👤 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, 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articles
Xiaoli Shi, Xueli Jia, Wei Liu +5 more · 2025 · Stem cells translational medicine · Oxford University Press · added 2026-04-24
Zinc finger protein 750 (ZNF750) has been identified as a potential tumor suppressor across multiple malignancies. Nevertheless, the specific involvement of ZNF750 in the regulation of mesenchymal cel Show more
Zinc finger protein 750 (ZNF750) has been identified as a potential tumor suppressor across multiple malignancies. Nevertheless, the specific involvement of ZNF750 in the regulation of mesenchymal cell differentiation and bone homeostasis has yet to be elucidated. In the current study, we observed a substantial presence of ZNF750 in bone tissue and noted alterations in its expression during osteogenic differentiation of mesenchymal progenitor cells. Functional experiments indicated that ZNF750 promoted osteogenic differentiation while impeding adipogenic differentiation from mesenchymal stem/progenitor cells. Further mechanistic investigations revealed that ZNF750 transcriptionally suppressed the expression of Snail family transcriptional repressor 1 (SNAI1) by binding to the proximal promoter region of Snai1 gene, thereby activating Wnt/β-catenin signaling. SNAI1 exerted opposing effects on cell differentiation towards osteoblasts and adipocytes in comparison to ZNF750. The overexpression of SNAI1 counteracted the dysregulated osteogenic and adipogenic differentiation induced by ZNF750. Furthermore, the transplantation of Znf750-silenced bone marrow stromal cells into the marrow of wild-type mice resulted in a reduction in cancellous and cortical bone mass, alongside a decrease in osteoblasts and an increase in marrow adipocytes, while the number of osteoclasts remained unchanged. This study presents the first demonstration that ZNF750 regulates the differentiation of osteoblasts and adipocytes from mesenchymal stem/progenitor cells by transcriptionally deactivating SNAI1 signaling, thereby contributing to the maintenance of bone homeostasis. It suggests that ZNF750 may represent a promising therapeutic target for metabolic bone disorders such as osteoporosis. Show less
no PDF DOI: 10.1093/stcltm/szaf013
SNAI1
Yiqiao Wang, Jie Wang, Shihao Huang +7 more · 2025 · Scientific reports · Nature · added 2026-04-24
Hepatocellular carcinoma (HCC) is a highly aggressive malignancy with poor prognosis, driven by complex molecular mechanisms that remain inadequately understood. Among these, the ubiquitin-proteasome Show more
Hepatocellular carcinoma (HCC) is a highly aggressive malignancy with poor prognosis, driven by complex molecular mechanisms that remain inadequately understood. Among these, the ubiquitin-proteasome system plays a crucial role in regulating protein stability and function, with E3 ubiquitin ligases emerging as key players in cancer progression. Here, we identify Tripartite Motif-containing 6 (TRIM6), an E3 ubiquitin ligase, as a critical regulator of HCC metastasis. We demonstrate that TRIM6 is significantly upregulated in HCC tissues and correlates with poor overall survival. Mechanistically, we uncover that STAT3 directly regulates TRIM6 by binding to its promoter and enhancing its transcription. Functionally, TRIM6 promotes epithelial-mesenchymal transition (EMT) and cell invasion by upregulating the key EMT transcription factor Snail1. Importantly, we reveal that TRIM6 interacts with and ubiquitinates DDX58 (RIG-I), leading to its proteasomal degradation. The degradation of DDX58 by TRIM6 alleviates its inhibitory effects on Snail1, thereby facilitating EMT and enhancing the invasive potential of HCC cells. These findings establish the STAT3-TRIM6-DDX58-Snail1 axis as a pivotal pathway in HCC progression, offering novel insights into the molecular underpinnings of HCC metastasis and highlighting TRIM6 as a potential therapeutic target and prognostic biomarker in HCC. Show less
no PDF DOI: 10.1038/s41598-025-96548-9
SNAI1
Anyue Wu, Shengze Li, Chunyang Feng +7 more · 2025 · Advanced science (Weinheim, Baden-Wurttemberg, Germany) · Wiley · added 2026-04-24
Metastatic spread of cancer is the leading cause of death in patients with epithelial ovarian cancer (EOC), and elucidation of the molecular mechanisms underlying this process is a major focus of canc Show more
Metastatic spread of cancer is the leading cause of death in patients with epithelial ovarian cancer (EOC), and elucidation of the molecular mechanisms underlying this process is a major focus of cancer research. Fibroblast growth factor-inducible 14 (Fn14) has been shown to regulate wound repair, inflammation, angiogenesis, and chemoresistance, but its functional role in metastasis in EOC is still unknown. Here it is reported that Fn14 is identified as a cancer metastasis suppressor that inhibits the migratory and invasive potential of EOC cells by down-regulating epithelial-mesenchymal transition (EMT). Mechanistically, it is identified that Fn14 promotes acetylation-dependent protein degradation of Slug, a key transcriptional factor associated with EMT. The deacetylase Sirtuin 2 (SIRT2) has been reported to be involved in the deacetylation of Slug protein to stabilize it and then prevent its degradation in the nucleus. The results showed that Fn14 alters the subcellular localization of (SIRT2) by interacting with SIRT2, leading to reduced SIRT2 shuttling into the nucleus and subsequently promoting the acetylated degradation of Slug. Collectively, the work has demonstrated for the first time that Fn14 inhibits EOC metastasis by regulating SIRT2-mediated Slug deacetylation, providing a new perspective and method for the development of future novel therapeutic strategies for the treatment of EOC metastasis. Show less
no PDF DOI: 10.1002/advs.202501552
SNAI1
Jing Li, Zan Song, Xue Dong +12 more · 2025 · Cell death & disease · Nature · added 2026-04-24
