👤 Yinghui 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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Wu-Wei Wang, Wuji Wang, Wuqing Wang, Wusan Wang, X E Wang, X F Wang, X O Wang, X S Wang, X Wang, X-T Wang, Xi Wang, Xi-Hong Wang, Xi-Rui Wang, Xia Wang, Xian Wang, Xian-e Wang, Xianding Wang, Xianfeng Wang, Xiang Wang, Xiang-Dong Wang, Xiangcheng Wang, Xiangding Wang, Xiangdong Wang, Xiangguo Wang, Xianghua Wang, Xiangkun Wang, Xiangrong Wang, Xiangru Wang, Xiangwei Wang, Xiangyu Wang, Xianna Wang, Xianqiang Wang, Xianrong Wang, Xianshi Wang, Xianshu Wang, Xiansong Wang, Xiantao Wang, Xianwei Wang, Xianxing Wang, Xianze Wang, Xianzhe Wang, Xianzong Wang, Xiao Ling Wang, Xiao Qun Wang, Xiao Wang, Xiao-Ai Wang, Xiao-Fei Wang, Xiao-Hui Wang, Xiao-Jie Wang, Xiao-Juan Wang, Xiao-Lan Wang, Xiao-Li Wang, Xiao-Lin Wang, Xiao-Ming Wang, Xiao-Pei Wang, Xiao-Qian Wang, Xiao-Qun Wang, Xiao-Tong Wang, Xiao-Xia Wang, Xiao-Yi Wang, Xiao-Yun Wang, Xiao-jian WANG, Xiao-liang Wang, Xiaobin Wang, Xiaobo Wang, Xiaochen Wang, Xiaochuan Wang, Xiaochun Wang, Xiaodan Wang, Xiaoding Wang, Xiaodong Wang, Xiaofang Wang, Xiaofei Wang, Xiaofen Wang, Xiaofeng Wang, Xiaogang Wang, Xiaohong Wang, Xiaohu Wang, Xiaohua Wang, Xiaohui Wang, Xiaojia Wang, Xiaojian Wang, Xiaojiao Wang, Xiaojie Wang, Xiaojing Wang, Xiaojuan Wang, Xiaojun Wang, Xiaokun Wang, Xiaole Wang, Xiaoli Wang, Xiaoliang Wang, Xiaolin Wang, Xiaoling Wang, Xiaolong Wang, Xiaolu Wang, Xiaolun Wang, Xiaoman Wang, Xiaomei Wang, Xiaomeng Wang, Xiaomin Wang, Xiaoming Wang, Xiaona Wang, Xiaonan Wang, Xiaoning Wang, Xiaoqi Wang, Xiaoqian Wang, Xiaoqin Wang, Xiaoqing Wang, Xiaoqiu Wang, Xiaoqun Wang, Xiaorong Wang, Xiaorui Wang, Xiaoshan Wang, Xiaosong Wang, Xiaotang Wang, Xiaoting Wang, Xiaotong Wang, Xiaowei Wang, Xiaowen Wang, Xiaowu Wang, Xiaoxia Wang, Xiaoxiao Wang, Xiaoxin Wang, Xiaoxin X Wang, Xiaoxuan Wang, Xiaoya Wang, Xiaoyan Wang, Xiaoyang Wang, Xiaoye Wang, Xiaoying Wang, Xiaoyu Wang, Xiaozhen Wang, Xiaozhi Wang, Xiaozhong Wang, Xiaozhu Wang, Xichun Wang, Xidi Wang, Xietong Wang, Xifeng Wang, Xifu Wang, Xijun Wang, Xike 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, Xueyi 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, 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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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
Danyang Zhang, Xiaoshi He, Ting Wang +4 more · 2024 · Molecules (Basel, Switzerland) · MDPI · added 2026-04-24
Methylglyoxal-induced ROS elevation is the primary cause of neuronal damage. Metformin is a traditional hypoglycemic drug that has been reported to be beneficial to the nervous system. In this study, Show more
Methylglyoxal-induced ROS elevation is the primary cause of neuronal damage. Metformin is a traditional hypoglycemic drug that has been reported to be beneficial to the nervous system. In this study, flavonoids were found to enhance the protective effect of metformin when added at a molar concentration of 0.5%. The structure-activity relationship (SAR) analysis indicated that ortho- substitution in the B ring, and the absence of double bonds between the 2 and 3 position combined with the gallate substitution with R configuration at the 3 position in the C ring played crucial roles in the synergistic effects, which could be beneficial for designing a combination of the compounds. Additionally, the mechanism study revealed that a typical flavonoid, EGCG, enhanced ROS scavenging and anti-apoptotic ability via the BCL2/Bax/Cyto C/Caspase-3 pathway, and synergistically inhibited the expression of GSK-3β, BACE-1, and APP in PC-12 cells when used in combination with metformin. The dose of metformin used in the combination was only 1/4 of the conventional dose when used alone. These results suggested that ROS-mediated apoptosis and the pathways related to amyloid plaques (Aβ) formation can be the targets for the synergistic neuroprotective effects of flavonoids and metformin. Show less
📄 PDF DOI: 10.3390/molecules29102306
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
Debomoy K Lahiri, Bryan Maloney, Ruizhi Wang +4 more · 2024 · Ageing research reviews · Elsevier · added 2026-04-24
Several proteins play critical roles in vulnerability or resistance to neurodegenerative disorders such as Alzheimer's disease (AD), Parkinson's disease (PD), and frontotemporal dementia (FTD). Regula Show more
