👤 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, 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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 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articles
Yining Liu, Mu Yang, Lin Fan +6 more · 2024 · International journal of biological macromolecules · Elsevier · added 2026-04-24
The β-catenin has two intrinsically disordered regions in both C- and N-terminal domains that trigger the formation of phase-separated condensates. Variants in its C-terminus are associated with famil Show more
The β-catenin has two intrinsically disordered regions in both C- and N-terminal domains that trigger the formation of phase-separated condensates. Variants in its C-terminus are associated with familial exudative vitreoretinopathy (FEVR), yet the pathogenesis and the role of these variants in inducing abnormal condensates, are unclear. In this study, we identified a novel heterozygous frameshift variant, c.2104-2105insCC (p.Gln703ProfsTer33), in CTNNB1 from a FEVR-affected family. This variant encodes an unstable truncated protein that was unable to activate Wnt signal transduction, which could be rescued by the inhibition of proteasome or phosphorylation. Further functional experiments revealed the propensity of the Gln703ProfsTer33 variant to form cytoplasmic condensates, exhibiting a lower turnover rate after fluorescent bleaching due to enhanced interaction with AXIN1. LiCl, which specifically blocks GSK3β-mediated phosphorylation, restored signal transduction, cell proliferation, and junctional integrity in primary human retinal microvascular endothelial cells over-expressed with Gln703ProfsTer33. Finally, experiments on two reported FEVR-associated mutations in the C-terminal domain of β-catenin exhibited several functional defects similar to the Gln703ProfsTer33. Together, our findings unravel that the C-terminal region of β-catenin is pivotal for the regulation of AXIN1/β-catenin interaction, acting as a switch to mediate nucleic and cytosolic condensates formation that is implicated in the pathogenesis of FEVR. Show less
no PDF DOI: 10.1016/j.ijbiomac.2023.128570
AXIN1
Xixi Li, Yuka Ichiba, Takuya Watanabe +8 more · 2024 · NPJ science of food · Nature · added 2026-04-24
In a series of studies on blood-brain barrier transportable peptides, a soybean dipeptide, Tyr-Pro, penetrated the mouse brain parenchyma after oral intake and improved short and long memory impairmen Show more
In a series of studies on blood-brain barrier transportable peptides, a soybean dipeptide, Tyr-Pro, penetrated the mouse brain parenchyma after oral intake and improved short and long memory impairment in acute Alzheimer's model mice. Here, we aimed to clarify the anti-dementia effects of this peptide administered to SAMP8 mice prior to dementia onset. At the end of the 25-week protocol in 16-week-old SAMP8 mice, Tyr-Pro (10 mg/kg/day) significantly improved the reduced spatial learning ability compared with that in the control and amino acid (Tyr + Pro) groups as indicated by the results of Morris water maze tests conducted for five consecutive days. The hippocampus and cortex regions of SAMP8 harvested after the test showed lower amyloid ß (Aß) accumulation in the Tyr-Pro group than those in the control and amino acid groups. Consistent with the lower level of Aß, decreased expression of ß-secretase (BACE1) and markedly increased expression (4-times higher) of insulin degrading enzyme (IDE) were obtained compared to those in the control group. Collectively, we demonstrated that long-term daily intake of the dipeptide Tyr-Pro in SAMP8 mice may be sufficient for maintaining cognitive ability by preventing excess Aß accumulation through downregulated BACE1 and particularly upregulated IDE. Show less
📄 PDF DOI: 10.1038/s41538-024-00360-0
BACE1
Miao Zheng, Can Wang, Min HU +5 more · 2024 · Metabolic brain disease · Springer · added 2026-04-24
Type 2 diabetes mellitus (T2DM) is a metabolic disorder that is characterized by insulin resistance and hyperglycemia. It is also known to be a risk factor for Alzheimer's disease (AD). Insulin plays Show more
Type 2 diabetes mellitus (T2DM) is a metabolic disorder that is characterized by insulin resistance and hyperglycemia. It is also known to be a risk factor for Alzheimer's disease (AD). Insulin plays a crucial role in regulating the body's metabolism and is responsible for activating the Phosphoinotide-3-Kinase (PI3K)/Protein Kinase B (Akt) signaling pathway. This pathway is activated when insulin binds to the insulin receptor on nerve cells, and it helps regulate the metabolism of glucose and lipids. Dysfunction in the insulin signaling pathway can lead to a decrease in brain insulin levels and insulin sensitivity, thereby inducing disruptions in insulin signal transduction and leading to disorders in brain energy metabolism. Moreover, these dysfunctions also contribute to the accumulation of β-amyloid (Aβ) deposition and the hyperphosphorylation of Tau protein, both of which are characteristic features of AD. Therefore, this article focuses on insulin resistance to reveal the complex mechanism between brain insulin resistance and AD occurrence in T2DM. On this basis, this article further summarizes the biological effects and mechanisms of antidiabetic drugs on the two diseases, aiming to provide new ideas for the discovery of drugs for the treatment of T2DM combined with AD. Show less
📄 PDF DOI: 10.1007/s11011-024-01472-y
BACE1
Yulian Zou, Chengyan Wang, Huang Li +5 more · 2024 · Frontiers in pharmacology · Frontiers · added 2026-04-24
Clinical studies have shown that epileptic seizures worsen Alzheimer's disease (AD) pathology and related cognitive deficits; however, the underlying mechanism is unclear. To assess the effects of sei Show more