Vaccinia-related kinase 1 (VRK1) is involved in numerous cellular processes, including DNA repair, cell cycle and cell proliferation. However, its roles and molecular mechanism underlying the progress Show more
Vaccinia-related kinase 1 (VRK1) is involved in numerous cellular processes, including DNA repair, cell cycle and cell proliferation. However, its roles and molecular mechanism underlying the progression of hepatocellular carcinoma (HCC) are yet largely unexplored. Here, we demonstrated that VRK1 expression is elevated in HCC tumor tissues, which is associated with high tumor stage and poor prognosis in HCC patients. In vitro and in vivo experiments manifested that VRK1 overexpression significantly promotes cell proliferation, colony formation, migration and tumor growth of HCC by inducing epithelial-mesenchymal transition (EMT) program. Mechanistically, immunoprecipitation combined with mass spectrometry analysis determined that VRK1 interacts with CHD1L, which mediates the phosphorylation of CHD1L at serine 122 site. RNA-seq revealed that one of the key downstream target genes of VRK1 is SNAI1, by which VRK1 promotes EMT process and HCC progression. Furthermore, VRK1 upregulates SNAI1 expression through phosphorylating CHD1L. In conclusion, these findings suggested that VRK1/CHD1L/SNAI1 axis acts as a cancer-driving pathway to promote the proliferation and EMT of HCC, indicating that targeting VRK1 may be an attractive therapeutic strategy of HCC. Show less
no PDF DOI: 10.1038/s41419-025-07641-w
SNAI1
Di Lu, Gulibositan Aji, Guanyu Li +8 more · 2025 · The Journal of clinical investigation · added 2026-04-24
Fibrosis is the final common pathway leading to end-stage chronic kidney disease (CKD). However, the function of protein palmitoylation in renal fibrosis and the underlying mechanisms remain unclear. Show more
Fibrosis is the final common pathway leading to end-stage chronic kidney disease (CKD). However, the function of protein palmitoylation in renal fibrosis and the underlying mechanisms remain unclear. In this study, we observed that expression of the palmitoyltransferase ZDHHC18 was significantly elevated in unilateral ureteral obstruction (UUO) and folic acid-induced (FA-induced) renal fibrosis mouse models and was significantly upregulated in fibrotic kidneys of patients with CKD. Functionally, tubule-specific deletion of ZDHHC18 attenuated tubular epithelial cells' partial epithelial-mesenchymal transition (EMT) and then reduced the production of profibrotic cytokines and alleviated tubulointerstitial fibrosis. In contrast, ZDHHC18 overexpression exacerbated progressive renal fibrosis. Mechanistically, ZDHHC18 catalyzed the palmitoylation of HRAS, which was pivotal for its translocation to the plasma membrane and subsequent activation. HRAS palmitoylation promoted downstream phosphorylation of MEK/ERK and further activated Ras-responsive element-binding protein 1 (RREB1), enhancing SMAD binding to the Snai1 cis-regulatory regions. Taken together, our findings suggest that ZDHHC18 plays a crucial role in renal fibrogenesis and represents a potential therapeutic target for combating kidney fibrosis. Show less
no PDF DOI: 10.1172/JCI180242
SNAI1
Rulan Ma, Hongmei Nie, Caijing Mo +3 more · 2025 · European journal of medical research · BioMed Central · added 2026-04-24
The effect of coiled-coil domain-containing 154 (CCDC154) in liver cancer (LC) remains unexplored. The objective of this study was to investigate the role of CCDC154 in LC and its underlying mechanism Show more
The effect of coiled-coil domain-containing 154 (CCDC154) in liver cancer (LC) remains unexplored. The objective of this study was to investigate the role of CCDC154 in LC and its underlying mechanism. The analysis of CCDC154 expression and prognosis was performed using UALCAN, Human Protein Atlas and Kaplan-Meier plotter websites. Protein expression was measured using Western blotting assay. Lentivirus was used to silence CCDC154 expression in LC cells. The proliferation and apoptosis of LC cells was evaluated by cell counting assay, colony formation assay and flow cytometry. The migration and invasion of LC cells were investigated using scratch wound-healing assay and Transwell assay. The results showed that CCDC154 was highly expressed in LC and related to tumor grade and stage. High CCDC154 expression was associated with to poor outcomes in LC patients. Silencing of CCDC154 inhibited proliferation, migration and invasion of LC cells. It also increased apoptosis in LC cells. After CCDC154 knockdown, the expression of Twist, Vimentin and Snail was down-regulated. Overexpression of Snail abated the inhibitory caused by CCDC154 knockdown on LC cell growth. CCDC154 knockdown suppressed LC development through reducing Snail expression. Show less
no PDF DOI: 10.1186/s40001-025-02290-3
SNAI1
Yiqiao Wang, Shihao Huang, Yangbai Cai +5 more · 2025 · Biochimica et biophysica acta. Molecular basis of disease · Elsevier · added 2026-04-24
Programmed cell death protein 5 (PDCD5) is involved in apoptosis and is regarded as a tumor suppressor in various tumors. However, its role and underlying molecular mechanisms in hepatocellular carcin Show more
Programmed cell death protein 5 (PDCD5) is involved in apoptosis and is regarded as a tumor suppressor in various tumors. However, its role and underlying molecular mechanisms in hepatocellular carcinoma (HCC) remain unclear. PDCD5-overexpressing cell and xenograft tumor models were developed. Cell Counting Kit-8, 5-Ethynyl-2'-deoxyuridine, wound healing, Transwell, flow cytometry, immunohistochemistry, and hematoxylin-eosin staining were employed to explore the effects of PDCD5 on HCC cell behaviors and tumor growth. The enzyme-linked immunosorbent assay and western blot were used to detect pyroptosis-related marker levels. The molecular mechanisms underlying PDCD5's role in HCC were investigated through transcriptome sequencing and coimmunoprecipitation. SRI-011381, a TGF-β signaling activator, was applied to evaluate the impact of PDCD5 in modulating the TGF-β/Smad2/3/Snail pathway. PDCD5 expression was reduced in HCC cells. Overexpression of PDCD5 inhibited HCC cell proliferation, migration, invasion, and xenograft tumor growth. Additionally, PDCD5 overexpression promoted apoptosis and pyroptosis, with corresponding increases in inflammatory factors and Caspase-1, GSDMD, and NLRP3 protein levels. Mechanistically, PDCD5 bound to receptor-regulated Smads (Smad2/3), inhibiting the TGF-β pathway. Treatment with the TGF-β pathway activator SRI-011381 significantly counteracted the inhibitory effects of PDCD5 overexpression on HCC progression. Our findings suggest that PDCD5 impedes the progression of HCC by promoting pyroptosis via regulation of TGF-β/Smad2/3/Snail pathway, which could be a possible therapeutic target for HCC. Show less
