👤 Xianglong Li

🔍 Search 📋 Browse 🏷️ Tags ❤️ Favourites ➕ Add 🧪 BiometalDB 🧬 Extraction
3991
Articles
2551
Name variants
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, 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, Xiying 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
Xiaoyan Qin, Dingheng Hu, Qi Li +6 more · 2025 · Molecular medicine (Cambridge, Mass.) · BioMed Central · added 2026-04-24
Liver X receptor α (LXRα) plays an important role in inflammatory immune response induced by hepatic ischemia-reperfusion injury (IRI) and acute rejection (AR). Macrophage M1-polarization play an impo Show more
Liver X receptor α (LXRα) plays an important role in inflammatory immune response induced by hepatic ischemia-reperfusion injury (IRI) and acute rejection (AR). Macrophage M1-polarization play an important role in the occurrence and development of AR. Although the activation of LXR has anti-inflammatory effects, the role of LXRα in AR after liver transplantation (LT) has not been elucidated. We aimed to investigate LXRα anti-inflammatory and macrophage polarization regulation effects and mechanisms in acute rejection rat models. LXRα anti-inflammatory and liver function protective effects was initially measured in primary Kupffer cells and LT rat models. Subsequently, a flow cytometry assay was used to detect the regulation effect of LXRα in macrophage polarization. HE staining, TUNEL and ELISA were used to evaluate the co-treatment effects of TO901317 and tacrolimus on hepatic apoptosis and liver acute rejection after LT. In this study, we found that LPS can inhibit the expression of LXRα and activate MAPK pathway and PI3K/AKT/mTOR. We also found that LXRα agonist (TO901317) could improve liver function and rat survival after LT by activating the level of ABCA1 and inhibiting MAPK. TO901317 could inhibit macrophage M1-polarization by activating PI3K/AKT/mTOR signal pathway to improve the liver lesion of AR rats after liver transplantation. Additionally, co-treatment with TO901317 and tacrolimus more effectively alleviated the damaging effects of AR following LT than either drug alone. Our results suggest that the activation of LXRα can improve liver function and rat survival after LT by regulate ABCA1/MAPK and PI3K/AKT/mTOR signaling axis in macrophages. Show less
no PDF DOI: 10.1186/s10020-025-01153-1
NR1H3
Guoshang Ji, Junxing Zhang, Hui Sheng +9 more · 2025 · International immunopharmacology · Elsevier · added 2026-04-24
Endometritis in dairy cows involves complex molecular regulatory mechanisms. Therefore, uncovering the molecular regulatory mechanisms of endometritis in dairy cows is crucial to understand its develo Show more
Endometritis in dairy cows involves complex molecular regulatory mechanisms. Therefore, uncovering the molecular regulatory mechanisms of endometritis in dairy cows is crucial to understand its development, prevention, and treatment. This study aimed to screen and validate key genes associated with endometritis using transcriptome sequencing of blood samples and previously obtained metabolomic sequencing data. Based on gain-of-function and loss-of-function experiments on the gene, multiple techniques, including qRT-PCR, western blotting, detection of reactive oxygen species (ROS), measurement of mitochondrial membrane potential, EdU assay, flow cytometry, and CCK-8 assay were used to explore the function of the key gene in lipopolysaccharide (LPS)-stimulated bovine endometrial epithelial cells (BEECs). The results identified 536 differentially expressed genes (DEGs) between healthy cows and those with endometritis. These DEGs were significantly enriched in apoptosis and HIF-1 signaling pathways. Weighted gene co-expression network analysis of transcriptomic and metabolomic data identified CD83, CTNNAL1, LRRC25, and NR1H3 as potential key genes for endometritis in dairy cows, with CD83 being more significantly expressed in LPS-induced BEECs. Consequently, in vitro functional studies were performed on CD83. In overexpression experiments, downregulation of the expression of inflammatory markers interleukin (IL)-1β, IL-6, and IL-8 and reduced ROS release primarily indicated the role of CD83 in attenuating the inflammatory response of BEECs. Furthermore, overexpression of CD83 regulated the S/G2 phase transition of BEECs by affecting the mRNA and protein expression of proliferation marker genes, thereby promoting proliferation of BEECs. The increased EdU positivity and the cell proliferation rate further provided evidence for the promotion of cell proliferation after overexpression of CD83. Additionally, overexpression of CD83 attenuated LPS-stimulated mitochondrial damage in BEECs, as well as the downregulation of apoptosis marker gene expression. In contrast, knockdown of CD83 expression showed the opposite trend. In summary, CD83 attenuated the inflammatory response of BEECs, promoted their proliferation, and inhibited apoptosis. This study provided basic data for understanding the mechanisms of endometritis regulation at the gene level in dairy cows. Show less
no PDF DOI: 10.1016/j.intimp.2025.114183
NR1H3
Wenqi Liao, You Li, Haoyan Zhao +1 more · 2025 · Histology and histopathology · added 2026-04-24
To observe the effect of the Lian-Dou-Qing-Mai (LDQM) formula on lipid metabolism in mice and explore its mechanism from the perspective of regulating the PPARγ/LXRα/ABCA1 signaling pathway. THP-1 cel Show more
To observe the effect of the Lian-Dou-Qing-Mai (LDQM) formula on lipid metabolism in mice and explore its mechanism from the perspective of regulating the PPARγ/LXRα/ABCA1 signaling pathway. THP-1 cells were induced to transform into foam cells with ox-LDL. Atherosclerosis (AS) models were constructed using a high-fat diet in ApoE In the cell model, LDQM could inhibit the formation of THP-1 macrophage-derived foam cells and the expression of inflammatory factors, promote macrophage cholesterol efflux, increase the expression of IL-10, and activate the PPARγ-LXRα-ABCA1/ABCG1 pathway. Additional IL-10 treatment further promotes LDQM-induced cholesterol efflux in THP-1 cells; LDQM may affect the PPARγ/LXRα/ABCA1 signaling pathway through IL-10, regulate lipid metabolism, reduce serum inflammatory expression and lipid deposition, and improve the formation of atheroplaques. Show less
no PDF DOI: 10.14670/HH-18-803
NR1H3
Tian-Hao Lan, Wei Li, Xin Wang +12 more · 2025 · iScience · Elsevier · added 2026-04-24
Colorectal cancer (CRC) is a prevalent digestive system malignancy accompanied by peritoneal metastasis occurring in 7% of cases. Methyltransferase-like 3 (METTL3) promoted the progression of CRC wher Show more
Colorectal cancer (CRC) is a prevalent digestive system malignancy accompanied by peritoneal metastasis occurring in 7% of cases. Methyltransferase-like 3 (METTL3) promoted the progression of CRC whereas its function in peritoneal metastasis was incompletely understood. Here, we found that METTL3 was upregulated in peritoneal metastasis tissues of CRC patients compared with CRC tissues. By sequencing the mRNA of above tissues, we discovered that METTL3-mediated N6-methyladenosine (m6A) modification regulated the downstream target Show less
