin-Jian Li, Xin-Ping Li, Xin-Tao Li, Xin-Ya Li, Xin-Yu Li, Xin-Yue Li, Xin-Zhu Li, Xinbin Li, Xing Li, Xing-Wang Li, Xingchen Li, Xingcheng Li, Xingfang Li, Xinghuan Li, Xinghui Li, Xingli Li, Xinglong Li, Xingwang Li, Xingxing Li, Xingya Li, Xingye Li, Xingyu Li, Xingyuan Li, Xinhai Li, Xinhua Li, Xinhui Li, Xining Li, Xinjia Li, Xinjian Li, Xinke Li, Xinle Li, Xinli Li, Xinlin Li, Xinmei Li, Xinmiao Li, Xinmin Li, Xinming Li, Xinpeng Li, Xinping Li, Xinrong Li, Xinrui Li, Xinsheng Li, Xinwei Li, Xinxin Li, Xinxiu Li, Xinyan Li, Xinyang Li, Xinyao Li, Xinye Li, Xinyi Li, Xinyu Li, Xinyuan Li, Xinzhi Li, Xinzhong Li, Xiong Bing Li, Xiong Li, Xiongfeng Li, Xionghao Li, Xionghui Li, Xiu-Ling Li, Xiucui Li, Xiufeng Li, Xiujuan Li, Xiuli Li, Xiuling Li, Xiumei Li, Xiuqi Li, Xiurong Li, Xiushen Li, Xiushi Li, Xiuzhen Li, Xixi Li, Xiyue Li, Xiyun Li, Xu Li, Xu-Bo Li, Xu-Wei Li, Xu-Zhao Li, Xuan Li, Xuan-Ling Li, Xuanfei Li, Xuanxuan Li, Xuanzheng Li, Xudong Li, Xue Cheng Li, Xue Li, Xue-Er Li, Xue-Fei Li, Xue-Hua Li, Xue-Lian Li, Xue-Min Li, Xue-Nan Li, Xue-Peng Li, Xue-Yan Li, Xue-Ying Li, Xue-jing Li, Xue-zhi Li, Xuebiao Li, Xueer Li, Xuefei Li, Xuefeng Li, Xuehua Li, Xuejie Li, Xuejun Li, Xuekun Li, Xuelian Li, Xuelin Li, Xueling Li, Xuemei Li, Xuemin Li, Xuening Li, Xuepeng Li, Xueqin Li, Xueren Li, Xueshan Li, Xuesong Li, Xueting Li, Xuewang Li, Xuewei Li, Xuewen Li, Xueyang Li, Xueyi Li, Xueying Li, Xuezhong Li, Xuhang Li, Xuhong Li, Xuhua Li, Xujun Li, Xun Li, Xunjia Li, Xuri Li, Xutong Li, Xuyi Li, Xuze Li, Y H Li, Y L Li, Y Li, Y M Li, Y X Li, Y-Y Li, Ya Li, Ya-Feng Li, Ya-Ge Li, Ya-Jun Li, Ya-Li Li, Ya-Pei Li, Ya-Qiang Li, Ya-Ting Li, Ya-Zhou Li, YaJie Li, Yadong Li, Yahui Li, Yajiao Li, Yajing Li, Yajuan Li, Yajun Li, Yakui Li, Yalan Li, Yali Li, Yalin Li, Yan Bing Li, Yan Li, Yan Ning Li, Yan-Chun Li, Yan-Guang Li, Yan-Hong Li, Yan-Hua Li, Yan-Li Li, Yan-Nan Li, Yan-Xue Li, Yan-Yan Li, Yan-Yu Li, Yanan Li, Yanbin Li, Yanbing Li, Yanbo Li, Yanchang Li, Yanchuan Li, Yanchun Li, Yandong Li, Yanfeng Li, Yang Li, Yangxue Li, Yangyang Li, Yanhui Li, Yani Li, Yanjiao Li, Yanjie Li, Yanjing Li, Yanjun Li, Yanli Li, Yanlin Li, Yanling Li, Yanlong Li, Yanmei Li, Yanmin Li, Yanming Li, Yanni Li, Yanping Li, Yanqing Li, Yansen Li, Yanshu Li, Yansong Li, Yantao Li, Yanwei Li, Yanwu Li, Yanxi Li, Yanxiang Li, Yanxin Li, Yanyan Li, Yanying Li, Yanze Li, Yanzhong Li, Yao Li, Yaobo Li, Yaochen Li, Yaodong Li, Yaofu Li, Yaojia Li, Yaokun Li, Yaoqi Li, Yaoyao Li, Yaqi Li, Yaqiang Li, Yaqiao Li, Yaqin Li, Yaqing Li, Yaqiong Li, Yarong Li, Yawei Li, Yaxi Li, Yaxian Li, Yaxiong Li, Yaxuan Li, Yaying Li, Yayu Li, Yazhou Li, Ye Li, Yehong Li, Yeshan Li, Yetian Li, Yi Li, Yi-Heng Li, Yi-Ling Li, Yi-Ning Li, Yi-Shuan J Li, Yi-Ting Li, Yi-Wen Li, Yi-Yang Li, Yi-Ying Li, Yi-Yun Li, YiPing Li, YiQing Li, Yibo Li, Yiche Li, Yicun Li, Yifan Li, Yifei Li, Yifeng Li, Yige Li, Yihan Li, Yihao Li, Yiheng Li, Yihong Li, Yijian Li, Yijie Li, Yijing Li, Yiju Li, Yikang Li, Yike Li, Yilang Li, Yiliang Li, Yilong Li, Yimei Li, Yimeng Li, Yiming Li, Yin Li, Yinan Li, Ying Li, Ying-Bo Li, Ying-Lan Li, Ying-Qin Li, Ying-Qing Li, Ying-na Li, Yinggao Li, Yinghao Li, Yinghua Li, Yinghui Li, Yingjian Li, Yingjie Li, Yingjun Li, Yinglin Li, Yingnan Li, Yingpu Li, Yingqin Li, Yingrui Li, Yingshuo Li, Yingxi Li, Yingxia Li, Yingyi Li, Yingying Li, Yinhao Li, Yining Li, Yinliang Li, Yinxiong Li, Yinyan Li, Yinzhen Li, Yipeng Li, Yiqiang Li, Yirun Li, Yitong Li, Yiwei Li, Yiwen Li, Yixi Li, Yixiang Li, Yixiao Li, Yixin Li, Yixing Li, Yixuan Li, Yixue Li, Yiyang Li, Yizhe Li, Yong Li, Yong-Jian Li, Yong-Jun Li, Yong-Liang Li, Yongchao Li, Yonghao Li, Yonghe Li, Yongjia Li, Yongjiang Li, Yongjin Li, Yongjing Li, Yongjun Li, Yongkai Li, Yongle Li, Yongli Li, Yongmei Li, Yongnan Li, Yongpeng Li, Yongping Li, Yongqi Li, Yongqiang Li, Yongqiu Li, Yongsen Li, Yongsheng Li, Yongting Li, Yongxiang Li, Yongxin Li, Yongxue Li, Yongze Li, Yongzhe Li, Yongzhen Li, Yongzheng Li, You Li, You Ran Li, You-Mei Li, Youchen Li, Youjun Li, Youming Li, Youran Li, Yousheng Li, Youwei Li, Yu Li, Yu-Cheng Li, Yu-Chia Li, Yu-Hang Li, Yu-Hao Li, Yu-He Li, Yu-Hui Li, Yu-I Li, Yu-Jin Li, Yu-Jui Li, Yu-Kun Li, Yu-Lin Li, Yu-Sheng Li, Yu-Xiang Li, Yu-Ye Li, Yu-Ying Li, Yu-quan Li, Yuan Hao Li, Yuan Li, Yuan-Hai Li, Yuan-Jing Li, Yuan-Tao Li, Yuan-Yuan Li, Yuan-hao Li, Yuanchang Li, Yuanchuang Li, Yuancong Li, Yuandong Li, Yuanfang Li, Yuanfei Li, Yuanhao Li, Yuanhe Li, Yuanheng Li, Yuanhong Li, Yuanhua Li, Yuanjing Li, Yuanmei Li, Yuanyou Li, Yuanyuan Li, Yuanze Li, Yubin Li, Yubo Li, Yuchan Li, Yuchao Li, Yucheng Li, Yuchuan Li, Yuchun Li, Yudong Li, Yue Li, Yue-Chun Li, Yue-Jia Li, Yue-Ming Li, Yue-Rui Li, Yue-Ting Li, Yue-Ying Li, YueQiang Li, Yuefei Li, Yuefeng Li, Yueguo Li, Yuehua Li, Yuemei Li, Yueping Li, Yueqi Li, Yueting Li, Yuezheng Li, Yufan Li, Yufen Li, Yufeng Li, Yuguang Li, Yuhan Li, Yuhang Li, Yuhong Li, Yuhua Li, Yuhuang Li, Yuhui Li, Yujie Li, Yujun Li, Yukun Li, Yuli Li, Yulin Li, Yuling Li, Yulong Li, Yumao Li, Yumei Li, Yumiao Li, Yumin Li, Yun Li, Yun-Da Li, Yun-Lin Li, Yun-Peng Li, Yun-tian Li, Yuna Li, Yunan Li, Yunchu Li, Yunfeng Li, Yunjiu Li, Yunlong Li, Yunlun Li, Yunman Li, Yunmin Li, Yunpeng Li, Yunqi Li, Yunrui Li, Yunshen Li, Yunsheng Li, Yunting Li, Yunxi Li, Yunxiao Li, Yunxu Li, Yunyun Li, Yunze Li, Yuping Li, Yuqi Li, Yuqian Li, Yuqing Li, Yuqiu Li, Yuquan Li, Yushan Li, Yutang Li, Yutian Li, Yuting Li, Yutong Li, Yuwei Li, Yuxi Li, Yuxiang Li, Yuxin Li, Yuxiu Li, Yuxuan Li, Yuyan Li, Yuying Li, Yuyun Li, Yuzhe Li, Yvonne Li, Z Li, Z-H Li, Zaibo Li, Ze Li, Ze-An Li, Zecai Li, Zechuan Li, Zehan Li, Zehua Li, Zejian Li, Zemin Li, Zengyang Li, Zequn Li, Zesong Li, Zexu Li, Zeyu Li, Zeyuan Li, Zezhi Li, Zhan Li, Zhandong Li, Zhang Li, Zhanjun Li, Zhankui Li, Zhanquan Li, Zhantao Li, Zhao Li, Zhao-Cong Li, Zhao-Yang Li, Zhaobing Li, Zhaohan Li, Zhaojin Li, Zhaoliang Li, Zhaolun Li, Zhaoping Li, Zhaosha Li, Zhaoshui Li, Zhaoyong Li, Zhe Li, Zhehui Li, Zhen Li, Zhen-Hua Li, Zhen-Jia Li, Zhen-Li Li, Zhen-Xi Li, Zhen-Yu Li, Zhen-Yuan Li, Zhenbei Li, Zhencheng Li, Zhencong Li, Zhenfei Li, Zhenfen Li, Zheng Li, Zheng-Dao Li, Zhengda Li, Zhenghao Li, Zhenghui Li, Zhengjie Li, Zhengliang Li, Zhenglong Li, Zhengnan Li, Zhengpeng Li, Zhengrui Li, Zhenguang Li, Zhengwei Li, Zhengyang Li, Zhengyao Li, Zhengying Li, Zhengyu Li, Zhenhao Li, Zhenhua Li, Zhenhui Li, Zhenjia Li, Zhenjun Li, Zhenli Li, Zhenlu Li, Zhenming Li, Zhenshu Li, Zhenyan Li, Zhenyu Li, Zhenzhe Li, Zhenzhou Li, Zheyun Li, Zhi Li, Zhi-Bin Li, Zhi-Gang Li, Zhi-Jian Li, Zhi-Peng Li, Zhi-Wei Li, Zhi-Xing Li, Zhi-Yong Li, Zhi-Yuan Li, Zhi-qiang Li, Zhibin Li, Zhichao Li, Zhifan Li, Zhifei Li, Zhigang Li, Zhigao Li, Zhihao Li, Zhihong Li, Zhihua Li, Zhihui Li, Zhijia Li, Zhijie Li, Zhijun Li, Zhilei Li, Zhimei Li, Zhiming Li, Zhipeng Li, Zhiping Li, Zhiqiang Li, Zhiqiong Li, Zhiquan Li, Zhirong Li, Zhisheng Li, Zhiwei Li, Zhixiong Li, Zhixuan Li, Zhiyang Li, Zhiyi Li, Zhiyong Li, Zhiyu Li, Zhiyuan Li, Zhizhong Li, Zhizong Li, Zhong Li, Zhong-Xin Li, Zhongcai Li, Zhongding Li, Zhonggen Li, Zhonghua Li, Zhongjie Li, Zhonglian Li, Zhonglin Li, Zhongwen Li, Zhongxia Li, Zhongxian Li, Zhongxuan Li, Zhongyu Li, Zhongzhe Li, Zhou Li, Zhouhua Li, Zhouxiang Li, Zhu Li, Zhuang Li, Zhuangzhuang Li, Zhuanjian Li, Zhuo Li, Zhuo-Rong Li, Zhuoran Li, Zhuorong Li, Zi-Zhan Li, Zichao Li, Zihai Li, Zihan Li, Zihao Li, Zihua Li, Zihui Li, Zijian Li, Zijing Li, Zili Li, Ziliang Li, Zilin Li, Zilu Li, Zimeng Li, Ziming Li, Zipeng Li, Ziqi Li, Ziqiang Li, Ziqing Li, Ziru Li, Zirui Li, Ziwen Li, Zixiao Li, Ziyang Li, Ziyu Li, Ziyue Li, Ziyun Li, Zizhuo Li, Zong-Xue Li, Zongchao Li, Zongdi Li, Zongfang Li, Zonghong Li, Zonghua Li, Zongjun Li, Zonglin Li, Zongyi Li, Zongyu Li, Zongyun Li, Zongzhe Li, Zu-Ling Li, Zu-guo Li, Zulong Li, Zunjiang Li, Zuo-Lin Li
articles