no PDF DOI: 10.1016/j.bbadis.2025.167696
SNAI1
Nan Wu, Qian Sun, Liehao Yang +8 more · 2025 · International journal of biological macromolecules · Elsevier · added 2026-04-24
The treatment of metastatic melanoma has long posed a complex challenge within clinical practice. Previous studies have found that EMT transcription factors are essential in the development of various Show more
The treatment of metastatic melanoma has long posed a complex challenge within clinical practice. Previous studies have found that EMT transcription factors are essential in the development of various cancers through their induction of EMT. Here, we demonstrate that Snail2 expression is dramatically increased in melanoma and is associated with an adverse prognosis. Elevated Snail2 in melanoma cells enhanced migratory and invasive capabilities in vitro and in vivo. Furthermore, RNA-Seq analysis revealed a significant reduction of IGFBP3 expression in melanoma cells overexpressing Snail2. IGFBP3 might mitigate the Snail2's ability to promote melanoma metastasis via the PI3K-AKT pathway. Moreover, Snail2 and HDAC3 collaborate to suppress IGFBP3 transcription through H3K4 deacetylation and H4K5 delactylation. Additionally, the combination of HDAC3 and p-GSK-3β inhibitors significantly improved the treatment outcomes for lung metastasis in melanoma in vivo. The results of our study indicate that Snail2, HDAC3, and IGFBP3 play significant roles in melanoma progression and represent promising therapeutic targets. Show less
no PDF DOI: 10.1016/j.ijbiomac.2025.140310
SNAI1
Wenhao Cheng, Shunfang Liu, Jingliang He +8 more · 2025 · Biochemical and biophysical research communications · Elsevier · added 2026-04-24
Colorectal cancer (CRC) is a fatal cancer prevalent worldwide, and epithelial-mesenchymal transition (EMT) is a key factor in tumor invasion and metastasis. Piperine, a natural alkaloid known for its Show more
Colorectal cancer (CRC) is a fatal cancer prevalent worldwide, and epithelial-mesenchymal transition (EMT) is a key factor in tumor invasion and metastasis. Piperine, a natural alkaloid known for its antitumor properties, faces limitations in clinical use due to its moderate potency. To address this, our team synthesized and validated a new derivative, HJJ₃₅, which has shown potent antitumor activity against CRC cells. We assessed HJJ₃₅'s inhibitory effects on the colon cancer cell line HCT116 through MTT, colony formation, and assays for cell migration and invasion. To uncover HJJ₃₅'s molecular mechanisms, we utilized transcriptomics, weighted gene co-expression network analysis (WGCNA), and machine learning to identify key EMT-related genes. Western blot and immunofluorescence experiments confirmed the expression changes of these key proteins. Our findings indicate that HJJ₃₅ significantly suppressed the proliferation, migration, and invasion of HCT116 cells in vitro, outperforming piperine. We discovered that HJJ₃₅ downregulated the expression of COL12A1, PJA2, VCAN, MEF2C, DPYD, and DDR2 genes in HCT116 cells, which resulted in a decrease in the EMT regulator SNAI1, thus inhibiting EMT in these cells. In summary, this study presents novel evidence that the piperine derivative HJJ₃₅ inhibits the migration and invasion of colorectal cancer cells through SNAI1-mediated EMT. Show less
no PDF DOI: 10.1016/j.bbrc.2025.151323
SNAI1
Jianpeng Xiao, Jie Wang, Jialun Li +11 more · 2025 · Nature communications · Nature · added 2026-04-24
The STAT3 pathway promotes epithelial-mesenchymal transition, migration, invasion and metastasis in cancer. STAT3 upregulates the transcription of the key epithelial-mesenchymal transition transcripti Show more
The STAT3 pathway promotes epithelial-mesenchymal transition, migration, invasion and metastasis in cancer. STAT3 upregulates the transcription of the key epithelial-mesenchymal transition transcription factor SNAIL in a DNA binding-independent manner. However, the mechanism by which STAT3 is recruited to the SNAIL promoter to upregulate its expression is still elusive. In our study, the lysine methylation binding protein L3MBTL3 is positively associated with metastasis and poor prognosis in female patients with breast cancer. L3MBTL3 also promotes epithelial-mesenchymal transition and metastasis in breast cancer. Mechanistic analysis reveals that L3MBTL3 interacts with STAT3 and recruits STAT3 to the SNAIL promoter to increase SNAIL transcription levels. The interaction between L3MBTL3 and STAT3 is required for SNAIL transcription upregulation and metastasis in breast cancer, while the methylated lysine binding activity of L3MBTL3 is not required for these functions. In conclusion, L3MBTL3 and STAT3 synergistically upregulate SNAIL expression to promote breast cancer metastasis. Show less
no PDF DOI: 10.1038/s41467-024-55617-9
SNAI1
Yi Li, Wenhui Dang, Ting Jiao +2 more · 2025 · Molecular medicine reports · added 2026-04-24
Lung adenocarcinoma (LUAD) is a leading cause of cancer‑related death due to its aggressive nature and metastatic potential. The present study aimed to explore the expression of phospholipid phosphata Show more
