👤 Xueyi Wang

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Also published as: A Wang, Ai-Ling Wang, Ai-Ting Wang, Aihua Wang, Aijun Wang, Aili Wang, Aimin Wang, Aiting Wang, Aixian Wang, Aiyun Wang, Aizhong Wang, Alexander Wang, Alice Wang, Allen Wang, Anlai Wang, Anli Wang, Annette Wang, Anni Wang, Anqi Wang, Anthony Z Wang, Anxiang Wang, Anxin Wang, Ao Wang, Aoli Wang, B R Wang, B Wang, Baihan Wang, Baisong Wang, Baitao Wang, Bangchen Wang, Banghui Wang, Bangmao Wang, Bangshing Wang, Bao Wang, Bao-Long Wang, Baocheng Wang, Baofeng Wang, Baogui Wang, Baojun Wang, Baoli Wang, Baolong Wang, Baoming Wang, Baosen Wang, Baowei Wang, Baoying Wang, Baoyun Wang, Bei Bei Wang, Bei Wang, Beibei Wang, Beilan Wang, Beilei Wang, Ben Wang, Benjamin H Wang, Benzhong Wang, Bi Wang, Bi-Dar Wang, Biao Wang, Bicheng Wang, Bijue Wang, Bin Wang, Bin-Xue Wang, Binbin Wang, Bing Qing Wang, Bing Wang, Binghai Wang, Binghan Wang, Bingjie Wang, Binglong Wang, Bingnan Wang, Bingyan Wang, Bingyu Wang, Binquan Wang, Biqi Wang, Bo Wang, Bochu Wang, Boyu Wang, Bruce Wang, C Wang, C Z Wang, Cai Ren Wang, Cai-Hong Wang, Cai-Yun Wang, Cailian Wang, Caiqin Wang, Caixia Wang, Caiyan Wang, Can Wang, Cangyu Wang, Carol A Wang, Catherine Ruiyi Wang, Cenxuan Wang, Chan Wang, Chang Wang, Chang-Yun Wang, Changduo Wang, Changjing Wang, Changliang Wang, Changlong Wang, Changqian Wang, Changtu Wang, Changwei Wang, Changying Wang, Changyu Wang, Changyuan Wang, Changzhen Wang, Chao Wang, Chao-Jun Wang, Chao-Yung Wang, Chaodong Wang, Chaofan Wang, Chaohan Wang, Chaohui Wang, Chaojie Wang, Chaokui Wang, Chaomeng Wang, Chaoqun Wang, Chaoxian Wang, Chaoyi Wang, Chaoyu Wang, Chaozhan Wang, Charles C N Wang, Chau-Jong Wang, Chen Wang, Chen-Cen Wang, Chen-Ma Wang, Chen-Yu Wang, Chenchen Wang, Chenfei Wang, Cheng An Wang, Cheng Wang, Cheng-Cheng Wang, Cheng-Jie Wang, Cheng-zhang Wang, Chengbin Wang, Chengcheng Wang, Chenggang Wang, Chenghao Wang, Chenghua Wang, Chengjian Wang, Chengjun Wang, Chenglin Wang, Chenglong Wang, Chengniu Wang, Chengqiang Wang, Chengshuo Wang, Chenguang Wang, Chengwen Wang, Chengyan Wang, Chengyu Wang, Chengze Wang, Chenji Wang, Chenliang Wang, Chenwei Wang, Chenxi Wang, Chenxin Wang, Chenxuan Wang, Chenyang Wang, Chenyao Wang, Chenyin Wang, Chenyu Wang, Chenzi Wang, Chi Chiu Wang, Chi Wang, Chi-Ping Wang, Chia-Chuan Wang, Chia-Lin Wang, Chien-Hsun Wang, Chien-Wei Wang, Chih-Chun Wang, Chih-Hao Wang, Chih-Hsien Wang, Chih-Liang Wang, Chih-Yang Wang, Chih-Yuan Wang, Chijia Wang, Ching C Wang, Ching-Jen Wang, Chiou-Miin Wang, Chong Wang, Chongjian Wang, Chonglong Wang, Chongmin Wang, Chongze Wang, Christina Wang, Christine Wang, Chu Wang, Chuan Wang, Chuan-Chao Wang, Chuan-Hui Wang, Chuan-Jiang Wang, Chuan-Wen Wang, Chuang Wang, Chuanhai Wang, Chuansen Wang, Chuansheng Wang, Chuanxin Wang, Chuanyue Wang, Chuduan Wang, Chun Wang, Chun-Chieh Wang, Chun-Juan Wang, Chun-Li Wang, Chun-Lin Wang, Chun-Ting Wang, Chun-Xia Wang, Chung-Hsi Wang, Chung-Hsing Wang, Chung-Teng Wang, Chunguo Wang, Chunhong Wang, Chuning Wang, Chunjiong Wang, Chunjuan Wang, Chunle Wang, Chunli Wang, Chunlong Wang, Chunmei Wang, Chunsheng Wang, Chunting Wang, Chunxia Wang, Chunxue Wang, Chunyan Wang, Chunyang Wang, Chunyi Wang, Chunyu Wang, Chuyao Wang, Cindy Wang, Ciyang Wang, Cong Wang, Congcong Wang, Congrong Wang, Congrui Wang, Cui Wang, Cui-Fang Wang, Cui-Shan Wang, Cuili Wang, Cuiling Wang, Cuizhe Wang, Cun-Yu Wang, Cunchuan Wang, Cunyi Wang, D Wang, Da Wang, Da-Cheng Wang, Da-Li Wang, Da-Yan Wang, Da-Zhi Wang, Dadong Wang, Dai Wang, Daijun Wang, Daiwei Wang, Daixi Wang, Dajia Wang, Dake Wang, Dali Wang, Dalong Wang, Dalu Wang, Dan Wang, Dan-Dan Wang, Danan Wang, Dandan Wang, Danfeng Wang, Dang Wang, Dangfeng Wang, Danling Wang, Danqing Wang, Danxin Wang, Danyang Wang, Dao Wen Wang, Dao-Wen Wang, Dao-Xin Wang, Daolong Wang, Daoping Wang, Daozhong Wang, Dapeng Wang, Daping Wang, Daqi Wang, Daqing Wang, David Q H Wang, David Q-H Wang, David Wang, Dawei Wang, Dayan Wang, Dayong Wang, Dazhi Wang, De-He Wang, Dedong Wang, Dehao Wang, Deli Wang, Delin Wang, Delong Wang, Demin Wang, Deming Wang, Dengbin Wang, Dennis Qing Wang, Dennis Wang, Deqi Wang, Deshou Wang, Dezhong Wang, Di Wang, Dinghui Wang, Dingting Wang, Dingxiang Wang, Dong D Wang, Dong Hao Wang, Dong Wang, Dong-Dong Wang, Dong-Jie Wang, Dong-Mei Wang, DongWei Wang, Dongdong Wang, Donggen Wang, Donghao Wang, Donghong Wang, Donghui Wang, Dongliang Wang, Donglin Wang, Dongmei Wang, Dongqin Wang, Dongshi Wang, Dongxia Wang, Dongxu Wang, Dongyan Wang, Dongyang Wang, Dongyi Wang, Dongying Wang, Dongyu Wang, Doudou Wang, Du Wang, Duan Wang, Duanyang Wang, Duo-Ping Wang, E Wang, Edward Wang, En-bo Wang, En-hua Wang, Endi Wang, Enhua Wang, Er-Jin Wang, Erfei Wang, Erika Y Wang, Ermao Wang, Erming Wang, Ertao Wang, Eryao Wang, Eunice S Wang, Exing Wang, F Wang, Fa-Kai Wang, Fan Wang, Fanchang Wang, Fang Wang, Fang-Tao Wang, Fangfang Wang, Fangjie Wang, Fangjun Wang, Fangyan Wang, Fangyong Wang, Fangyu Wang, Fanhua Wang, Fanwen Wang, Fanxiong Wang, Fei Wang, Fei-Fei Wang, Fei-Yan Wang, Feida Wang, Feifei Wang, Feijie Wang, Feimiao Wang, Feixiang Wang, Feiyan Wang, Fen Wang, Feng Wang, Feng-Sheng Wang, Fengchong Wang, Fengge Wang, Fenghua Wang, Fengliang Wang, Fenglin Wang, Fengling Wang, Fengqiang Wang, Fengyang Wang, Fengying Wang, Fengyong Wang, Fengyun Wang, Fengzhen Wang, Fengzhong Wang, Fu Wang, Fu-Sheng Wang, Fu-Yan Wang, Fu-Zhen Wang, Fubao Wang, Fubing Wang, Fudi Wang, Fuhua Wang, Fuqiang Wang, Furong Wang, Fuwen Wang, Fuxin Wang, Fuyan Wang, G Q Wang, G Wang, G-W Wang, Gan Wang, Gang Wang, Ganggang Wang, Ganglin Wang, Gangyang Wang, Ganyu Wang, Gao T Wang, Gao Wang, Gaofu Wang, Gaopin Wang, Gavin Wang, Ge Wang, Geng Wang, Genghao Wang, Gengsheng Wang, Gongming Wang, Guan Wang, Guan-song Wang, Guandi Wang, Guanduo Wang, Guang Wang, Guang-Jie Wang, Guang-Rui Wang, Guangdi Wang, Guanghua Wang, Guanghui Wang, Guangliang Wang, Guangming Wang, Guangsuo Wang, Guangwen Wang, Guangyan Wang, Guangzhi Wang, Guanrou Wang, Guanru Wang, Guansong Wang, Guanyun Wang, Gui-Qi Wang, Guibin Wang, Guihu Wang, Guihua Wang, Guimin Wang, Guiping Wang, Guiqun Wang, Guixin Wang, Guixue Wang, Guiying Wang, Guo-Du Wang, Guo-Hua Wang, Guo-Liang Wang, Guo-Ping Wang, Guo-Quan Wang, Guo-hong Wang, GuoYou Wang, Guobin Wang, Guobing Wang, Guodong Wang, Guohang Wang, Guohao Wang, Guoliang Wang, Guoling Wang, Guoping Wang, Guoqian Wang, Guoqiang Wang, Guoqing Wang, Guorong Wang, Guowen Wang, Guoxiang Wang, Guoxiu Wang, Guoyi Wang, Guoying Wang, Guozheng Wang, H J Wang, H Wang, H X Wang, H Y Wang, H-Y Wang, Hai Bo Wang, Hai Wang, Hai Yang Wang, Hai-Feng Wang, Hai-Jun Wang, Hai-Long Wang, Haibin Wang, Haibing Wang, Haibo Wang, Haichao Wang, Haichuan Wang, Haifei Wang, Haifeng Wang, Haihe Wang, Haihong Wang, Haihua Wang, Haijiao Wang, Haijing Wang, Haijiu Wang, Haikun Wang, Hailei Wang, Hailin Wang, Hailing Wang, Hailong Wang, Haimeng Wang, Haina Wang, Haining Wang, Haiping Wang, Hairong Wang, Haitao Wang, Haiwei Wang, Haixia Wang, Haixin Wang, Haixing Wang, Haiyan Wang, Haiying Wang, Haiyong Wang, Haiyun Wang, Haizhen Wang, Han Wang, Hanbin Wang, Hanbing Wang, Hanchao Wang, Handong Wang, Hang Wang, Hangzhou Wang, Hanmin Wang, Hanping Wang, Hanqi Wang, Hanying Wang, Hanyu Wang, Hanzhi Wang, Hao Wang, Hao-Ching Wang, Hao-Hua Wang, Hao-Tian Wang, Hao-Yu Wang, Haobin Wang, Haochen Wang, Haohao Wang, Haohui Wang, Haojie Wang, Haolong Wang, Haomin Wang, Haoming Wang, Haonan Wang, Haoping Wang, Haoqi Wang, Haoran Wang, Haowei Wang, Haoxin Wang, Haoyang Wang, Haoyu Wang, Haozhou Wang, He Wang, He-Cheng Wang, He-Ling Wang, He-Ping Wang, He-Tong Wang, Hebo Wang, Hechuan Wang, Heling Wang, Hemei Wang, Heming Wang, Heng Wang, Heng-Cai Wang, Hengjiao Wang, Hengjun Wang, Hequn Wang, Hesuiyuan Wang, Heyong Wang, Hezhi Wang, Hong Wang, Hong Yi Wang, Hong-Gang Wang, Hong-Hui Wang, Hong-Kai Wang, Hong-Qin Wang, Hong-Wei Wang, Hong-Xia Wang, Hong-Yan Wang, Hong-Yang Wang, Hong-Ying Wang, Hongbin Wang, Hongbing Wang, Hongbo Wang, Hongcai Wang, Hongda Wang, Hongdan Wang, Hongfang Wang, Hongjia Wang, Hongjian Wang, Hongjie Wang, Hongjuan Wang, Hongkun Wang, Honglei Wang, Hongli Wang, Honglian Wang, Honglun Wang, Hongmei Wang, Hongpin Wang, Hongqian Wang, Hongshan Wang, Hongsheng Wang, Hongtao Wang, Hongwei Wang, Hongxia Wang, Hongxin Wang, Hongyan Wang, Hongyang Wang, Hongyi Wang, Hongyin Wang, Hongying Wang, Hongyu Wang, Hongyuan Wang, Hongyue Wang, Hongyun Wang, Hongze Wang, Hongzhan Wang, Hongzhuang Wang, Horng-Dar Wang, Houchun Wang, Hsei-Wei Wang, Hsueh-Chun Wang, Hu WANG, Hua Wang, Hua-Qin Wang, Hua-Wei Wang, Huabo Wang, Huafei Wang, Huai-Zhou Wang, Huaibing Wang, Huaili Wang, Huaizhi Wang, Huajin Wang, Huajing Wang, Hualin Wang, Hualing Wang, Huan Wang, Huan-You Wang, Huang Wang, Huanhuan Wang, Huanyu Wang, Huaquan Wang, Huating Wang, Huawei Wang, Huaxiang Wang, Huayang Wang, Huei Wang, Hui Miao Wang, Hui Wang, Hui-Hui Wang, Hui-Li Wang, Hui-Nan Wang, Hui-Yu Wang, HuiYue Wang, Huie Wang, Huiguo Wang, Huihua Wang, Huihui Wang, Huijie Wang, Huijun Wang, Huilun Wang, Huimei Wang, Huimin Wang, Huina Wang, Huiping Wang, Huiquan Wang, Huiqun Wang, Huishan Wang, Huiting Wang, Huiwen Wang, Huixia Wang, Huiyan Wang, Huiyang Wang, Huiyao Wang, Huiying Wang, Huiyu Wang, Huizhen Wang, Huizhi Wang, Huming Wang, I-Ching Wang, Iris X Wang, Isabel Z Wang, J J Wang, J P Wang, J Q Wang, J Wang, J Z Wang, J-Y Wang, Jacob E Wang, James Wang, Jeffrey Wang, Jen-Chun Wang, Jen-Chywan Wang, Jennifer E Wang, Jennifer T Wang, Jennifer X Wang, Jenny Y Wang, Jeremy R Wang, Jeremy Wang, Ji M Wang, Ji Wang, Ji-Nuo Wang, Ji-Yang Wang, Ji-Yao Wang, Ji-zheng Wang, Jia Bei Wang, Jia Bin Wang, Jia Wang, Jia-Liang Wang, Jia-Lin Wang, Jia-Mei Wang, Jia-Peng Wang, Jia-Qi Wang, Jia-Qiang Wang, Jia-Ying Wang, Jia-Yu Wang, Jiabei Wang, Jiabo Wang, Jiafeng Wang, Jiafu Wang, Jiahao Wang, Jiahui Wang, Jiajia Wang, Jiakun Wang, Jiale Wang, Jiali Wang, Jialiang Wang, Jialin Wang, Jialing Wang, Jiamin Wang, Jiaming Wang, Jian Wang, Jian'an Wang, Jian-Bin Wang, Jian-Guo Wang, Jian-Hong Wang, Jian-Long Wang, Jian-Wei Wang, Jian-Xiong Wang, Jian-Yong Wang, Jian-Zhi Wang, Jian-chun Wang, Jianan Wang, Jianbing Wang, Jianbo Wang, Jianding Wang, Jianfang Wang, Jianfei Wang, Jiang Wang, Jiangbin Wang, Jiangbo Wang, Jianghua Wang, Jianghui Wang, Jiangong Wang, Jianguo Wang, Jianhao Wang, Jianhua Wang, Jianhui Wang, Jiani Wang, Jianjiao Wang, Jianjie Wang, Jianjun Wang, Jianle Wang, Jianli Wang, Jianlin Wang, Jianliu Wang, Jianlong Wang, Jianmei Wang, Jianmin Wang, Jianning Wang, Jianping Wang, Jianqin Wang, Jianqing Wang, Jianqun Wang, Jianru Wang, Jianshe Wang, Jianshu Wang, Jiantao Wang, Jianwei Wang, Jianwu Wang, Jianxiang Wang, Jianxin