Clinical studies have shown that epileptic seizures worsen Alzheimer's disease (AD) pathology and related cognitive deficits; however, the underlying mechanism is unclear. To assess the effects of seizures on the progression of AD, chronic temporal lobe epilepsy was induced in five familial AD mutation (5×FAD) mice by kindling with the chemoconvulsant pentylenetetrazole (PTZ) at 3-3.5 months of age. The amyloidogenic pathway, tauopathy, synaptic damage, neuronal death, neurological inflammatory response and associated kinase signaling pathway dysregulation were examined at 9 months of age. We found that APP, p-APP, BACE1, Aβ and kinase-associated p-tau levels were elevated after PTZ kindling in 5×FAD mice. In addition, PTZ kindling exacerbated hippocampal synaptic damage and neuronal cell death, as determined by scanning electron microscopy and terminal deoxynucleotidyl transferase-mediated deoxyuridine triphosphate nick-end labeling (TUNEL) staining, respectively. Finally, the levels of the neuroinflammation markers GFAP and Iba1, as well as the inflammatory cytokine IL-1β, were increased after PTZ insult. PTZ kindling profoundly exacerbated extracellular regulated kinase (ERK)-death-associated protein kinase (DAPK) signaling pathway overactivation, and acute ERK inhibitor treatment downregulated Aβ production and p-APP and p-tau levels in epileptic 5×FAD mice. In addition, long-term use of the antiseizure drug carbamazepine (CBZ) alleviated seizure-induced accelerated amyloid and tau pathology and ERK-DAPK overactivation in 5×FAD mice. Collectively, these results demonstrate that seizure-induced increases in AD-like neuropathology in 5×FAD mice are partially regulated by the ERK-DAPK pathway, suggesting that the ERK-DAPK axis could be a new therapeutic target for the treatment of AD patients with comorbid seizures. Show less
📄 PDF DOI: 10.3389/fphar.2024.1500105
BACE1

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J Zeng, L Hua, Y Yang +3 more · 2024 · Nan fang yi ke da xue xue bao = Journal of Southern Medical University · added 2026-04-24
To explore the mechanism by which Three-month-old male APP/PS1 transgenic mice and wild-type C57BL/6 mice were both randomized into control group, model group, donepezil (1.67 mg/kg) group, and YGS (7 Show more
To explore the mechanism by which Three-month-old male APP/PS1 transgenic mice and wild-type C57BL/6 mice were both randomized into control group, model group, donepezil (1.67 mg/kg) group, and YGS (7.5 g/kg) group and received the corresponding treatments Compared with the control mice, APP/PS1 mice showed significant impairment of learning and memory abilities, increased degeneration or necrosis of hippocampal and cortical neurons, pathological scores, Aβ-positive plaques, elevated Aβ YGS improves learning and memory changes in APP/PS1 mice by ameliorating neuronal damage and Aβ pathology in the brain and regulating brain fluid metabolism. Show less
no PDF DOI: 10.12122/j.issn.1673-4254.2024.10.20
BACE1
Hongxin Xiang, Li Zeng, Linlin Hou +8 more · 2024 · Nature communications · Nature · added 2026-04-24
Accurate molecular representation of compounds is a fundamental challenge for prediction of drug targets and molecular properties. In this study, we present a molecular video-based foundation model, n Show more
Accurate molecular representation of compounds is a fundamental challenge for prediction of drug targets and molecular properties. In this study, we present a molecular video-based foundation model, named VideoMol, pretrained on 120 million frames of 2 million unlabeled drug-like and bioactive molecules. VideoMol renders each molecule as a video with 60-frame and designs three self-supervised learning strategies on molecular videos to capture molecular representation. We show high performance of VideoMol in predicting molecular targets and properties across 43 drug discovery benchmark datasets. VideoMol achieves high accuracy in identifying antiviral molecules against common diverse disease-specific drug targets (i.e., BACE1 and EP4). Drugs screened by VideoMol show better binding affinity than molecular docking, revealing the effectiveness in understanding the three-dimensional structure of molecules. We further illustrate interpretability of VideoMol using key chemical substructures. Show less
📄 PDF DOI: 10.1038/s41467-024-53742-z
BACE1
Ye-Ran Wang, Xiao-Qin Zeng, Jun Wang +10 more · 2024 · Acta neuropathologica · Springer · added 2026-04-24
The profile of autoantibodies is dysregulated in patients with Alzheimer's disease (AD). Autoantibodies to beta-site amyloid precursor protein (APP)-cleaving enzyme 1 (BACE1) are present in human bloo Show more
The profile of autoantibodies is dysregulated in patients with Alzheimer's disease (AD). Autoantibodies to beta-site amyloid precursor protein (APP)-cleaving enzyme 1 (BACE1) are present in human blood. This study aims to investigate the clinical relevance and pathophysiological roles of autoantibodies to BACE1 in AD. Clinical investigations were conducted in two independent cohorts, the Chongqing cohort, and the Australian Imaging, Biomarkers, and Lifestyle (AIBL) cohort. The Chongqing cohort included 55 AD patients, 28 patients with non-AD dementia, and 70 cognitively normal subjects (CN). The AIBL cohort included 162 Aβ-PET Show less
📄 PDF DOI: 10.1007/s00401-024-02814-x
BACE1
Xingyi Zhao, Qiaoguan Hu, Xiaoqian Wang +11 more · 2024 · European journal of medicinal chemistry · Elsevier · added 2026-04-24
Alzheimer's disease (AD) is the most common form of dementia among the elderly, accounting for 60 %-70 % of cases. At present, the pathogenesis of this condition remains unclear, but the hydrolysis of Show more