Lung adenocarcinoma (LUAD) is a leading cause of cancer‑related death due to its aggressive nature and metastatic potential. The present study aimed to explore the expression of phospholipid phosphatase 2 (PPAP2C) in LUAD, and its effect on cell migration and invasion, with a particular focus on its association with the ERK/JNK signaling pathway and epithelial‑mesenchymal transition (EMT). The expression of PPAP2C in LUAD was analyzed using data from The Cancer Genome Atlas database. Pearson's correlation coefficient analysis was used to assess the correlation between PPAP2C and genes such as MAPK1, MAPK3, MAPK8, CDH1, CDH2 and SNAI1. Subsequently, the PPAP2C gene was silenced in A549 and H1299 LUAD cell lines using siRNA vectors, followed by assessments of gene expression, cell migration, invasion and protein interaction using reverse transcription‑quantitative PCR, western blotting, wound healing assay, Transwell invasion assay, molecular docking analysis, co‑immunoprecipitation and immunofluorescence staining. The results showed that PPAP2C was significantly upregulated in LUAD tissues compared with that in normal tissues. In addition, high levels of PPAP2C were significantly correlated with MAPK3, MAPK8, CDH1 and SNAI1. Notably, PPAP2C silencing significantly inhibited cell migration and invasion. Additionally, it reduced the phosphorylation levels of ERK and JNK proteins. PPAP2C showed specific binding sites with ERK1, and co‑precipitated with ERK1 in both A549 and H1299 cells. Furthermore, PPAP2C silencing decreased the expression levels of N‑cadherin and Snail, while increasing E‑cadherin expression, thereby inhibiting EMT. In conclusion, PPAP2C may be highly expressed in LUAD tissues, and could promote cell migration and invasion by activating the ERK/JNK signaling pathway and inducing EMT. These findings provide a novel potential target for the diagnosis and treatment of LUAD. Show less
no PDF DOI: 10.3892/mmr.2024.13392
SNAI1
Jin-Bao Wang, Shi-Lin Ding, Xiao-Song Liu +3 more · 2025 · Current molecular medicine · Bentham Science · added 2026-04-24
Colorectal cancer (CRC) is a malignant tumor. Slug has been found to display a key role in diversified cancers, but its relevant regulatory mechanisms in CRC development are not fully explored. Hence, Show more
Colorectal cancer (CRC) is a malignant tumor. Slug has been found to display a key role in diversified cancers, but its relevant regulatory mechanisms in CRC development are not fully explored. Hence, exploring the function and regulatory mechanisms of Slug is critical for the treatment of CRC. Protein expressions of Slug, N-cadherin, E-cadherin, Snail, HIF-1α, SUMO- 1, Drp1, Opa1, Mfn1/2, PGC-1α, NRF1, and TFAM were measured through western blot. To evaluate the protein expression of Slug and SUMO-1, an immunofluorescence assay was used. Cell migration ability was tested through transwell assay. The SUMOylation of Slug was examined through CO-IP assay. Slug displayed higher expression and facilitated tumor metastasis in CRC. In addition, hypoxia treatment was discovered to upregulate HIF-1α, Slug, and SUMO-1 levels, as well as induce Slug SUMOylation. Slug SUMOylation markedly affected mitochondrial biosynthesis, fusion, and mitogen-related protein expression levels to trigger mitochondrial stress. Additionally, the induced mitochondrial stress by hypoxia could be rescued by Slug inhibition and TAK-981 treatment. Our study expounded that hypoxia affects mitochondrial stress and facilitates tumor metastasis of CRC through Slug SUMOylation. Show less
no PDF DOI: 10.2174/0115665240271525231112121008
SNAI1
Anna K Waldmann, Dustin A Ammendolia, Andrew M Sydor +4 more · 2025 · PLoS pathogens · PLOS · added 2026-04-24
[This corrects the article DOI: 10.1371/journal.ppat.1013507.].
no PDF DOI: 10.1371/journal.ppat.1013816
VPS13C
Dazhi Li, Xinbo Wang, Bodan Hu +6 more · 2025 · bioRxiv : the preprint server for biology · Cold Spring Harbor Laboratory · added 2026-04-24
Bridge-like lipid transfer proteins (BLTPs) play central roles in redistributing lipids from their primary site of synthesis in the endoplasmic reticulum to other organelles. They comprise bridge-doma Show more
Bridge-like lipid transfer proteins (BLTPs) play central roles in redistributing lipids from their primary site of synthesis in the endoplasmic reticulum to other organelles. They comprise bridge-domains spanning between organelles at contact sites that allow lipids to transit the cytosol between adjacent membranes. The assembly of BLTPs into complexes with adaptor proteins enables their lipid transfer ability. To address the mechanisms underlying assembly and regulation of BLTP complexes, we used cryo-EM to resolve the structure of one such BLTP, the Parkinson's protein VPS13C, at near-atomic resolution. The structure identifies a lipid-transfer-nonpermissive conformation, where the built-in C-terminal VAB adaptor module blocks the end of the lipid transfer bridge, interfering with lipid delivery. We also identify calmodulin, central to calcium signaling, as a VPS13 partner, suggesting calcium regulation of VPS13 function. Altogether, this structure of intact VPS13C serves as starting point to understand its regulation and, more broadly, that of other BLTPs. Show less
no PDF DOI: 10.1101/2025.11.10.687702
VPS13C
Anna K Waldmann, Dustin A Ammendolia, Andrew M Sydor +4 more · 2025 · PLoS pathogens · PLOS · added 2026-04-24
Salmonella enterica serovar Typhimurium (S. Typhimurium) is a facultative intracellular bacterial pathogen that grows within a specialized membrane-bound compartment known as the Salmonella-containing Show more