Wang, Jianye Wang, Jianying Wang, Jianyong Wang, Jianyu Wang, Jianzhang Wang, Jianzhi Wang, Jiao Wang, Jiaojiao Wang, Jiapan Wang, Jiaping Wang, Jiaqi Wang, Jiaqian Wang, Jiatao Wang, Jiawei Wang, Jiawen Wang, Jiaxi Wang, Jiaxin Wang, Jiaxing Wang, Jiaxuan Wang, Jiayan Wang, Jiayang Wang, Jiayi Wang, Jiaying Wang, Jiayu Wang, Jiazheng Wang, Jiazhi Wang, Jie Jin Wang, Jie Wang, Jieda Wang, Jieh-Neng Wang, Jiemei Wang, Jieqi Wang, Jieyan Wang, Jieyu Wang, Jifei Wang, Jiheng Wang, Jihong Wang, Jiliang Wang, Jilin Wang, Jin Wang, Jin'e Wang, Jin-Bao Wang, Jin-Cheng Wang, Jin-Da Wang, Jin-E Wang, Jin-Juan Wang, Jin-Liang Wang, Jin-Xia Wang, Jin-Xing Wang, Jincheng Wang, Jindan Wang, Jinfei Wang, Jinfeng Wang, Jinfu Wang, Jing J Wang, Jing Wang, Jing-Hao Wang, Jing-Huan Wang, Jing-Jing Wang, Jing-Long Wang, Jing-Min Wang, Jing-Shi Wang, Jing-Wen Wang, Jing-Xian Wang, Jing-Yi Wang, Jing-Zhai Wang, Jingang Wang, Jingchun Wang, Jingfan Wang, Jingfeng Wang, Jingheng Wang, Jinghong Wang, Jinghua Wang, Jinghuan Wang, Jingjing Wang, Jingkang Wang, Jinglin Wang, Jingmin Wang, Jingnan Wang, Jingqi Wang, Jingru Wang, Jingtong Wang, Jingwei Wang, Jingwen Wang, Jingxiao Wang, Jingyang Wang, Jingyi Wang, Jingying Wang, Jingyu Wang, Jingyue Wang, Jingyun Wang, Jingzhou Wang, Jinhai Wang, Jinhao Wang, Jinhe Wang, Jinhua Wang, Jinhuan Wang, Jinhui Wang, Jinjie Wang, Jinjin Wang, Jinkang Wang, Jinling Wang, Jinlong Wang, Jinmeng Wang, Jinning Wang, Jinping Wang, Jinqiu Wang, Jinrong Wang, Jinru Wang, Jinsong Wang, Jintao Wang, Jinxia Wang, Jinxiang Wang, Jinyang Wang, Jinyu Wang, Jinyue Wang, Jinyun Wang, Jinzhu Wang, Jiou Wang, Jipeng Wang, Jiqing Wang, Jiqiu Wang, Jisheng Wang, Jiu Wang, Jiucun Wang, Jiun-Ling Wang, Jiwen Wang, Jixuan Wang, Jiyan Wang, Jiying Wang, Jiyong Wang, Jizheng Wang, John Wang, Jou-Kou Wang, Joy Wang, Ju Wang, Juan Wang, Jue Wang, Jueqiong Wang, Jufeng Wang, Julie Wang, Juling Wang, Jun Kit Wang, Jun Wang, Jun Yi Wang, Jun-Feng Wang, Jun-Jie Wang, Jun-Jun Wang, Jun-Ling Wang, Jun-Sheng Wang, Jun-Sing Wang, Jun-Zhuo Wang, Jundong Wang, Junfeng Wang, Jung-Pan Wang, Junhong Wang, Junhua Wang, Junhui Wang, Junjiang Wang, Junjie Wang, Junjun Wang, Junkai Wang, Junke Wang, Junli Wang, Junlin Wang, Junling Wang, Junmei Wang, Junmin Wang, Junpeng Wang, Junping Wang, Junqin Wang, Junqing Wang, Junrui Wang, Junsheng Wang, Junshi Wang, Junshuang Wang, Junwen Wang, Junxiao Wang, Junya Wang, Junying Wang, Junyu Wang, Justin Wang, Jutao Wang, Juxiang Wang, K Wang, Kai Wang, Kai-Kun Wang, Kai-Wen Wang, Kaicen Wang, Kaihao Wang, Kaihe Wang, Kaihong Wang, Kaijie Wang, Kaijuan Wang, Kailu Wang, Kaiming Wang, Kaining Wang, Kaiting Wang, Kaixi Wang, Kaixu Wang, Kaiyan Wang, Kaiyuan Wang, Kaiyue Wang, Kan Wang, Kangli Wang, Kangling Wang, Kangmei Wang, Kangning Wang, Ke Wang, Ke-Feng Wang, KeShan Wang, Kehan Wang, Kehao Wang, Kejia Wang, Kejian Wang, Kejun Wang, Keke Wang, Keming Wang, Kenan Wang, Keqing Wang, Kesheng Wang, Kexin Wang, Keyan Wang, Keyi Wang, Keyun Wang, Kongyan Wang, Kuan Hong Wang, Kui Wang, Kun Wang, Kunhua Wang, Kunpeng Wang, Kunzheng Wang, L F Wang, L M Wang, L Wang, L Z Wang, L-S Wang, Laidi Wang, Laijian Wang, Laiyuan Wang, Lan Wang, Lan-Wan Wang, Lan-lan Wang, Lanlan Wang, Larry Wang, Le Wang, Le-Xin Wang, Ledan Wang, Lee-Kai Wang, Lei P Wang, Lei Wang, Lei-Lei Wang, Leiming Wang, Leishen Wang, Leli Wang, Leran Wang, Lexin Wang, Leying Wang, Li Chun Wang, Li Dong Wang, Li Wang, Li-Dong Wang, Li-E Wang, Li-Juan Wang, Li-Li Wang, Li-Na Wang, Li-San Wang, Li-Ting Wang, Li-Xin Wang, Li-Yong Wang, LiLi Wang, Lian Wang, Lianchun Wang, Liang Wang, Liang-Yan Wang, Liangfu Wang, Lianghai Wang, Liangli Wang, Liangliang Wang, Liangxu Wang, Lianshui Wang, Lianyong Wang, Libo Wang, Lichan Wang, Lichao Wang, Liewei Wang, Lifang Wang, Lifei Wang, Lifen Wang, Lifeng Wang, Ligang Wang, Lihong Wang, Lihua Wang, Lihui Wang, Lijia Wang, Lijin Wang, Lijing Wang, Lijuan Wang, Lijun Wang, Liling Wang, Lily Wang, Limeng Wang, Limin Wang, Liming Wang, Lin Wang, Lin-Fa Wang, Lin-Yu Wang, Lina Wang, Linfang Wang, Ling Jie Wang, Ling Wang, Ling-Ling Wang, Lingbing Wang, Lingda Wang, Linghua Wang, Linghuan Wang, Lingli Wang, Lingling Wang, Lingyan Wang, Lingzhi Wang, Linhua Wang, Linhui Wang, Linjie Wang, Linli Wang, Linlin Wang, Linping Wang, Linshu Wang, Linshuang Wang, Lintao Wang, Linxuan Wang, Linying Wang, Linyuan Wang, Liping Wang, Liqing Wang, Liqun Wang, Lirong Wang, Litao Wang, Liting Wang, Liu Wang, Liusong Wang, Liuyang Wang, Liwei Wang, Lixia Wang, Lixian Wang, Lixiang Wang, Lixin Wang, Lixing Wang, Lixiu Wang, Liyan Wang, Liyi Wang, Liying Wang, Liyong Wang, Liyuan Wang, Liyun Wang, Long Wang, Longcai Wang, Longfei Wang, Longsheng Wang, Longxiang Wang, Lou-Pin Wang, Lu Wang, Lu-Lu Wang, Lueli Wang, Lufang Wang, Luhong Wang, Luhui Wang, Lujuan Wang, Lulu Wang, Luofu Wang, Luping Wang, Luting Wang, Luwen Wang, Luxiang Wang, Luya Wang, Luyao Wang, Luyun Wang, Lynn Yuning Wang, M H Wang, M Wang, M Y Wang, M-J Wang, Maiqiu Wang, Man Wang, Mangju Wang, Manli Wang, Mao-Xin Wang, Maochun Wang, Maojie Wang, Maoju Wang, Mark Wang, Mei Wang, Mei-Gui Wang, Mei-Xia Wang, Meiding Wang, Meihui Wang, Meijun Wang, Meiling Wang, Meixia Wang, Melissa T Wang, Meng C Wang, Meng Wang, Meng Yu Wang, Meng-Dan Wang, Meng-Lan Wang, Meng-Meng Wang, Meng-Ru Wang, Meng-Wei Wang, Meng-Ying Wang, Meng-hong Wang, Mengge Wang, Menghan Wang, Menghui Wang, Mengjiao Wang, Mengjing Wang, Mengjun Wang, Menglong Wang, Menglu Wang, Mengmeng Wang, Mengqi Wang, Mengru Wang, Mengshi Wang, Mengwen Wang, Mengxiao Wang, Mengya Wang, Mengyao Wang, Mengying Wang, Mengyuan Wang, Mengyue Wang, Mengyun Wang, Mengze Wang, Mengzhao Wang, Mengzhi Wang, Mian Wang, Miao Wang, Mimi Wang, Min Wang, Min-sheng Wang, Ming Wang, Ming-Chih Wang, Ming-Hsi Wang, Ming-Jie Wang, Ming-Wei Wang, Ming-Yang Wang, Ming-Yuan Wang, Mingchao Wang, Mingda Wang, Minghua Wang, Minghuan Wang, Minghui Wang, Mingji Wang, Mingjin Wang, Minglei Wang, Mingliang Wang, Mingmei Wang, Mingming Wang, Mingqiang Wang, Mingrui Wang, Mingsong Wang, Mingxi Wang, Mingxia Wang, Mingxun Wang, Mingya Wang, Mingyang Wang, Mingyi Wang, Mingyu Wang, Mingzhi Wang, Mingzhu Wang, Minjie Wang, Minjun Wang, Minmin Wang, Minxian Wang, Minxiu Wang, Minzhou Wang, Miranda C Wang, Mo Wang, Mofei Wang, Monica Wang, Mu Wang, Mutian Wang, Muxiao Wang, Muxuan Wang, N Wang, Na Wang, Nan Wang, Nana Wang, Nanbu Wang, Nannan Wang, Nanping Wang, Neng Wang, Ni Wang, Niansong Wang, Ning Wang, Ningjian Wang, Ningli Wang, Ningyuan Wang, Nuan Wang, Oliver Wang, Ouchen Wang, P Jeremy Wang, P L Wang, P N Wang, P Wang, Pai Wang, Pan Wang, Pan-Pan Wang, Panfeng Wang, Panliang Wang, Pei Chang Wang, Pei Wang, Pei-Hua Wang, Pei-Jian Wang, Pei-Juan Wang, Pei-Wen Wang, Pei-Yu Wang, Peichang Wang, Peigeng Wang, Peihe Wang, Peijia Wang, Peijuan Wang, Peijun Wang, Peilin Wang, Peipei Wang, Peirong Wang, Peiwen Wang, Peixi Wang, Peiyao Wang, Peiyin Wang, Peng Wang, Peng-Cheng Wang, Pengbo Wang, Pengchao Wang, Pengfei Wang, Pengjie Wang, Pengju Wang, Penglai Wang, Penglong Wang, Pengpu Wang, Pengtao Wang, Pengxiang Wang, Pengyu Wang, Pin Wang, Ping Wang, Pingchuan Wang, Pingfeng Wang, Pingping Wang, Pintian Wang, Po-Jen Wang, Pu Wang, Q Wang, Q Z Wang, Qi Wang, Qi-Bing Wang, Qi-En Wang, Qi-Jia Wang, Qi-Qi Wang, Qian Wang, Qian-Liang Wang, Qian-Wen Wang, Qian-Zhu Wang, Qian-fei Wang, Qianbao Wang, Qiang Wang, Qiang-Sheng Wang, Qiangcheng Wang, Qianghu Wang, Qiangqiang Wang, Qianjin Wang, Qianliang Wang, Qianqian Wang, Qianrong Wang, Qianru Wang, Qianwen Wang, Qianxu Wang, Qiao Wang, Qiao-Ping Wang, Qiaohong Wang, Qiaoqi Wang, Qiaoqiao Wang, Qifan Wang, Qifei Wang, Qifeng Wang, Qigui Wang, Qihao Wang, Qihua Wang, Qijia Wang, Qiming Wang, Qin Wang, Qing Jun Wang, Qing K Wang, Qing Kenneth Wang, Qing Mei Wang, Qing Wang, Qing-Bin Wang, Qing-Dong Wang, Qing-Jin Wang, Qing-Liang Wang, Qing-Mei Wang, Qing-Yan Wang, Qing-Yuan Wang, Qing-Yun Wang, QingDong Wang, Qingchun Wang, Qingfa Wang, Qingfeng Wang, Qinghang Wang, Qingliang Wang, Qinglin Wang, Qinglu Wang, Qingming Wang, Qingping Wang, Qingqing Wang, Qingshi Wang, Qingshui Wang, Qingsong Wang, Qingtong Wang, Qingyong Wang, Qingyu Wang, Qingyuan Wang, Qingyun Wang, Qingzhong Wang, Qinqin Wang, Qinrong Wang, Qintao Wang, Qinwen Wang, Qinyun Wang, Qiong Wang, Qiqi Wang, Qirui Wang, Qishan Wang, Qiu-Ling Wang, Qiu-Xia Wang, Qiuhong Wang, Qiuli Wang, Qiuling Wang, Qiuning Wang, Qiuping Wang, Qiushi Wang, Qiuting Wang, Qiuyan Wang, Qiuyu Wang, Qiwei Wang, Qixue Wang, Qiyu Wang, Qiyuan Wang, Quan Wang, Quan-Ming Wang, Quanli Wang, Quanren Wang, Quanxi Wang, Qun Wang, Qunxian Wang, Qunzhi Wang, R Wang, Ran Wang, Ranjing Wang, Ranran Wang, Re-Hua Wang, Ren Wang, Rencheng Wang, Renjun Wang, Renqian Wang, Renwei Wang, Renxi Wang, Renxiao Wang, Renyuan Wang, Rihua Wang, Rikang Wang, Rixiang Wang, Robert Yl Wang, Rong Wang, Rong-Chun Wang, Rong-Rong Wang, Rong-Tsorng Wang, RongRong Wang, Rongjia Wang, Rongping Wang, Rongyun Wang, Ru Wang, RuNan Wang, Ruey-Yun Wang, Rufang Wang, Ruhan Wang, Rui Wang, Rui-Hong Wang, Rui-Min Wang, Rui-Ping Wang, Rui-Rui Wang, Ruibin Wang, Ruibing Wang, Ruibo Wang, Ruicheng Wang, Ruifang Wang, Ruijing Wang, Ruimeng Wang, Ruimin Wang, Ruiming Wang, Ruinan Wang, Ruining Wang, Ruiquan Wang, Ruiwen Wang, Ruixian Wang, Ruixin Wang, Ruixuan Wang, Ruixue Wang, Ruiying Wang, Ruizhe Wang, Ruizhi Wang, Rujie Wang, Ruling Wang, Ruming Wang, Runci Wang, Runuo Wang, Runze Wang, Runzhi Wang, Ruo-Nan Wang, Ruo-Ran Wang, Ruonan Wang, Ruosu Wang, Ruoxi Wang, Rurong Wang, Ruting Wang, Ruxin Wang, Ruxuan Wang, Ruyue Wang, S L Wang, S S Wang, S Wang, S X Wang, Sa A Wang, Sa Wang, Saifei Wang, Saili Wang, Sainan Wang, Saisai Wang, Sangui Wang, Sanwang Wang, Sasa Wang, Sen Wang, Seok Mui Wang, Seungwon Wang, Sha Wang, Shan Wang, Shan-Shan Wang, Shang Wang, Shangyu Wang, Shanshan Wang, Shao-Kang Wang, Shaochun Wang, Shaohsu Wang, Shaokun Wang, Shaoli Wang, Shaolian Wang, Shaoshen Wang, Shaowei Wang, Shaoyi Wang, Shaoying Wang, Shaoyu Wang, Shaozheng Wang, Shasha Wang, Shau-Chun Wang, Shawn Wang, Shen Wang, Shen-Nien Wang, Shenao Wang, Sheng Wang, Sheng-Min Wang, Sheng-Nan Wang, Sheng-Ping Wang, Sheng-Quan Wang, Sheng-Yang Wang, Shengdong Wang, Shengjie Wang, Shengli Wang, Shengqi Wang, Shengya Wang, Shengyao Wang, Shengyu Wang, Shengyuan Wang, Shenqi Wang, Sheri Wang, Shi Wang, Shi-Cheng Wang, Shi-Han Wang, Shi-Qi Wang, Shi-Xin Wang, Shi-Yao Wang, Shibin Wang, Shichao Wang, Shicung Wang, Shidong Wang, Shifa Wang, Shifeng Wang, Shih-Wei Wang, Shihan Wang, Shihao Wang, Shihua Wang, Shijie Wang, Shijin Wang, Shijun Wang, Shikang Wang, Shimiao Wang, Shiqi Wang, Shiqiang Wang, Shitao Wang, Shitian Wang, Shiwen Wang, Shixin Wang, Shixuan Wang, Shiyang