no PDF DOI: 10.1016/j.isci.2025.113165
NRXN3
Yongxue Li, Lihao Lin, Wenhui Zhang +3 more · 2025 · Discover oncology · Springer · added 2026-04-24
Meningioma is a common primary central nervous system tumor that can cause a heavy burden on patients. Despite its well-established treatment modalities, pharmacological treatments are not sufficientl Show more
Meningioma is a common primary central nervous system tumor that can cause a heavy burden on patients. Despite its well-established treatment modalities, pharmacological treatments are not sufficiently abundant. Therefore, we explored potential therapeutic targets for meningiomas by integrating genomic and proteomic data. We integrated meningioma data from the UK Biobank and Finnish databases and subsequently explored potential therapeutic targets for meningiomas through multi-omics data using bioinformatics techniques and Mendelian randomization. These targets were finally evaluated using phenotype-wide association group analysis. We found that BET1L, COL17A1, CFAP43, SH3PXD2A, TTC28, ZNRF3, SLK, AKR1C3, NRXN3, and RSPO3 can be potential therapeutic targets for meningiomas. This study provides evidence and explores the biological significance of BET1L, COL17A1, CFAP43, SH3PXD2A, TTC28, ZNRF3, SLK, AKR1C3, NRXN3, and RSPO3 as potential therapeutic targets for meningiomas, providing new insights into the development of targeted therapy for meningiomas. Show less
no PDF DOI: 10.1007/s12672-025-03318-0
NRXN3
Fawang Du, Hanchao Wang, Zhihong Chen +7 more · 2025 · Journal of asthma and allergy · added 2026-04-24
Asthma severity assessment is essential for asthma management. Transcriptomics contributes substantially to asthma pathogenesis. Then, this study aimed to explore asthma severity-associated transcript Show more
Asthma severity assessment is essential for asthma management. Transcriptomics contributes substantially to asthma pathogenesis. Then, this study aimed to explore asthma severity-associated transcriptomics profile and promising biomarkers for asthma severity prediction. In discovery cohort, induced sputum cells from 3 non-severe and 3 severe asthma patients were collected and analyzed using RNA-seq. Multivariate analysis was performed to explore asthma severity-associated transcriptomics profile and differential expressed genes (DEGs). The Kyoto Encyclopedia of Genes and Genomes (KEGG) and Gene Ontology (GO) were used for pathway enrichment analysis. Subsequently, based on the previous study and clinical experience, the mRNA expressions of 6 overlapped asthma severity-associated DEGs and Distinct asthma severity-associated transcriptomics profile was identified in induced sputum cells in discovery cohort. Then, 345 DEGs were found, of which 38 terms and 32 pathways were enriched using GO and KEGG, respectively. In validation cohort, the mRNA expressions of Collectively, this study provides the first identification of the association between induced sputum cells transcriptomics profile and asthma severity, indicating the potential value of transcriptomics for asthma management. The study also reveals the promising value of serum C3 for predicting asthma severity in clinical practice. Show less
no PDF DOI: 10.2147/JAA.S517140
NRXN3
Xiaojun Yang, Bowen Zhang, Fuyuan Wen +8 more · 2025 · International journal of molecular sciences · MDPI · added 2026-04-24
This study aims to identify genetically influenced metabolites (GIMs) associated with SSBP and elucidate their regulatory pathways through metabolome genome-wide association studies (mGWASs). Untarget Show more
This study aims to identify genetically influenced metabolites (GIMs) associated with SSBP and elucidate their regulatory pathways through metabolome genome-wide association studies (mGWASs). Untargeted metabolomics and genome-wide genotyping were performed on 54 participants from the Systematic Epidemiological Study of Salt Sensitivity (EpiSS). The mGWAS was conducted on 970 plasma metabolites, and their potential biological mechanisms were explored. The multivariable logistic regression model and mendelian randomization (MR) were employed to investigate the association and causal relationship between GIMs and SSBP. Metabolomic analysis was performed on 100 subjects in the replication analysis to validate the GIMs identified in the discovery set and their causal association with SSBP. The mGWAS revealed associations between 1485 loci and 18 metabolites. After performing linkage disequilibrium analysis, 368 independent mQTLs were identified and annotated to 141 genes. These functional genes were primarily implicated in the signal transduction of sinoatrial node and atrial cardiac muscle cells. Five key genes were identified using CytoHubba, including Show less
no PDF DOI: 10.3390/ijms26104538
NRXN3
Xia Chen, Shengkun Zhang, Yujuan Qi +17 more · 2025 · Human molecular genetics · Oxford University Press · added 2026-04-24
Mesenchymal cells constitute the primary structural support elements within endometriotic lesions, yet their pivotal roles in endometriotic pathogenesis remain largely uncharted. This study aimed to c Show more
Mesenchymal cells constitute the primary structural support elements within endometriotic lesions, yet their pivotal roles in endometriotic pathogenesis remain largely uncharted. This study aimed to construct a single-cell atlas of endometriosis using samples from three ovarian tissues affected by endometriosis and three normal ovarian tissues. Through the utilization of scRNA-seq, we have unveiled six distinct mesenchymal subclusters in normal and endometriosis-afflicted ovaries, elucidating the diverse functions of mesenchymal populations in endometriosis. Our comprehensive analysis has revealed that mesenchymal cells predominantly engage in three key functions: ribosome-mediated protein synthesis and processing, cell adhesion facilitating intercellular support and communication, and a range of metabolic processes. Furthermore, our findings have identified several pivotal differentially expressed genes (e.g. C3, FN1, COL3A1, COL1A1, NRXN3), primarily associated with the complement and coagulation cascades, extracellular matrix (ECM) regulation, ECM receptor interactions, and cell adhesion molecules. In essence, our study provides a comprehensive transcriptomic dataset and novel insights into adhesive molecule and integrin networks within mesenchymal subclusters in endometriosis. This, in effect, has deepened the understanding of the pathomechanisms governing this condition. Show less
no PDF DOI: 10.1093/hmg/ddaf065
NRXN3
Linghui Xiang, Ruiling Xu, Xiaoxia Zhou +3 more · 2025 · Journal of affective disorders · Elsevier · added 2026-04-24
The comorbidity of major depressive disorder (MDD) and Parkinson's disease (PD) were prevalent and has a profound impact on patients. However, whether this comorbidity results from specific pathologic Show more