Several proteins play critical roles in vulnerability or resistance to neurodegenerative disorders such as Alzheimer's disease (AD), Parkinson's disease (PD), and frontotemporal dementia (FTD). Regulation of these proteins is critical to maintaining healthy neurohomeostasis. In addition to transcription factors regulating gene transcription and microRNAs regulating mRNA translation, natural antisense transcripts (NATs) regulate mRNA levels, splicing, and translation. NATs' roles are significant in regulating key protein-coding genes associated with neurodegenerative disorders. Elucidating the functions of these NATs could prove useful in treating or preventing diseases. NAT activity is not restricted to mRNA translation; it can also regulate DNA (de)methylation and other gene expression steps. NATs are noncoding RNAs (ncRNAs) encoded by DNA sequences overlapping the pertinent protein genes. These NATs have complex structures, including introns and exons, and therefore bind their target genes, precursor mRNAs (pre-mRNAs), and mature RNAs. They can occur at the 5'- or 3'-ends of a mRNA-coding sequence or internally to a parent gene. NATs can downregulate translation, e.g., microtubule-associated protein tau (MAPT) antisense-1 gene (MAPT-AS1), or upregulate translation, e.g., β-Amyloid site Cleaving Enzyme 1 (BACE1) antisense gene (BACE1-AS). Regulation of NATs can parallel pathogenesis, wherein a "pathogenic" NAT (e.g., BACE1-AS) is upregulated under pathogenic conditions, while a "protective" NAT (e.g., MAPT-AS1) is downregulated under pathogenic conditions. As a relatively underexplored endogenous control mechanism of protein expression, NATs may present novel mechanistic targets to prevent or ameliorate aging-related disorders. Show less
📄 PDF DOI: 10.1016/j.arr.2024.102336
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
Peng Chen, Zhilei Guo, Jiexin Lei +1 more · 2024 · Phytotherapy research : PTR · Wiley · added 2026-04-24
Neuroinflammation may play an important role in the development of Alzheimer's disease (AD). Previous studies have reported that lipopolysaccharide (LPS)-induced neuroinflammation causes memory impair Show more
Neuroinflammation may play an important role in the development of Alzheimer's disease (AD). Previous studies have reported that lipopolysaccharide (LPS)-induced neuroinflammation causes memory impairments and behavioral disorders. We investigated the potential preventive effects of punicalin (PUN), a polyphenolic component of pomegranate, on LPS-induced memory deficiency and anxiety- and depression-like behaviors, along with the underlying mechanisms. LPS-treated cultured microglial BV2 cells and BV2 cell/Neuro-2a (N2a) cell coculture system were investigated for anti-neuroinflammatory effects of PUN in vitro. The in vivo experiments involved mice administered a 4-week course of oral gavage with 1500 mg/kg/d PUN before intraperitoneal LPS (250 mg/kg daily 7 times) injections. The in vitro results demonstrated that PUN inhibited the LPS-induced inflammatory cytokine (IL-18, IL-1β, TNF-ɑ, and IL-6) production in BV2 cells and protected N2a cells from synaptic damage mediated by BV2 microglia-induced neuroinflammation. In in vivo studies, it was observed that PUN improved memory impairment and anxiety- and depression-like behaviors caused by LPS and reduced the expression of inflammatory proteins such as iNOS, COX-2, IL-1β, IL-2, IL-6, and TNF-α. Furthermore, PUN inhibited the LPS-induced production of MDA; increased the activities of CAT, SOD, and GSH-Px, and inhibited LPS-induced Aβ Show less
no PDF DOI: 10.1002/ptr.8219
BACE1
Sujun Jiang, Guoen Cai, Zhimin Yang +5 more · 2024 · ACS nano · ACS Publications · added 2026-04-24
The association between dysfunctional microglia and amyloid-β (Aβ) is a fundamental pathological event and increases the speed of Alzheimer's disease (AD). Additionally, the pathogenesis of AD is intr Show more