Alzheimer's disease (AD) is the most common form of dementia among the elderly, accounting for 60 %-70 % of cases. At present, the pathogenesis of this condition remains unclear, but the hydrolysis of acetylcholine (ACh) is thought to play a role. Acetylcholinesterase (AChE) can break down ACh transmission from the presynaptic membrane and stop neurotransmitters' excitatory effect on the postsynaptic membrane, which plays a key role in nerve conduction. Acetylcholinesterase inhibitors (AChEIs) can delay the hydrolysis of acetylcholine (ACh), which represents a key strategy for treating AD. Due to its complex etiology, AD has proven challenging to treat. Various inhibitors and antagonists targeting key enzymes and proteins implicated in the disease's pathogenesis have been explored as potential therapeutic agents. These include Glycogen Synthase Kinase 3β (GSK-3β) inhibitors, β-site APP Cleaving Enzyme (BACE-1) inhibitors, Monoamine Oxidase (MAO) inhibitors, Phosphodiesterase inhibitors (PDEs), N-methyl--aspartic Acid (NMDA) antagonists, Histamine 3 receptor antagonists (H3R), Serotonin receptor subtype 4 (5-HT4R) antagonists, Sigma1 receptor antagonists (S1R) and soluble Epoxide Hydrolase (sEH) inhibitors. The drug development strategy of multi-target-directed ligands (MTDLs) offers unique advantages in the treatment of complex diseases. On the one hand, it can synergistically enhance the therapeutic efficacy of single-target drugs. On the other hand, it can also reduce the side effects. In this review, we discuss the design strategy of dual inhibitors based on acetylcholinesterase and the structure-activity relationship of these drugs. Show less
no PDF DOI: 10.1016/j.ejmech.2024.116810
BACE1
Xinhua Zhou, Zeyu Zhu, Shaoming Kuang +8 more · 2024 · Pharmaceuticals (Basel, Switzerland) · MDPI · added 2026-04-24
Alzheimer's disease (AD) is a neurodegenerative disorder associated with age. A wealth of evidence indicates that the amyloid β (Aβ) aggregates result from dyshomeostasis between Aβ production and cle Show more
Alzheimer's disease (AD) is a neurodegenerative disorder associated with age. A wealth of evidence indicates that the amyloid β (Aβ) aggregates result from dyshomeostasis between Aβ production and clearance, which plays a pivotal role in the pathogenesis of AD. Consequently, therapies targeting Aβ reduction represent a promising strategy for AD intervention. Tetramethylpyrazine nitrone (TBN) is a novel tetramethylpyrazine derivative with potential for the treatment of AD. Previously, we demonstrated that TBN markedly enhanced cognitive functions and decreased the levels of Aβ, APP, BACE 1, and hyperphosphorylated tau in 3×Tg-AD mice. However, the mechanism by which TBN inhibits Aβ deposition is still unclear. In this study, we employed APP/PS1 mice treated with TBN (60 mg/kg, ig, bid) for six months, and N2a/APP695swe cells treated with TBN (300 μM) to explore the mechanism of TBN in Aβ reduction. Our results indicate that TBN significantly alleviated cognitive impairment and reduced Aβ deposition in APP/PS1 mice. Further investigation of the underlying mechanisms revealed that TBN decreased the expression of APP and BACE1, activated the AMPK/mTOR/ULK1 autophagy pathway, inhibited the PI3K/AKT/mTOR/ULK1 autophagy pathway, and decreased the phosphorylation levels of JNK and ERK in APP/PS1 mice. Moreover, TBN was found to significantly reduce the mRNA levels of APP and BACE1, as well as those of SP1, CTCF, TGF-β, and NF-κB, transcription factors involved in regulating gene expression. Additionally, TBN was observed to decrease the level of Show less
📄 PDF DOI: 10.3390/ph17081005
BACE1
Xiaorui Ai, Zeyu Cao, Zhaoru Ma +5 more · 2024 · International journal of molecular sciences · MDPI · added 2026-04-24
With the rapid progress in deciphering the pathogenesis of Alzheimer's disease (AD), it has been widely accepted that the accumulation of misfolded amyloid β (Aβ) in the brain could cause the neurodeg Show more
With the rapid progress in deciphering the pathogenesis of Alzheimer's disease (AD), it has been widely accepted that the accumulation of misfolded amyloid β (Aβ) in the brain could cause the neurodegeneration in AD. Although much evidence demonstrates the neurotoxicity of Aβ, the role of Aβ in the nervous system are complex. However, more comprehensive studies are needed to understand the physiological effect of Aβ Show less
📄 PDF DOI: 10.3390/ijms25158336
BACE1
Cui-Cui Ge, Xin-Yu Li, Wen-Hao Qiao +9 more · 2024 · Fitoterapia · Elsevier · added 2026-04-24
The fruits of Alpinia oxyphylla (Alpiniae Oxyphyllae Fructus, AOF) are one of the "Four Famous South Medicines" in China. In this study, beta-site amyloid protein precursor cleaving enzyme 1 (BACE1) w Show more
The fruits of Alpinia oxyphylla (Alpiniae Oxyphyllae Fructus, AOF) are one of the "Four Famous South Medicines" in China. In this study, beta-site amyloid protein precursor cleaving enzyme 1 (BACE1) was applied to explore the active components in AOF responsible for type 2 diabetes mellitus (T2DM)-related cognitive disorder. As a result, 24 compounds including three unreported ones (1, 3, 4) were isolated from AOF. Compound 1 is an unusual carbon‑carbon linked diarylheptanoid dimer, and compound 4 is the first case of 3,4-seco-eudesmane sesquiterpenoid with a 5/6-bicyclic skeleton. Four diarylheptanoids (3, 5-7), one flavonoid (9) and two sesquiterpenoids (14 and 20) showed BACE1 inhibitory activity, of which the most active 6 was revealed to be a non-competitive and anti-competitive mixed inhibitor. Docking simulation suggested that OH-4' of 6 played important roles in maintaining activity by forming hydrogen bonds with Ser36 and Ile126 residues. Compounds 3, 5, 9 and 20 displayed neuroprotective effects against amyloid β (Aβ)-induced damage in BV2 cells. Mechanism study revealed that compounds 5 and 20 downregulated the expression of BACE1 and upregulated the expression of Lamp2 to exert effects. Thus, the characteristic diarylheptanoids and sesquiterpenoids in AOF had the efficacy to alleviate T2DM-related cognitive disorder by inhibiting BACE1 activity and reversing Aβ-induced neuronal damage. Show less
no PDF DOI: 10.1016/j.fitote.2024.106157