The comorbidity of major depressive disorder (MDD) and Parkinson's disease (PD) were prevalent and has a profound impact on patients. However, whether this comorbidity results from specific pathological processes or a mutual cause-and-effect relationship was largely controversial. Additionally, although MDD can appear before or after PD, the health impact of the comorbidity sequence is poorly understood. We used mendelian randomization (MR) and UK biobank (UKB) cohort to explore the associations between MDD and PD. MR was also utilized to investigate potential confounders. By classifying UKB patients into MDD first and PD first groups, we evaluated the health impact of the comorbidity sequence using Cox regression. Bidirectional MR and cohort study showed conflicting results. MR did not find associations between MDD followed by PD (odds ratio [OR] = 1.28, 95 % confidence interval [CI] = 0.85-1.94) or PD followed by MDD (OR = 0.99, 95 % CI = 0.97-1.01). However, the cohort study found a significant effect of MDD on PD (hazard ratio [HR] = 1.75, 95 % CI = 1.55-1.97) and PD on MDD (HR = 4.35, 95 % CI = 3.65-5.19). By performing MR on 4709 proteins, we identified ESD, LEAP2, NDRG3, NRXN3, and PLXNB2 as potential common causes of MDD and PD. Additionally, PD first group had higher risks of all-cause mortality (HR = 1.65, 95 % CI = 1.03-1.90), dementia (HR = 1.88, 95 % CI = 1.16-3.04), and aspiration pneumonia (HR = 1.89, 95 % CI = 1.09-3.27). Our study suggested the comorbidity of MDD and PD is likely the result of certain pathological processes. Additionally, patients with PD first had higher risks of several adverse outcomes. Show less
no PDF DOI: 10.1016/j.jad.2025.03.065
NRXN3
Deying Liu, Jiaxin Li, Chan Xu +7 more · 2025 · Human molecular genetics · Oxford University Press · added 2026-04-24
Mutations in four genes encoding the outer ring complex of nuclear pore complexes (NPCs), NUP85, NUP107, NUP133 and NUP160, cause monogenic steroid-resistant nephrotic syndrome (SRNS). Knockout of NUP Show more
Mutations in four genes encoding the outer ring complex of nuclear pore complexes (NPCs), NUP85, NUP107, NUP133 and NUP160, cause monogenic steroid-resistant nephrotic syndrome (SRNS). Knockout of NUP85, NUP107, or NUP133 in immortalized human podocytes activates CDC42, an important effector of SRNS pathogenesis. However, it is unknown whether or not loss of NUP160 dysregulates CDC42 in the podocytes. Here, we generated a podocyte-specific Nup160 knockout mouse model with double-fluorescent (mT/mG) Cre reporter genes using CRISPR/Cas9 and Cre/loxP technologies. We investigated nephrotic syndrome-associated phenotypes in the Nup160podo-/- mice, and performed single-cell transcriptomic and proteomic analysis of glomerular suspension cells and cultured primary podocytes, respectively. The Nup160podo-/- mice exhibited progressive proteinuria and fusion of podocyte foot processes. We found decreased Cdc42 protein and normal Cdc42 transcriptional level in the podocytes of the Nup160podo-/- mice using analysis of single-cell transcriptomes and proteomes. We subsequently observed that Cdc42 protein decreased in both kidney tissues and cultured primary podocytes of the Nup160podo-/- mice, although Cdc42 mRNA levels were elevated in the cultured primary podocytes of the Nup160podo-/- mice. We also found that Cdc42 activity was significantly reduced in the cultured primary podocytes of the Nup160podo-/- mice. In conclusion, loss of Nup160 dysregulated Cdc42 in the podocytes of the Nup160podo-/- mice with proteinuria and fusion of podocyte foot processes. Our findings suggest that the dysregulation of CDC42 may contribute to the pathogenesis of SRNS in patients with mutations in NUP160. Show less
no PDF DOI: 10.1093/hmg/ddaf064
NUP160

Novel

Yuhao Liu, Xiaoying Huang, Lubin Xu +3 more · 2025 · Clinical kidney journal · Oxford University Press · added 2026-04-24
Nucleoporins, as major components of nuclear pore complex, have been recently discovered to participate in organ development. Here, we report a young female patient with nephrotic proteinuria resistan Show more
Nucleoporins, as major components of nuclear pore complex, have been recently discovered to participate in organ development. Here, we report a young female patient with nephrotic proteinuria resistant to immune suppressant treatment and congenital ovarian insufficiency. Renal pathology confirmed focal segmental glomerulosclerosis and whole-exome sequencing revealed compound heterozygous mutations in Nucleoporin 160 ( Show less
no PDF DOI: 10.1093/ckj/sfae388
NUP160
Ling Yao, Yuanyuan Li, Ping Wang +2 more · 2025 · Pediatric nephrology (Berlin, Germany) · Springer · added 2026-04-24
Nucleoporins (Nups) are a class of proteins that assemble to form nuclear pore complexes, which are related to nucleocytoplasmic transport, gene expression, and the cell cycle. Pathogenic variants in Show more
Nucleoporins (Nups) are a class of proteins that assemble to form nuclear pore complexes, which are related to nucleocytoplasmic transport, gene expression, and the cell cycle. Pathogenic variants in six genes encoding Nups, NUP85, NUP93, NUP107, NUP133, NUP160, and NUP205, cause monogenic steroid-resistant nephrotic syndrome (SRNS), referred to as nucleoporin-associated SRNS. In this paper, we review the epidemiology, structure and function of Nups, pathogenesis, phenotypes and genotypes, and management of nucleoporin-associated SRNS as well as implications for genetic counseling. Affected individuals exhibit autosomal recessive isolated and syndromic SRNS, whose extrarenal manifestations include neurological disorders, growth and development disorders, cardiovascular disorders, and congenital malformations. The median ages at onset of NUP85-, NUP93-, NUP107-, NUP133-, NUP160-, and NUP205-associated SRNS are 7, 3, 4.1, 9, 7, and 2 years, respectively. Kidney biopsies reveal focal segmental glomerulosclerosis in 89% of patients. Most affected individuals are resistant to immunosuppressants. For the six subtypes of nucleoporin-associated SRNS, patients show progression to kidney failure at median ages of 8.5, 3.7, 6.9, 13, 15, and 7 years, respectively. Only two patients with NUP93-associated SRNS with nephrotic syndrome relapse post-transplant have been reported, and the recurrence rate is 12.5%. Next-generation sequencing using a targeted gene panel is recommended in cases of suspected nucleoporin-associated SRNS for genetic diagnosis. Renin-angiotensin-aldosterone system inhibitors are recommended for patients with nucleoporin-associated SRNS. Once genetic diagnosis is confirmed, immunosuppressant discontinuation should be considered, and kidney transplant is preferred when patients progress to kidney failure. Genetic counselling should be provided for asymptomatic siblings and future siblings of an affected individual. Further studies on the pathogenesis of nucleoporin-associated SRNS are needed to seek new therapeutic interventions. Show less