The association between dysfunctional microglia and amyloid-β (Aβ) is a fundamental pathological event and increases the speed of Alzheimer's disease (AD). Additionally, the pathogenesis of AD is intricate and a single drug may not be enough to achieve a satisfactory therapeutic outcome. Herein, we reported a facile and effective gene therapy strategy for the modulation of microglia function and intervention of Aβ anabolism by ROS-responsive biomimetic exosome-liposome hybrid nanovesicles (designated as TSEL). The biomimetic nanovesicles codelivery β-site amyloid precursor protein cleaving enzyme-1 (BACE1) siRNA (siBACE1) and TREM2 plasmid (pTREM2) gene drug efficiently penetrate the blood-brain barrier and enhance the drug accumulation at AD lesions with the help of exosomes homing ability and angiopep-2 peptides. Specifically, an upregulation of TREM2 expression can reprogram microglia from a pro-inflammatory M1 phenotype to an anti-inflammatory M2 phenotype while also restoring its capacity to phagocytose Aβ and its nerve repair function. In addition, siRNA reduces the production of Aβ plaques at the source by knocking out the BACE1 gene, which is expected to further enhance the therapeutic effect of AD. The in vivo study suggests that TSEL through the synergistic effect of two gene drugs can ameliorate APP/PS1 mice cognitive impairment by regulating the activated microglial phenotype, reducing the accumulation of Aβ, and preventing the retriggering of neuroinflammation. This strategy employs biomimetic nanovesicles for the delivery of dual nucleic acids, achieving synergistic gene therapy for AD, thus offering more options for the treatment of AD. Show less
no PDF DOI: 10.1021/acsnano.3c13150
BACE1
Lijie He, Chunyan Zhang, Jing Wang · 2024 · Beijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences · added 2026-04-24
To explore the expression relationship and significance of long chain non-coding RNA nuclear-enriched abundant transcript 1 (LncRNA NEAT1) and miR-27a-3p in serum and cerebrospinal fluid of patients w Show more
To explore the expression relationship and significance of long chain non-coding RNA nuclear-enriched abundant transcript 1 (LncRNA NEAT1) and miR-27a-3p in serum and cerebrospinal fluid of patients with Alzheimer disease (AD). Sixty-six AD patients received by the department of neurology of our hospital from October 2019 to September 2021 were gathered, according to the clinical dementia rating scale score, they were grouped into mild group (≤1 point, The MMSE score [21 (17, 25), 9(7, 11) The expression trends of NEAT1 and miR-27a-3p in the serum and cerebrospinal fluid of AD patients are consistent, the level of NEAT1 is increased, and the level of miR-27a-3p is decreased. The levels of the two are negatively correlated, which is related to the degree of Aβ deposition in the brain of AD patients and is involved in the progression of AD. Show less
no PDF DOI: 10.19723/j.issn.1671-167X.2024.02.002
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
Jingqi Wang, Paul A Gleeson, Lou Fourriere · 2024 · Traffic (Copenhagen, Denmark) · Blackwell Publishing · added 2026-04-24
Alzheimer's disease is associated with increased levels of amyloid beta (Aβ) generated by sequential intracellular cleavage of amyloid precursor protein (APP) by membrane-bound secretases. However, th Show more
Alzheimer's disease is associated with increased levels of amyloid beta (Aβ) generated by sequential intracellular cleavage of amyloid precursor protein (APP) by membrane-bound secretases. However, the spatial and temporal APP cleavage events along the trafficking pathways are poorly defined. Here, we use the Retention Using Selective Hooks (RUSH) to compare in real time the anterograde trafficking and temporal cleavage events of wild-type APP (APPwt) with the pathogenic Swedish APP (APPswe) and the disease-protective Icelandic APP (APPice). The analyses revealed differences in the trafficking profiles and processing between APPwt and the APP familial mutations. While APPwt was predominantly processed by the β-secretase, BACE1, following Golgi transport to the early endosomes, the transit of APPswe through the Golgi was prolonged and associated with enhanced amyloidogenic APP processing and Aβ secretion. A 20°C block in cargo exit from the Golgi confirmed β- and γ-secretase processing of APPswe in the Golgi. Inhibition of the β-secretase, BACE1, restored APPswe anterograde trafficking profile to that of APPwt. APPice was transported rapidly through the Golgi to the early endosomes with low levels of Aβ production. This study has revealed different intracellular locations for the preferential cleavage of APPwt and APPswe and Aβ production, and the Golgi as the major processing site for APPswe, findings relevant to understand the molecular basis of Alzheimer's disease. Show less
no PDF DOI: 10.1111/tra.12932
BACE1