BACE1
Yalan Pu, Jie Yang, Qiuling Pan +6 more · 2024 · The Journal of biological chemistry · Elsevier · added 2026-04-24
Microsomal glutathione transferase 3 (MGST3) regulates eicosanoid and glutathione metabolism. These processes are associated with oxidative stress and apoptosis, suggesting that MGST3 might play a rol Show more
Microsomal glutathione transferase 3 (MGST3) regulates eicosanoid and glutathione metabolism. These processes are associated with oxidative stress and apoptosis, suggesting that MGST3 might play a role in the pathophysiology of Alzheimer's disease. Here, we report that knockdown (KD) of MGST3 in cell lines reduced the protein level of beta-site amyloid precursor protein cleaving enzyme 1 (BACE1) and the resulting amyloidogenesis. Interestingly, MGST3 KD did not alter intracellular reactive oxygen species level but selectively reduced the expression of apoptosis indicators which could be associated with the receptor of cysteinyl leukotrienes, the downstream metabolites of MGST3 in arachidonic acid pathway. We then showed that the effect of MGST3 on BACE1 was independent of cysteinyl leukotrienes but involved a translational mechanism. Further RNA-seq analysis identified that regulator of G-protein signaling 4 (RGS4) was a target gene of MGST3. Silencing of RGS4 inhibited BACE1 translation and prevented MGST3 KD-mediated reduction of BACE1. The potential mechanism was related to AKT activity, as the protein level of phosphorylated AKT was significantly reduced by silencing of MGST3 and RGS4, and the AKT inhibitor abolished the effect of MGST3/RGS4 on phosphorylated AKT and BACE1. Together, MGST3 regulated amyloidogenesis by controlling BACE1 protein expression, which was mediated by RGS4 and downstream AKT signaling pathway. Show less
📄 PDF DOI: 10.1016/j.jbc.2024.107530
BACE1
Lin-Jie Tan, Wen-Ju Lei, Mi-Min Liu +4 more · 2024 · Bioorganic chemistry · Elsevier · added 2026-04-24
Developing multitargeted ligands as promising therapeutics for Alzheimer's disease (AD) has been considered important. Herein, a novel class of cinnamamide/ester-triazole hybrids with multifaceted eff Show more
Developing multitargeted ligands as promising therapeutics for Alzheimer's disease (AD) has been considered important. Herein, a novel class of cinnamamide/ester-triazole hybrids with multifaceted effects on AD was developed based on the multitarget-directed ligands strategy. Thirty-seven cinnamamide/ester-triazole hybrids were synthesized, with most exhibiting significant inhibitory activity against Aβ-induced toxicity at a single concentration in vitro. The most optimal hybrid compound 4j inhibited copper-induced Aβ toxicity in AD cells. its action was superior to that of donepezil and memantine. It also moderately inhibited intracellular AChE activity and presented favorable bioavailability and blood-brain barrier penetration with low toxicity in vivo. Of note, it ameliorated cognitive impairment, neuronal degeneration, and Aβ deposition in Aβ Show less
no PDF DOI: 10.1016/j.bioorg.2024.107584
BACE1
Sirinapa Thangsiri, Uthaiwan Suttisansanee, Pankaj Koirala +4 more · 2024 · Saudi journal of biological sciences · Elsevier · added 2026-04-24
Plant phenolics have been known for various biological activities. This study aims to extract and examine the presence of phenolics in Bao mango (Mangifera indica L. var.) peel ethanolic extract (MPE) Show more
Plant phenolics have been known for various biological activities. This study aims to extract and examine the presence of phenolics in Bao mango (Mangifera indica L. var.) peel ethanolic extract (MPE). Further, antioxidant, anti-diabetic (α-amylase, and α-glucosidase inhibitory activity), and anti- Alzheimer's disease (AD) (acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and β-secretase (BACE-1) inhibitory activity) efficacy of MPE were determined. The results indicated that mangiferin (8755.89 mg/ 100 g extract) was the major phenolic compound in MPE. An antioxidant mechanism revealed that MPE had a higher radical scavenging ability (4266.70 µmol TE/g extract) compared to reducing power (FRAP) or oxygen radical absorption capacity (ORAC). Further Show less
📄 PDF DOI: 10.1016/j.sjbs.2024.104033
BACE1
Mengyun Qiao, Haitao Yang, Li Liu +9 more · 2024 · Toxics · MDPI · added 2026-04-24
Long-term exposure to lead (Pb) can result in chronic damage to the body through accumulation in the central nervous system (CNS) leading to neurodegenerative diseases, such as Alzheimer's disease (AD Show more
Long-term exposure to lead (Pb) can result in chronic damage to the body through accumulation in the central nervous system (CNS) leading to neurodegenerative diseases, such as Alzheimer's disease (AD). This study delves into the intricate role of miR-671/CDR1as regulation in the etiology of AD-like lesions triggered by chronic Pb exposure in adult mice. To emulate the chronic effects of Pb, we established a rodent model spanning 10 months of controlled Pb administration, dividing 52 C57BL/6J mice into groups receiving varying concentrations of Pb (1, 2, or 4 g/L) alongside an unexposed control. Blood Pb levels were monitored using serum samples to ensure accurate dosing and to correlate with observed toxicological outcomes. Utilizing the Morris water maze, a robust behavioral assay for assessing cognitive functions, we documented a dose-dependent decline in learning and memory capabilities among the Pb-exposed mice. Histopathological examination of the hippocampal tissue revealed tell-tale signs of AD-like neurodegeneration, characterized by the accumulation of amyloid plaques and neurofibrillary tangles. At the molecular level, a significant upregulation of AD-associated genes, namely amyloid precursor protein (APP), β-secretase 1 (BACE1), and tau, was observed in the hippocampal tissue of Pb-exposed mice. This was accompanied by a corresponding surge in the protein levels