Jing Wang, Xueying Yan, Wenfei Wang +6 more · 2025 · Pharmaceutics · MDPI · added 2026-04-24
no PDF DOI: 10.3390/pharmaceutics17010094
RAB21
Yajie Zhang, Yang Li, Wentao Huang +7 more · 2025 · International journal of surgery (London, England) · added 2026-04-24
Gastroesophageal reflux disease (GERD) and asthma are commonly co-occurring conditions, with shared genetic factors identified. However, the specific loci and the influence of common genetic architect Show more
Gastroesophageal reflux disease (GERD) and asthma are commonly co-occurring conditions, with shared genetic factors identified. However, the specific loci and the influence of common genetic architecture remain undefined. We obtained genome-wide association study (GWAS) summary statistics for GERD (71 522 cases and 261 079 controls) and asthma (56 167 cases and 352 255 controls). Using linkage disequilibrium score regression (LDSC), we assessed genetic correlations between GERD and asthma. Bidirectional Mendelian randomization (MR) was performed to investigate potential causal relationships, followed by cross-trait GWAS meta-analysis and colocalization analysis to identify shared risk loci. Additionally, summary-data-based MR and transcriptome-wide association study were conducted to pinpoint common functional genes. Finally, we analyzed gene expression profiles in both healthy individuals and GERD patients using esophageal single-cell RNA sequencing (scRNA-seq) data. We identified a significant genetic correlation between GERD and asthma ( rg  = 0.37, P = 6.19 × 10 -38 ) and a significant causal effect of GERD on asthma [odds ratio (OR) = 1.22, P = 1.54 × 10 -5 ]. Cross-trait meta-analyses revealed 56 shared risk loci between GERD and asthma, including 51 loci that were newly identified. Three loci (rs61937247, rs7960225, and rs769670) exhibited evidence of colocalization. Gene-level analyses pinpointed three novel shared genes ( RBM6, SUOX , and MPHOSPH9 ) between GERD and asthma. scRNA-seq analysis uncovered heightened expression of these genes in immune cells of patients diagnosed with GERD. Our study has discovered novel shared genetic loci and candidate genes between GERD and asthma, providing further insights into the genetic susceptibility of comorbidity and potential mechanisms of the two diseases. Show less
no PDF DOI: 10.1097/JS9.0000000000003283
RBM6
Ruoyang Liu, Yu Liu, Long Zhang +7 more · 2025 · Journal of cellular and molecular medicine · Blackwell Publishing · added 2026-04-24
RBM6, implicated in the progression of multiple tumour types but unexplored in prostate tumours, was found to indicate potential therapeutic implications due to its elevated expression in prostate tum Show more
RBM6, implicated in the progression of multiple tumour types but unexplored in prostate tumours, was found to indicate potential therapeutic implications due to its elevated expression in prostate tumours. To elucidate its molecular function, scratch tests, transwell migration and invasion assays were conducted, with PCR and western blot analyses verifying molecular regulatory relationships. RNA pulldown and RNA immunoprecipitation tests were also employed to investigate underlying mechanisms. Results indicate that RBM6 enhances prostate cell migration by suppressing CDH1, yet ZEB1 overexpression alleviates this suppression. Notably, under these conditions, RBM6's inhibitory effect on MMP16 becomes more pronounced, reducing cell migration ability. Thus, under normal conditions, RBM6 promotes prostate tumour cell migration, but in the context of high ZEB1 expression, it inhibits migration. This shift in RBM6's regulatory capacity towards downstream genes underscores the importance of considering objective conditions in studying RBM6 molecules. Show less
no PDF DOI: 10.1111/jcmm.70397
RBM6
Fuyu Zhao, Jianan Zhao, Yang Li +7 more · 2025 · Frontiers in genetics · Frontiers · added 2026-04-24
Fibromyalgia (FM) is a complex autoimmune disorder characterized by widespread pain and fatigue, with significant diagnostic challenges due to the absence of specific biomarkers. This study aims to id Show more
Fibromyalgia (FM) is a complex autoimmune disorder characterized by widespread pain and fatigue, with significant diagnostic challenges due to the absence of specific biomarkers. This study aims to identify and validate potential genetic markers for FM to facilitate earlier diagnosis and intervention. We analyzed gene expression data from the Gene Expression Omnibus (GEO) to identify differentially expressed genes (DEGs) associated with FM. Comprehensive enrichment analyses, including Gene Ontology (GO), the Kyoto Encyclopedia of Genes and Genomes (KEGG), and Reactome pathways, were performed to elucidate the biological functions and disease associations of the candidate genes. We used the eXtreme Gradient Boosting (XGBoost) algorithm to develop a diagnostic model, which was validated using independent datasets. Three genes, namely, dual-specificity tyrosine phosphorylation-regulated kinase 3 The study successfully identifies three diagnostic biomarkers for FM, supported by both bioinformatics analysis and machine learning models. These findings could significantly improve diagnostic accuracy for FM, leading to better patient management and treatment outcomes. Show less
no PDF DOI: 10.3389/fgene.2025.1535541
RGS17
Shuzhi Zhao, Yili Zhang, Chenxin Li +2 more · 2025 · Biochemical and biophysical research communications · Elsevier · added 2026-04-24
The pyroptosis of retinal Müller cells is intricately linked to the pathogenesis of diabetic retinopathy (DR). Ubiquitin-fold modifier 1 (UFM1)-mediated UFMylation plays an important role in insulin a Show more
The pyroptosis of retinal Müller cells is intricately linked to the pathogenesis of diabetic retinopathy (DR). Ubiquitin-fold modifier 1 (UFM1)-mediated UFMylation plays an important role in insulin and diabetes mellitus metabolism and regulates cell death such as apoptosis and pyroptosis. UFM1-specific protease 2 (UFSP2) mediates the maturation of the UFM1 precursor and thus affects UFMylation reaction. However, its role in DR remains unknown. The aim of our study was to determine the mechanism and upstream regulation of UFSP2 on the pyroptosis of rat retinal Müller cells. Pathological changes, UFSP2 expression and succinate accumulation were determined in retinal tissues of db/db diabetic mice via Hematoxylin and eosin and immunofluorescence staining and biochemical analysis. High glucose (HG) was used to construct a DR cell model using rat retinal Müller cells (rMC-1). Ufsp2 RNA interference and overexpression plasmids were constructed to determine the effects of UFSP2. Pyroptosis and reactive oxygen species (ROS) levels were assessed via flow cytometry. Inflammatory cytokine (IL-1β and IL-18) levels and key molecular markers related to pyroptosis (NLRP3, ASC, Caspase-1p20, GSDMD-N) were measured by enzyme linked immunosorbent assay and Western blot, respectively. Succinate-mediated H3K3me3 enrichment in Ufsp2 promoter region was measured by chromatin immunoprecipitation. In vivo experiments revealed that the UFSP2 expression and succinate levels were increased in retinal tissues of db/db diabetic mice with thinning of retinal thickness. Moreover, in vitro experiments showed that The mRNA and protein levels of Ufsp2 exhibited a time-dependent increase under HG conditions. Upon Ufsp2 knockdown, the elevated oxidative stress, inflammatory responses, and pyroptosis stimulated by HG were significantly suppressed. The effect of Ufsp2 overexpression on pyroptosis and inflammatory responses was consistent with the HG stimulation, whereas the UFSP2-induced heightened levels of pyroptosis as well as the inflammatory state were significantly reversed when co-administered with NLRP3 inhibitor or ROS inhibitor. Further activating NLRP3 inflammasome using LPS + ATP stimulation revealed that the knockdown of Ufsp2 resulted in inhibited pyroptosis levels and inflammatory responses, while the Ufsp2 overexpression markedly increased pyroptosis and inflammatory responses. Lastly, succinate was demonstrated to influence Ufsp2 transcription, as well as the expression of H3K3me3 and its enrichment in the Ufsp2 promoter region, ultimately affecting pyroptosis and inflammatory responses. Succinate-mediated Ufsp2 transcription promotes pyroptosis in rMC-1 cells by activating NLRP3 inflammasome and oxidative stress. Show less