Heng-Cai Wang, Wei Yang, Ling Xu +6 more · 2024 · Advanced healthcare materials · Wiley · added 2026-04-24
Microglia-mediated inflammation is involved in the pathogenesis of Alzheimer's disease (AD), whereas human fibroblast growth factor 21 (hFGF21) has demonstrated the ability to regulate microglia activ Show more
Microglia-mediated inflammation is involved in the pathogenesis of Alzheimer's disease (AD), whereas human fibroblast growth factor 21 (hFGF21) has demonstrated the ability to regulate microglia activation in Parkinson's disease, indicating a potential therapeutic role in AD. However, challenges such as aggregation, rapid inactivation, and the blood-brain barrier hinder its effectiveness in treating AD. This study develops targeted delivery of hFGF21 to activated microglia using BV2 cell membrane-coated PEGylated liposomes (hFGF21@BCM-LIP), preserving the bioactivity of hFGF21. In vitro, hFGF21@BCM-LIP specifically targets Aβ Show less
no PDF DOI: 10.1002/adhm.202400125
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
Tianshu Shi, Siyu Shen, Yong Shi +21 more · 2024 · Nature metabolism · Nature · added 2026-04-24
Ageing increases susceptibility to neurodegenerative disorders, such as Alzheimer's disease (AD). Serum levels of sclerostin, an osteocyte-derived Wnt-β-catenin signalling antagonist, increase with ag Show more
Ageing increases susceptibility to neurodegenerative disorders, such as Alzheimer's disease (AD). Serum levels of sclerostin, an osteocyte-derived Wnt-β-catenin signalling antagonist, increase with age and inhibit osteoblastogenesis. As Wnt-β-catenin signalling acts as a protective mechanism for memory, we hypothesize that osteocyte-derived sclerostin can impact cognitive function under pathological conditions. Here we show that osteocyte-derived sclerostin can cross the blood-brain barrier of old mice, where it can dysregulate Wnt-β-catenin signalling. Gain-of-function and loss-of-function experiments show that abnormally elevated osteocyte-derived sclerostin impairs synaptic plasticity and memory in old mice of both sexes. Mechanistically, sclerostin increases amyloid β (Aβ) production through β-catenin-β-secretase 1 (BACE1) signalling, indicating a functional role for sclerostin in AD. Accordingly, high sclerostin levels in patients with AD of both sexes are associated with severe cognitive impairment, which is in line with the acceleration of Αβ production in an AD mouse model with bone-specific overexpression of sclerostin. Thus, we demonstrate osteocyte-derived sclerostin-mediated bone-brain crosstalk, which could serve as a target for developing therapeutic interventions against AD. Show less
📄 PDF DOI: 10.1038/s42255-024-00989-x
BACE1
Yuting Ding, Wenkang Luan, Xuanlin Shen +2 more · 2024 · Neurotoxicity research · Springer · added 2026-04-24
Traumatic brain injury (TBI) is one of the important risk factors for the development of Alzheimer's disease (AD). However, the molecular mechanism by which TBI promotes the progression of AD is not e Show more
Traumatic brain injury (TBI) is one of the important risk factors for the development of Alzheimer's disease (AD). However, the molecular mechanism by which TBI promotes the progression of AD is not elucidated. In this study, we showed that the abnormal production of E2F1 is a major factor in promoting the neuropathological and cognitive deterioration of AD post-TBI. We found that repeated mild TBI can aggravate the neuropathology of AD in APP/PS1 mice. At the same time, the co-expression of E2F1 and beta-site APP cleaving enzyme 1 (BACE1) was upregulated when the mouse hippocampus was dissected. BACE1 is recognized as a rate-limiting enzyme for the production of Aβ. Here, we speculate that E2F1 may play a role in promoting BACE1 expression in AD. Therefore, we collected peripheral blood from patients with AD. Interestingly, there is a positive correlation between E2F1 and brain-derived neurotrophic factor-antisense (BDNF-AS), whereas BDNF-AS in AD can promote the expression of BACE1 and exhibit a neurotoxic effect. We established a cell model and found a regulatory relationship between E2F1 and BDNF-AS. Therefore, based on our results, we concluded that E2F1 regulates BDNF-AS, promotes the expression of BACE1, and affects the progression of AD. Furthermore, E2F1 mediates the TBI-induced neurotoxicity of AD. Show less
📄 PDF DOI: 10.1007/s12640-024-00695-2