of APP, BACE1, amyloid-β (Aβ), and phosphorylated tau (p-tau), further implicating Pb in the dysregulation of these key AD markers. The expression of CDR1as, a long non-coding RNA implicated in AD pathogenesis, was found to be suppressed in Pb-exposed mice. This observation suggests a potential mechanistic link between Pb-induced neurotoxicity and the dysregulation of the CDR1as/miR-671 axis, which warrants further investigation. Moreover, our study identified a dose-dependent alteration in the intracellular and extracellular levels of the transcription factor nuclear factor-kappa B (NF-κB). This finding implicates Pb in the modulation of NF-κB signaling, a pathway that plays a pivotal role in neuroinflammation and neurodegeneration. In conclusion, our findings underscored the deleterious effects of Pb exposure on the CNS, leading to the development of AD-like pathology. The observed modulation of NF-κB signaling and miR-671/CDR1as regulation provides a plausible mechanistic framework for understanding the neurotoxic effects of Pb and its potential contribution to AD pathogenesis. Show less
📄 PDF DOI: 10.3390/toxics12060410
BACE1
Xin Zhang, Wen Ma, Huanyi Liu +6 more · 2024 · Journal of neuropathology and experimental neurology · Oxford University Press · added 2026-04-24
The common neurodegenerative disorder Alzheimer disease (AD) is characterized by memory dysfunction and cognitive decline in the elderly. Neuropathological features include aggregated β-amyloid (Aβ) a Show more
The common neurodegenerative disorder Alzheimer disease (AD) is characterized by memory dysfunction and cognitive decline in the elderly. Neuropathological features include aggregated β-amyloid (Aβ) accumulation, neuroinflammation, and oxidative stress in the brain. Daphnetin (DAPH), a natural coumarin derivative, has the potential for inhibiting inflammatory and oxidative responses. We explored neuroprotective roles of DAPH treatment in the APP/PS1 transgenic mouse AD model. DAPH ameliorated spatial learning disabilities in Morris water maze tests and reduced Aβ deposition, assessed by immunohistochemistry. It also reduced the Aβ content in supernatants of neurons from fetal APP/PS1 mice, assessed by cell-based soluble ELISA. Molecular docking and fluorescence resonance energy transfer-based assay results suggested that DAPH could directly inhibit BACE1 activity. Furthermore, in vitro experiments utilizing isolated rat neurons assessing RNA expression profiling, immunofluorescence, TUNEL assay, and Western-blot analysis, suggested the potential of DAPH for regulating BDNF and GM-CSF expression and mitigating Aβ1-42-induced cortical injury, synaptic loss, and apoptosis. HO-1 and Nrf2 mRNA and protein expression were also increased in a dose-dependent manner. These results underscore the potential of DAPH as a neuroprotective agent in reversing memory deficits associated with AD and bolster its candidacy as a multitarget natural small-molecule drug for AD patients. Show less
no PDF DOI: 10.1093/jnen/nlae043
BACE1
Qifeng Shi, Xiangyu Sun, Hui Zhang +6 more · 2024 · International immunopharmacology · Elsevier · added 2026-04-24
Alzheimer's disease (AD) is a progressive neurodegenerative disease. Neuronal calcium overload plays an important role in Aβ deposition and neuroinflammation, which are strongly associated with AD. Ho Show more
Alzheimer's disease (AD) is a progressive neurodegenerative disease. Neuronal calcium overload plays an important role in Aβ deposition and neuroinflammation, which are strongly associated with AD. However, the specific mechanisms by which calcium overload contributes to neuroinflammation and AD and the relationship between them have not been elucidated. Phospholipase C (PLC) is involved in regulation of calcium homeostasis, and CN-NFAT1 signaling is dependent on intracellular Ca Show less
no PDF DOI: 10.1016/j.intimp.2024.112259
BACE1
Chen-Lu Li, Gui-Feng Zhou, Xiao-Yong Xie +7 more · 2024 · Experimental neurology · Elsevier · added 2026-04-24
Staufen-1 (STAU1) is a double-stranded RNA-binding protein (RBP) involved in a variety of pathological conditions. In this study, we investigated the potential role of STAU1 in Alzheimer's disease (AD Show more
Staufen-1 (STAU1) is a double-stranded RNA-binding protein (RBP) involved in a variety of pathological conditions. In this study, we investigated the potential role of STAU1 in Alzheimer's disease (AD), in which two hallmarks are well-established as cerebral β-amyloid protein (Aβ) deposition and Tau-centered neurofibrillary tangles. We found that STAU1 protein level was significantly increased in cells that stably express full-length APP and the brain of APP/PS1 mice, an animal model of AD. STAU1 knockdown, as opposed to overexpression, significantly decreased the protein levels of β-amyloid converting enzyme 1 (BACE1) and Aβ. We further found that STAU1 extended the half-life of the BACE1 mRNA through binding to the 3' untranslated region (3'UTR). Transcriptome analysis revealed that STAU1 enhanced the expression of growth arrest and DNA damage 45 β (GADD45B) upstream of P38 MAPK signaling, which contributed to STAU1-induced regulation of Tau phosphorylation at Ser396 and Thr181. Together, STAU1 promoted amyloidogenesis by inhibiting BACE1 mRNA decay, and augmented Tau phosphorylation through activating GADD45B in relation to P38 MAPK. Targeting STAU1 that acts on both amyloidogenesis and tauopathy may serve as an optimistic approach for AD treatment. Show less
no PDF DOI: 10.1016/j.expneurol.2024.114805
BACE1
Chunbin Sun, Shanshan Dong, Weiwei Chen +3 more · 2024 · Phytomedicine : international journal of phytotherapy and phytopharmacology · Elsevier · added 2026-04-24
Alzheimer's disease (AD) is the most common neurodegenerative disease. Intestinal flora and its metabolism play a significant role in ameliorating central nervous system disorders, including AD, throu Show more