no PDF DOI: 10.1016/j.bbrc.2025.152614
RMC1
Ying-Ying Zhu, Shi-Yue Qin, Hai Xie +5 more · 2025 · International journal of ophthalmology · added 2026-04-24
To investigate the effects and the underlying mechanism(s) of conbercept on the phagocytosis of hard exudates (HEs) by Müller glia in diabetic retinopathy (DR). Twenty-one eyes from 17 patients with d Show more
To investigate the effects and the underlying mechanism(s) of conbercept on the phagocytosis of hard exudates (HEs) by Müller glia in diabetic retinopathy (DR). Twenty-one eyes from 17 patients with diabetic macular edema (DME) underwent optical coherence tomography (OCT) imaging to examine the changes of HEs before and after intravitreal conbercept injection (IVC). The area of HEs showed minimal change after the first IVC (1.39±1.41 to 1.38±1.3 mm Conbercept reduces HEs in DR by enhancing Müller glia phagocytosis possibly through activating PPARγ-CD36 axis, which is mediated by inhibition of VEGF signaling. Modulation of Müller glia phagocytic capacity might provide a novel therapeutic strategy to treat DR and DME. Show less
no PDF DOI: 10.18240/ijo.2025.07.07
RMC1
Shangyu Liu, Haijun Tang, Shanhang Li +11 more · 2025 · FASEB bioAdvances · added 2026-04-24
Osteosarcoma (OS) is highly malignant and easily prone to lung metastasis. The mechanisms of lung metastasis in OS remain unclear. The single-cell RNA sequencing (scRNA-seq) samples in this study incl Show more
Osteosarcoma (OS) is highly malignant and easily prone to lung metastasis. The mechanisms of lung metastasis in OS remain unclear. The single-cell RNA sequencing (scRNA-seq) samples in this study included six primary osteosarcoma samples (published in-house data), two lung metastasis samples (GSE152048), and four normal bone tissue samples (GSE169396). To identify potential targets for metastasis, bulk RNA sequencing data from four primary tumors and four lung metastases (in-house data) were also analyzed. scRNA-seq identified five tumor cell subpopulations. CytoTRACE and lung metastasis scores indicated that the C1 subpopulation was most closely associated with lung metastasis. By intersecting lung metastasis-related genes identified via hdWGCNA analysis with differentially expressed genes from bulk RNA sequencing, Show less
no PDF DOI: 10.1096/fba.2024-00161
SEC16B
Ruo-Xin Zhang, An-Qi Li, Xin-Yuan Zhao +7 more · 2025 · Diabetologia · Springer · added 2026-04-24
Glucose homeostasis, essential for metabolic health, requires coordinated insulin and glucagon activity to maintain blood glucose balance. Dysregulation of glucose homeostasis causes hyperglycaemia an Show more
Glucose homeostasis, essential for metabolic health, requires coordinated insulin and glucagon activity to maintain blood glucose balance. Dysregulation of glucose homeostasis causes hyperglycaemia and glucose intolerance, hallmark features of type 2 diabetes. While SEC16 homologue B (SEC16B), an endoplasmic reticulum export factor, has been linked to obesity, type 2 diabetes and lipid metabolism, its role in glucose regulation remains poorly defined. This study aims to investigate SEC16B's contribution to glucose homeostasis by systematically dissecting its conserved physiological mechanisms across species. To interrogate SEC16B's role, we combined Drosophila genetics (RNA interference-mediated dSec16 knockdown) with murine models (Sec16b deletion) under standard or high-fat diet conditions. Glucose and insulin tolerance tests assessed glucose homeostasis. Mechanistic insights into beta cell dysfunction were derived from immunostaining, glucose-stimulated insulin secretion assays and RNA-seq profiling of murine pancreatic islets. Both disruption of dSec16 in Drosophila and Sec16b deletion in mice triggered glucose intolerance under standard diet conditions, recapitulating conserved metabolic dysfunction. In addition, Sec16b loss impaired glycaemic control in mice fed a high-fat diet. Mechanistically, Sec16b deficiency impairs insulin secretion by downregulating cholinergic signalling and compromising intracellular Ca Our study reveals SEC16B, a genome-wide association study-identified obesity risk gene, as an evolutionarily conserved regulator of glucose homeostasis. By linking SEC16B to cholinergic-driven insulin secretion and calcium dynamics, we resolve a mechanistic gap in beta cell dysfunction and metabolic disease. This finding provides novel insights into the mechanisms underlying glucose homeostasis and may enhance our understanding of potential treatments for metabolic diseases. Show less
no PDF DOI: 10.1007/s00125-025-06501-8
SEC16B
Xiaotao Jiang, Hui Wu, Ning Yan +14 more · 2025 · Research (Washington, D.C.) · added 2026-04-24
The development of an immunosuppressive microenvironment is a critical factor in stomach carcinogenesis. Polymorphonuclear myeloid-derived suppressor cells (PMN-MDSCs) serve a pivotal function in medi Show more
The development of an immunosuppressive microenvironment is a critical factor in stomach carcinogenesis. Polymorphonuclear myeloid-derived suppressor cells (PMN-MDSCs) serve a pivotal function in mediating immune suppression. However, the precise mechanisms underlying PMN-MDSCs infiltration into the tumor immune microenvironment (TIME) and their immunosuppressive functions remain poorly understood. In this investigation, we observed that PMN-MDSCs were up-regulated during stomach carcinogenesis, with gastric cancer (GC) cells secreting CCL26 to promote the infiltration of PMN-MDSCs into the TIME via the CX3CR1 receptor. The infiltrating CX3CR1 Show less
no PDF DOI: 10.34133/research.1002
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Lijun Zhou, Mei Liu, Fujun Liu +10 more · 2025 · Oncogene · Nature · added 2026-04-24
Breast cancer (BC) is the most prevalent malignancy among women worldwide. Growing evidence highlights the crucial role of circular RNAs (circRNAs) in BC carcinogenesis; however, their underlying mech Show more
Breast cancer (BC) is the most prevalent malignancy among women worldwide. Growing evidence highlights the crucial role of circular RNAs (circRNAs) in BC carcinogenesis; however, their underlying mechanisms remain largely unknown. In this study, we identify circCLASP1, which is significantly upregulated in BC tissues (n = 65) and serum samples (n = 61). Its expression correlates with lymph node metastasis, ki67 expression, and tumor size. Receiver operation characteristic (ROC) curve analysis reveals area under the curve (AUC) values of 0.8196 (BC tissues) and 0.8902 (BC serum), respectively. Functionally, circCLASP1 knockdown significantly suppresses BC cell proliferation, migration, and invasion. Mechanistically, circCLASP1 prevents the ubiquitin-mediated degradation of GLI1 protein by facilitating its interaction with CCT2, thereby stabilizing GLI1. Moreover, circCLASP1 enhances the nuclear accumulation of GLI1, leading to increased SNAIL expression and thereby upregulating the expression of CCL2 and CCL5, which in turn promotes macrophage M2 polarization, ultimately resulting in BC progression and subsequent lung metastasis. Further analysis reveals that U2AF2 regulates circCLASP1 biogenesis. Collectively, these findings demonstrate that circCLASP1 promotes BC progression and an immunosuppressive microenvironment via the CCT2/GLI1/SNAIL axis, highlighting its potential as a prognostic biomarker and therapeutic target for BC. Show less