no PDF DOI: 10.1007/s00467-024-06494-3
NUP160
Hongyu Yan, Long Shi, Yang Li +1 more · 2025 · Biology · MDPI · added 2026-04-24
Sarcopenia is a common age-related skeletal muscle disorder that lacks diagnostic and therapeutic options. Emerging evidence suggests that cuproptosis, a copper-dependent form of regulated cell death, Show more
Sarcopenia is a common age-related skeletal muscle disorder that lacks diagnostic and therapeutic options. Emerging evidence suggests that cuproptosis, a copper-dependent form of regulated cell death, contributes to muscle atrophy, yet the underlying associations remain poorly understood. To address this gap, we integrated two GEO datasets (GSE1428 and GSE25941) for differential expression analysis and applied weighted gene co-expression network analysis (WGCNA) to identify disease-related modules. Cuproptosis-related genes (CRGs) from GeneCards database were intersected with DEGs and WGCNA gene modules to obtain sarcopenia-associated cuproptosis DEGs (SAR-CUP DEGs). Functional enrichment was performed using GO, KEGG, GSEA and GSVA. Hub genes were further identified through three machine learning algorithms (LASSO, RF, and SVM). Regulatory networks were constructed via NetworkAnalyst and GeneMANIA database. A diagnostic model was also developed and later validated in an independent dataset (GSE136344). Experimental validation was performed in a D-galactose-induced sarcopenia cell model. We identified 367 DEGs and 7 co-expression modules, among which 14 SAR-CUP DEGs were mainly enriched in mitochondrial energy metabolism pathways. Machine learning methods highlighted Show less
no PDF DOI: 10.3390/biology14121642
PABPC4
Xianqi Shen, Zijian Li, Yuchuan Shi +5 more · 2025 · Translational andrology and urology · added 2026-04-24
Poly(A) binding protein cytoplasmic 4 (PABPC4) has been regarded as a prognostic marker in many malignancies. In this study, we evaluated PABPC4 expression at both messenger ribonucleic acid (mRNA) an Show more
Poly(A) binding protein cytoplasmic 4 (PABPC4) has been regarded as a prognostic marker in many malignancies. In this study, we evaluated PABPC4 expression at both messenger ribonucleic acid (mRNA) and protein levels. The prognostic value of PABPC4 in patients with prostate cancer (PCa) was also investigated. The Cancer Genome Atlas (TCGA) database, Gene Expression Omnibus (GEO) database, our analysis of Chinese Prostate Cancer Genome and Epigenome Atlas (CPGEA), and 65 pairs of ribonucleic acid (RNA) sequencing data from our center were employed to detect the expression of PABPC4 in PCa tissues. Tissue microarrays (TMAs) were utilized to detect the expression of the PABPC4 protein, and survival analysis as well as risk factor analysis were conducted. In the 65 pairs of sequencing data, the expression of PABPC4 in tumor tissues was significantly higher than that in paired adjacent tissues (P<0.001), and its expression also presented significant differences among different Gleason groups (P=0.041). In the CPGEA data, the expression of PABPC4 in tumor tissues was significantly higher than that in control tissues (P<0.001), and the expression of PABPC4 in M1 patients was higher than that in M0 patients, although no significant statistical difference was shown (P=0.051). In the TCGA data, the expression of PABPC4 in tumor tissues was significantly higher than that in control tissues (P<0.001). The expression of pT3/4 (pathological tumor stage 3 and pathological tumor stage 4) in high-stage tumor tissues was significantly higher than that in low-stage tumor tissues (pT2) (P=0.02), the expression of pT3/4 in GSE21034 and GSE32571 tumor tissues was significantly higher than that in control tissues (P<0.001), and the expression of pT3/4 in primary tumor tissues was higher than that in metastatic tissues in GSE6752 (P<0.001). The TCGA data revealed that patients with high PABPC4 expression had poorer overall survival (OS) than those with low PABPC4 expression (P=0.04), and the TMA data indicated that patients with high PABPC4 expression had a poor prognosis (P=0.004). Our study demonstrated that PABPC4 was overexpressed at mRNA and protein levels in PCa. We found that patients with high PABPC4 expression had a shorter biochemical recurrence (BCR)-free survival and OS, showing its value as a prognostic biomarker in patients with PCa. Show less
no PDF DOI: 10.21037/tau-2025-19
PABPC4
Chenchen Zhao, Yan Qin, Haixin Huang +6 more · 2025 · Veterinary sciences · MDPI · added 2026-04-24
Swine acute diarrhea syndrome coronavirus (SADS-CoV) is a novel enteric coronavirus that causes severe clinical diarrhea and intestinal pathological injury in pigs. Selective autophagy is an important Show more
Swine acute diarrhea syndrome coronavirus (SADS-CoV) is a novel enteric coronavirus that causes severe clinical diarrhea and intestinal pathological injury in pigs. Selective autophagy is an important mechanism of host defense against virus invasion. However, the mechanism through which SADS-CoV-mediated selective autophagy mediates the innate immune response remains unknown. Here, we report that the host protein PABPC4 can inhibit SADS-CoV replication through targeting and degrading its N protein. Furthermore, we demonstrate that PABPC4 recruits MARCHF8 (an E3 ubiquitin ligase), which ubiquitinates the N protein and is degraded via NDP52/CALCOCO2 (a selective autophagy cargo receptor). Taken together, these findings reveal a new mechanism by which PABPC4 inhibits virus replication, and reveal a new target for antiviral drug development. Show less
no PDF DOI: 10.3390/vetsci12030257
PABPC4
Shuanghui Chen, Yan Lu, Hao Chen +6 more · 2025 · Molecular biology and evolution · Oxford University Press · added 2026-04-24
The Kirgiz, a Turkic-speaking ethnic group with a rich nomadic heritage, represent a pivotal population for understanding human migration and adaptation in Central Asia. However, their genetic origins Show more
The Kirgiz, a Turkic-speaking ethnic group with a rich nomadic heritage, represent a pivotal population for understanding human migration and adaptation in Central Asia. However, their genetic origins and admixture history remain largely unexplored. Here, we present the first comprehensive genomic study of Kirgiz populations from Xinjiang, China (XJ.KGZ, n = 36) and their counterparts in Kyrgyzstan (KRG), integrating genome-wide data of 2,406 global individuals. Our analyses reveal four primary ancestry components in XJ.KGZ: East Asian (41.7%), Siberian (25.6%), West Eurasian (25.2%), and South Asian (7.6%). Despite close genetic affinity (FST = 0.13%), XJ.KGZ and KRG diverged ∼447 years ago, with limited gene flow post-split. A two-wave admixture model elucidates their demographic history: an initial East-West Eurasian mixture ∼2,225 years ago, likely reflecting west-east contacts during the period of the Warring States and the Qin Dynasty, followed by secondary admixture events (∼875 to 425 years ago) linked to historical migrations under Mongol and post-Mongol rule. Local adaptation signatures implicate genes critical for cellular tight junction (e.g. PATJ), pathogen invasion (e.g. OR14I1), and cardiac functions (e.g. RYR2) with allele frequency deviations suggesting ancestry-specific selection. While no classical high-altitude adaptation genes (e.g. EPAS1) showed selection signals, RYR2 and C10orf67-implicated in hypoxia response in Tibetan fauna-displayed Western ancestry bias, hinting at convergent adaptation mechanisms. This study advances our understanding of the genetic makeup and admixture history of the Kirgiz people and provides novel insights into human dispersal in Central Asia. Show less