Alzheimer's disease (AD) is the most common neurodegenerative disease. Intestinal flora and its metabolism play a significant role in ameliorating central nervous system disorders, including AD, through bidirectional interactions between the gut-brain axis. A naturally occurring alkaloid compound called berberine (BBR) has neuroprotective properties and prevents Aβ-induced microglial activation. Additionally, BBR can suppress the synthesis of Aβ and decrease BACE1 expression. However, it is still unclear if BBR therapy can alleviate AD by changing the gut flora. In this study, we examined whether a partial alleviation of AD could be achieved with BBR treatment and the molecular mechanisms involved. We did this by analyzing alterations in Aβ plaques, neurons, and related neuroinflammation-related markers in the brain and the transcriptome of the mouse brain. The relationship between the intestinal flora of 5xFAD model mice and BBR treatment was investigated using high-throughput sequencing analysis of 16S rRNA from mouse feces. The findings demonstrated that treatment with BBR cleared Aβ plaques, alleviated neuroinflammation, and ameliorated spatial memory dysfunction in AD. BBR significantly alleviated intestinal inflammation, decreased intestinal permeability, and could improve intestinal microbiota composition in 5xFAD mice. Show less
no PDF DOI: 10.1016/j.phymed.2024.155624
BACE1
Peng Shu, Jiaxin Mo, Zunjiang Li +3 more · 2024 · Aging · Impact Journals · added 2026-04-24
Application of retinol (Vitamin A, VA) in skincare is limited for instability, poor water solubility, and skin intolerance that combats skin aging. We employed computer-aided virtual screening and cel Show more
Application of retinol (Vitamin A, VA) in skincare is limited for instability, poor water solubility, and skin intolerance that combats skin aging. We employed computer-aided virtual screening and cell experiments with transcriptomics, thereby unveiling the comprehensive gene expression and regulation pathway of photoaging HaCaT cell treated with ferulic acid (FA) in synergizing with VA. Through network pharmacology analysis, the combined use of VA and FA exhibited highly correlated cross-targets with skin aging acting on EGFR, PTPN1, ESR2, GSK3B, BACE1, PYGL, PTGS2 and APP. The indicators of oxidative stress, such as SOD, GSH, MDA, CAT and ROS in HaCaT cells after co-administration, were significantly improved from those in photoaging group ( Show less
📄 PDF DOI: 10.18632/aging.205749
BACE1
Shan He, Junhe Shi, Lina Ma +4 more · 2024 · Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · Elsevier · added 2026-04-24
Total ginsenosides (TG), the major active constituents of ginseng, have been proven to be beneficial in treatment of Alzheimer's disease (AD). However, the underlying mechanism of TG remains unclear. Show more
Total ginsenosides (TG), the major active constituents of ginseng, have been proven to be beneficial in treatment of Alzheimer's disease (AD). However, the underlying mechanism of TG remains unclear. APP/PS1 mice and N2a/APP695 cells were used as in vivo and in vitro model, respectively. Morris water maze (MWM) was used to investigate behavioral changes of mice; neuronal pathological changes were assessed by hematoxylin and eosin (H&E) and nissl staining; immunofluorescence staining was used to examine amyloid beta (Aβ) deposition; Western blotting and quantitative real-time polymerase chain reaction (qRT-PCR) were used to examine the expression of relative amyloidogenic genes and proteins. Moreover, the antagonist of PPARγ, GW9662, was used to determine whether the effects of TG on Aβ production were associated with PPARγ activity. TG treatment increased the spatial learning and memory abilities of APP/PS1 mice while decreasing the Aβ accumulation in the cortex and hippocampus. In N2a/APP695 cells, TG treatment attenuated the secretion of Aβ1-40 and Aβ1-42 acting as an PPARγ agonist by inhibiting the translocation of NF-κB p65. Additionally, TG treatment also decreased the expression of amyloidogenic pathway related gene BACE1, PS1 and PS2. TG treatment reduced the production of Aβ both in vivo and in vitro. Activating PPARγ might be a potential therapeutic target of TG in facilitating Aβ clearance and ameliorating cognitive deficiency in APP/PS1 mice. Show less
no PDF DOI: 10.1016/j.biopha.2024.116577
BACE1
Xiao-Yun Li, Gui-Feng Zhou, Xiong-Yong Xie +6 more · 2024 · Molecular biology reports · Springer · added 2026-04-24
Mitochondrial Ts translation elongation factor (TSFM) is an enzyme that catalyzes exchange of guanine nucleotides. By forming a complex with mitochondrial Tu translation elongation factor (TUFM), TSFM Show more
Mitochondrial Ts translation elongation factor (TSFM) is an enzyme that catalyzes exchange of guanine nucleotides. By forming a complex with mitochondrial Tu translation elongation factor (TUFM), TSFM participates in mitochondrial protein translation. We have previously reported that TUFM regulates translation of beta-site APP cleaving enzyme 1 (BACE1) via ROS (reactive oxygen species)-dependent mechanism, suggesting a potential role in amyloid precursor protein (APP) processing associated with Alzheimer's disease (AD), which led to the speculation that TSFM may regulate APP processing in a similar way to TUFM. Here, we report that in cultured cells, knockdown or overexpression TSFM did not change protein levels in BACE1 and APP. Besides, the levels of cytoplasmic ROS and mitochondrial superoxide, in addition to ATP level, cell viability and mitochondrial membrane potential were not significantly altered by TSFM knockdown in the short term. Further transcriptome analysis revealed that expression of majority of mitochondrial genes were not remarkably changed by TSFM silencing. The possibility of TSFM involved in cardiomyopathy and cancer development was uncovered using bioinformatics analysis. Collectively, short-term regulation of TSFM level in cultured cells does not cause a significant change in proteins involved in APP processing, levels in ROS and ATP associated with mitochondrial function. Whereas our study could contribute to comprehend certain clinical features of TSFM mutations, the roles of TSFM in cardiomyopathy and cancer development might deserve further investigation. Show less