Wang, Shiyao Wang, Shiyin Wang, Shiyu Wang, Shiyuan Wang, Shiyue Wang, Shizhi Wang, Shouli Wang, Shouling Wang, Shouzhi Wang, Shu Wang, Shu-Huei Wang, Shu-Jin Wang, Shu-Ling Wang, Shu-Na Wang, Shu-Song Wang, Shu-Xia Wang, Shu-qiang Wang, Shuai Wang, Shuaiqin Wang, Shuang Wang, Shuang-Shuang Wang, Shuang-Xi Wang, Shuangyuan Wang, Shubao Wang, Shudan Wang, Shuge Wang, Shuguang Wang, Shuhe Wang, Shuiliang Wang, Shuiyun Wang, Shujin Wang, Shukang Wang, Shukui Wang, Shun Wang, Shuning Wang, Shunjun Wang, Shunran Wang, Shuo Wang, Shuping Wang, Shuqi Wang, Shuqing Wang, Shuren Wang, Shusen Wang, Shusheng Wang, Shushu Wang, Shuu-Jiun Wang, Shuwei Wang, Shuxia Wang, Shuxin Wang, Shuya Wang, Shuye Wang, Shuyue Wang, Shuzhe Wang, Shuzhen Wang, Shuzhong Wang, Shyi-Gang P Wang, Si Wang, Sibo Wang, Sidan Wang, Sihua Wang, Sijia Wang, Silas L Wang, Silu Wang, Simeng Wang, Siqi Wang, Siqing Wang, Siwei Wang, Siyang Wang, Siyi Wang, Siying Wang, Siyu Wang, Siyuan Wang, Siyue Wang, Song Wang, Songjiao Wang, Songlin Wang, Songping Wang, Songsong Wang, Songtao Wang, Sophie H Wang, Stephani Wang, Su'e Wang, Su-Guo Wang, Su-Hua Wang, Sufang Wang, Sugai Wang, Sui Wang, Suiyan Wang, Sujie Wang, Sujuan Wang, Suli Wang, Sun Wang, Supeng Perry Wang, Suxia Wang, Suyun Wang, Suzhen Wang, T Q Wang, T Wang, T Y Wang, Taian Wang, Taicheng Wang, Taishu Wang, Tammy C Wang, Tao Wang, Taoxia Wang, Teng Wang, Tengfei Wang, Theodore Wang, Thomas T Y Wang, Tian Wang, Tian-Li Wang, Tian-Lu Wang, Tian-Tian Wang, Tian-Yi Wang, Tiancheng Wang, Tiange Wang, Tianhao Wang, Tianhu Wang, Tianhui Wang, Tianjing Wang, Tianjun Wang, Tianlin Wang, Tiannan Wang, Tianpeng Wang, Tianqi Wang, Tianqin Wang, Tianqing Wang, Tiansheng Wang, Tiansong Wang, Tiantian Wang, Tianyi Wang, Tianying Wang, Tianyuan Wang, Tielin Wang, Tienju Wang, Tieqiao Wang, Timothy C Wang, Ting Chen Wang, Ting Wang, Ting-Chen Wang, Ting-Hua Wang, Ting-Ting Wang, Tingting Wang, Tingye Wang, Tingyu Wang, Tom J Wang, Tong Wang, Tong-Hong Wang, Tongsong Wang, Tongtong Wang, Tongxia Wang, Tongxin Wang, Tongyao Wang, Tony Wang, Tzung-Dau Wang, Victoria Wang, Vivian Wang, W Wang, Wanbing Wang, Wanchun Wang, Wang Wang, Wangxia Wang, Wanliang Wang, Wanxia Wang, Wanyao Wang, Wanyi Wang, Wanyu Wang, Wayseen Wang, Wei Wang, Wei-En Wang, Wei-Feng Wang, Wei-Lien Wang, Wei-Qi Wang, Wei-Ting Wang, Wei-Wei Wang, Weicheng Wang, Weiding Wang, Weidong Wang, Weifan Wang, Weiguang Wang, Weihao Wang, Weihong Wang, Weihua Wang, Weijian Wang, Weijie Wang, Weijun Wang, Weilin Wang, Weiling Wang, 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Wang, Xin Wang, Xin Wei Wang, Xin-Hua Wang, Xin-Liang Wang, Xin-Ming Wang, Xin-Peng Wang, Xin-Qun Wang, Xin-Shang Wang, Xin-Xin Wang, Xin-Yang Wang, Xin-Yue Wang, Xinbo Wang, Xinchang Wang, Xinchao Wang, Xinchen Wang, Xincheng Wang, Xinchun Wang, Xindi Wang, Xindong Wang, Xing Wang, Xing-Huan Wang, Xing-Jin Wang, Xing-Jun Wang, Xing-Lei Wang, Xing-Ping Wang, Xing-Quan Wang, Xingbang Wang, Xingchen Wang, Xingde Wang, Xingguo Wang, Xinghao Wang, Xinghui Wang, Xingjie Wang, Xingjin Wang, Xinglei Wang, Xinglong Wang, Xingqin Wang, Xinguo Wang, Xingxin Wang, Xingxing Wang, Xingye Wang, Xingyu Wang, Xingyue Wang, Xingyun Wang, Xinhui Wang, Xinjing Wang, Xinjun Wang, Xinke Wang, Xinkun Wang, Xinli Wang, Xinlin Wang, Xinlong Wang, Xinmei Wang, Xinqi Wang, Xinquan Wang, Xinran Wang, Xinrong Wang, Xinru Wang, Xinrui Wang, Xinshuai Wang, Xintong Wang, Xinwen Wang, Xinxin Wang, Xinyan Wang, Xinyang Wang, Xinye Wang, Xinyi Wang, Xinying Wang, Xinyu Wang, Xinyue Wang, Xinzhou Wang, Xiong Wang, Xiongjun Wang, Xiru Wang, Xitian Wang, Xiu-Lian Wang, Xiu-Ping Wang, Xiufen Wang, Xiujuan Wang, Xiujun Wang, Xiurong Wang, Xiuwen Wang, Xiuyu Wang, Xiuyuan Hugh Wang, Xixi Wang, Xixiang Wang, Xiyan Wang, Xiyue Wang, Xizhi Wang, Xu Wang, Xu-Hong Wang, Xuan Wang, Xuan-Ren Wang, Xuan-Ying Wang, Xuanwen Wang, Xuanyi Wang, Xubo Wang, Xudong Wang, Xue Wang, Xue-Feng Wang, Xue-Hua Wang, Xue-Lei Wang, Xue-Lian Wang, Xue-Rui Wang, Xue-Yao Wang, Xue-Ying Wang, Xuebin Wang, Xueding Wang, Xuedong Wang, Xuefei Wang, Xuefeng Wang, Xueguo Wang, Xuehao Wang, Xuejie Wang, Xuejing Wang, Xueju Wang, Xuejun Wang, Xuekai Wang, Xuelai Wang, Xuelian Wang, Xuelin Wang, Xuemei Wang, Xuemin Wang, Xueping Wang, Xueqian Wang, Xueqin Wang, Xuesong Wang, Xueting Wang, Xuewei Wang, Xuewen Wang, Xuexiang Wang, Xueyan Wang, Xueying Wang, Xueyun Wang, Xuezhen Wang, Xuezheng Wang, Xufei Wang, Xujing Wang, Xuliang Wang, Xumeng Wang, Xun Wang, Xuping Wang, Xuqiao Wang, Xuru Wang, Xusheng Wang, Xv Wang, Y Alan Wang, Y B Wang, Y H Wang, Y L Wang, Y P Wang, Y Wang, Y Y Wang, Y Z Wang, Y-H Wang, Y-S Wang, Ya Qi Wang, Ya Wang, Ya Xing Wang, Ya-Han Wang, Ya-Jie Wang, Ya-Long Wang, Ya-Nan Wang, Ya-Ping Wang, Ya-Qin Wang, Ya-Zhou Wang, Yachen Wang, Yachun Wang, Yadong Wang, Yafang Wang, Yafen Wang, Yahong Wang, Yahui Wang, Yajie Wang, Yajing Wang, Yajun Wang, Yake Wang, Yakun Wang, Yali Wang, Yalin Wang, Yaling Wang, Yalong Wang, Yan Ming Wang, Yan Wang, Yan-Chao Wang, Yan-Chun Wang, Yan-Feng Wang, Yan-Ge Wang, Yan-Jiang Wang, Yan-Jun Wang, Yan-Ming Wang, Yan-Yang Wang, Yan-Yi Wang, Yan-Zi Wang, Yana Wang, Yanan Wang, Yanbin Wang, Yanbing Wang, Yanchun Wang, Yancun Wang, Yanfang Wang, Yanfei Wang, Yanfeng Wang, Yang Wang, Yang-Yang Wang, Yange Wang, Yanggan Wang, Yangpeng Wang, Yangyang Wang, Yangyufan Wang, Yanhai Wang, Yanhong Wang, Yanhua Wang, Yanhui Wang, Yani Wang, Yanjin Wang, Yanjun Wang, Yankun Wang, Yanlei Wang, Yanli Wang, Yanliang Wang, Yanlin Wang, Yanling Wang, Yanmei Wang, Yanming Wang, Yanni Wang, Yanong Wang, Yanping Wang, Yanqing Wang, Yanru Wang, Yanting Wang, Yanwen Wang, Yanxia Wang, Yanxing Wang, Yanyang Wang, Yanyun Wang, Yanzhe Wang, Yanzhu Wang, Yao Wang, Yaobin Wang, Yaochun Wang, Yaodong Wang, Yaohe Wang, Yaokun Wang, Yaoling Wang, Yaolou Wang, Yaoxian Wang, Yaoxing Wang, Yaozhi Wang, Yapeng Wang, Yaping Wang, Yaqi Wang, Yaqian Wang, Yaqiong Wang, Yaru Wang, Yatao Wang, Yating Wang, Yawei Wang, Yaxian Wang, Yaxin Wang, Yaxiong Wang, Yaxuan Wang, Yayu Wang, Yazhou Wang, Ye Wang, Ye-Ran Wang, Yefu Wang, Yeh-Han Wang, Yehan Wang, Yeming Wang, Yen-Feng Wang, Yen-Sheng Wang, Yeou-Lih Wang, Yeqi Wang, Yezhou Wang, Yi Fan Wang, Yi Lei Wang, Yi Wang, Yi-Cheng Wang, Yi-Chuan Wang, Yi-Ming Wang, Yi-Ni Wang, Yi-Ning Wang, Yi-Shan Wang, Yi-Shiuan Wang, Yi-Shu Wang, Yi-Tao Wang, Yi-Ting Wang, Yi-Wen Wang, Yi-Xin Wang, Yi-Xuan Wang, Yi-Yi Wang, Yi-Ying Wang, Yi-Zhen Wang, Yi-sheng Wang, YiLi Wang, Yian Wang, Yibin Wang, Yibing Wang, Yichen Wang, Yicheng Wang, Yichuan Wang, Yifan Wang, Yifei Wang, Yigang Wang, Yige Wang, Yihan Wang, Yihao Wang, Yihe Wang, Yijin Wang, Yijing Wang, Yijun Wang, Yikang Wang, Yike Wang, Yilin Wang, Yilu Wang, Yimeng Wang, Yiming Wang, Yin Wang, Yin-Hu Wang, Yinan Wang, Yinbo Wang, Yindan Wang, Ying Wang, Ying-Piao Wang, Ying-Wei Wang, Ying-Zi Wang, Yingbo Wang, Yingcheng Wang, Yingchun Wang, Yingfei Wang, Yingge Wang, Yinggui Wang, Yinghui Wang, Yingjie Wang, Yingmei Wang, Yingna Wang, Yingping Wang, Yingqiao Wang, Yingtai Wang, Yingte Wang, Yingwei Wang, Yingwen Wang, Yingxiong Wang, Yingxue Wang, Yingyi Wang, Yingying Wang, Yingzi Wang, Yinhuai Wang, Yining E Wang, Yinong Wang, Yinsheng Wang, Yintao Wang, Yinuo Wang, Yinxiong Wang, Yinyin Wang, Yiou Wang, Yipeng Wang, Yiping Wang, Yiqi Wang, Yiqiao Wang, Yiqin Wang, Yiqing Wang, Yiquan Wang, Yirong Wang, Yiru Wang, Yirui Wang, Yishan Wang, Yishu Wang, Yitao Wang, Yiting Wang, Yiwei Wang, Yiwen Wang, Yixi Wang, Yixian Wang, Yixuan Wang, Yiyan Wang, Yiyi Wang, Yiying Wang, Yizhe Wang, Yong Wang, Yong-Bo Wang, Yong-Gang Wang, Yong-Jie Wang, Yong-Jun Wang, Yong-Tang Wang, Yongbin Wang, Yongdi Wang, Yongfei Wang, Yongfeng Wang, Yonggang Wang, Yonghong Wang, Yongjie Wang, Yongjun Wang, Yongkang Wang, Yongkuan Wang, Yongli Wang, Yongliang Wang, Yonglun Wang, Yongmei Wang, Yongming Wang, Yongni Wang, Yongqiang Wang, Yongqing Wang, Yongrui Wang, Yongsheng Wang, Yongxiang Wang, Yongyi Wang, Yongzhong Wang, You Wang, Youhua Wang, Youji Wang, Youjie Wang, Youli Wang, Youzhao Wang, Youzhi Wang, Yu Qin Wang, Yu Tian Wang, Yu Wang, Yu'e Wang, Yu-Chen Wang, Yu-Fan Wang, Yu-Fen Wang, Yu-Hang Wang, Yu-Hui Wang, Yu-Ping Wang, Yu-Ting Wang, Yu-Wei Wang, Yu-Wen Wang, Yu-Ying Wang, Yu-Zhe Wang, Yu-Zhuo Wang, Yuan Wang, Yuan-Hung Wang, Yuanbo Wang, Yuanfan Wang, Yuanjiang Wang, Yuanli Wang, Yuanqiang Wang, Yuanqing Wang, Yuanyong Wang, Yuanyuan Wang, Yuanzhen Wang, Yubing Wang, Yubo Wang, Yuchen Wang, Yucheng Wang, Yuchuan Wang, Yudong Wang, Yue Wang, Yue-Min Wang, Yue-Nan 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Zhizheng Wang, Zhizhong Wang, Zhong Wang, Zhong-Hao Wang, Zhong-Hui Wang, Zhong-Ping Wang, Zhong-Yu Wang, ZhongXia Wang, Zhongfang Wang, Zhongjing Wang, Zhongli Wang, Zhonglin Wang, Zhongqun Wang, Zhongsu Wang, Zhongwei Wang, Zhongyi Wang, Zhongyu Wang, Zhongyuan Wang, Zhongzhi Wang, Zhou Wang, Zhou-Ping Wang, Zhoufeng Wang, Zhouguang Wang, Zhuangzhuang Wang, Zhugang Wang, Zhulin Wang, Zhulun Wang, Zhuo Wang, Zhuo-Hui Wang, Zhuo-Jue Wang, Zhuo-Xin Wang, Zhuowei Wang, Zhuoying Wang, Zhuozhong Wang, Zhuqing Wang, Zi Wang, Zi Xuan Wang, Zi-Hao Wang, Zi-Qi Wang, Zi-Yi Wang, Zicheng Wang, Zifeng Wang, Zihan Wang, Ziheng Wang, Zihua Wang, Zihuan Wang, Zijian Wang, Zijie Wang, Zijue Wang, Zijun Wang, Zikang Wang, Zikun Wang, Ziliang Wang, Zilin Wang, Ziling Wang, Zilong Wang, Zining Wang, Ziping Wang, Ziqi Wang, Ziqian Wang, Ziqiang Wang, Ziqing Wang, Ziqiu Wang, Zitao Wang, Ziwei Wang, Zixi Wang, Zixia Wang, Zixian Wang, Zixiang Wang, Zixu Wang, Zixuan Wang, Ziyi Wang, Ziying Wang, Ziyu Wang, Ziyun Wang, Zongbao Wang, Zonggui Wang, Zongji Wang, Zongkui Wang, Zongqi Wang, Zongwei Wang, Zou Wang, Zulong Wang, Zumin Wang, Zun Wang, Zunxian Wang, Zuo Wang, Zuoheng Wang, Zuoyan Wang, Zusen Wang
articles
Qian ZHANG, Xiao Ling Wang, Yu Li Hou +9 more · 2025 · Biomedical and environmental sciences : BES · added 2026-04-24
To reveal the effects and potential mechanisms by which synaptic vesicle glycoprotein 2A (SV2A) influences the distribution of amyloid precursor protein (APP) in the trans-Golgi network (TGN), endolys Show more