Salmonella enterica serovar Typhimurium (S. Typhimurium) is a facultative intracellular bacterial pathogen that grows within a specialized membrane-bound compartment known as the Salmonella-containing vacuole (SCV). The molecular composition and regulatory mechanisms governing SCV dynamics remain incompletely understood. In this study, we employed proximity-dependent biotin identification (BioID) to analyze the SCV proteome during infection. For this, we targeted the UltraID biotin ligase to the SCV by fusing it to a type 3 secreted effector. We demonstrate that the bacteria express and translocate the effector-UltraID fusion protein directly into host cells for labeling of the cytosolic face of the SCV surface. Proteomic analysis of biotinylated proteins revealed previously undescribed proteins associated with the SCV, including regulators of vesicular trafficking, cellular metabolism and lipid transport. Among these, VPS13C, a lipid transporter and membrane contact site protein, was identified as a critical regulator of SCV morphology and fission. Functional studies revealed that VPS13C also promotes ER-SCV contact formation, controls SCV positioning in host cells, and facilitates cell-to-cell spread by the bacteria. Together, our findings highlight the utility of BioID as a tool to study host-pathogen interactions in the context of infection and characterize VPS13C as a novel modulator of the intracellular life cycle of S. Typhimurium. Show less
no PDF DOI: 10.1371/journal.ppat.1013507
VPS13C
Yeon J Lee, Khaja Syed, Oriol Busquets +6 more · 2025 · bioRxiv : the preprint server for biology · Cold Spring Harbor Laboratory · added 2026-04-24
Parkinson's disease (PD) arises from genetic and environmental factors. Human genetics has identified mutations in ~20 inherited familial genes linked to monogenic forms of PD. To investigate the effe Show more
Parkinson's disease (PD) arises from genetic and environmental factors. Human genetics has identified mutations in ~20 inherited familial genes linked to monogenic forms of PD. To investigate the effects of individual familial PD mutations, human pluripotent embryonic stem cells (hPSCs) carrying 12 distinct familial PD mutations were differentiated into midbrain lineage cells, including dopaminergic (mDA) neurons. Global gene expression and pre-mRNA splicing patterns were analyzed in midbrain cultures carrying pathogenic PD mutations in the Show less
no PDF DOI: 10.1101/2024.02.28.582420
VPS13C
Oriol Busquets, Hanqin Li, Khaja Mohieddin Syed +24 more · 2025 · bioRxiv : the preprint server for biology · Cold Spring Harbor Laboratory · added 2026-04-24
Parkinson's disease (PD) is a neurodegenerative disorder caused by complex genetic and environmental factors. Genome-edited human pluripotent stem cells (hPSCs) offer a unique experimental platform to Show more
Parkinson's disease (PD) is a neurodegenerative disorder caused by complex genetic and environmental factors. Genome-edited human pluripotent stem cells (hPSCs) offer a unique experimental platform to advance our understanding of PD etiology by enabling the generation of disease-relevant cell types carrying patient mutations along with isogenic control cells. To facilitate this approach, we generated a collection of 65 human stem cell lines genetically engineered to harbor high risk or causal variants in genes associated with PD ( Show less
no PDF DOI: 10.1101/2024.02.12.579917
VPS13C
Hang Yu, Jinghao Li, Tingting Lu +2 more · 2025 · Glia · Wiley · added 2026-04-24
NACHT, LRR, and PYD domains-containing protein 3 (NLRP3) inflammasome plays a pivotal role in the progression of cerebral ischemia/reperfusion injury (CI/RI). We aimed to investigate the implication o Show more
NACHT, LRR, and PYD domains-containing protein 3 (NLRP3) inflammasome plays a pivotal role in the progression of cerebral ischemia/reperfusion injury (CI/RI). We aimed to investigate the implication of WW domain-containing protein 2 (WWP2), an E3 ubiquitin ligase, in CI/RI and its mechanism. Microglia were subjected to oxygen-glucose deprivation/reoxygenation, and mice were subjected to middle cerebral artery occlusion (MCAO) for modeling. WWP2 was reduced in the brain tissues of mice with MCAO/R. WWP2 overexpression in microglia inhibited the NLRP3 inflammasome activation to alleviate MCAO/R-induced injury and microglia-induced neurotoxicity. WWP2 inhibited the mitochondrial translocation of NLRP3 by degrading mitochondrial antiviral-signaling protein (MAVS) to block its interaction with NLRP3, and MAVS overexpression in microglia promoted the NLRP3 activation to exacerbate MCAO/R and neurotoxicity. The nuclear export of TAR DNA-binding protein 43 (TDP-43) in MCAO/R promoted the WWP2 degradation via the (UG)n element of the 3'UTR of WWP2. TDP-43 overexpression also impaired the blockade of NLRP3 activation and exacerbated neurotoxicity in the presence of WWP2. Overall, our investigations demonstrate that nuclear export of TDP-43 in microglia activates NLRP3 inflammasome and exacerbates CI/RI by blocking MAVS degradation through (UG)n element-mediated instability of WWP2. Show less
no PDF DOI: 10.1002/glia.70077
WWP2
Bin Zhao, Jiacheng Li, Zunxian Wang +3 more · 2025 · Communications biology · Nature · added 2026-04-24
Colorectal cancer (CRC) remains one of the most prevalent and lethal malignancies worldwide, with cancer stemness and metastasis being critical factors contributing to poor prognosis. While circular R Show more
Colorectal cancer (CRC) remains one of the most prevalent and lethal malignancies worldwide, with cancer stemness and metastasis being critical factors contributing to poor prognosis. While circular RNAs are emerging as important regulators in cancer progression, the role of circGIGYF1 in CRC development is poorly understood. Here, we found that downregulated circGIGYF1 is linked to poor survival rate in CRC patients. circGIGYF1 inhibits CRC stemness, epithelial-mesenchymal transition, and metastatic potential both in vitro and in vivo. Mechanistically, circGIGYF1 promotes the interaction between WWP2 and HOXD13, enhancing HOXD13 ubiquitination and subsequent degradation. This degradation prevented HOXD13 from binding to the CTNNB1 promoter, thereby suppressing Wnt/β-catenin signalling pathway activation. Importantly, circGIGYF1 overexpression or HOXD13 knockdown significantly reduces tumor growth and liver metastasis in mouse models. These findings reveal a circGIGYF1/WWP2/HOXD13/β-catenin regulatory axis in CRC progression and highlight circGIGYF1 as a potential therapeutic target for developing strategies to combat CRC metastasis and recurrence. Show less
no PDF DOI: 10.1038/s42003-025-08280-9