BACE1
Yuxuan Ma, Wuxiang Sun, Jing Bai +11 more · 2024 · CNS neuroscience & therapeutics · Blackwell Publishing · added 2026-04-24
Alzheimer's disease (AD) is a significant global health concern, and it is crucial that we find effective methods to prevent or slow down AD progression. Recent studies have highlighted the essential Show more
Alzheimer's disease (AD) is a significant global health concern, and it is crucial that we find effective methods to prevent or slow down AD progression. Recent studies have highlighted the essential role of blood vessels in clearing Aβ, a protein that contributes to AD. Scientists are exploring blood biomarkers as a potential tool for future AD diagnosis. One promising method that may help prevent AD is remote ischemic conditioning (RIC). RIC involves using sub-lethal ischemic-reperfusion cycles on limbs. However, a comprehensive understanding of how RIC can prevent AD and its long-term effectiveness is still lacking. Further research is essential to fully comprehend the potential benefits of RIC in preventing AD. Female wild-type (WT) and APP/PS1 transgenic rats, aged 12 months, underwent ovariectomy and were subsequently assigned to WT, APP/PS1, and APP/PS1 + RIC groups. RIC was conducted five times a week for 4 weeks. The rats' depressive and cognitive behaviors were evaluated using force swimming, open-field tests, novel objective recognition, elevated plus maze, and Barnes maze tests. Evaluation of the neurovascular unit (NVU), synapses, vasculature, astrocytes, and microglia was conducted using immunofluorescence staining (IF), Western blot (WB), and transmission electron microscopy (TEM). Additionally, the cerebro-vasculature was examined using micro-CT, and cerebral blood flow (CBF) was measured using Speckle Doppler. Blood-brain barrier (BBB) permeability was determined by measuring the Evans blue leakage. Finally, Aβ levels in the rat frontal cortex were measured using WB, ELISA, or IF staining. RIC enhanced memory-related protein expression and rescued depressive-like behavior and cognitive decline in APP/PS1 transgenic rats. Additionally, the intervention protected NVU in the rat frontal cortex, as evidenced by (1) increased expression of TJ (tight junction) proteins, pericyte marker PDGFRβ, and glucose transporter 1 (GLUT1), as well as decreased VCAM1; (2) mitigation of ultrastructure impairment in neuron, cerebral vascular, and astrocyte; (3) upregulation of A2 astrocyte phenotype markers and downregulation of A1 phenotype markers, indicating a shift toward a healthier phenotype. Correspondingly, RIC intervention alleviated neuroinflammation, as evidenced by the decreased Iba1 level, a microglia marker. Meanwhile, RIC intervention elevated CBF in frontal cortex of the rats. Notably, RIC intervention effectively suppressed Aβ toxicity, as demonstrated by the enhancement of α-secretase and attenuation of β-secretase (BACE1) and γ- secretase and Aβ1-42 and Aβ1-40 levels as well. Chronic RIC intervention exerts vascular and neuroprotective roles, suggesting that RIC could be a promising therapeutic strategy targeting the BBB and NVU during AD development. Show less
📄 PDF DOI: 10.1111/cns.14613
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
Zhifang Wang, Jingpei Zhou, Bin Zhang +4 more · 2024 · Behavioural brain research · Elsevier · added 2026-04-24
The primary aim of this study was to examine the correlation between the formation of Aβ plaques and autophagy, which is regulated by β-asarone and the lncRNA BACE1-AS. Additionally, the study sought Show more
The primary aim of this study was to examine the correlation between the formation of Aβ plaques and autophagy, which is regulated by β-asarone and the lncRNA BACE1-AS. Additionally, the study sought to explore potential targets of the drug in inhibiting the deposition of toxic AD-related proteins and restoring impaired mitochondrial and autophagic functions. SHY5Y cells were utilized to construct a stable Alzheimer's disease (AD) model, followed by the utilization of interference and overexpression lentiviruses targeting BACE1-AS to establish a cell model. The cells were categorized into five groups, including a normal group, siRNA/BACE1 group, and β-asarone group. The fluorescence quantitative PCR technique was employed to assess the disparity in BACE1 mRNA expression, while changes in immunofluorescence (IF) were observed to determine