To reveal the effects and potential mechanisms by which synaptic vesicle glycoprotein 2A (SV2A) influences the distribution of amyloid precursor protein (APP) in the trans-Golgi network (TGN), endolysosomal system, and cell membranes and to reveal the effects of SV2A on APP amyloid degradation. Colocalization analysis of APP with specific tagged proteins in the TGN, ensolysosomal system, and cell membrane was performed to explore the effects of SV2A on the intracellular transport of APP. APP, β-site amyloid precursor protein cleaving enzyme 1 (BACE1) expressions, and APP cleavage products levels were investigated to observe the effects of SV2A on APP amyloidogenic processing. APP localization was reduced in the TGN, early endosomes, late endosomes, and lysosomes, whereas it was increased in the recycling endosomes and cell membrane of SV2A-overexpressed neurons. Moreover, Arl5b (ADP-ribosylation factor 5b), a protein responsible for transporting APP from the TGN to early endosomes, was upregulated by SV2A. SV2A overexpression also decreased APP transport from the cell membrane to early endosomes by downregulating APP endocytosis. In addition, products of APP amyloid degradation, including sAPPβ, Aβ These results demonstrated that SV2A promotes APP transport from the TGN to early endosomes by upregulating Arl5b and promoting APP transport from early endosomes to recycling endosomes-cell membrane pathway, which slows APP amyloid degradation. Show less
no PDF DOI: 10.3967/bes2025.049
BACE1
Chenchen Wang, Xiaolei Song, Xiaowan Zhang +4 more · 2025 · Materials today. Bio · Elsevier · added 2026-04-24
Alzheimer's disease (AD) presents significant challenges due to its intricate pathogenic mechanisms and the limited efficacy of single-target therapies. In this study, we investigated the potential of Show more
Alzheimer's disease (AD) presents significant challenges due to its intricate pathogenic mechanisms and the limited efficacy of single-target therapies. In this study, we investigated the potential of chlorogenic acid (CHA), a multifunctional natural active compound, in AD therapy by developing a trifunctional nanocarrier (MC-H/R/si). CHA was effectively conjugated with iron-based metal-organic frameworks (MIL/Fe-100) through chelation interaction. The resulting nanocomplex (MC) not only enhances the bioavailability of CHA but also facilitates a synergistic antioxidant effect between CHA and MIL/Fe-100. Importantly, CHA can chelate Zn Show less
📄 PDF DOI: 10.1016/j.mtbio.2025.101841
BACE1
Jianhua Xia, Haiqin Chen, Yuying Wang +10 more · 2025 · Autophagy · Taylor & Francis · added 2026-04-24
The silkworm
no PDF DOI: 10.1080/15548627.2025.2510843
BACE1
Lei Xia, Junjie Li, Yayan Pang +12 more · 2025 · Science advances · Science · added 2026-04-24
β-Site amyloid precursor protein (APP)-cleaving enzyme 1 (BACE1) is the rate-limiting enzyme for amyloid-β (Aβ) generation and is considered promising drug target for Alzheimer's disease (AD). The co- Show more
β-Site amyloid precursor protein (APP)-cleaving enzyme 1 (BACE1) is the rate-limiting enzyme for amyloid-β (Aβ) generation and is considered promising drug target for Alzheimer's disease (AD). The co-chaperone BAG3 (Bcl-2-associated athanogene 3) plays an important role in maintaining intracellular protein homeostasis by regulating heat shock protein 70 (HSP70). Here, we reported that BAG3 expression was significantly elevated in AD. It interacted with and stabilized BACE1 by delaying its degradation through ubiquitin-proteasome and autophagy-lysosomal pathways. BAG3 Show less
📄 PDF DOI: 10.1126/sciadv.adt7981
BACE1
Yuhan Nong, Jung Soo Kim, Litian Jia +2 more · 2025 · Journal of Alzheimer's disease : JAD · SAGE Publications · added 2026-04-24
The accumulation of amyloid-β (Aβ) peptides is a hallmark of Alzheimer's disease (AD). Central to AD pathology is the production of Aβ peptides through the amyloidogenic processing of amyloid-β protei Show more
The accumulation of amyloid-β (Aβ) peptides is a hallmark of Alzheimer's disease (AD). Central to AD pathology is the production of Aβ peptides through the amyloidogenic processing of amyloid-β protein precursor (AβPP) by β-secretase (BACE-1) and γ-secretase. Recent studies have shifted focus from Aβ plaque deposits to the more toxic soluble Aβ oligomers. One significant way in which Aβ peptides impair neuronal information processing is by influencing neurotransmitter receptor function. These receptors, including adrenergic, acetylcholine, dopamine, 5-HT, glutamate, and gamma-aminobutyric acid (GABA) receptors, play a crucial role in regulating synaptic transmission, which underlies perceptual and cognitive functions. This review explores how Aβ interacts with these key neurotransmitter receptors and how these interactions contribute to neural dysfunction in AD. Moreover, we examine how agonists and antagonists of these receptors influence Aβ pathology, offering new perspectives on potential therapeutic strategies to curb AD progression effectively and improve patients' quality of life. Show less
📄 PDF DOI: 10.1177/13872877251342273
BACE1
Xin Liu, Jun-He Cui, Chuang Luan +5 more · 2025 · International journal of biological macromolecules · Elsevier · added 2026-04-24
Alzheimer's disease (AD), the most common neurodegenerative disease in humans, has been a major medical challenge. Lactoferrin (Ltf) in salivary glands might be identified as a potential detectable bi Show more
Alzheimer's disease (AD), the most common neurodegenerative disease in humans, has been a major medical challenge. Lactoferrin (Ltf) in salivary glands might be identified as a potential detectable biomarker in AD and a therapeutic target for AD. Pharmaceutical studies directly addressing this biomarker, though, are scarce. Using a computational strategy for drug repurposing, we explored the proximal neighborhood of Ltf by exploring its interactome and regulatory constellations. We aimed to focus on the discovery of potential therapeutic agents for AD. Based on extensive analytical evaluation comprising structural congruence scales, profiling disease clusters, pathway enrichment analyses as well as molecular docking, SPR, in vivo studies, and immunofluorescence assays, our research identified three candidate repurposed drugs: Lovastatin, SU-11652, and SB-239063. Taken together, these results highlight strong binding affinities of the drug candidates to Ltf. In vitro studies showed that such compounds decrease β-amyloid (Aβ) production by increasing the fluorescence signal emitted by Ltf in N2a-sw cells, and that they act by modulating the expression of amyloidogenic pathway-associated enzymes (BACE1 and APH1α). In addition, in vivo studies showed a concomitant reduction in the expression levels of amyloidogenic pathway-related enzymes (BACE1 or APH1α). Thus, computational studies have focused on Ltf interactions that may recommend drug repurposing strategies and options for AD. Show less
no PDF DOI: 10.1016/j.ijbiomac.2025.144230
BACE1
Wenjing Feng, Mengwei Ju, Tao Wang +7 more · 2025 · Alzheimer's research & therapy · BioMed Central · added 2026-04-24
Oxysterols, gut metabolites, and N6-methyladenosine (m6A) are extensively implicated in the pathogenesis of cognitive dysfunction, while their alterations in different stages of mild cognitive impairm Show more
Oxysterols, gut metabolites, and N6-methyladenosine (m6A) are extensively implicated in the pathogenesis of cognitive dysfunction, while their alterations in different stages of mild cognitive impairment (MCI) have not been elucidated. Therefore, this study was conducted to explore the associations of oxysterols, gut metabolites, and m6A methylation profiles in early MCI (EMCI) and late MCI (LMCI) individuals. Liquid chromatography-mass spectrometry, untargeted metabolomic analysis, and m6A mRNA Epitranscriptomic Microarray were used to detect the characteristics of serum oxysterols (n = 35/group), fecal gut metabolites (n = 30/group), and m6A in whole blood (n = 4/group) respectively. The concentration of serum β-amyloid (Aβ) was detected with ELISA (n = 25/group). The gene expression of amyloid precursor protein (APP) and its key enzyme β-secretase (BACE1) in whole blood were measured by quantitative real-time PCR (n = 25/group). EMCIs and LMCIs, especially LMCIs, exhibited poorer performance in almost all global and multidimensional cognitive tests. Serum 27-hydroxycholesterol (27-OHC) and 24S-hydroxycholesterol (24S-OHC) were elevated in EMCI and LMCI groups. Changes in gut metabolites occurred mainly in the EMCI group, in which several gut metabolites, including Procyanidin dimer B7 and Phorbol myristate, were significantly decreased. The m6A methylation landscape of EMCIs and LMCIs obviously differed from Controls. Hypomethylated mRNAs accounted for the majority and were mainly accompanied by downregulated mRNAs, which was consistent with the downregulated expression of the m6A writer methyltransferase-like 4 (METTL4). 27-OHC and 24S-OHC combined with various gut metabolites significantly distinguished between MCI subgroups from healthy controls (EMCI/Control: AUC = 0.877; LMCI/Control: AUC = 0.952). Heatmap revealed the correlation between Phorbol myristate and differentially m6A-methylated mRNAs. Differentially expressed gut metabolites and methylated mRNAs were commonly enriched in 34 KEGG metabolic pathways, including cholesterol metabolism and neurodegenerative disease-related pathways. Our study explored the altered oxysterols, gut metabolites, and m6A methylation and their associations in different stages of MCI. The potential function of aberrant gut metabolites in oxysterols and m6A methylation driving MCI progression warrants further mechanistic investigation. Show less
📄 PDF DOI: 10.1186/s13195-025-01743-5
BACE1
Zhijuan Tang, Fang Wang, Jintao Lv +7 more · 2025 · Neurotoxicology · Elsevier · added 2026-04-24
Excessive aluminum exposure is a contributing factor in several neurodegenerative diseases. Natural plant compounds such as Licochalcone A have been shown to have significant neuroprotective effects i Show more
Excessive aluminum exposure is a contributing factor in several neurodegenerative diseases. Natural plant compounds such as Licochalcone A have been shown to have significant neuroprotective effects in vivo and in vitro. In this study, we aim to elucidate the neuroprotective effect of Licochalcone A against aluminum chloride-induced neurotoxicity and its possible mechanism. Adult zebrafish and PC12 cells were used as animal and cell models. Zebrafish and PC12 cells were treated with excessive aluminum trichloride (100 μg/L aluminum chloride hexahydrate solutions for zebrafish or 500 μM Al-malt solution for PC12 cells) to cause neuronal damage. The neuroprotective effect of Licochalcone A was evaluated by measuring ROS production, Aβ Show less
no PDF DOI: 10.1016/j.neuro.2025.04.011
BACE1
Nan Wang, Xin-Zhu Li, Xiao-Wen Jiang +10 more · 2025 · Molecular neurobiology · Springer · added 2026-04-24
Alzheimer's disease (AD) is a multifactorial neuropathology characterized by the accumulation of amyloid-beta (Aβ) plaques, neurofibrillary tangles (NFTs) and cholinergic system dysfunction. At presen Show more