WWP2
Fan Wu, Chunlan Li, Xianrang Song +1 more · 2025 · Cellular signalling · Elsevier · added 2026-04-24
Cisplatin is a widely used chemotherapeutic agent in the treatment of non-small cell lung cancer (NSCLC), but cisplatin resistance remains a significant clinical challenge. Lysosomal transmembrane pro Show more
Cisplatin is a widely used chemotherapeutic agent in the treatment of non-small cell lung cancer (NSCLC), but cisplatin resistance remains a significant clinical challenge. Lysosomal transmembrane protein 5 (LAPTM5) is a lysosomal membrane protein implicated in macroautophagy/autophagy, although its precise mechanism has yet to be fully elucidated.In this study, we demonstrated that LAPTM5 promotes cisplatin resistance in NSCLC by maintaining lysosomal membrane stability and preserving autophagic flux. Mechanistic investigations showed that LAPTM5 competes with LAMP1 for binding to WWP2, thereby inhibiting LAMP1 ubiquitination and degradation, which ultimately preserves lysosomal membrane stability. LAPTM5 knockdown increases lysosomal membrane permeability, leading to the release of cathepsin D (CTSD), which elevates intracellular reactive oxygen species (ROS) levels; further destabilizing the lysosomal membrane and accelerating cell death. Our findings elucidate the mechanism by which LAPTM5 contributes to cisplatin resistance through lysosomal membrane stabilization and identify LAPTM5 as a potential therapeutic target for overcoming cisplatin resistance in NSCLC. Show less
no PDF DOI: 10.1016/j.cellsig.2025.111834
WWP2
Jiao Gong, Huiru Sun, Kaiyuan Wang +26 more · 2025 · Nature communications · Nature · added 2026-04-24
Genomic structural variants (SVs) are a major source of genetic diversity in humans. Here, through long-read sequencing of 945 Han Chinese genomes, we identify 111,288 SVs, including 24.56% unreported Show more
Genomic structural variants (SVs) are a major source of genetic diversity in humans. Here, through long-read sequencing of 945 Han Chinese genomes, we identify 111,288 SVs, including 24.56% unreported variants, many with predicted functional importance. By integrating human population-level phenotypic and multi-omics data as well as two humanized mouse models, we demonstrate the causal roles of two SVs: one SV that emerges at the common ancestor of modern humans, Neanderthals, and Denisovans in GSDMD for bone mineral density and one modern-human-specific SV in WWP2 impacting height, weight, fat, craniofacial phenotypes and immunity. Our results suggest that the GSDMD SV could serve as a rapid and cost-effective biomarker for assessing the risk of cisplatin-induced acute kidney injury. The functional conservation from human to mouse and widespread signals of positive natural selection suggest that both SVs likely influence local adaptation, phenotypic diversity, and disease susceptibility across diverse human populations. Show less
no PDF DOI: 10.1038/s41467-025-56661-9
WWP2
Rongrong Luo, Xiying Li, Ruyun Gao +13 more · 2025 · Genomics, proteomics & bioinformatics · Oxford University Press · added 2026-04-24
Autoantibodies hold promise for diagnosing lung cancer. However, their effectiveness in early-stage detection needs improvement. In this study, we investigated novel IgG and IgM autoantibodies for det Show more
Autoantibodies hold promise for diagnosing lung cancer. However, their effectiveness in early-stage detection needs improvement. In this study, we investigated novel IgG and IgM autoantibodies for detecting early-stage lung adenocarcinoma (Early-LUAD) by employing a multi-step approach, including Human Proteome Microarray (HuProtTM) discovery, focused microarray verification, and ELISA validation, on 1246 individuals consisting of 634 patients with Early-LUAD (stage 0-I), 280 patients with benign lung disease (BLD), and 332 normal healthy controls (NHCs). HuProtTM selected 417 IgG/IgM candidates, and focused microarray further verified 55 significantly elevated IgG/IgM autoantibodies targeting 32 tumor-associated antigens in Early-LUAD compared to BLD/NHC/BLD+NHC. A novel panel of 10 autoantibodies (ELAVL4-IgM, GDA-IgM, GIMAP4-IgM, GIMAP4-IgG, MGMT-IgM, UCHL1-IgM, DCTPP1-IgM, KCMF1-IgM, UCHL1-IgG, and WWP2-IgM) demonstrated a sensitivity of 70.5% and a specificity of 77.0% or 80.0% for distinguishing Early-LUAD from BLD or NHC in ELISA validation. Positive predictive values for distinguishing Early-LUAD from BLD with nodules ≤ 8 mm, 9-20 mm, and > 20 mm significantly increased from 47.27%, 52.00%, and 62.90% [low-dose computed tomography (LDCT) alone] to 79.17%, 71.13%, and 87.88% (10-autoantibody panel combined with LDCT), respectively. The combined risk score (CRS), based on the 10-autoantibody panel, sex, and imaging maximum diameter, effectively stratified the risk for Early-LUAD. Individuals with 10 ≤ CRS ≤ 25 and CRS > 25 indicated a higher risk of Early-LUAD compared to the reference (CRS < 10), with adjusted odds ratios of 5.28 [95% confidence interval (CI): 3.18-8.76] and 9.05 (95% CI: 5.40-15.15), respectively. This novel panel of IgG and IgM autoantibodies offers a complementary approach to LDCT in distinguishing Early-LUAD from benign nodules. Show less
no PDF DOI: 10.1093/gpbjnl/qzae085
WWP2
Ran You, Yanwei Li, Yuteng Jiang +10 more · 2025 · Journal of advanced research · Elsevier · added 2026-04-24
Acute kidney injury (AKI) is associated with high morbidity and mortality rates. The molecular mechanisms underlying AKI are currently being extensively investigated. WWP2 is an E3 ligase that regulat Show more