📄 PDF DOI: 10.1007/s11033-024-09426-4
BACE1
Ying Li, Yanan Zhang, Qing Wang +8 more · 2024 · Neurological research · Taylor & Francis · added 2026-04-24
Previous studies have revealed that Propane-2-sulfonic acid octadec-9-enyl-amide(N15) exerts a protective role in the inflammatory response after ischemic stroke and in neuronal damage. However, littl Show more
Previous studies have revealed that Propane-2-sulfonic acid octadec-9-enyl-amide(N15) exerts a protective role in the inflammatory response after ischemic stroke and in neuronal damage. However, little is known about N15 in Alzheimer's disease (AD). The aim of this study was to investigate the effects of N15 on AD and explore the underlying molecular mechanism. AD mice model was established by lateral ventricular injection with Aβ N15 treatment significantly reduced neurocognitive dysfunction, which also significantly activated the expression of PPARα/γ at an optimal dose of 200 mg/kg. Administration of N15 alleviated the formation of Aβ amyloid in the hippocampus of AD mice, enhanced the BDNF mRNA expression, decreased the mRNA and protein levels of PS1 and BACE1, upregulated ADAM10 mRNA and protein levels. N15 exerts its neuroprotective effects through the activation of PPARα/γ and may be a potential drug for the treatment of AD. Show less
no PDF DOI: 10.1080/01616412.2024.2325313
BACE1
Ruonan Wang, Shijia Kang, Zirui Zhao +7 more · 2024 · International journal of molecular sciences · MDPI · added 2026-04-24
Alzheimer's disease (AD) is the most common progressive neurodegenerative disease. The accumulation of amyloid-beta (Aβ) plaques is a distinctive pathological feature of AD patients. The aims of this Show more
Alzheimer's disease (AD) is the most common progressive neurodegenerative disease. The accumulation of amyloid-beta (Aβ) plaques is a distinctive pathological feature of AD patients. The aims of this study were to evaluate the therapeutic effect of chicoric acid (CA) on AD models and to explore its underlying mechanisms. APPswe/Ind SH-SY5Y cells and 5xFAD mice were treated with CA. Soluble Aβ1-42 and Aβ plaque levels were analyzed by ELISA and immunohistochemistry, respectively. Transcriptome sequencing was used to compare the changes in hippocampal gene expression profiles among the 5xFAD mouse groups. The specific gene expression levels were quantified by qRT-PCR and Western blot analysis. It was found that CA treatment reduced the Aβ1-42 levels in the APPswe/Ind cells and 5xFAD mice. It also reduced the Aβ plaque levels as well as the APP and BACE1 levels. Transcriptome analysis showed that CA affected the synaptic-plasticity-related genes in the 5xFAD mice. The levels of L1CAM, PSD-95 and synaptophysin were increased in the APPswe/Ind SH-SY5Y cells and 5xFAD mice treated with CA, which could be inhibited by administering siRNA-L1CAM to the CA-treated APPswe/Ind SH-SY5Y cells. In summary, CA reduced Aβ levels and increased the expression levels of synaptic-function-related markers via L1CAM in AD models. Show less
📄 PDF DOI: 10.3390/ijms25063408
BACE1

M

Wen Li, Jie Yu, Yilian Yang +6 more · 2024 · Cardiovascular diagnosis and therapy · added 2026-04-24
Previous studies have confirmed that choline exerts anti-fibrotic effect in the heart by activating the M Proliferation of cardiac fibroblasts was induced by transforming growth factor (TGF)-β1 The ex Show more
Previous studies have confirmed that choline exerts anti-fibrotic effect in the heart by activating the M Proliferation of cardiac fibroblasts was induced by transforming growth factor (TGF)-β1 The expression of miR-29b decreased when treated with TGF-β1 (P=0.0389) and increased after choline stimulated (P=0.0001). Overexpression of miR-29b could reverse the high expression of collagen I (P<0.0001), α-SMA (P=0.0007), and CTGF (P=0.0038) induced by TGF-β1, whereas inhibition of miR-29b had a tendency to even further increase the expression of fibrosis markers. Meanwhile, inhibition of miR-29b could reverse the anti-fibrotic effect of choline, increasing the expression of collagen I (P=0.0040), α-SMA (P=0.0001), and CTGF (P=0.0185), and promoting the fibroblast proliferation and migration. Moreover, BACE1 protein level, increased after TGF-β1 treatment (P=0.0037) and reversed by overexpression of miR-29b (P=0.0493). Choline could reduce the increase of BACE1 induced by TGF-β1 (P=0.0264), and 4-diphenylacetoxy-N-methyl-piperidine methiodide (4-DAMP) increased the expression of BACE1 (P=0.0060). Furthermore, overexpression of BACE1 could reverse the protective effect of miR-29b in cardiac fibrosis, increasing the protein level of collagen I (P=0.0404). The results suggested that M Show less
📄 PDF DOI: 10.21037/cdt-23-309
BACE1
Q Li, Z Chen, Y Zhang +7 more · 2024 · Hong Kong medical journal = Xianggang yi xue za zhi · added 2026-04-24
The coronavirus disease 2019 (COVID-19) pandemic has caused extensive disruption of public health worldwide. There were reports of COVID-19 patients having multiple complications. This study investiga Show more