Alzheimer's disease (AD) is a multifactorial neuropathology characterized by the accumulation of amyloid-beta (Aβ) plaques, neurofibrillary tangles (NFTs) and cholinergic system dysfunction. At present, there is no effective treatment strategy for AD. Our previous research showed that ZJQ-3F acts as an inhibitor of AChE/BACE1/GSK3β, and showed good blood-brain barrier permeability, appropriate bioavailability and oral safety. In order to further study, the protective effect of ZJQ-3F on APP/PS1/Tau transgenic mice was determined. APP/PS1/Tau transgenic mice model of AD was treated with ZJQ-3F from the age of 8 to 12 months, and then behavioral tests was conducted. Western blot, immunohistochemistry and immunofluorescence staining were used to evaluate the level of tau protein, Aβ plaques and synaptic function. Our results revealed that administration of ZJQ-3F could improve the cognitive function of APP/PS1/Tau transgenic mice. In addition, compared with APP/PS1/Tau mice, the protein expression levels of tau protein phosphorylation site at Ser396, Thr212 and Thr181 in the cortex and hippocampus of ZJQ-3F treated mice was significantly decreased. Moreover, the results showed that ZJQ-3F significantly reduced the deposition of Aβ in the cortex and hippocampus. Furthermore, the results indicated that the protein expression levels of PSD95, SYP and SYT in the cortex and hippocampus were increased markedly after ZJQ-3F was given. Our studies suggest that the chronic administration of ZJQ-3F can improve learning and memory ability, reduce tau protein phosphorylation, reduce Aβ deposition and improve synaptic dysfunction in APP/PS1/Tau transgenic model of AD, indicating that ZJQ-3F can be used as a multi-target inhibitor to slow down the progress of AD. Show less
📄 PDF DOI: 10.1007/s12035-025-04982-7
BACE1
Zhizhong Wang, Zhiyong Li, Ailong Lin +4 more · 2025 · PloS one · PLOS · added 2026-04-24
Amyloid cerebrovascular disease, primarily driven by the accumulation of amyloid-beta (Aβ) peptides, is intricately linked to neurodegenerative disorders like Alzheimer's disease. BACE1 (beta-site amy Show more
Amyloid cerebrovascular disease, primarily driven by the accumulation of amyloid-beta (Aβ) peptides, is intricately linked to neurodegenerative disorders like Alzheimer's disease. BACE1 (beta-site amyloid precursor protein cleaving enzyme 1) plays a critical role in the production of Aβ, making it a key therapeutic target. In the current work, a CNS library of ChemDiv database containing 44085 compounds was screened against the BACE1 protein. Initially, a structure-based pharmacophore hypothesis was constructed, followed by virtual screening, with the screened hits docked to the BACE1 protein to determine the optimal binding modes. The docking results were examined using the glide gscore and chemical interactions of the docked molecules. The cutoff value of -5 kcal/mol was used to select hits with high binding affinities. A total of seven hits were chosen based on the glide g score. Furthermore, the possible binding mechanisms of the docked ligands were investigated, and it was discovered that all seven selected ligands occupied the same site in the predicted binding pocket of protein. The bioactivity scores of the compounds demonstrated that the chosen compounds possess the features of lead compounds. The toxicity risks and ADMET features of the selected hits were anticipated, and four compounds, J032-0080, SC13-0774, V030-0915, and V006-5608 were chosen for stability analysis. The selected hits were extremely stable and strongly bound to the BACE1 pocket, and conformational changes caused by RMSD, RMSF, and protein-ligand interactions were assessed using MD modeling. Similarly, principal component analysis revealed a large static number of hydrogen bonds. The MM/GBSA binding free energies maps revealed a significant energy contribution in the binding of selected hits to BACE1. The binding free energy landscapes indicated that the hits were bound with a high binding affinity. Thus, the hits could serve as lead compounds in biophysical investigations to limit the biological activity of the BACE1 protein. Show less
📄 PDF DOI: 10.1371/journal.pone.0317716
BACE1
Danyang Zhang, Xiaoshi He, Yinbo Wang +8 more · 2025 · International journal of molecular sciences · MDPI · added 2026-04-24
Diabetes constitutes a risk factor for cognitive impairment, whereas insulin resistance serves as the shared pathogenesis underlying both diabetes and cognitive decline. The use of metformin for treat Show more
Diabetes constitutes a risk factor for cognitive impairment, whereas insulin resistance serves as the shared pathogenesis underlying both diabetes and cognitive decline. The use of metformin for treating cognitive impairment remains controversial. The present study found that hesperetin, a flavanone derived from citrus peel, enhanced metformin's efficacy in reducing blood sugar levels, improving insulin sensitivity, and ameliorating cognitive impairment in diabetic rats. Additionally, it reduced the required dosage of metformin to one-third of its conventional dose. Transcriptome analysis and 16S rRNA sequencing revealed that the activation of insulin and cyclic-adenosine monophosphate response element binding protein (CREB)/brain-derived neurotrophic factor (BDNF) pathways benefited from the regulation of gut microbiota and the promotion of short-chain fatty acid (SCFA) producers such as Show less
📄 PDF DOI: 10.3390/ijms26051923
BACE1
Lijun Liu, Jie Du, Huan Liu +2 more · 2025 · Xi bao yu fen zi mian yi xue za zhi = Chinese journal of cellular and molecular immunology · added 2026-04-24
Objective To explore the mechanism of lncRNA-BC200 (BC200) targeting the ubiquitination of Beta-site APP cleaving enzyme 1 (BACE1) and regulating the repair of nerve cell injury. Methods Mouse hippoca Show more
Objective To explore the mechanism of lncRNA-BC200 (BC200) targeting the ubiquitination of Beta-site APP cleaving enzyme 1 (BACE1) and regulating the repair of nerve cell injury. Methods Mouse hippocampal neuron cell line HT22 was divided into four groups: control group, oxygen-glucose deprivation/reoxygenation(OGD/R) group, OGD/R+si-NC group and OGD/R+si-BC200 group. In order to further explore the relationship between BC200 and BACE1, HT22 cells were divided into four groups: OGD/R group, OGD/R+si-BC200 group, OGD/R+si-BC200+NC group and OGD/R+si-BC200+ BACE1 group. Twenty male C57BL/6J mice were randomly assigned to the following four groups: control group, middle cerebral artery occlusion (MCAO) group, MCAO+si-BC200 group and MCAO+si-BC200+BACE1 group. The mRNA expression levels of BC200 and BACE1 in cells were measured by real-time quantitative reverse transcription polymerase chain reaction. The expressions of c-caspase-3, B-cell lymphoma 2 (Bcl2), Bcl2 associated X protein(BAX) and BACE1 were detected by western blot, and the apoptotic cells were detected by terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL) test. Results Compared with the control group, the activity of HT22 cells in OGD/R group decreased significantly, and the percentage of apoptotic cells increased significantly. Compared with OGD/R+si-NC group, the activity of HT22 cells in OGD/R+si-BC200 group increased significantly, and the percentage of apoptotic cells decreased significantly. Compared with the control group, the expression of BACE1 protein in HT22 cells in OGD/R group was significantly enhanced. Compared with OGD/R+si-NC group, the expression of BACE1 protein in HT22 cells in OGD/R+si-BC200 group decreased significantly. It was observed that after OGD/R treatment, the ubiquitination level of BACE1 decreased significantly and the expression of BACE1 protein increased significantly. After transfection with si-BC200, the ubiquitination level of BACE1 protein increased significantly, while the expression of BACE1 protein decreased significantly. Compared with OGD/R+si-BC200+NC group, the percentage of apoptotic cells, the expression of c-caspase-3 and Bax protein in HT22 cells in OGD/R+si-BC200+BACE1 group increased significantly, and the expression of Bcl2 protein decreased significantly. Compared with the control group, the number of cerebral infarction areas and TUNEL positive cells in MCAO group increased significantly, and the survival number of neurons decreased significantly. Compared with the MCAO group, the number of cerebral infarction areas and TUNEL positive cells in MCAO+si-BC200 group decreased significantly, and the survival number of neurons increased significantly, while the addition of BACE1 reversed the improvement of si-BC200 transfection. Conclusion The combination of BC200 and BACE1 inhibit the ubiquitination of BACE1, and participate in mediating the expression enhancement of BACE1 induced by OGD/R. Specific blocking of BC200/BACE1 axis may be a potential therapeutic target to protect neurons from apoptosis induced by cerebral ischemia/reperfusion. Show less
no PDF
BACE1
Jin-Qiu Li, Xiao-Han Ma, Hui Dai +3 more · 2025 · Journal of ethnopharmacology · Elsevier · added 2026-04-24
The embryos of lotus (Nelumbo nucifera Gaertn.) is a famous traditional Chinese medicine used to treat insomnia, memory decline, and dementia for a long time. However, the underlying material basis an Show more
The embryos of lotus (Nelumbo nucifera Gaertn.) is a famous traditional Chinese medicine used to treat insomnia, memory decline, and dementia for a long time. However, the underlying material basis and mechanisms of this medicine are still unclear. Isoliensinine (IL) is a major alkaloid derived from lotus embryos. Our previous research has demonstrated that IL can exert strong anti-inflammatory and neuroprotective effects in vitro. To reveal the underlying therapeutic effect and mechanism of IL on Alzheimer's disease (AD)-like mice induced by AlCl The AD-like mice were modeled by intragastric injection (i.g.) of AlCl IL (1, 3, and 10 mg/kg) treatment effectively ameliorated cognitive impairment in AD-like model mice. IL inhibited the decrease of brain index and body weight in AD-like mice and alleviated neuronal damage in the cortex and hippocampus (DG, CA1, and CA3). IL decreased the levels of Ca IL has a significant therapeutic effect on pathological alterations and cognitive impairment in AlCl Show less
no PDF DOI: 10.1016/j.jep.2025.119567
BACE1
Danlei Bi, Hong Bao, Xiaoli Yang +18 more · 2025 · Neuron · Elsevier · added 2026-04-24
Neural hyperexcitability has been clinically associated with amyloid-β (Aβ) pathology and cognitive impairment in Alzheimer's disease (AD). Here, we show that decreased GABA
no PDF DOI: 10.1016/j.neuron.2025.01.030
BACE1
Yi Zhang, Yifei Wang, Fei Zhao · 2025 · Molecular neurobiology · Springer · added 2026-04-24