no PDF DOI: 10.1093/molbev/msaf196
PATJ
Zhigang Hu, Yingjie Cai, Chang Cao +5 more · 2025 · Poultry science · Elsevier · added 2026-04-24
Skin color of poultry, an important economic trait, is related to breed, feed, environment, and other factors. In recent years, China's duck industry has developed rapidly, and duck products are welco Show more
Skin color of poultry, an important economic trait, is related to breed, feed, environment, and other factors. In recent years, China's duck industry has developed rapidly, and duck products are welcomed by consumers. Different skin colors of ducks have different cooking methods. Black skinned duck, such as Yulin black duck, is more popular in China because they are considered more suitable for making soup, while other skin colors, such as Pekin duck, is used for roasting. In order to gain a deeper understanding of the genetic factors associated with differences in duck skin color, the transcriptomes and metabolomes of skin between Yulin black duck and Pekin duck from 15 (BSE15 vs. PSE15), 21 (BSE21 vs. PSE21) and 27 (BSE27 vs. PSE27) days of incubation were compared and analyzed. The transcriptome results showed that a total of 187 (118 up-regulated and 69 down-regulated), 417 (91 up-regulated and 326 down-regulated) and 137 (55 up-regulated and 82 down-regulated) differentially expressed genes (DEGs) were identified from BSE15 vs. PSE15, BSE21 vs. PSE21 and BSE27 vs. PSE27, respectively. The significantly enriched GO terms of biological process were positive regulation of melanin biosynthetic process, melanin biosynthetic process, cuticle development, melanin biosynthetic process from tyrosine, and melanocyte differentiation, which were potentially related to skin growth and development. Eleven significant pathways, highly enriched by DCT, TYR, ASIP, TYRP1, KIT, PHOSPHO2, CERS3, SGPP2, SPTLC3, DEGS2, PATJ, RBP7, AOX1, ETNPPL, HPGDS, and GAD1, were melanogenesis, tyrosine metabolism, vitamin B6 metabolism, sphingolipid metabolism, protein digestion and absorption, tight junction, alpha-linolenic acid metabolism, arachidonic acid metabolism, linoleic acid metabolism, nicotinate and nicotinamide metabolism, and alanine, aspartate and glutamate metabolism, which participated in regulating the development of duck skin during embryonic stage. The significantly different metabolites (SDMs) were mainly organoheterocyclic compounds, lipids and lipid-like molecules, organic oxygen compounds, organic acids and derivatives, including L-tyrosine, N-arachidonyl maleimide, glycerophospho-N-palmitoyl ethanolamine, LPE 22:4, and PC(0:0/18:0). which were mainly enriched in glycerophospholipid metabolism, arachidonic acid metabolism, linoleic acid metabolism, alpha-linoleic acid metabolism, and melanogenesis in metabolome, suggesting that these pathways may play important roles in skin development of duck during embryonic stage. Besides, the analysis of integrated transcriptome and metabolome indicated that the pathways, including glycerophospholipid metabolism, arachidonic acid metabolism, linoleic acid metabolism, and alpha-linolenic acid metabolism, could contribute to regulating skin development in embryonic duck. Our findings could help elucidate the genetic mechanisms underlying the development differences in duck skin color. Furthermore, the candidate genes and metabolites can be used to provide a valuable breeding strategy for the selection of specific duck breeds with ideal skin coloration. Show less
no PDF DOI: 10.1016/j.psj.2025.105403
PATJ
Xinxin Xiong, Danyang Wang, Liping Xu +7 more · 2025 · Journal for immunotherapy of cancer · added 2026-04-24
The highly organized structures of the immunological synapse (IS) are crucial for T cell activation. PDZ domains might be involved in the formation of the IS by serving as docking sites for protein in Show more
The highly organized structures of the immunological synapse (IS) are crucial for T cell activation. PDZ domains might be involved in the formation of the IS by serving as docking sites for protein interactions. In this study, we investigate the role of the PALS1-associated tight junction protein (PATJ), which contains 10 PDZ domains, in the formation of IS and its subsequent impact on T cell activation. To elucidate the function of PATJ, we generated murine models with conditional T cell-specific knockout of We observed a rapid increase in PATJ expression during T cell activation. Conditional knockout of Our study reveals an important role of PATJ in the formation of IS and provides an approach to improve the efficacy of CAR-T therapy. Show less
no PDF DOI: 10.1136/jitc-2024-010966
PATJ
Chenyang Wang, Kunpeng Li, Shun Wan +3 more · 2025 · Cell death & disease · Nature · added 2026-04-24
The persistent issues of drug resistance and tumor recurrence remain major challenges in bladder cancer (BCa) treatment, severely impacting patient outcomes. In this study, we found that Triosephospha Show more
The persistent issues of drug resistance and tumor recurrence remain major challenges in bladder cancer (BCa) treatment, severely impacting patient outcomes. In this study, we found that Triosephosphate isomerase 1 (TPI1) plays a crucial role in influencing gemcitabine (Gem) resistance in BCa. TPI1 is significantly upregulated in Gem-resistant BCa tissues, and the knockdown of TPI1 markedly increases Gem sensitivity and chemotherapy-induced apoptosis both in vivo and in vitro. Meanwhile, the same was validated in Gem-resistant strains. Mechanistically, transcriptome sequencing and transmission electron microscopy, among others, revealed that TPI1 promoted Gem-associated autophagy. Furthermore, mass spectrometry and co-immunoprecipitation assays demonstrated that TPI1 directly binds to the BH3 domain of Beclin-1. This interaction competitively disrupts the binding between Bcl-2 and Beclin-1, thereby relieving Bcl-2-mediated inhibition of Beclin-1. Furthermore, the interaction between TPI1 and Beclin-1 promotes the formation of PIK3C3-C1, which in turn enhances the interaction between PIK3C3-C1 and the ULK1 complex, thereby increasing the phosphorylation of Beclin-1 at Ser15. In addition, TPI1 also enhanced mitochondrial autophagy induced by Gem in BCa cells and tissues. Importantly, a transcription factor, c-Myc, that regulates TPI1 expression was also identified, and dual luciferase and Chromatin immunoprecipitation-quantitative PCR (ChIP-qPCR) analysis showed that c-Myc binds primarily to the promoter region of TPI1. Our results suggest that TPI1 plays an important role in regulating the formation of autophagic complexes, and that promoting autophagy significantly increased Gem resistance in BCa. Show less