no PDF DOI: 10.1038/s41388-025-03627-2
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Shichao Wang, Xing Zhao, Mingyang Li +2 more · 2025 · International journal of clinical and experimental pathology · added 2026-04-24
Glioma is a highly aggressive malignancy with no effective treatment. This study investigates the role of protein tyrosine phosphatase receptor type N (PTPRN) in glioma progression. The U87 human glio Show more
Glioma is a highly aggressive malignancy with no effective treatment. This study investigates the role of protein tyrosine phosphatase receptor type N (PTPRN) in glioma progression. The U87 human glioma cell line was used to monitor proliferation, invasion, and migration during PTPRN knockdown. The viability, migration, and invasion were analyzed using the Cell Counting Kit-8 assay, transwell migration, and invasion assays. Additionally, the expression of proteins associated with the cell cycle was examined using western blotting. The knockdown of PTPRN resulted in a reduction in glioma cell proliferation, migration, and invasion, as well as the expression of cell cycle markers like Show less
no PDF DOI: 10.62347/GABE3607
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Yifei Lu, Tian Xia, Yongjia Jin +8 more · 2025 · Pediatric surgery international · Springer · added 2026-04-24
Rhabdomyosarcoma (RMS) is the most common pediatric soft tissue sarcoma. FOXO1 fusion indicates poor prognosis and lead to dysregulation of transcriptioanal network. This study aims to investigate cli Show more
Rhabdomyosarcoma (RMS) is the most common pediatric soft tissue sarcoma. FOXO1 fusion indicates poor prognosis and lead to dysregulation of transcriptioanal network. This study aims to investigate clinical characteristics and therapeutic targets concerning FOXO1 fusion status. 65 pediatric RMS patients were enrolled. Clinical data were analyzed using Kaplan-Meier estimates and Cox regression. Surgically resected tumor tissues were subject to single-cell RNA sequencing (scRNA-seq). Patient-derived xenograft (PDX) was establish and dissociated to cells for high-throughput drug screening. Among the 65 patinets (36 patients with embryonal RMSs (ERMSs), 15 patients with alveolar RMSs (ARMSs) and 14 patients with other types of RMSs), 73.3% of ARMSs were defined as fusion positive (FP) while 6 ERMS (ERMS)s were also FP. Cox regression analysis identified FOXO1 fusion as a risk factor alone and combined with pathologic subtype, sex and age or metastasis status. scRNA-seq revealed distinct transcription factor networks between FP and FN RMS, showing up-regulated activity of OLIG2, NHLH1, SNAI1, TFF3 and other TFs related to neural development and differentiation. MAPK, PI3K-Akt, and mTOR pathways were enriched in FP-RMS tumor cells. High-throughput drug screening of PDX-derived cells identified sensitive drugs targeting FP-RMS specific signatures. AMG-337 was selected and validated for its anti-tumor effect. FOXO1 fusion status influences RMS clinical outcomes, including rare FP-ERMS cases. scRNA-seq combined with drug screening identified MET as a promising therapeutic target in FP-RMS. Show less
no PDF DOI: 10.1007/s00383-025-06241-1
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Beibei Bie, Hong Bai, Yingnan Li +2 more · 2025 · IUBMB life · Wiley · added 2026-04-24
G-patch domain-containing protein 2 (GPATCH2), a member of the G-patch domain-containing family, has been implicated in tumor cell growth, but the link between GPATCH2 and hepatocellular carcinoma (HC Show more
G-patch domain-containing protein 2 (GPATCH2), a member of the G-patch domain-containing family, has been implicated in tumor cell growth, but the link between GPATCH2 and hepatocellular carcinoma (HCC) remains uncertain. In the current study, comprehensive bioinformatics analysis revealed that GPATCH2 was markedly upregulated in HCC and positively correlated with aggressive clinicopathological features, including histologic grade, AFP, albumin level, and adjacent hepatic tissue inflammation, as well as miserable outcomes in HCC. GPATCH2 also has certain diagnostic value for HCC, histologic grade, and 1-, 3-, and 5-year survival outcomes. Functionally, loss-of-function experiments disclosed that silencing GPATCH2 suppressed HCC cell proliferation, migration, invasion, and xenograft tumor growth in the subcutaneous mouse model. Silencing GPATCH2 also resulted in an increase in the expression level of CDH1, while causing a decrease in the expression levels of FN1, TWIST1, SNAI1, and SNAI2. Rescue experiments further confirmed SNAI2 as a critical downstream effector mediating GPATCH2-driven oncogenic activity in HCC. Mechanistically, GPATCH2 was uncovered to be transcriptionally activated by the transcription factor Yin Yang 1 (YY1), and can mediate the role of YY1 in promoting HCC progression and elevating SNAI2 expression. Taken together, GPATCH2 is a YY1-regulated oncogenic driver that promotes HCC advancement through SNAI2, highlighting its potential as a diagnostic, prognostic, and therapeutic target for HCC. Show less
no PDF DOI: 10.1002/iub.70070
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Wenyong Li, Rudi Lv, Husong Su +4 more · 2025 · Scientific reports · Nature · added 2026-04-24
The Kruppel-like factor 15(KLF15) gene functions as a crucial transcriptional modulator involved in numerous cellular processes such as differentiation, proliferation, growth, and programmed cell deat Show more
The Kruppel-like factor 15(KLF15) gene functions as a crucial transcriptional modulator involved in numerous cellular processes such as differentiation, proliferation, growth, and programmed cell death. The epithelial-to-mesenchymal transition (EMT) provides malignant cells with the adaptability and movement necessary for tumor advancement and spread, with zinc finger E-box binding homeobox 1(ZEB1) playing a pivotal role as a transcriptional factor in EMT. This investigation initially examined the association between the KLF15 protein and EMT associated transcription factors such as ZEB1, Slug, and Snail, along with marker proteins like E-cadherin and β-catenin in bladder cancer. Furthermore, we explored their connections with clinicopathological attributes and conducted prognostic analyses. Immunohistochemical techniques were utilized to ascertain the presence of KLF15 protein and EMT-associated transcription factor proteins, along with their marker proteins in 110 specimens of bladder cancer tissues. Concurrently, clinicopathological data and postoperative survival statistics were amassed. The rates of KLF15 and Slug protein expression were linked with pathological differentiation, lymphatic involvement, and pTNM staging. The protein expression rates of ZEB1, Slug, Snail, E-cadherin, and β-catenin also showed associations with lymphatic metastasis and pTNM stages. Notably, the expression of KLF15, the coexpression of KLF15 and ZEB1, and lymphatic metastasis emerged as independent prognostic indicators for the overall survival rates in bladder cancer cases. EMT enhances the risk of tumor recurrence and reduces overall survival durations in bladder cancer cases. Furthermore, KLF15 is a significant contributor to the EMT pathway in bladder cancer, primarily through its interaction with the transcription factor ZEB1. KLF15 and ZEB1 might serve as key biomarkers for metastasis and prognosis, offering potential new targets for therapeutic intervention in bladder cancer. Show less
no PDF DOI: 10.1038/s41598-025-22698-5
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Qian Li, Lifang Ye, Sriharsha Talapaneni +8 more · 2025 · American journal of physiology. Heart and circulatory physiology · added 2026-04-24
Endothelial-to-mesenchymal transition (EndMT) has been implicated in inflammatory vascular pathologies such as atherosclerosis. The nonfibrillar collagen type VIII functions as a pivotal player in ath Show more