Acute kidney injury (AKI) is associated with high morbidity and mortality rates. The molecular mechanisms underlying AKI are currently being extensively investigated. WWP2 is an E3 ligase that regulates cell proliferation and differentiation. Whether WWP2 plays a regulatory role in AKI remains to be elucidated. We aimed to investigate the implication of WWP2 in AKI and its underlying mechanism in the present study. We utilized renal tissues from patients with AKI and established AKI models in global or tubule-specific knockout (cKO) mice strains to study WWP2's implication in AKI. We also systemically analyzed ubiquitylation omics and proteomics to decipher the underlying mechanism. In the present study, we found that WWP2 expression significantly increased in the tubules of kidneys with AKI. Global or tubule-specific knockout of WWP2 significantly aggravated renal dysfunction and tubular injury in AKI kidneys, whereas WWP2 overexpression significantly protected tubular epithelial cells against cisplatin. WWP2 deficiency profoundly affected autophagy in AKI kidneys. Further analysis with ubiquitylation omics, quantitative proteomics and experimental validation suggested that WWP2 mediated poly-ubiquitylation of CDC20, a negative regulator of autophagy. CDC20 was significantly decreased in AKI kidneys, and selective inhibiting CDC20 with apcin profoundly alleviated renal dysfunction and tubular injury in the cisplatin model with or without WWP2 cKO, indicating that CDC20 may serve as a downstream target of WWP2 in AKI. Inhibiting autophagy with 3-methyladenine blocked apcin's protection against cisplatin-induced renal tubular cell injury. Activating autophagy by rapamycin significantly protected against cisplatin-induced AKI in WWP2 cKO mice, whereas inhibiting autophagy by 3-methyladenine further aggravated apoptosis in cisplatin-exposed WWP2 KO cells. Taken together, our data indicated that the WWP2/CDC20/autophagy may be an essential intrinsic protective mechanism against AKI. Further activating WWP2 or inhibiting CDC20 may be novel therapeutic strategies for AKI. Show less
no PDF DOI: 10.1016/j.jare.2024.06.015
WWP2
Yu Li, Tao Zhang, Lin Zhou +4 more · 2025 · International immunopharmacology · Elsevier · added 2026-04-24
Elevated circulating lactate serves as a critical biomarker in sepsis, yet the epigenetic mechanisms by which lactate influences disease progression remain unclear. This study aims to identify lactate Show more
Elevated circulating lactate serves as a critical biomarker in sepsis, yet the epigenetic mechanisms by which lactate influences disease progression remain unclear. This study aims to identify lactate-associated genes in sepsis, decode their regulatory roles, and assess their potential as therapeutic targets. We performed transcriptome-wide bioinformatic analyses to identify lactylation-related differentially expressed genes (DEGs) between sepsis patients and healthy controls. Pathway enrichment highlighted immune signaling circuits. Five DEGs (ZC3H4, RBM10, PCBP2, RBM25, HNRNPM) were prioritized via ROC analysis, and their combined expression formed a prognostic signature with strong predictive power (AUC > 0.85). Validation in murine sepsis-induced acute lung injury (ALI) models (cecal ligation-puncture and LPS challenge) confirmed significant upregulation of these five genes by qRT-PCR. RBM25 was selected for deeper functional study. Mechanistic assays implicate an RBM25-Acly axis that couples altered metabolism to histone lactylation and transcriptional reprogramming. Notably, we propose the RBM25-Acly axis that couples altered metabolism to histone lactylation and transcriptional reprogramming. Our work uncovers a novel metabolic-epigenetic circuit in sepsis driven by lactylation, with RBM25 and its regulation of ACLY as a key node. The lactylation-based gene signature offers a high-fidelity prognostic tool, and targeting the RBM25-Acly pathway may open new therapeutic avenues. These findings lay a foundation for precision interventions that integrate metabolic and epigenetic strategies in sepsis care. Show less
no PDF DOI: 10.1016/j.intimp.2025.115177
ZC3H4
Cong Li, Jiale Han, Tingjin Chang +5 more · 2025 · BMC genomics · BioMed Central · added 2026-04-24
Sichuan donkeys are small-statured donkeys native to the plateau and mountainous regions of southwestern China. They are well-suited for transportation tasks in mountainous terrain and exhibit remarka Show more
Sichuan donkeys are small-statured donkeys native to the plateau and mountainous regions of southwestern China. They are well-suited for transportation tasks in mountainous terrain and exhibit remarkable adaptability to the harsh environment, characterized by low temperatures and hypoxia. Adaptation to the local environment has shaped their unique genomic characteristics and is an important source of genetic variation. However, the genome-wide landscape of Sichuan donkeys remains undescribed. In this study, we obtained whole-genome sequencing data from 17 Sichuan donkeys and combined this data with published data of 99 donkeys from 9 other donkey breeds. We aimed to elucidate the population structure, genetic diversity, genetic differentiation, and selection pressure of Sichuan donkeys at the whole-genome level. Population structure and genetic diversity analysis showed that Sichuan donkeys were less influenced by the hybridization of foreign donkey breeds. They maintained a relatively pure lineage of Chinese native donkeys and exhibited higher genetic diversity. The study also found that Sichuan donkeys were genetically closest to Tibetan and Yunnan donkeys. Although their effective population size around 1000 years ago was smaller compared to Tibetan and Yunnan donkeys, it was still larger than that of other donkey breeds. Moreover, selective signature analysis (θπ, CLR, F This study clarified the genetic diversity, genetic differentiation, and effective population size of Sichuan donkeys by comparing them with other donkey breeds. Our findings contribute to deeper understanding of the high-altitude adaptability of Sichuan donkeys, and provide valuable information for the conservation and breeding of the breed. Show less
no PDF DOI: 10.1186/s12864-025-12254-w
ZNF668
Yunxi Li, In-Hee Lee, Sek Won Kong · 2025 · medRxiv : the preprint server for health sciences · Cold Spring Harbor Laboratory · added 2026-04-24
Despite widely acknowledged sex differences in lipid metabolism and risks for cardiovascular disease, genetic associations contributing to such differences remain incompletely characterized. Here, we Show more