no PDF DOI: 10.1038/s41419-025-08368-4
PIK3C3
Jiangming Wei, Xiaobo Wei, Lexiu Deng +4 more · 2025 · Scientific reports · Nature · added 2026-04-24
Dysregulation of macrophage autophagy plays a critical role in sepsis-induced acute lung injury (ALI); however, its underlying mechanism remains unclear. In this study, we aimed to identify the regula Show more
Dysregulation of macrophage autophagy plays a critical role in sepsis-induced acute lung injury (ALI); however, its underlying mechanism remains unclear. In this study, we aimed to identify the regulatory pathway involving the PIK3C3-MAPK14 signaling axis that drives ALI progression by controlling autophagy and macrophage polarization. Using machine learning transcriptomic analysis, MAPK14 was identified as a core gene associated with ALI, and multi-omics integration confirmed its upregulated expression in ALI tissues. MAPK14 localization to pro-inflammatory macrophages was determined using single-cell sequencing. Furthermore, we observed a significant positive correlation between MAPK14 and autophagy-related genes. Molecular docking and kinetic simulations revealed high-affinity interactions between PIK3C3 and MAPK14 (ΔG-bind = -127.722 ± 33.269 kJ/mol). In vitro experiments followed by Western Blot(WB) and RT-q polymerase chain reaction (PCR) assays demonstrated that lipopolysaccharide stimulation upregulated MAPK14 expression through downregulation of PIK3C3 expression, resulting in impaired autophagic flux (LC3-II/Ⅰ↓, TOM20↑, P62↑, HSP60↑). Flow cytometry and enzyme-linked immunosorbent assay (ELISA) confirmed a shift toward pro-inflammatory (M1) macrophage polarization. RNA pull-down assay directly captured the PIK3C3-MAPK14 complex, and functional validation showed that PIK3C3 overexpression significantly inhibited MAPK14 protein expression, whereas PIK3C3 knockdown enhanced it. In conclusion, targeting the PIK3C3-MAPK14 axis is a promising therapeutic strategy for ALI. Show less
no PDF DOI: 10.1038/s41598-025-27088-5
PIK3C3
Yu-Hang Li, Yan Cheng, Bing-Qian Zhao +7 more · 2025 · Journal of virology · added 2026-04-24
Classical swine fever virus (CSFV) is a highly contagious and lethal pathogen that poses a major threat to the global swine industry. Despite its economic impact, no specific antiviral therapies are c Show more
Classical swine fever virus (CSFV) is a highly contagious and lethal pathogen that poses a major threat to the global swine industry. Despite its economic impact, no specific antiviral therapies are currently available, underscoring the urgent need to elucidate virus-host interactions for therapeutic innovation. In this study, we screened a glucose metabolism-targeted small-molecule library and identified Vps34-IN-1, a selective inhibitor of phosphatidylinositol 3-kinase class III (VPS34/PIK3C3), as a potent suppressor of CSFV replication in a dose-dependent manner. Time-of-addition experiments demonstrate that Vps34-IN-1 predominantly interferes with the late stage of the viral life cycle. Consistently, siRNA-mediated knockdown of VPS34 significantly impairs viral replication, confirming its role as a critical host dependency factor. Mechanistically, pharmacological inhibition or genetic silencing of VPS34 disrupts CSFV-induced autophagic flux. Notably, the CSFV non-structural protein p7 engages in a specific interaction with UVRAG, a pivotal constituent of the VPS34 complex II, and appears to potentiate VPS34-UVRAG complex assembly, thereby facilitating autophagosome-lysosome fusion. Collectively, these findings uncover an unappreciated role of VPS34 in sustaining CSFV replication and highlight its potential as a viable target for host-oriented antiviral intervention. CSFV remains a major pathogen of global concern, causing severe disease in swine and incurring substantial economic losses in the pig industry. The absence of effective antiviral agents underscores the pressing need for host-targeted therapeutic strategies. In this study, we identified Vps34-IN-1, a selective inhibitor of VPS34, as a potent suppressor of CSFV replication in a dose-dependent manner. Remarkably, Vps34-IN-1 also exhibits potent inhibitory activity against other economically important swine viruses, including BVDV, PRV, and PEDV, demonstrating its potential as a broad-spectrum antiviral agent. Knockdown experiments further validated VPS34 as an essential host factor required for CSFV propagation. Mechanistically, the viral p7 protein engages in a specific interaction with UVRAG, a pivotal constituent of the VPS34 complex II, thereby potentially augmenting VPS34-UVRAG complex assembly and facilitating autophagosome-lysosome fusion. These findings delineate VPS34 as a compelling host-oriented antiviral target and open new therapeutic avenues for the control of CSF and other economically significant swine viral diseases. Show less
no PDF DOI: 10.1128/jvi.01641-25
PIK3C3
Zi-Zhan Li, Kan Zhou, Jinmei Wu +5 more · 2025 · Research (Washington, D.C.) · added 2026-04-24
Cancer persists as one of the most formidable global public health crises and socioeconomic burdens of our era, compelling the scientific community to develop innovative and diversified therapeutic mo Show more
Cancer persists as one of the most formidable global public health crises and socioeconomic burdens of our era, compelling the scientific community to develop innovative and diversified therapeutic modalities to revolutionize clinical management and enhance patient outcomes. The recent seminal discovery by Swamynathan et al. has unveiled menadione, a vitamin K precursor, as a potent inducer of triaptosis-a novel regulated cell death pathway mediated through the oxidative modulation of phosphatidylinositol 3-kinase PIK3C3/VPS34. This mechanistically distinct cell death paradigm, characterized by its intimate association with endosomal dysfunction and oxidative stress-induced cellular catastrophe, has demonstrated remarkable therapeutic efficacy in preclinical prostate cancer models, outperforming conventional therapeutic regimens and emerging as a potential paradigm-shifting strategy in oncology. This comprehensive review provides a critical synthesis of the triaptosis discovery landscape, elucidating its molecular intricacies and pathophysiological implications. We systematically examine the multifaceted roles of endosomal biology in oncogenesis and tumor progression, while offering a nuanced perspective on redox homeostasis in malignant cells and the therapeutic potential of oxidative stress modulation. Furthermore, we address the inherent dichotomy of oxidative stress induction in cancer therapy, balancing its therapeutic promise against potential adverse effects. Looking toward the horizon of cancer research, we explore transformative therapeutic strategies leveraging triaptosis induction and its potential applications beyond oncology, aiming to catalyze a new era of precision medicine that ultimately enhances patient survival and quality of life. Show less