Alzheimer's disease (AD) is the most common form of dementia and seriously affects people's quality of life. In recent years, many circulating microRNAs (miRNAs) have been reported as potential diagno Show more
Alzheimer's disease (AD) is the most common form of dementia and seriously affects people's quality of life. In recent years, many circulating microRNAs (miRNAs) have been reported as potential diagnostic biomarkers for AD. However, there are no reliable miRNAs for early diagnosis of AD because miRNAs are dynamically changing during the disease process. The present study was to seek reliable biomarkers for early diagnosis of AD by detecting changes in miRNAs in plasma from young APPswe/PS1Δ9 double-transgenic mice (APP/PS1 mice) using a quantitative real-time PCR (qRT-PCR) method. Some behavioral experiments and pathological tests were used to characterize the progress of AD in APP/PS1 transgenic mice. The results showed that the expression levels of several plasma miRNAs targeting BACE1 and APP showed consistent trends in the early stages of APP/PS1 mice. The expression levels of miR-34a-5p, miR-29c-3p, miR-107-3p, and miR-101a-3p in the plasma of APP/PS1 female mice decreased with cognitive decline, demonstrating their potential as biomarkers for early diagnosis of female AD patients. The expression levels of these miRNAs fluctuated significantly in APP/PS1 male mice, and the reason for this difference may be related to the biological sex differences in AD. This fluctuation may serve as an indicative risk signal for the early stage of AD in male patients. Show less
no PDF DOI: 10.1007/s12035-025-04743-6
BACE1
Xuan-Ling Li, Zhi-Heng Lin, Si-Ru Chen +7 more · 2025 · Phytomedicine : international journal of phytotherapy and phytopharmacology · Elsevier · added 2026-04-24
People with mild cognitive impairment (MCI) carry a considerable risk of developing dementia. Studies have shown that female sex hormones have long-lasting neuroprotective and anti-aging properties, a Show more
People with mild cognitive impairment (MCI) carry a considerable risk of developing dementia. Studies have shown that female sex hormones have long-lasting neuroprotective and anti-aging properties, and the increased risk of MCI and AD is associated with the lack of estrogen during menopause. Previous studies have shown that Tiao Geng Decoction (TGD) may have antioxidant and anti apoptotic properties, which may prevent neurodegenerative diseases. However, whether TGD is effective in improving mild cognitive impairment due to postmenopausal estrogen deficiency and its potential pharmacological mechanisms remain unclear. The aim of this study was to investigate the possible pharmacological mechanisms of TGD in preventing postmenopausal MCI. We utilized RNA-seq technology to screen for differentially expressed genes (DEGs) and enrichment pathways in the hippocampal tissue of different groups of mice. Additionally, we adopted single-cell sequencing technology to study the cell types of Alzheimer's disease (AD) group and Normal Control (NC) group, the differential marker genes of each cell subgroup, and the GO enrichment analysis of each cell type. Both RNA sequencing and single-cell sequencing results showed a significant correlation between TGD and NF-κb pathway in improving mild cognitive impairment in postmenopausal women. The experimental verification results showed that the spatial learning and memory abilities of APP/PS1 model mice were weakened after ovariectomy, and the reproductive cycle on vaginal smears was in the interphase of diestrus. The levels of serum E2, and P-tau181 in mice were significantly down regulated, while the levels of brain tissue homogenate A β 42, IL-1 β, and IL-18 were significantly up-regulated, indicating successful modeling. Combining Western blotting, RT-qPCR, and transmission electron microscopy analyses, it was found that the low estrogen environment induced by oophorectomy can activate the NF-κb signaling pathway, activate the expression of NLRP3 inflammasome and A β secretase BACE1, and induce neuroinflammatory damage in hippocampal astrocytes. These results conform to the modeling characteristics of MCI. After TGD intervention, the spatial learning and memory abilities of MCI mice were significantly improved. The pharmacological validation results indicated that high concentration doses of TGD had a more significant effect on MCI. Subsequently, we used high concentration TGD (0.32 g/ml) as the traditional Chinese medicine group for further validation, protein blotting and RT-qPCR results indicated that TGD can effectively stimulate the secretion of ER α and ER β, inhibit the NF-κb pathway, downregulate BACE1, and inhibit the expression of NLRP3 inflammasome related proteins. In addition, the immunofluorescence results of hippocampal astrocytes showed that TGD can effectively facilitate the expression of AQP1 and significantly lower the sedimentation of A β compared with the model group. Our research suggests that there is a high correlation between a low estrogen environment and the occurrence and development of MCI. TGD may regulate the ERs/NF - κ b/AQP1 signaling pathway, promote estrogen secretion, activate AQP1, reduce A β deposition, reverse MCI neuroinflammatory injury, improve mild cognitive impairment, and prevent the occurrence of AD. This study revealed for the first time that TGD may be a potential new alternative drug for preventing and improving menopausal MCI. Show less
no PDF DOI: 10.1016/j.phymed.2025.156391
BACE1
Yanan Xu, Zelin Wang, Tiewen Jia +1 more · 2025 · PloS one · PLOS · added 2026-04-24
Systemic lupus erythematosus (SLE) is a complex and incurable autoimmune disease, so several drug remission for SLE symptoms have been developed and used at present. However, treatment varies by patie Show more
Systemic lupus erythematosus (SLE) is a complex and incurable autoimmune disease, so several drug remission for SLE symptoms have been developed and used at present. However, treatment varies by patient and disease activity, and existing medications for SLE were far from satisfactory. Novel drug targets to be found for SLE therapy are still needed. Mendelian randomization (MR), an observational study way, was performed to explore potential drug targets for SLE using protein quantitative trait loci (pQTL) from recently published genome-wide association studies (GWAS) of cerebrospinal fluid (CSF) and plasma proteins, which obtained genetic instruments for 154 CSF proteins of 971 participants, and 734 plasma proteins of 23591 participants. Bidirectional Mendelian randomization analysis, colocalization analysis, and phenotype scanning were performed to find key proteins for SLE. In addition, external data verification was implemented to further consolidate the Mendelian randomization findings. Candidate proteins as targets to find drugs and discuss the druggability. Finally, Network pharmacology and molecular docking methods were used to verify the effects of Voclosporin and Cyclosporine on SLE targets. Protein-protein interaction (PPI) and core target analysis of candidate drugs and SLE overlapping targets were performed to identify potential hub targets and interactions. The affinity between drug targets and SLE targets was confirmed by molecular docking. In the preliminary analysis, we identified four key proteins as possible drug targets in CSF and plasma proteins, included ICAM-1(P = 4.62E-05, OR = 0.90(0.86, 0.95)), sICAM-1(P = 4.62E-05, OR = 0.49(0.35, 0.69)), FCG2B (P = 7.63E-11, OR = 0.57(0.48, 0.67)), PPP3CA; PPP3R1 (P = 5.47E-07, OR = 0.66(0.57, 0.78)). Among them, ICAM1 was detected in both CSF and plasma proteins. By excluding reverse causality, confounding factors, and linkage disequilibrium (LD), we identified PPP3CA; PPP3R1 as novel drug targets for SLE, including Voclosporin and Cyclosporine. Finally, the Drugbank database shows that novel drugs contain 33 targets for treating SLE. PPI suggested that SIRT1, ACE, PTGS2, and BACE1 were pivotal targets for SLE treatment. In addition, the molecular docking showed that the bioactive molecules of Voclosporin and Cyclosporine had a good affinity with the target of SLE. Our integrative analysis suggested that levels of circulating PPP3CA; PPP3R1 had causal effects on SLE risk and served as potential treatment targets. Moreover, this study provides new evidence for Voclosporin as an SLE treatment through Mendelian randomization and Network pharmacology, and warrants further clinical investigation. Show less
📄 PDF DOI: 10.1371/journal.pone.0316481
BACE1
Yijia Feng, Shengya Wang, Danlu Yang +13 more · 2025 · Alzheimer's & dementia : the journal of the Alzheimer's Association · Wiley · added 2026-04-24
Interferon-induced transmembrane protein 3 (IFITM3) modulates γ-secretase in Alzheimer's Disease (AD). Although IFITM3 knockout reduces amyloid β protein (Aβ) production, its cell-specific effect on A Show more
Interferon-induced transmembrane protein 3 (IFITM3) modulates γ-secretase in Alzheimer's Disease (AD). Although IFITM3 knockout reduces amyloid β protein (Aβ) production, its cell-specific effect on AD remains unclear. Single nucleus RNA sequencing (snRNA-seq) was used to assess IFITM3 expression. Adeno-associated virus-BI30 (AAV-BI30) was injected to reduce IFITM3 expression in the cerebrovascular endothelial cells (CVECs). The effects on AD phenotypes in cells and AD mice were examined through behavioral tests, two-photon imaging, flow cytometry, Western blot, immunohistochemistry, and quantitative polymerase chain reaction assay (qPCR). IFITM3 expression was increased in the CVECs of patients with AD. Overexpression of IFITM3 in primary endothelial cells enhanced Aβ generation through regulating beta-site APP cleaving enzyme 1 (BACE1) and γ-secretase. Aβ further increased IFITM3 expression, creating a vicious cycle. Knockdown of IFITM3 in CVECs decreased Aβ accumulation within cerebrovascular walls, reduced Alzheimer's-related pathology, and improved cognitive performance in AD transgenic mice. Knockdown of IFITM3 in CVECs alleviates AD pathology and cognitive impairment. Targeting cerebrovascular endothelial IFITM3 holds promise for AD treatment. Interferon-induced transmembrane protein 3 (IFITM3) expression was increased in the cerebrovascular endothelial cells (CVECs) of patients with Alzheimer's Disease (AD). Cerebrovascular endothelial IFITM3 regulates amyloid β protein (Aβ) generation through regulating beta-site APP cleaving enzyme 1 (BACE1) and γ-secretase. Knockdown of IFITM3 in CVECs reduces Aβ deposits and improves cognitive impairments in AD transgenic mice. Cerebrovascular endothelial IFITM3 could be a potential target for the treatment of AD. Show less