Endothelial-to-mesenchymal transition (EndMT) has been implicated in inflammatory vascular pathologies such as atherosclerosis. The nonfibrillar collagen type VIII functions as a pivotal player in atherogenesis, but its role in EndMT is not well understood. We assessed the role of the α 1 chain of collagen type VIII (COL8A1) in inflammatory EndMT. Single-cell RNA-seq analysis of murine and human endothelial cells exposed to atherogenic stimuli in vivo revealed increased COL8A1 expression. Immunofluorescent analyses showed that COL8A1 expression was increased in murine atherosclerotic lesions, coinciding with the decreased expression of the endothelial marker platelet endothelial cell adhesion molecule-1. Treatment of human aortic endothelial cells (HAECs) with tumor necrosis factor-α (TNF-α) induced inflammatory EndMT. Interestingly, TNF-α treatment had a biphasic effect on COL8A1 expression in HAECs, with an initial downregulation followed by upregulation at 5 days of treatment. HAECs were then subjected to either exogenous recombinant COL8A1 (rcol8a1) exposure, lentiviral COL8A1 overexpression, or COL8A1 siRNA inhibition. Functionally, COL8A1 knockdown in HAECs suppressed endothelial gene programs, impaired tube formation, and enhanced NF-κB/Snail activation. Conversely, recombinant COL8A1 or lentiviral overexpression preserved endothelial morphology and markers and attenuated TNF-α-induced EndMT. Our findings suggest that COL8A1 is a key regulator of endothelial stability during inflammatory stress. Its transient inhibition facilitates early EndMT via NF-kB/Snail signaling, whereas its later induction in advanced disease reflects endothelial remodeling within atherosclerotic lesions. These findings identify COL8A1 as both a biomarker and a potential therapeutic target in vascular disease. Show less
no PDF DOI: 10.1152/ajpheart.00339.2025
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Jianzhi Wu, Yijie Li, Yun Yang +7 more · 2025 · Phytomedicine : international journal of phytotherapy and phytopharmacology · Elsevier · added 2026-04-24
Idiopathic pulmonary fibrosis (IPF) is a chronic and progressive fatal disease characterized by the activation of lung fibroblasts (LFs). Wogonoside (WG), a natural compound with multiple pharmacologi Show more
Idiopathic pulmonary fibrosis (IPF) is a chronic and progressive fatal disease characterized by the activation of lung fibroblasts (LFs). Wogonoside (WG), a natural compound with multiple pharmacological properties including anti-fibrotic activities, shows promise in treating IPF. This study aims to investigate the pharmacological effects and underlying mechanisms of WG on LF activation and the progression of IPF. Initially, we validated the anti-fibrotic properties of WG using a bleomycin (Bleomycin)-induced IPF model in mice, followed by RNA sequencing to identify its pharmacological targets. Subsequent in vitro experiments assessed the activities of key enzymes involved in the whole processes of glycolysis and lactic acid production, the changes of cellular energy metabolism and mitophagy-related pathways in LFs treated with transforming growth factor beta (TGF-β) or WG. Finally, reverse validation experiments were performed by further administration of lactic acid or cyclosporin A (CsA) into mice. We demonstrated that WG reduced the production of lactic acid and the lactylation of lactate of snail homolog 1 (Snail1) at K9 site by promoting pyruvate kinase isozymes R/l (PKLR) and inhibiting glyceraldehyde-3-phosphate dehydrogenase (GAPDH), while triggered mitophagy and reduced reactive oxygen species production and mtDNA release by promoting peroxisome proliferator-activated receptor gamma coactivator 1α (PGC1α) and PTEN-induced kinase 1 (PINK1)/PARKIN pathways. These two processes compatibly inhibited the TGF-β transcription and ultimately LF activation, which were reversed by lactic acid supplementation or mitophagy depletion in mice. Overall, our findings first underscore the potential pharmacological benefits of WG in the treatment of IPF by impeding lactate accumulation and mitophagy damage, thereby providing a novel theoretical framework for therapies targeting pulmonary diseases. Show less
no PDF DOI: 10.1016/j.phymed.2025.157240
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Guoyin Li, Yukui Zhao, Yubo He +4 more · 2025 · Frontiers in oncology · Frontiers · added 2026-04-24
Gliomas, particularly glioblastoma, are aggressive brain tumors with poor prognosis and unmet therapeutic needs. Structural maintenance of chromosomes 4 (SMC4), a core component of the condensin compl Show more
Gliomas, particularly glioblastoma, are aggressive brain tumors with poor prognosis and unmet therapeutic needs. Structural maintenance of chromosomes 4 (SMC4), a core component of the condensin complex, is dysregulated in multiple cancers, but its role in glioma metabolism and metastasis remains unclear. Using integrated multi-omics analyses of glioma datasets, we assessed SMC4 expression and its correlation with clinical outcomes. Functional studies in U-251MG and LN229 glioma cells including CCK-8, EdU, cell cycle, Transwell, and wound-healing assays were combined with subcutaneous xenograft and tail-vein metastasis mouse models to evaluate SMC4's effects on proliferation, migration, invasion, and metastasis. ECAR/OCR and rescue experiments validated SMC4's role in glycolysis. Luciferase reporter and ChIP assays identified nuclear factor I A (NFIA) as an upstream transcriptional regulator of SMC4. A prognostic model (SRRS) was developed via LASSO regression and validated across cohorts. SMC4 was significantly overexpressed in glioma tissues, with higher expression correlating with advanced tumor grades and poorer patient survival (AUC > 0.82). Mechanistically, SMC4 promoted G1/S cell cycle transition and proliferation SMC4 drives glioma progression through dual mechanisms TGF-β/SMAD-mediated metastasis and LDHA-dependent glycolysis regulated by NFIA. This extends beyond its known role in TGF-β activation by identifying NFIA as an upstream regulator and metabolic reprogramming as a novel function. The SRRS and nomogram provide robust tools for prognosis and personalized therapy, supporting the NFIA/SMC4 axis and downstream effectors as potential therapeutic targets for glioma. Show less
no PDF DOI: 10.3389/fonc.2025.1624370
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Qianzhu Jiang, Huiting Li · 2025 · Journal of bioenergetics and biomembranes · Springer · added 2026-04-24
Myocardial fibrosis (MF) is a key pathological process driving heart failure, characterized by excessive extracellular matrix (ECM) deposition and impaired cardiac function. Although myocyte-specific Show more
Myocardial fibrosis (MF) is a key pathological process driving heart failure, characterized by excessive extracellular matrix (ECM) deposition and impaired cardiac function. Although myocyte-specific enhancer factor 2 A (MEF2A) is implicated in cardiac fibroblast activation, its role in MF remains unclear. We manipulated MEF2A expression in cardiac fibroblasts (CFs) through knockdown and overexpression, and assessed fibrosis markers, migration, and RhoA signaling. Binding of MEF2A to the Snail1 promoter was predicted using JASPAR and validated by chromatin immunoprecipitation (ChIP) and luciferase reporter assays. Rescue experiments with Snail1 overexpression and RhoA inhibition were performed. An angiotensin II (Ang II)-induced MF mouse model was used to evaluate cardiac function by echocardiography and to assess collagen deposition through picrosirius red (PSR) staining. MEF2A was significantly upregulated in Ang II-induced fibrotic hearts and CFs. MEF2A knockdown reduced α-SMA and Col1a1 expression, inhibited CF migration, and suppressed activation of the Snail1/RhoA/α-SMA pathway. ChIP and luciferase assays confirmed the direct binding of MEF2A to the Snail1 promoter. Inhibition of RhoA signaling reversed MEF2A-induced myofibroblast activation and migration. Rescue experiments showed that Snail1 overexpression restored the fibrotic phenotype suppressed by MEF2A knockdown. In vivo, MEF2A knockdown improved left ventricular function, reduced collagen deposition (PSR staining), and lowered heart weight/tibia length ratios. MEF2A promotes myocardial fibrosis by directly activating Snail1 and engages the RhoA/α-SMA pathway. Targeting MEF2A offers a promising therapeutic strategy to attenuate MF and improve heart function. Show less