no PDF DOI: 10.34133/research.0880
PIK3C3
Yufang Zuo, Xuan Liu, Yajun Pang +7 more · 2025 · Frontiers in oncology · Frontiers · added 2026-04-24
Hepatoid carcinoma of the ovary (HCO) is a highly uncommon and aggressive neoplasm originating from the surface epithelial cells of the ovary, characterized by hepatocyte-like differentiation. To date Show more
Hepatoid carcinoma of the ovary (HCO) is a highly uncommon and aggressive neoplasm originating from the surface epithelial cells of the ovary, characterized by hepatocyte-like differentiation. To date, most information on HCO is derived from case reports, with fewer than 50 documented cases globally. In this case report, we present a detailed account of the diagnosis, treatment, and prognosis of a patient diagnosed as having bilateral HCO, which is even rarer. Targeted next-generation sequencing revealed somatic mutations in PIK3C3 and TP53, with no BRCA1/2 alterations, and a molecular profile consistent with microsatellite stability and low tumor mutational burden. We also review the current literature to situate our findings within the broader context of existing knowledge. Given the rarity of bilateral HCO, our objective is to contribute to the existing body of knowledge by providing a comprehensive description of its clinical features, molecular characteristics, and treatment strategies. This effort may enhance understanding of this rare malignancy and offer insights to improve patient outcomes in clinical practice. Show less
no PDF DOI: 10.3389/fonc.2025.1631424
PIK3C3
Zhiyun Tao, Wenjuan Xu, Weitao Song +7 more · 2025 · Poultry science · Elsevier · added 2026-04-24
While spermatogenesis has been extensively characterized in mammals, its molecular underpinnings in avian species remain largely unexplored. To address this knowledge gap, we performed single-cell tra Show more
While spermatogenesis has been extensively characterized in mammals, its molecular underpinnings in avian species remain largely unexplored. To address this knowledge gap, we performed single-cell transcriptomic profiling of duck testes across developmental stages (10-week immature vs. 23-week mature). Our analysis generated a comprehensive cellular atlas comprising 54,702 cells, resolving eight germ cell clusters (three spermatogonia [SPG], three spermatocytes [SPC], two spermatozoa [SPT]) and nine somatic populations, including peritubular myoid cells, immune subsets (T cells, macrophages, granulocytes), endothelial cells, Leydig cells, and three Sertoli cell subtypes, each defined by unique marker gene signatures. Furthermore, novel marker genes were identified, including EXFABP for granulocyte, ARHGAP15 for T cell regulation, FDX1 specific to Leydig cells (LC), and TSSK3/TSSK2 linked to elongated spermatid formation (SPT). Notably, we identified some novel molecular markers distinguishing these populations. Pseudotemporal trajectory reconstruction of germline development revealed stage-specific enrichment of ribosome, endoplasmic reticulum protein processing, and autophagy pathways. Core regulators MRPL13, MRPL2, MRPL22, MRPS14, MRPS7 (ribosome), HSPA5 (ER stress response), and PIK3C3 (autophagy) emerged as molecular hubs showing progressive downregulation during differentiation. Comparative transcriptomic analysis of germ cells and Sertoli cells between immature (IMT) and mature (MT) testes revealed significant enrichment of the spliceosome pathway in both germ and Sertoli cells. Critical spliceosome components SNRPG, SF3B3, and SNRPF exhibited coordinated downregulation during testicular maturation, suggesting their role as negative regulators of spermatogenic progression. This study establishes the first high-resolution cellular blueprint of avian spermatogenesis, delineating regulatory networks of duck testis cell development. Our findings provide valuable datasets and mechanistic insights into the evolutionary specialization of reproductive strategies in poultry. Show less
no PDF DOI: 10.1016/j.psj.2025.105715
PIK3C3
Xingyu Tao, Yanan Wang, Jiangbo Jin +10 more · 2025 · Journal of advanced research · Elsevier · added 2026-04-24
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) poses a substantial global threat. SARS-CoV-2 nonstructural proteins (NSPs) are essential for impeding the host replication mechanism while Show more
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) poses a substantial global threat. SARS-CoV-2 nonstructural proteins (NSPs) are essential for impeding the host replication mechanism while also assisting in the production and organization of new viral components. However, NSPs are not incorporated into viral particles, and their subsequent fate within host cells remains poorly understood. Additionally, their role in viral pathogenesis requires further investigation. This study aimed to discover the ultimate fate of NSP6 in host cells and to elucidate its role in viral pathogenesis. We investigated the effects of NSP6 on cell death and explored the underlying mechanism; moreover, we examined the degradation mechanism of NSP6 in human cells, along with analysing its correlation with coronavirus disease 2019 (COVID-19) severity in patient peripheral blood mononuclear cells (PBMCs). NSP6 was demonstrated to induce cell death. Specifically, NSP6 interacted with EI24 autophagy-associated transmembrane protein (EI24) to increase intracellular Ca This study reveals that KLHL22-mediated ubiquitination controls NSP6 stability and that NSP6 induces autophagic cell death via calcium overload, highlighting its cytotoxic role and suggesting therapeutic strategies that target calcium signaling or promote NSP6 degradation as potential interventions against COVID-19. Show less
no PDF DOI: 10.1016/j.jare.2025.05.031
PIK3C3
Songfen Wu, Haicai Zhuang, Xidan Zhou +1 more · 2025 · Frontiers in behavioral neuroscience · Frontiers · added 2026-04-24
NRBF2, a component of autophagy-associated PIK3C3/VPS34-containing phosphatidylinositol 3-kinase complex, plays a crucial role in learning and memory processes, yet its specific impact on memory and t Show more
NRBF2, a component of autophagy-associated PIK3C3/VPS34-containing phosphatidylinositol 3-kinase complex, plays a crucial role in learning and memory processes, yet its specific impact on memory and the underlying molecular mechanisms remains unclear. Here, we utilized NRBF2 knockout mice to examine its influence on the time course of fear memory. Employing quantitative PCR, Western blot analysis, behavioral tests, and electrophysiology, we investigated the mechanisms through which NRBF2 affects memory processing. We observed an increase in This study offer new insights into the role of NRBF2 and highlight the potential of targeting NRBF2 as a therapeutic strategy for addressing cognitive deficits associated with various disorders. Show less