Despite widely acknowledged sex differences in lipid metabolism and risks for cardiovascular disease, genetic associations contributing to such differences remain incompletely characterized. Here, we performed a sex-stratified genome-wide association study (GWAS) for four lipid profiles to identify loci exhibiting differential effects between males and females. Using whole-genome sequencing data from All of Us Research Program comprising 124,920 participants of diverse ancestry, we conducted GWAS analyses separately in males, females, and a pooled cohort. Our analyses validated previous findings on genes associated with lipid metabolism. In addition, we have found 5 genes showing significant sex-heterogeneous effects, including Show less
no PDF DOI: 10.1101/2025.11.21.25340771
ZPR1
Fangyan Wang, Peng Li, Qiuxu Liu +3 more · 2024 · Genes · MDPI · added 2026-04-24
Quantitative reverse transcription PCR (qRT-PCR) can screen applicable reference genes of species, and reference genes can be used to reduce experimental errors. Sudan grass (
📄 PDF DOI: 10.3390/genes15020210
ACP2
Yu Liang, Guangshang Zhong, Yangyang Li +6 more · 2024 · Biochemical genetics · Springer · added 2026-04-24
The pivotal role of lysosomal function in preserving neuronal homeostasis is recognized, with its dysfunction being implicated in neurodegenerative processes, notably in Parkinson's disease (PD). Yet, Show more
The pivotal role of lysosomal function in preserving neuronal homeostasis is recognized, with its dysfunction being implicated in neurodegenerative processes, notably in Parkinson's disease (PD). Yet, the molecular underpinnings of lysosome-related genes (LRGs) in the context of PD remain partially elucidated. We collected RNA-seq data from the brain substantia nigra of 30 PD patients and 20 normal subjects from the GEO database. We obtained molecular classification clusters from the screened lysosomal expression patterns. The lysosome-related diagnostic model of Parkinson's disease was constructed by XGBoost and Random Forest. And we validated the expression patterns of signature LRGs in the diagnostic model by constructing a PD rat model. Finally, the linkage between PD and cancer through signature genes was explored. The expression patterns of the 33 LRGs screened can be divided into two groups of PD samples, enabling exploration of the variance in biological processes and immune elements. Cluster A had a higher disease severity. Subsequently, critical genes were sieved through the application of machine learning methodologies culminating in the identification of two intersecting feature genes (ACP2 and LRP2). A PD risk prediction model was constructed grounded on these signature genes. The model's validity was assessed through nomogram evaluation, which demonstrated robust confidence validity. Then we analyzed the correlation analysis, immune in-filtration, biological function, and rat expression validation of the two genes with common pathogenic genes in Parkinson's disease, indicating that these two genes play an important role in the pathogenesis of PD. We then selected ACP2, which had a significant immune infiltration correlation, as the entry gene for the pan-cancer analysis. The pan-cancer analysis revealed that ACP2 has profound associations with prognostic indicators, immune infiltration, and tumor-related regulatory processes across various neoplasms, suggesting its potential as a therapeutic target in a range of human diseases, including PD and cancers. Our study comprehensively analyzed the molecular grouping of LRGs expression patterns in Parkinson's disease, and the disease progression was more severe in cluster A. And the PD diagnosis model related to LRGs is constructed. Finally, ACP2 is a potential target for the relationship between Parkinson's disease and tumor. Show less
📄 PDF DOI: 10.1007/s10528-023-10652-x
ACP2
Lei Gao, Haifang Jiang, Minze Li +8 more · 2024 · Journal of genetics and genomics = Yi chuan xue bao · Elsevier · added 2026-04-24
Lipid remodeling is crucial for cold tolerance in plants. However, the precise alternations of lipidomics during cold responses remain elusive, especially in maize (Zea mays L.). In addition, the key Show more
Lipid remodeling is crucial for cold tolerance in plants. However, the precise alternations of lipidomics during cold responses remain elusive, especially in maize (Zea mays L.). In addition, the key genes responsible for cold tolerance in maize lipid metabolism have not been identified. Here, we integrate lipidomic, transcriptomic, and genetic analysis to determine the profile of lipid remodeling caused by cold stress. We find that the homeostasis of cellular lipid metabolism is essential for maintaining cold tolerance of maize. Also, we detect 210 lipid species belonging to 13 major classes, covering phospholipids, glycerides, glycolipids, and free fatty acids. Various lipid metabolites undergo specific and selective alterations in response to cold stress, especially mono-/di-unsaturated lysophosphatidic acid, lysophosphatidylcholine, phosphatidylcholine, and phosphatidylinositol, as well as polyunsaturated phosphatidic acid, monogalactosyldiacylglycerol, diacylglycerol, and triacylglycerol. In addition, we identify a subset of key enzymes, including ketoacyl-acyl-carrier protein synthase II (KAS II), acyl-carrier protein 2 (ACP2), male sterility33 (Ms33), and stearoyl-acyl-carrier protein desaturase 2 (SAD2) involved in glycerolipid biosynthetic pathways are positive regulators of maize cold tolerance. These results reveal a comprehensive lipidomic profile during the cold response of maize and provide genetic resources for enhancing cold tolerance in crops. Show less
no PDF DOI: 10.1016/j.jgg.2023.07.004
ACP2
Jun-Ren Lai, Li Gong, Yan Liu +3 more · 2024 · Sheng li xue bao : [Acta physiologica Sinica] · added 2026-04-24
This study aimed to analyze the impact of single nucleotide polymorphism (SNP) of
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ADCY3