the stable interference titre and action time of the lentiviruses. Additionally, western blotting (WB) and fluorescence quantitative PCR were employed to evaluate the expression of proteins and mRNAs associated with AD and autophagy. The findings demonstrated a significant elevation in BACE1 expression levels in brain tissue among individuals with AD compared to those without the condition. Moreover, the results indicated that the introduction of β-asarone led to an increase in the expression of the BACE1-AS gene in the cell group transfected with plasmid H12732. Furthermore, it was observed that β-asarone enhanced the expression levels of shRNA and BACE1 after 72 h. In contrast, β-asarone suppressed the expression of PS1, Aβ, BACE1, APP, and p62, while promoting the expression of syn, LC3 I/II, and Beclin-1. Based on these findings, it can be concluded that β-Asarone exerts a comprehensive influence on the expression of proteins associated with AD and synaptic function. β-Asarone exhibits the potential to mitigate Aβ deposition by impeding the expression of lncBACE1, thereby facilitating autophagy through the suppression of BACE1's inhibitory impact on autophagy. This complements the self-enhancing effect of autophagy. Show less
no PDF DOI: 10.1016/j.bbr.2024.114896
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
Tingting Jia, Hongbo Wang, Wenya Chi +7 more · 2024 · International journal of pharmaceutics · Elsevier · added 2026-04-24
Cleavage of Amyloid precursor protein (APP) by the β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the rate-limiting step in the production of amyloid-β (Aβ) synaptotoxins. The siRNA-med Show more
Cleavage of Amyloid precursor protein (APP) by the β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the rate-limiting step in the production of amyloid-β (Aβ) synaptotoxins. The siRNA-mediated silencing to attenuate the expression of BACE1 to ameliorate cognitive dysfunction in mice had been investigated. To improve therapeutic gene delivery to the central nervous system, cationic copolymer poly(ethylene glycol)-b-poly[N-(N'-{N''-[N'''-(2-aminoethyl)-2-aminoethyl]-2-aminoethyl}-2-aminoethyl)aspartamide]-cholesterol was synthesized, then RVG29 and Tet1 peptides were exploited as ligands to construct a dual-targeting brain gene delivery polyion complex (Tet1/RVG29-PIC). The cell uptake of a coculture cell model showed that the Tet1/RVG29-PIC exhibited notable transport characteristics and possessed affinity towards nerve cells. In vivo transfection, Tet1/RVG29-PIC possessed the highest expression of luciferase in brain compared with that of RVG29-PIC or Tet1-PIC, which were 1.25 and 1.22 times respectively. Silence BACE1 expression using siRNA-expressing plasmid loaded Tet1/RVG29-PIC that improved behavioral deficits in the APP/PS1 mouse model, demonstrating the favorable brain delivery properties of Tet1/RVG29-PIC by synergistical engagement of GT1B and nicotinic acetylcholine receptors. Our results suggested that the nanoformulation has the potential to be exploited as a multistage-targeting gene vector for the CNS disease therapy. Show less
no PDF DOI: 10.1016/j.ijpharm.2023.123727
BACE1
Xiaozhen Wang, Wenjing Gan, Meimei Kang +5 more · 2024 · Brain research · Elsevier · added 2026-04-24
Clinical studies have shown that asthma is a risk factor for dementia or Alzheimer's disease (AD). To investigate whether asthma aggravates AD in APP/PS1 mice and explore the potential mechanisms, an Show more
Clinical studies have shown that asthma is a risk factor for dementia or Alzheimer's disease (AD). To investigate whether asthma aggravates AD in APP/PS1 mice and explore the potential mechanisms, an asthma model was established using six-month-old APP/PS1 mice, and montelukast was used as a therapeutic agent in APP/PS1 mice with asthma. The Morris water maze test showed that asthma aggravates spatial learning and memory abilities. Asthma also upregulates the NF-κB inflammatory pathway in APP/PS1 mice and promotes the expression of beta-site amyloid precursor protein cleaving enzyme 1 (BACE1), amyloid-β (Aβ) deposition, neuronal damage, synaptic plasticity deficiency, activation of microglia and astrocytes. The level of LTD4 and its receptor CysLT1R in the hippocampus of APP/PS1 mice after the asthma modeling was established was higher than that in APP/PS1 mice, suggesting that asthma may affect the pathology of AD through LTD4 and its receptor Cys-LT1R. Montelukast ameliorates these pathological changes and cognitive impairment. These results suggest that asthma aggravates AD pathology and cognitive impairment of APP/PS1 mice via upregulation of the NF-κB inflammatory pathway, and montelukast ameliorates these pathological changes. Show less