no PDF DOI: 10.1007/s10863-025-10075-w
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Qiusheng Li, Changjing Wang, Guiying Wang · 2025 · Scientific reports · Nature · added 2026-04-24
COL4A1, a key component of the basement membrane, has been increasingly implicated in tumor progression, yet its role in colon cancer remains incompletely understood. In this study, we conducted a com Show more
COL4A1, a key component of the basement membrane, has been increasingly implicated in tumor progression, yet its role in colon cancer remains incompletely understood. In this study, we conducted a comprehensive integrative analysis using transcriptomic data from the TCGA-COAD cohort, combined with functional validation in colon cancer cell lines. Gene set enrichment analysis (GSEA) revealed that high COL4A1 expression was associated with oncogenic pathways including epithelial-mesenchymal transition (EMT), KRAS signaling, and inflammatory responses. Immune infiltration analysis indicated that COL4A1 expression negatively correlated with CD8 Show less
no PDF DOI: 10.1038/s41598-025-17230-8
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Qing Wang, Wei He, Shilong Han +6 more · 2025 · Cancer medicine · Wiley · added 2026-04-24
Colorectal cancer (CRC) metastasis remains a major cause of mortality, driven by epithelial-to-mesenchymal transition (EMT) and invasion. Programmed cell death 4 (Pdcd4), a tumor suppressor, is known Show more
Colorectal cancer (CRC) metastasis remains a major cause of mortality, driven by epithelial-to-mesenchymal transition (EMT) and invasion. Programmed cell death 4 (Pdcd4), a tumor suppressor, is known to inhibit translation via interaction with eukaryotic initiation factor 4A (eIF4A). Previous studies have established that Pdcd4 suppresses stress-activated protein kinase 1-interacting protein 1 (Sin1) translation through the mTORC2-Akt axis, thereby downregulating Snail expression and EMT in CRC cells. However, whether Pdcd4 directly regulates Slug, another critical EMT transcription factor, remains unexplored. PDCD4 shRNA and SLUG siRNA were used to knock down Pdcd4 and Slug in colorectal cancer cells, respectively. The sucrose gradient fractionation was performed to determine SLUG translation. A luciferase reporter assay was used to determine the role of the SLUG 5' untranslated region (5'UTR) on Pdcd4 inhibition. The effect of Slug on promoting invasion was determined by Matrigel invasion assays. Knockdown of Pdcd4 in colorectal cancer cells increased Slug protein levels without altering SLUG mRNA abundance. Sucrose gradient fractionation revealed that Pdcd4 knockdown elevated the proportion of SLUG mRNA in polysome fractions, demonstrating Pdcd4-mediated suppression of SLUG translation. To validate the mechanism, the SLUG 5'UTR was cloned and fused to a luciferase reporter and named SLUG-5'UTR-Luc. Pdcd4 knockdown markedly enhanced SLUG-5'UTR-Luc activity; whereas, ectopic Pdcd4 expression suppressed it, indicating that the SLUG 5'UTR is critical for Pdcd4-mediated translational repression. Treatment with the eIF4A inhibitor silvestrol substantially reduced Slug protein levels and SLUG-5'UTR-Luc activity. In addition, Pdcd4 overexpression decreased Slug protein abundance and restored E-cadherin expression. Notably, Slug knockdown in Pdcd4-deficient cells rescued E-cadherin expression and abrogated the invasive phenotype. These findings suggest that up-regulation of Slug translation by Pdcd4 knockdown contributes to enhanced invasion. Pdcd4 suppresses colorectal cancer invasion by translationally downregulating Slug expression. Show less
no PDF DOI: 10.1002/cam4.71145
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Zhongwei Zhang, Meiding Wang, Xinyu Gao +3 more · 2025 · Cellular signalling · Elsevier · added 2026-04-24
Peritoneal metastasis (PM) in gastric cancer (GC) remains a formidable clinical challenge. Although exosomes are critical mediators of tumor-microenvironment communication, their mechanistic role in l Show more
Peritoneal metastasis (PM) in gastric cancer (GC) remains a formidable clinical challenge. Although exosomes are critical mediators of tumor-microenvironment communication, their mechanistic role in linking mesothelial-mesenchymal transition (MMT) to peritoneal dissemination remains poorly understood. This study elucidates a GC-derived exosomal microRNA (miRNA)-driven pathway that orchestrates peritoneal metastasis. Integrated exosomal miRNA sequencing and The Cancer Genome Atlas (TCGA) analysis identified miR-196a-5p as highly enriched in GC-derived exosomes. Functional assays, including in vitro co-culture experiments, and in vivo PM models, demonstrated that GC-derived exosomal miR-196a-5p directly induces MMT in peritoneal mesothelial cells (HMrSV5) and contributed to the formation of metastatic tumors. Mechanistically, miR-196a-5p binds the 3'-untranslated region (UTR) of F-box protein 45 (FBXO45), an E3 ubiquitin ligase, suppressing its expression and thereby stabilizing snail family transcriptional repressor 1 (Snai1)-a key transcription factor in epithelial-mesenchymal transition (EMT). RNA immunoprecipitation sequencing (RIP seq), dual-luciferase reporter assays, co-immunoprecipitation (CO-IP), and rescue experiments validated the miR-196a-5p/FBXO45/Snai1 axis. Notably, miR-196a-5p disrupts FBXO45-mediated Snai1 ubiquitination and degradation, promoting MMT-driven peritoneal niche remodeling and metastatic progression. These findings reveal a novel exosome-mediated mechanism underlying GC dissemination and highlight miR-196a-5p and FBXO45 as promising therapeutic targets for PM. Show less
no PDF DOI: 10.1016/j.cellsig.2025.112039
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Han-Tao Jiang, Li-Ping Shen, Meng-Qi Pang +5 more · 2025 · Frontiers in immunology · Frontiers · added 2026-04-24
Idiopathic frozen shoulder (FS) can lead to difficulties in daily activities and significantly impact the quality of life. Early diagnosis and treatment can help alleviate symptoms and restore shoulde Show more
Idiopathic frozen shoulder (FS) can lead to difficulties in daily activities and significantly impact the quality of life. Early diagnosis and treatment can help alleviate symptoms and restore shoulder function. Therefore, we aimed to explore the diagnostic biomarkers and potential mechanisms of FS from a transcriptomics perspective. Total RNA was extracted from tissue samples of 15 FS and 11 controls. At the outset, we conducted differential expression analysis, weighted gene co-expression network analysis (WGCNA), and utilized the cytoHubba plugin, complemented by two machine learning algorithms, receiver operating characteristic (ROC) analysis, and expression level evaluation to identify biomarkers for FS. Subsequently, a nomogram was constructed based on the biomarkers. Additionally, we conducted enrichment and immune infiltration analyses to explore the mechanisms associated with these biomarkers. Finally, we confirmed the expression patterns of the biomarkers at the clinical level through reverse transcription-quantitative polymerase chain reaction (RT-qPCR). This study established a link between FS biomarkers that have strong diagnostic potential and specific immune responses, highlighting possible targets for diagnosing and treating FS. Show less