📄 PDF DOI: 10.1002/alz.14543
BACE1
Zhuoze Wu, Xiaojie Liu, Yuntai Wang +3 more · 2025 · Neuroscience bulletin · Springer · added 2026-04-24
Alzheimer's disease (AD), a neurodegenerative disorder with complex etiologies, manifests through a cascade of pathological changes before clinical symptoms become apparent. Among these early changes, Show more
Alzheimer's disease (AD), a neurodegenerative disorder with complex etiologies, manifests through a cascade of pathological changes before clinical symptoms become apparent. Among these early changes, alterations in the expression of non-coding RNAs (ncRNAs) have emerged as pivotal events. In this study, we focused on the aberrant expression of ncRNAs and revealed that Lamr1-ps1, a pseudogene of the laminin receptor, significantly exacerbates early spatial learning and memory deficits in APP/PS1 mice. Through a combination of bioinformatics prediction and experimental validation, we identified the miR-29c/Bace1 pathway as a potential regulatory mechanism by which Lamr1-ps1 influences AD pathology. Importantly, augmenting the miR-29c-3p levels in mice ameliorated memory deficits, underscoring the therapeutic potential of targeting miR-29c-3p in early AD intervention. This study not only provides new insights into the role of pseudogenes in AD but also consolidates a foundational basis for considering miR-29c as a viable therapeutic target, offering a novel avenue for AD research and treatment strategies. Show less
📄 PDF DOI: 10.1007/s12264-024-01336-6
BACE1
Qiuyun Tian, Junjie Li, Bin Wu +16 more · 2025 · The Journal of clinical investigation · added 2026-04-24
Posttranslational modification (PTM) of the amyloid precursor protein (APP) plays a critical role in Alzheimer's disease (AD). Recent evidence reveals that lactylation modification, as a novel PTM, is Show more
Posttranslational modification (PTM) of the amyloid precursor protein (APP) plays a critical role in Alzheimer's disease (AD). Recent evidence reveals that lactylation modification, as a novel PTM, is implicated in the occurrence and development of AD. However, whether and how APP lactylation contributes to both the pathogenesis and cognitive function in AD remains unknown. Here, we observed a reduction in APP lactylation in AD patients and AD model mice and cells. Proteomic mass spectrometry analysis further identified lysine 612 (APP-K612la) as a crucial site for APP lactylation, influencing APP amyloidogenic processing. A lactyl-mimicking mutant (APPK612T) reduced amyloid-β peptide (Aβ) generation and slowed down cognitive deficits in vivo. Mechanistically, APPK612T appeared to facilitate APP trafficking and metabolism. However, lactylated APP entering the endosome inhibited its binding to BACE1, suppressing subsequent cleavage. Instead, it promoted protein interaction between APP and CD2-associated protein (CD2AP), thereby accelerating the endosomal-lysosomal degradation pathway of APP. In the APP23/PS45 double-transgenic mouse model of AD, APP-Kla was susceptible to L-lactate regulation, which reduced Aβ pathology and repaired spatial learning and memory deficits. Thus, these findings suggest that targeting APP lactylation may be a promising therapeutic strategy for AD in humans. Show less
📄 PDF DOI: 10.1172/JCI184656
BACE1
Xiaolei Song, Chenchen Wang, Qin Ding +8 more · 2025 · Journal of controlled release : official journal of the Controlled Release Society · Elsevier · added 2026-04-24
Alzheimer's disease (AD) is an irreversible and progressive neurodegenerative disorder. The vicious circle between amyloid-β peptide (Aβ) overgeneration and microglial dysfunction is an important path Show more
Alzheimer's disease (AD) is an irreversible and progressive neurodegenerative disorder. The vicious circle between amyloid-β peptide (Aβ) overgeneration and microglial dysfunction is an important pathological event that promotes AD progression. However, therapeutic strategies toward only Aβ or microglial modulation still have many problems. Herein, inspired by the Aβ transportation, an Aβ-derived peptide (CKLVFFAED) engineered biomimetic nanodelivery system (MK@PC-R NPs) is reported for realizing BBB penetration and reprogram neuron and microglia in AD lesion sites. This hollow mesoporous Prussian blue-based MK@PC-R NPs carrying curcumin and miRNA-124 can down-regulate β secretase expression, thereby inhibiting Aβ production and reducing Aβ-induced neurotoxicity. Meanwhile, MK@PC-R NPs with excellent antioxidant and anti-inflammatory properties could normalize the microglial phenotype and promote Aβ degradation, providing neuroprotection. As expected, after treatment with MK@PC-R NPs, the Aβ burdens, neuron damages, neuroinflammation, and memory deficits of transgenic AD mice (APP/PS1 mice) are significantly attenuated. Overall, this biomimetic nanodelivery system with anti-Aβ and anti-inflammatory properties provides a promising strategy for the multi-target therapy of early AD. Show less
no PDF DOI: 10.1016/j.jconrel.2024.12.060
BACE1
Huijie Yang, Fangyu Wang, Peijun Zhao +12 more · 2025 · International journal of biological macromolecules · Elsevier · added 2026-04-24
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by hyperphosphorylation of tau, neuroinflammation, and amyloid-beta (Aβ) plaques. Lead (Pb) exposure has been linked to an increa Show more
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by hyperphosphorylation of tau, neuroinflammation, and amyloid-beta (Aβ) plaques. Lead (Pb) exposure has been linked to an increased risk of AD and neuroinflammation. The purpose of this study is to determine if black soybean peptide (BSP1) may reduce neuroinflammation caused by Pb and associated AD-like pathology. Pb exposure was given to mouse hippocampus HT22 cells in the presence or absence of BSP1, positive control resveratrol (Rsv), or the SIRT1 inhibitor EX-527. Our findings suggest that BSP1 downregulates the expression of beta-secretase (BACE1) and amyloid precursor protein (APP), inhibits tau phosphorylation, and reduces Aβ1-42 deposition. In addition, BSP1 effectively alleviated Pb-induced neuroinflammation by reducing the phosphorylation of NF-κB and the expression of pro-inflammatory cytokines (IL-1β, TNF-α, NLRP3, and IL-18). BSP1 provides neuroprotective effect via phosphorylating LKB1 and AMPK, inhibiting mTOR signaling, and activating the AMPK/SIRT1 pathway. These results suggest that BSP1 may be therapeutically beneficial for preventing or treating AD by reducing Pb-induced neuroinflammation. Show less
no PDF DOI: 10.1016/j.ijbiomac.2024.138404
BACE1
Yubo Han, Zhenhua Quan, Miao Tian +4 more · 2025 · Immunopharmacology and immunotoxicology · Taylor & Francis · added 2026-04-24
Obesity is a chronic inflammatory disorder, which promotes the progression of metabolic disorders. MicroRNA (miR)-6838-5p is dysregulated and participates in the progression of several disorder models Show more
Obesity is a chronic inflammatory disorder, which promotes the progression of metabolic disorders. MicroRNA (miR)-6838-5p is dysregulated and participates in the progression of several disorder models. To explore the role and mechanism of miR-6838-5p in insulin resistance. Mice were fed with high-fat diet (HFD) to construct an obesity animal model. The role of miR-6838-5p was evaluated by insulin tolerance test (ITT), glucose tolerance test (GTT), homeostasis model assessment of insulin resistance (HOMA-IR) analysis, enzyme-linked immunosorbent assay (ELISA) and western blot assays. The potential target of miR-6838-5p was screened through the starBase online website and confirmed by the luciferase assay. HFD supply induced a prominent increase in the body weight, white adipose tissue (WAT) weight, the area under the curve (AUC) of GTT and ITT, HOMA-IR, the serum level of insulin and the serum concentrations and relative protein levels of interleukin (IL)-1β, IL-6 and monocyte chemoattractant protein-1 (MCP-1) accompanied with reduced levels of IL-10 in mice. The level of miR-6838-5p was reduced in HFD-fed mice. Upregulation of miR-6838-5p partly reversed the above-mentioned indicators. Moreover, miR-6838-5p directly targeted to β-site amyloid precursor protein cleaving enzyme1 (BACE1) and negatively regulated the BACE1 expression. Downregulation of BACE1 improved insulin sensitivity and inflammatory mediators release involving in AKT/GSK3β signaling pathway in HFD-fed mice. Besides, overexpression of BACE1 counteracted the depressant role of miR-6838-5p overexpression in insulin resistance and inflammatory factors release in HFD-fed mice. MiR-6838-5p/BACE1 axis regulated insulin resistance and inflammatory factors release in HFD-fed mice. Show less
no PDF DOI: 10.1080/08923973.2024.2430668
BACE1
Hai-Hui Guo, Chun-Xu Li, Min Yang +5 more · 2025 · Phytochemistry · Elsevier · added 2026-04-24
Gentidelasides A-G (1-7) seven unreported loganin derivatives and fourteen known compounds (8-21) were isolated from the flowers of Gentiana delavayi Franch. Their structures including absolute config Show more
Gentidelasides A-G (1-7) seven unreported loganin derivatives and fourteen known compounds (8-21) were isolated from the flowers of Gentiana delavayi Franch. Their structures including absolute configurations were unambiguously elucidated by analysis of extensive NMR spectroscopy, ECD, and HRESIMS, as well as enzymatic hydrolysis. In vitro bioassay, compound 7 showed obvious inhibitory effects on the production of Aβ40 and Aβ42, with IC Show less
no PDF DOI: 10.1016/j.phytochem.2024.114333
BACE1
Zhengyu Wang, Dan Wu, Xinyi Hu +5 more · 2025 · Journal of ethnopharmacology · Elsevier · added 2026-04-24
Chronic sleep deprivation (CSD) can result in neuronal damage, synaptic dysfunction, Aβ production, neuroinflammation, and ultimately cognitive deterioration. WuYou Decoction (WYD), a contemporary pre Show more