no PDF DOI: 10.1016/j.brainres.2023.148711
BACE1
Meng Han Liu, Yong Tang, Li Qun Qu +11 more · 2024 · Phytomedicine : international journal of phytotherapy and phytopharmacology · Elsevier · added 2026-04-24
Raddeanin A is a triterpenoid isolated from Anemone raddeana Regel. It exhibits a broad spectrum of biological activities such as anti-tumor and anti-inflammatory, however, its neuroprotective effect Show more
Raddeanin A is a triterpenoid isolated from Anemone raddeana Regel. It exhibits a broad spectrum of biological activities such as anti-tumor and anti-inflammatory, however, its neuroprotective effect in targeting Alzheimer's disease (AD) remains uninvestigated. To provide scientific base for the development of novel AD drug by clarifying the neuroprotective effect and molecular mechanisms of raddeanin A in both in vitro and in vivo AD model. To confirm the neuroprotective role of raddeanin A in the treatment of AD, its mechanisms and effects on β-amyloidosis and Aβ fibrillation was studied in U87 cells. Besides, the improvement on cognitive deficit, pathological defects, reactive astrocyte clusters, inhibition on neuronal inflammation and apoptosis were further studied in 3 x Tg-AD mice model of AD. Real-time PCR, western blot, dot blot, biolayer interferometry and bioinformatics analysis were used to confirm the in vitro effect and targets of raddeanin A on β-amyloidosis and its associated protein network. A series of experiments including Morris water maze, H&E staining, nissl staining and immunofluorescence analysis were conducted to confirm the protective behavioral effect of raddeanin A in the in vivo AD mice model. Raddeanin A was identified to reduce β-amyloidosis in U87 cells and 3 x Tg-AD mice model of AD by decreasing level of BACE1, APP, APP-β and Aβ. Raddeanin A improved behavioral, spatial memory and learning ability in the AD mice. In the cortex and hippocampus, raddeanin A improved the morphology and arrangement of neurons, lower the level of reactive astrocyte marker GFAP and apoptotic marker proteins Bax/Bcl2 ratio. Moreover, raddeanin A upregulated the mRNA and protein level of Prkcα in the hippocampus of AD mice whose neuroprotective effect was exerted possibly via the activation of protein kinase C. As a novel natural agent targeting β-amyloidosis, our results provide the first evidence of the multiple in vitro and in vivo neuroprotective effect of raddeanin A, suggesting its potential therapeutic application in preventing or alleviating the symptoms of AD. Show less
no PDF DOI: 10.1016/j.phymed.2023.155121
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
Ming-Ti Lv, He-Cheng Wang, Xiao-Wen Meng +8 more · 2024 · CNS neuroscience & therapeutics · Blackwell Publishing · added 2026-04-24
FoxO1 is an important target in the treatment of Alzheimer's disease (AD). However, FoxO1-specific agonists and their effects on AD have not yet been reported. This study aimed to identify small molec Show more
FoxO1 is an important target in the treatment of Alzheimer's disease (AD). However, FoxO1-specific agonists and their effects on AD have not yet been reported. This study aimed to identify small molecules that upregulate the activity of FoxO1 to attenuate the symptoms of AD. FoxO1 agonists were identified by in silico screening and molecular dynamics simulation. Western blotting and reverse transcription-quantitative polymerase chain reaction assays were used to assess protein and gene expression levels of P21, BIM, and PPARγ downstream of FoxO1 in SH-SY5Y cells, respectively. Western blotting and enzyme-linked immunoassays were performed to explore the effect of FoxO1 agonists on APP metabolism. N-(3-methylisothiazol-5-yl)-2-(2-oxobenzo[d]oxazol-3(2H)-yl) acetamide (compound D) had the highest affinity for FoxO1. Compound D activated FoxO1 and regulated the expression of its downstream target genes, P21, BIM, and PPARγ. In SH-SY5Y cells treated with compound D, BACE1 expression levels were downregulated, and the levels of Aβ We present a novel small-molecule FoxO1 agonist with good anti-AD effects. This study highlights a promising strategy for new drug discovery for AD. Show less