no PDF DOI: 10.3389/fimmu.2025.1559422
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Wenna Jiang, Meng Wang, Jiayi Wang +14 more · 2025 · Nature communications · Nature · added 2026-04-24
β-Hydroxybutyrylation (Kbhb) modification regulates protein molecular fates in either physiology or pathology, including cancer. However, the function and regulatory mechanism of Kbhb remain completel Show more
β-Hydroxybutyrylation (Kbhb) modification regulates protein molecular fates in either physiology or pathology, including cancer. However, the function and regulatory mechanism of Kbhb remain completely unknown in cancer metastasis. Here, we report that β-hydroxybutyrate (BHB) is clinically associated with the progression of pancreatic cancer and functionally promotes pancreatic cancer cell metastasis. Mechanistically, BHB induces Kbhb modification of Snail at lysine 152 to enhance Snail stabilization, which is regulated by Kbhb modification enzyme CREB-binding protein (CBP), and subsequently prevents Snail degradation by blocking recognition of E3 ubiquitin ligases FBXL14. Furthermore, either targeting Snail Kbhb modification or CBP inhibitor decreases cancer metastasis and enhances the therapeutic efficacy of gemcitabine in pancreatic cancer cells. Collectively, our study reveals that Kbhb of Snail is critical to promote metastasis and provides a potential therapeutic strategy. Show less
no PDF DOI: 10.1038/s41467-025-61541-3
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Yue Li, Zhe Zheng, Yanze Li +14 more · 2025 · Nature communications · Nature · added 2026-04-24
Ischemic injury induces a partial mesenchymal shift in endothelial cells (ECs), contributing to impaired vascular regeneration. However, the molecular regulators of this transitional state remain poor Show more
Ischemic injury induces a partial mesenchymal shift in endothelial cells (ECs), contributing to impaired vascular regeneration. However, the molecular regulators of this transitional state remain poorly defined. To address this, we performed circular RNA profiling of endothelial cells under ischemic-like conditions and identified a marked upregulation of a circular RNA, named circATXN1. Functional studies revealed that circATXN1 knockdown modulates endothelial phenotype and vascular response after ischemia. Functional studies have shown that knockdown of circATXN1 can regulate the endothelial cell phenotype and vascular response after ischemia. Mechanistically, circATXN1 knockdown enhances the demethylase protein ALKBH5 to reduce the RNA methylation level of the key transcription factor SLUG, thereby stabilizing SLUG. In animal models, suppression of circATXN1 enhances angiogenesis and improves recovery following ischemic injury. Here, we show that circATXN1 regulates partial endothelial-to-mesenchymal transition (EndMT) and angiogenesis by controlling SLUG mRNA methylation dynamics, highlighting its potential as a therapeutic target in ischemic disease. Show less
no PDF DOI: 10.1038/s41467-025-61596-2
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Maozhong Yao, Keyan Zhong, Xinbin Zheng +4 more · 2025 · Journal of cellular and molecular medicine · Blackwell Publishing · added 2026-04-24
Endothelial-to-mesenchymal transition (EndMT) induced by dysfunctional pulmonary artery endothelial cells (PAECs) is regarded as an initiating and pivotal factor in pulmonary hypertension (PH). This s Show more
Endothelial-to-mesenchymal transition (EndMT) induced by dysfunctional pulmonary artery endothelial cells (PAECs) is regarded as an initiating and pivotal factor in pulmonary hypertension (PH). This study focuses on identifying a novel therapeutic target for regulating EndMT in PH. A comprehensive analysis of 2 hypoxic PAECs datasets yielded 310 overlapping upregulated and 229 downregulated differentially expressed genes (DEGs). These upregulated DEGs were primarily enriched in HIF-1 signalling pathway and glycolysis/gluconeogenesis, while downregulated only in spliceosome, as indicated by KEGG. Through PPI network analysis and the application of MCC algorithms, 5 hub genes were identified among these upregulated DEGs: GAPDH, LDHA, ALDOA, PFKL, and PFKP. Their enrichment in the 2 aforementioned pathways was confirmed by cross-pathway DEGs analysis and ClueGo. Among the hub genes, LDHA was chosen as the key gene based upon expression and correlation analysis of the validation set from PH patients. Subsequent GSEA also revealed the enrichment of LDHA in these 2 pathways. Additionally, the increased expression of LDHA protein in tissues and cells was confirmed, and the elevated enzymatic activity of LDHA in clinical serum samples was also verified. From 2 online databases, 4 LDHA inhibitors were filtered out, and the stable binding between the inhibitors and the LDHA protein was confirmed through molecular docking and molecular dynamics simulation. Finally, the experimental results indicated that one of the inhibitors FX11 reversed EndMT by inhibiting the lactate-SNAI1 axis, thereby alleviating hypoxia-induced PH. The potential of LDHA as a therapeutic target for PH by modulating EndMT was proposed in this study. Show less
no PDF DOI: 10.1111/jcmm.70692
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Bowen Liu, Mengyue Wang, Changhuo Cen +6 more · 2025 · Cellular and molecular life sciences : CMLS · Springer · added 2026-04-24
HUWE1, a member of HECT E3 ubiquitin ligase family, is implicated in a variety of cellular processes. Recent studies find that HUWE1 also plays critical roles in germ cell development and inactivation Show more
HUWE1, a member of HECT E3 ubiquitin ligase family, is implicated in a variety of cellular processes. Recent studies find that HUWE1 also plays critical roles in germ cell development and inactivation of HUWE1 causes germ cell loss in both male and female mice. In this study, we found that Huwe1 was also highly expressed in testicular Sertoli cells. Inactivation of Huwe1 in Sertoli cells resulted in loss of cell polarity, which in turn caused germ cells loss and male infertility. Further study revealed that dysregulation in the expression of cytoskeletal and adhesion-related molecules, as well as a significant increase in EMT-related trans-factors SNAI1&2 in Huwe1-deficient Sertoli cells. Intriguingly, the protein level of WT1 was significantly increased in Huwe1-deficient Sertoli cells, and overexpression of Wt1 in Sertoli cells also caused the defects in spermatogenesis which was consistent with Huwe1 CKO mouse model. Furthermore, the defect of spermatogenesis in Huwe1 CKO mice was partially rescued by deleting one allele of Wt1 gene. Mechanistic studies revealed that WT1 interacts with HUWE1 protein and it could be ubiquitinated by HUWE1. Our study demonstrates that HUWE1 is involved in the establishment of Sertoli cell polarity mainly by regulating the protein level of WT1 gene. Show less
no PDF DOI: 10.1007/s00018-025-05779-6
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Sijie Gu, Haoran Feng, Xiaomei Li +10 more · 2025 · Molecular therapy : the journal of the American Society of Gene Therapy · Elsevier · added 2026-04-24
Preventing the progression from acute kidney injury (AKI) to chronic kidney disease (CKD) remains a considerable clinical challenge. In this study, we elucidate the role of WNT5A in accelerating the A Show more