no PDF DOI: 10.3389/fnbeh.2025.1529522
PIK3C3
Guoshuai Xu, Qinghong Zhang, Renjia Cheng +2 more · 2025 · Autophagy · Taylor & Francis · added 2026-04-24
Macropinocytosis is a nonselective form of endocytosis that allows cancer cells to largely take up the extracellular fluid and its contents, including nutrients, growth factors, etc. We first elaborat Show more
Macropinocytosis is a nonselective form of endocytosis that allows cancer cells to largely take up the extracellular fluid and its contents, including nutrients, growth factors, etc. We first elaborate meticulously on the process of macropinocytosis. Only by thoroughly understanding this entire process can we devise targeted strategies against it. We then focus on the central role of the MTOR (mechanistic target of rapamycin kinase) complex 1 (MTORC1) in regulating macropinocytosis, highlighting its significance as a key signaling hub where various pathways converge to control nutrient uptake and metabolic processes. The article covers a comprehensive analysis of the literature on the molecular mechanisms governing macropinocytosis, including the initiation, maturation, and recycling of macropinosomes, with an emphasis on how these processes are hijacked by cancer cells to sustain their growth. Key discussions include the potential therapeutic strategies targeting macropinocytosis, such as enhancing drug delivery via this pathway, inhibiting macropinocytosis to starve cancer cells, blocking the degradation and recycling of macropinosomes, and inducing methuosis - a form of cell death triggered by excessive macropinocytosis. Targeting macropinocytosis represents a novel and innovative approach that could significantly advance the treatment of cancers that rely on this pathway for survival. Through continuous research and innovation, we look forward to developing more effective and safer anti-cancer therapies that will bring new hope to patients. Show less
no PDF DOI: 10.1080/15548627.2025.2452149
PIK3C3
Yunhang Zhang, Na Zhang, Yue Zhang +11 more · 2025 · Journal of virology · added 2026-04-24
Swine enteric coronaviruses pose a significant challenge to the global pig industry, inflicting severe diarrhea and high mortality rates among piglets, and resulting in substantial economic losses. In Show more
Swine enteric coronaviruses pose a significant challenge to the global pig industry, inflicting severe diarrhea and high mortality rates among piglets, and resulting in substantial economic losses. In our clinical practice, we observed that the addition of potassium molybdate (PM) to the feed could dramatically reduce diarrhea and diarrhea-related mortality in piglets. However, the underlying mechanisms remain elusive and merit further investigation. In this study, we revealed that PM effectively inhibited the infection of both aminopeptidase N (APN)-dependent coronaviruses, transmissible gastroenteritis virus (TGEV), and porcine respiratory coronavirus (PRCV), both Show less
no PDF DOI: 10.1128/jvi.01449-24
PIK3C3
Tzu-Lin Lee, Wen-Chi Shen, Ya-Chun Chen +9 more · 2025 · Autophagy · Taylor & Francis · added 2026-04-24
Epidemiology has shown a strong relationship between fine particulate matter (PM) exposure and cardiovascular disease. However, it remains unknown whether PM aggravates myocardial ischemia-reperfusion Show more
Epidemiology has shown a strong relationship between fine particulate matter (PM) exposure and cardiovascular disease. However, it remains unknown whether PM aggravates myocardial ischemia-reperfusion (I/R) injury, and the related mechanisms are unclear. Our previous study has shown that adipose stem cell-derived exosomes (ADSC-Exos) contain high levels of Show less
no PDF DOI: 10.1080/15548627.2024.2395799
PIK3C3
Xinruo Zhang, Jennifer A Brody, Mariaelisa Graff +122 more · 2025 · Nature communications · Nature · added 2026-04-24
Xinruo Zhang, Jennifer A Brody, Mariaelisa Graff, Heather M Highland, Nathalie Chami, Hanfei Xu, Zhe Wang, Kendra R Ferrier, Geetha Chittoor, Navya Shilpa Josyula, Mariah Meyer, Shreyash Gupta, Xihao Li, Zilin Li, Matthew A Allison, Diane M Becker, Lawrence F Bielak, Joshua C Bis, Meher Preethi Boorgula, Donald W Bowden, Jai G Broome, Erin J Buth, Christopher S Carlson, Kyong-Mi Chang, Sameer Chavan, Yen-Feng Chiu, Lee-Ming Chuang, Matthew P Conomos, Dawn L DeMeo, Mengmeng Du, Ravindranath Duggirala, Celeste Eng, Alison E Fohner, Barry I Freedman, Melanie E Garrett, Xiuqing Guo, Chris Haiman, Benjamin D Heavner, Bertha Hidalgo, James E Hixson, Yuk-Lam Ho, Brian D Hobbs, Donglei Hu, Qin Hui, Chii-Min Hwu, Rebecca D Jackson, Deepti Jain, Rita R Kalyani, Sharon L R Kardia, Tanika N Kelly, Ethan M Lange, Michael LeNoir, Changwei Li, Loic Le Marchand, Merry-Lynn N McDonald, Caitlin P McHugh, Alanna C Morrison, Take Naseri, NHLBI Trans-Omics for Precision Medicine (TOPMed) Consortium, Jeffrey O'Connell, Christopher J O'Donnell, Nicholette D Palmer, James S Pankow, James A Perry, Ulrike Peters, Michael H Preuss, D C Rao, Elizabeth A Regan, Sefuiva M Reupena, Dan M Roden, Jose Rodriguez-Santana, Colleen M Sitlani, Jennifer A Smith, Hemant K Tiwari, Ramachandran S Vasan, Zeyuan Wang, Daniel E Weeks, Jennifer Wessel, Kerri L Wiggins, Lynne R Wilkens, Peter W F Wilson, Lisa R Yanek, Zachary T Yoneda, Wei Zhao, Sebastian Zöllner, Donna K Arnett, Allison E Ashley-Koch, Kathleen C Barnes, John Blangero, Eric Boerwinkle, Esteban G Burchard, April P Carson, Daniel I Chasman, Yii-der Ida Chen, Joanne E Curran, Myriam Fornage, Victor R Gordeuk, Jiang He, Susan R Heckbert, Lifang Hou, Marguerite R Irvin, Charles Kooperberg, Ryan L Minster, Braxton D Mitchell, Mehdi Nouraie, Bruce M Psaty, Laura M Raffield, Alexander P Reiner, Stephen S Rich, Jerome I Rotter, M Benjamin Shoemaker, Nicholas L Smith, Kent D Taylor, Marilyn J Telen, Scott T Weiss, Yingze Zhang, Nancy Heard-Costa, Yan V Sun, Xihong Lin, L Adrienne Cupples, Leslie A Lange, Ching-Ti Liu, Ruth J F Loos, Kari E North, Anne E Justice Show less
Obesity is a major public health crisis associated with high mortality rates. Previous genome-wide association studies (GWAS) investigating body mass index (BMI) have largely relied on imputed data fr Show more
Obesity is a major public health crisis associated with high mortality rates. Previous genome-wide association studies (GWAS) investigating body mass index (BMI) have largely relied on imputed data from European individuals. This study leveraged whole-genome sequencing (WGS) data from 88,873 participants from the Trans-Omics for Precision Medicine (TOPMed) Program, of which 51% were of non-European population groups. We discovered 18 BMI-associated signals (P < 5 × 10 Show less
no PDF DOI: 10.1038/s41467-025-58420-2
POC5