Chronic sleep deprivation (CSD) can result in neuronal damage, synaptic dysfunction, Aβ production, neuroinflammation, and ultimately cognitive deterioration. WuYou Decoction (WYD), a contemporary prescription, has shown promise in enhancing sleep quality and cognitive performance in individuals with insomnia. However, the specific molecular mechanisms responsible for the neuroprotective effects of WYD on CSD remain incompletely understood. This study aimed to investigate the neuroprotective effects of WYD on the CSD model and its molecular mechanism. UHPLC-MS/MS analysis was utilized to analyze the active ingredients of WYD extract. The study employed the multi-platform water environment method to establish the CSD model in rats. Subsequent to treatment with varying doses of WYD in CSD rats, cognitive function and pathological alterations in hippocampus and cortex, including neuronal damage, synaptic dysfunction, Aβ production, and neuroinflammation, were evaluated through a combination of Morris Water Maze test, HE staining, Nissl staining, Golgi-Cox staining, Transmission electron microscope, ELISA, Immunohistochemistry staining, Immunofluorescence staining and Western blot. UHPLC-MS/MS analysis revealed a total of 99 active ingredients were identified from the WYD extract. The administration of WYD exhibited a mitigation of cognitive decline in the model of CSD, as evidenced by increased neuron count in the hippocampus and cortex, and improved density and length of dendritic spines in these brain regions. Furthermore, WYD was found to suppress the Aβ production, and inhibit the expression of BACE1, PS1, GFAP, IBA1, IL-1β, IL-6, TNF-α, phosphorylated IκBα (Ser32) and phosphorylated NF-κB p65 (Ser536) in the hippocampus and cortex, while also increasing the levels of PSD95, SYN1, ADAM10, IDE, SIRT1 and Nrf2. WYD exhibits neuroprotective properties in CSD, potentially through modulation of the Aβ-related enzymes and SIRT1/Nrf2/NF-κB pathway. Show less
no PDF DOI: 10.1016/j.jep.2024.118939
BACE1
Yisheng Chen, Xiaofeng Chen, Zhiwen Luo +16 more · 2025 · Journal of advanced research · Elsevier · added 2026-04-24
Alzheimer's Disease (AD), a progressive neurodegenerative disorder, is marked by cognitive deterioration and heightened neuroinflammation. The influence of Insulin-like Growth Factor 1 Receptor (IGF1R Show more
Alzheimer's Disease (AD), a progressive neurodegenerative disorder, is marked by cognitive deterioration and heightened neuroinflammation. The influence of Insulin-like Growth Factor 1 Receptor (IGF1R) and its post-translational modifications, especially sumoylation, is crucial in understanding the progression of AD and exploring novel therapeutic avenues. This study investigates the impact of exercise on the sumoylation of IGF1R and its role in ameliorating AD symptoms in APP/PS1 mice, with a specific focus on neuroinflammation and innovative therapeutic strategies. APP/PS1 mice were subjected to a regimen of moderate-intensity exercise. The investigation encompassed assessments of cognitive functions, alterations in hippocampal protein expressions, neuroinflammatory markers, and the effects of exercise on IGF1R and SUMO1 nuclear translocation. Additionally, the study evaluated the efficacy of KPT-330, a nuclear export inhibitor, as an alternative to exercise. Exercise notably enhanced cognitive functions in AD mice, possibly through modulations in hippocampal proteins, including Bcl-2 and BACE1. A decrease in neuroinflammatory markers such as IL-1β, IL-6, and TNF-α was observed, indicative of reduced neuroinflammation. Exercise modulated the nuclear translocation of SUMO1 and IGF1R in the hippocampus, thereby facilitating neuronal regeneration. Mutant IGF1R (MT IGF1R), lacking SUMO1 modification sites, showed reduced SUMOylation, leading to diminished expression of pro-inflammatory cytokines and apoptosis. KPT-330 impeded the formation of the IGF1R/RanBP2/SUMO1 complex, thereby limiting IGF1R nuclear translocation, inflammation, and neuronal apoptosis, while enhancing cognitive functions and neuron proliferation. Moderate-intensity exercise effectively mitigates AD symptoms in mice, primarily by diminishing neuroinflammation, through the reduction of IGF1R Sumoylation. KPT-330, as a potential alternative to physical exercise, enhances the neuroprotective role of IGF1R by inhibiting SUMOylation through targeting XPO1, presenting a promising therapeutic strategy for AD. Show less
📄 PDF DOI: 10.1016/j.jare.2024.03.025
BACE1
Kecheng Li, Xiaoli Zhou, Wenna Liu +4 more · 2025 · Cells · MDPI · added 2026-04-24
Sperm flagellum defects are tightly associated with male infertility. Centriolar satellites are small multiprotein complexes that recruit satellite proteins to the centrosome and play an essential rol Show more
Sperm flagellum defects are tightly associated with male infertility. Centriolar satellites are small multiprotein complexes that recruit satellite proteins to the centrosome and play an essential role in sperm flagellum biogenesis, but the precise mechanisms underlying this role remain unclear. Show less
📄 PDF DOI: 10.3390/cells14151135
BBS4
Qinfei Zhao, Weiquan Hu, Yu Xia +7 more · 2025 · Scientific reports · Nature · added 2026-04-24
Osteosarcoma, an aggressive bone malignancy predominantly affecting children and adolescents, is characterized by a poor prognosis and high mortality rates. The development of reliable prognostic tool Show more
Osteosarcoma, an aggressive bone malignancy predominantly affecting children and adolescents, is characterized by a poor prognosis and high mortality rates. The development of reliable prognostic tools is critical for advancing personalized treatment strategies. However, identifying robust gene signatures to predict osteosarcoma outcomes remains a significant challenge. In this study, we analyzed gene expression data from 138 osteosarcoma samples across two multicenter cohorts and identified 14 consensus prognosis-associated genes via univariate Cox regression analysis. Using 66 combinations of 10 machine learning (ML) algorithms, we developed a machine learning-derived prognostic signature (MLDPS) optimized by the average C-index across TARGET, GSE21257, and merged cohorts. The MLDPS effectively stratified osteosarcoma patients into high- and low-risk score groups, achieving strong predictive performance for 1-, 3-, and 5-year overall survival (AUC range: 0.852 - 0.963). The MLDPS, comprising seven genes (CTNNBIP1, CORT, DLX2, TERT, BBS4, SLC7A1, NKX2-3), exhibited superior predictive accuracy compared to 10 established gene signatures. The findings of the MLDPS carry significant clinical implications for osteosarcoma treatment. Patients with a high-risk score demonstrated worse prognosis, increased metastasis risk, reduced immune infiltrations, and greater sensitivity to immunotherapy. Conversely, low-risk patients exhibited prolonged survival and distinct drug sensitivities. These findings underscore the potential of MLDPS to guide risk stratification, inform personalized therapeutic strategies, and improve clinical management in osteosarcoma. Show less
📄 PDF DOI: 10.1038/s41598-025-00179-z
BBS4
Haoyang Ge, Chunling Shen, Wenfeng Xiong +7 more · 2025 · Cell & bioscience · BioMed Central · added 2026-04-24
Recent research has emphasized the significance of testis-specific serine proteases in regulating various aspects of sperm maturation and function. Among them, serine protease 55 (PRS55) plays an impo Show more
Recent research has emphasized the significance of testis-specific serine proteases in regulating various aspects of sperm maturation and function. Among them, serine protease 55 (PRS55) plays an important role in the energy metabolism of sperm and is essential for male fertility in mice. A recent case study further suggests its potential importance to human fertility. However, the underlying molecular mechanism by which PRS55 influences sperm function are still not well understood. The present study aims to investigate these mechanisms further. In this study, we found impaired mitochondrial function in Prss55 Our study demonstrates that PRSS55 interacts with BCKDK and BCKDHA, and regulates BCAA metabolism and energy homeostasis, thereby facilitating sperm migration. Our study provides a biological rationale for PRSS55 as a potential therapeutic target for the treatment of male infertility in clinical. Show less
📄 PDF DOI: 10.1186/s13578-025-01511-w
BCKDK
Moeko Sakamoto, Nao Hasuzawa, Lixiang Wang +12 more · 2025 · Frontiers in endocrinology · Frontiers · added 2026-04-24
Sodium-glucose cotransporter 2 inhibitors (SGLT2i) confer cardio-renal protection, and recent work implicates enhanced branched-chain amino acid (BCAA) catabolism as a potential mechanism in the heart Show more
Sodium-glucose cotransporter 2 inhibitors (SGLT2i) confer cardio-renal protection, and recent work implicates enhanced branched-chain amino acid (BCAA) catabolism as a potential mechanism in the heart. Whether SGLT2i also promotes renal BCAA catabolism is largely unknown. We hypothesized that SGLT2i enhances renal BCAA catabolism independently of glycemic effects. We conducted a prospective, single-center, open-label, nonrandomized, controlled clinical study in patients with type 2 diabetes stably treated with insulin, who were assigned to dapagliflozin (5 mg/day with dose-reduced insulin; n=8/9 completed) or insulin dose-up (n=5/8 completed). At 12 weeks, changes in urinary and plasma metabolites and short-chain acylcarnitines related to BCAA catabolism were quantified. To explore mechanisms, 10-week-old db/db mice received luseogliflozin (10 mg/kg/day, p.o.) or insulin glargine (10 U/day, s.c.) for 4 weeks; renal histology, mRNA and protein expression of key enzymes involved in BCAA catabolism, including branched-chain aminotransferase 2 (BCAT2), branched-chain ketoacid dehydrogenase (BCKDH), and BCKD kinase (BCKDK), were assessed. Dapagliflozin treatment induced greater increases in urinary excretion of three BCAA-derived metabolites-3-hydroxypropionic acid, C5-OH carnitine, and 3-hydroxybutyric acid-compared with insulin at comparable glycemic levels. In contrast, C4 carnitine (an earlier metabolite in valine catabolism) rose more with insulin. No corresponding between-group differences were detected in plasma metabolites. In db/db mice, luseogliflozin attenuated glomerular mesangial expansion and tubular epithelial atrophy, and reduced Col1a1 mRNA and TGF-β1 protein, compared with glargine at comparable glycemic levels. Luseogliflozin decreased the phosphorylated (inactive) form of the BCKDH E1α subunit (p-BCKDHA/BCKDHA) and lowered BCKDK protein. mRNA expression of amino acid transporters and BCAT2 expression was unchanged. Across complementary human and mouse studies, SGLT2 inhibition was suggested to enhance renal BCAA catabolism compared with insulin at comparable glycemic levels. In humans, increases in urinary BCAA-derived downstream metabolites without corresponding changes in plasma support a kidney-localized metabolic effect. In mice, SGLT2 inhibitor improved renal histopathology, and reduced phosphorylation-mediated inactivation of BCKDH. These findings provide mechanistic, translational evidence that SGLT2i modulate BCAA flux independently of glucose lowering, suggesting BCAA catabolism as a therapeutic axis in diabetic kidney disease. https://rctportal.mhlw.go.jp/en/detail?trial_id=UMIN000052955, identifier UMIN000052955. Show less
📄 PDF DOI: 10.3389/fendo.2025.1706838
BCKDK