The coronavirus disease 2019 (COVID-19) pandemic has caused extensive disruption of public health worldwide. There were reports of COVID-19 patients having multiple complications. This study investigated COVID-19 from a genetic perspective. We conducted RNA sequencing (RNA-Seq) analysis of respiratory tract samples from 24 patients with COVID-19. Eight patients receiving mechanical ventilation or extracorporeal membrane oxygenation were regarded as severe cases; the remaining 16 patients were regarded as non-severe cases. After quality control, statistical analyses were performed by logistic regression and the Kolmogorov-Smirnov test to identify genes associated with disease severity. Six genes were associated with COVID-19 severity in both statistical tests, namely RNA sequencing analysis showed that severe acute respiratory syndrome coronavirus 2 infection is associated with the overexpression of genes involved in nervous system disorders. Show less
no PDF DOI: 10.12809/hkmj2210178
BACE1
Miaomiao Zhang, Wanyao Wang, Qun Ye +11 more · 2024 · Alzheimer's research & therapy · BioMed Central · added 2026-04-24
Alzheimer's disease (AD) is a degenerative neurological disorder. Recent studies have indicated that histone deacetylases (HDACs) are among the most prominent epigenetic therapy targets and that HDAC Show more
Alzheimer's disease (AD) is a degenerative neurological disorder. Recent studies have indicated that histone deacetylases (HDACs) are among the most prominent epigenetic therapy targets and that HDAC inhibitors have therapeutic effects on AD. Here, we identified sodium valproate (VPA), a pan-HDAC inhibitor, and WT161, a novel HDAC6 selective inhibitor, as potential therapeutic agents for AD. Underlying molecular mechanisms were investigated. A cellular model, N2a-APPswe, was established via lentiviral infection, and the APPswe/PSEN1dE9 transgenic mouse model was employed in the study. LC-MS/MS was applied to quantify the concentration of WT161 in the mouse brain. Western blotting, immunohistochemical staining, thioflavin-S staining and ELISA were applied to detect protein expression in cells, tissues, or serum. RNA interference was utilized to knockdown the expression of specific genes in cells. The cognitive function of mice was assessed via the nest-building test, novel object recognition test and Morris water maze test. Previous studies have focused mainly on the impact of HDAC inhibitors on histone deacetylase activity. Our study discovered that VPA and WT161 can downregulate the expression of multiple HDACs, such as HDAC1 and HDAC6, in both AD cell and mouse models. Moreover, they also affect the expression of APP and APP secretases (BACE1, PSEN1, ADAM10). RNA interference and subsequent vitamin C induction further confirmed that the expression of APP and APP secretases is indeed regulated by HDAC1 and HDAC6, with the JNK pathway being the intermediate link in this regulatory process. Through the above pathways, VPA and WT161 effectively reduced Aβ deposition in both AD cell and mouse models and significantly improved cognitive function in AD mice. In general, we have discovered that the HDAC6-JNK-APP secretases cascade is an important pathway for VPA and WT161 to exert their therapeutic effects on AD. Investigations into the safety and efficacy of VPA and WT161 were also conducted, providing essential preclinical evidence for assessing these two epigenetic drugs for the treatment of AD. Show less
📄 PDF DOI: 10.1186/s13195-024-01384-0
BACE1
Yongfang Zhang, Xinyi Xie, Boyu Chen +11 more · 2024 · Genes & diseases · Elsevier · added 2026-04-24
Identified as the pathogenic genes of Alzheimer's disease (AD),
📄 PDF DOI: 10.1016/j.gendis.2023.02.051
BACE1
Feiye Zhou, Chunxiang Sheng, Xiaoqin Ma +11 more · 2024 · Cell death & disease · Nature · added 2026-04-24
Elevated circulating branched-chain amino acids (BCAAs) are tightly linked to an increased risk in the development of type 2 diabetes mellitus. The rate limiting enzyme of BCAA catabolism branched-cha Show more
Elevated circulating branched-chain amino acids (BCAAs) are tightly linked to an increased risk in the development of type 2 diabetes mellitus. The rate limiting enzyme of BCAA catabolism branched-chain α-ketoacid dehydrogenase (BCKDH) is phosphorylated at E1α subunit (BCKDHA) by its kinase (BCKDK) and inactivated. Here, the liver-specific BCKDK or BCKDHA knockout mice displayed normal glucose tolerance and insulin sensitivity. However, knockout of BCKDK in the liver inhibited hepatic glucose production as well as the expression of key gluconeogenic enzymes. No abnormal gluconeogenesis was found in mice lacking hepatic BCKDHA. Consistent with the vivo results, BT2-mediated inhibition or genetic knockdown of BCKDK decreased hepatic glucose production and gluconeogenic gene expressions in primary mouse hepatocytes while BCKDK overexpression exhibited an opposite effect. Whereas, gluconeogenic gene expressions were not altered in BCKDHA-silenced hepatocytes. Mechanistically, BT2 treatment attenuated the interaction of cAMP response element binding protein (CREB) with CREB-binding protein and promoted FOXO1 protein degradation by increasing its ubiquitination. Our findings suggest that BCKDK regulates hepatic gluconeogenesis through CREB and FOXO1 signalings, independent of BCKDHA-mediated BCAA catabolism. Show less
📄 PDF DOI: 10.1038/s41419-024-07071-0
BCKDK
Ling Zou, Wei Wang, Wenda Huang +7 more · 2024 · Heliyon · Elsevier · added 2026-04-24
Branched chain α-keto acid dehydrogenase kinase (BCKDK) is a key enzyme involved in the metabolism of branched-chain amino acids (BCAAs). Its potential as a therapeutic target and prognostic factor fo Show more
Branched chain α-keto acid dehydrogenase kinase (BCKDK) is a key enzyme involved in the metabolism of branched-chain amino acids (BCAAs). Its potential as a therapeutic target and prognostic factor for a variety of cancers has been widely reported. In this study, we investigated the expression of BCKDK in clinical glioma samples and found that BCKDK was significantly overexpressed in glioblastoma (GBM) and was associated with its poor prognosis. We further found that BCKDK is phosphorylated by tyrosine protein kinase Fyn at Y151, which increases its catalytic activity and stability, and demonstrate through Show less
📄 PDF DOI: 10.1016/j.heliyon.2024.e33663
BCKDK