Preventing the progression from acute kidney injury (AKI) to chronic kidney disease (CKD) remains a considerable clinical challenge. In this study, we elucidate the role of WNT5A in accelerating the AKI-to-CKD transition and its underlying mechanisms. Renal biopsies from patients with AKI showed marked upregulation of WNT5A and its receptor, CD146, in proximal tubules, with higher expression in patients with CKD progression. In murine AKI models, Wnt5a knockdown attenuated CKD progression. Conversely, proximal tubular overexpression of Wnt5a exacerbated renal fibrosis in ischemia-reperfusion injury (IRI) mice, which was alleviated by Box5, a specific WNT5A antagonist. In vitro, WNT5A overexpression in transforming growth factor β (TGF-β)-stimulated HK-2 cells promoted CD146 upregulation, activated JNK phosphorylation, and enhanced SNAI1 expression. The genetic silencing of WNT5A/CD146 and JNK inhibition suppresses SNAI1 expression and attenuates fibrotic responses. Mechanistically, JNK-mediated c-JUN phosphorylation promoted its interaction with KLF5 at the SNAI1 promoter, driving renal fibrosis. Elevated serum levels of soluble CD146 correlated with renal function in patients with AKI and were higher in patients exhibiting CKD progression. Inhibition of WNT5A could serve as a therapeutic target for delaying renal fibrosis in AKI progression. Show less
no PDF DOI: 10.1016/j.ymthe.2025.06.039
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Zhuo Zhang, Jingxia Li, Daneah Willis +2 more · 2025 · Toxicology and applied pharmacology · Elsevier · added 2026-04-24
Numerous studies have shown that exposure to cadmium [Cd(II)] contributes to the development of cancers in the lung and other organs. Cd(II) compounds are classified as confirmed human carcinogens; ho Show more
Numerous studies have shown that exposure to cadmium [Cd(II)] contributes to the development of cancers in the lung and other organs. Cd(II) compounds are classified as confirmed human carcinogens; however, the mechanisms underlying Cd(II)-induced carcinogenesis remain poorly understood. Small nucleolar RNA host gene 1 (SNHG1), a long non-coding RNA (lncRNA), has been identified as an oncogene. In this study, we investigated the role of SNHG1 in the invasion and migration of Cd(II)-transformed cells. Our findings revealed that SNHG1 expression was significantly elevated in Cd(II)-transformed cells compared to their passage-matched normal BEAS-2B counterparts. Silencing SNHG1 reduced the invasive and migratory capacities of Cd(II)-transformed cells and inhibited malignant transformation induced by long-term Cd exposure. Notably, ectopic expression of SNHG1 alone in BEAS-2B cells was sufficient to drive malignant transformation and enhance invasion and migration, underscoring its oncogenic potential. SRY-box 2 (Sox2), a transcription factor implicated in cancer cell proliferation, invasion, and migration, was found to be upregulated in Cd(II)-transformed cells, while SNHG1 knockdown led to decreased Sox2 protein levels. Similarly, ras-related C3 botulinum toxin substrate 1 (Rac1), a key regulator of cytoskeletal dynamics linked to tumor growth, invasion, and metastasis, was also elevated in Cd(II)-transformed cells. Knockdown of SNHG1 reduced Rac1 protein levels, and Rac1 knockout significantly suppressed invasion and migration. Additionally, we observed increased expression of Slug, a key transcription factor invovlved in epithelial-mesenchymal transition (EMT), and decreased expression of its downstream target E-cadherin in Cd(II)-transformed cells. Collectively, these results demonstrate that elevated SNHG1 promotes the expression of Sox2, Rac1, and Slug, thereby driving the invasive and migratory behavior of Cd(II)-transformed cells. Show less
no PDF DOI: 10.1016/j.taap.2025.117452
SNAI1
Yifan Li, Chengxian Jiang, Teng Ma +2 more · 2025 · Journal of cranio-maxillo-facial surgery : official publication of the European Association for Cranio-Maxillo-Facial Surgery · Elsevier · added 2026-04-24
This study aimed to investigate the role of the Midline1 gene in secondary palate development by analyzing its expression and function in palatal shelf fusion and morphology. Initially, twenty mouse e Show more
This study aimed to investigate the role of the Midline1 gene in secondary palate development by analyzing its expression and function in palatal shelf fusion and morphology. Initially, twenty mouse embryos were collected for each of the embryonic stages E13.5, E13.75, and E14.5. Whole-mount in situ hybridization was performed approximately ten times to optimize the experimental protocol and to analyze the expression pattern of Midline1 (MID1) in the palatal tissues at these developmental stages. Subsequently, palatal tissues from E13.5 embryos were treated with varying concentrations of Midline1 small interfering RNA (MID1 siRNA), and the knockdown efficiency was evaluated using Reverse Transcription Quantitative Polymerase Chain Reaction (RT-qPCR), with each concentration tested in triplicate. Based on the results, the most effective concentration, 100 nM MID1 siRNA, was selected for further experiments. Subsequently, twelve E13.5 palatal explants were allocated into two groups: six explants were treated with 100 nM MID1 siRNA (experimental group), and six with scrambled small interfering RNA(Scramble siRNA; control group). After 48 h of in vitro culture, hematoxylin and eosin (HE) staining was performed to evaluate the morphology of palatal shelf fusion. To evaluate apoptotic activity, Terminal deoxynucleotidyl transferase dUTP Nick-End Labeling (TUNEL) staining was performed on both experimental and control groups. Finally, immunohistochemistry and Western blot analyses were conducted to examine the expression levels of Matrix Metalloproteinase 8 (MMP8) and Snail Family Transcription Factors (Snail) proteins in three biological replicates from each group. Midline1 deficiency resulted in incomplete palatal shelf fusion and significantly reduced apoptosis. Additionally, the knockdown of Midline1 led to the upregulation of Snail and MMP8 gene expression, indicating that Midline1 plays a critical role in regulating epithelial-to-mesenchymal transition and maintaining cytoskeletal stability during palate development. Midline1 is essential for normal secondary palate development. Its dysregulation disrupts palatal shelf fusion and morphology, potentially contributing to craniofacial abnormalities such as cleft palate. These findings provide new insights into the molecular mechanisms underlying palate development and suggest that Midline1 could be a therapeutic target for addressing cleft palate and related defects. Show less
no PDF DOI: 10.1016/j.jcms.2025.06.006
SNAI1
Yixin Zhai, Cheng Li, Xiang He +4 more · 2025 · Annals of medicine · Taylor & Francis · added 2026-04-24
Anoikis is a new mode of cell death that has been shown to correlate significantly with tumors. However, the clinical prognostic significance of anoikis in lung squamous cell carcinoma (LUSC) remains Show more
Anoikis is a new mode of cell death that has been shown to correlate significantly with tumors. However, the clinical prognostic significance of anoikis in lung squamous cell carcinoma (LUSC) remains poorly studied. The differentially expressed ARGs and candidate genes were selected by the differential analysis to construct a predictive model. Independent prognostic gene was determined by Cox and LASSO analysis and we used the HCC95 and NCI H520 cell line to verify the gene function. We used the data from TCGA, GEO, GeneCards, and Harmonizome databases to analyze the immune microenvironment, functional enrichment, and drug sensitivity analysis. We identified 717 differentially expressed and selected 3 ARGs (FADD, SNAI1, and BAG4) to construct a predictive model. We found that SNAI1 is an independent prognostic gene and confirmed that knocking out the SNAI1 inhibited the HCC95 We used ARGs to construct a prognosis model for LUSC that can accurately predict the prognosis of LUSC patients. ARGs, especially SNAI1, play an essential role in developing LUSC. These findings could provide individualized treatment plans and new research ideas for LUSC patients. Show less
no PDF DOI: 10.1080/07853890.2025.2514944
SNAI1