📄 PDF DOI: 10.1111/cns.14140
BACE1
Jiahui Cai, Weixue Xiong, Xueqin Wang +2 more · 2024 · CNS neuroscience & therapeutics · Blackwell Publishing · added 2026-04-24
The hippocampus is a heterogeneous structure, comprising histologically and functionally distinguishable hippocampal subfields. The volume reductions in hippocampal subfields have been demonstrated to Show more
The hippocampus is a heterogeneous structure, comprising histologically and functionally distinguishable hippocampal subfields. The volume reductions in hippocampal subfields have been demonstrated to be linked with Alzheimer's disease (AD). The aim of our study is to investigate the hippocampal subfields' genetic architecture based on the Alzheimer's Disease Neuroimaging Initiative (ADNI) data set. After preprocessing the downloaded genetic variants and imaging data from the ADNI database, a co-sparse reduced rank regression model was applied to analyze the genetic architecture of hippocampal subfields volumes. Homology modeling, docking, molecular dynamics simulations, and Co-IP experiments for protein-protein interactions were used to verify the function of target protein on hippocampal subfields successively. After that, the association analysis between the candidated genes on the hippocampal subfields volume and clinical scales were performed. The results of the association analysis revealed five unique genetic variants (e.g., ubiquitin-specific protease 10 [USP10]) changed in nine hippocampal subfields (e.g., the granule cell and molecular layer of the dentate gyrus [GC-ML-DG]). Among five genetic variants, USP10 had the strongest interaction effect with BACE1, which affected hippocampal subfields verified by MD and Co-IP experiments. The results of association analysis between the candidated genes on the hippocampal subfields volume and clinical scales showed that candidated genes influenced the volume and function of hippocampal subfields. Current evidence suggests that hippocampal subfields have partly distinct genetic architecture and may improve the sensitivity of the detection of AD. Show less
📄 PDF DOI: 10.1111/cns.14110
BACE1
Aya Jishi, Di Hu, Yutong Shang +3 more · 2024 · Acta neuropathologica communications · BioMed Central · added 2026-04-24
Mitochondrial dysfunction and α-synuclein (αSyn) aggregation are key contributors to Parkinson's Disease (PD). While genetic and environmental risk factors, including mutations in mitochondrial-associ Show more
Mitochondrial dysfunction and α-synuclein (αSyn) aggregation are key contributors to Parkinson's Disease (PD). While genetic and environmental risk factors, including mutations in mitochondrial-associated genes, are implicated in PD, the precise mechanisms linking mitochondrial defects to αSyn pathology remain incompletely understood, hindering the development of effective therapeutic interventions. Here, we identify the loss of branched chain ketoacid dehydrogenase kinase (BCKDK) as a mitochondrial risk factor that exacerbates αSyn pathology by disrupting Complex I function. Our findings reveal a consistent downregulation of BCKDK in dopaminergic (DA) neurons from A53T-αSyn mouse models, PD patient-derived induced pluripotent stem (iPS) cells, and postmortem brain tissues. BCKDK deficiency leads to mitochondrial dysfunction, including reduced membrane potential and increased reactive oxygen species (ROS) production upon administration of a stressor, which in turn promotes αSyn oligomerization. Mechanistically, BCKDK interacts with the NDUFS1 subunit of Complex I to stabilize its function. Loss of BCKDK disrupts this interaction, leading to Complex I destabilization and enhanced αSyn aggregation. Notably, restoring BCKDK expression in neuron-like cells rescues mitochondrial integrity and restores Complex I activity. Similarly, in patient-derived iPS cells differentiated to form dopaminergic neurons, NDUFS1 and phosphorylated aSyn levels are partially restored upon BCKDK expression. These findings establish a mechanistic link between BCKDK deficiency, mitochondrial dysfunction, and αSyn pathology in PD, positioning BCKDK as a potential therapeutic target to mitigate mitochondrial impairment and neurodegeneration in PD. Show less
📄 PDF DOI: 10.1186/s40478-024-01915-8
BCKDK
Jue Liang, Xiaoyu Wang, Francisco Ortiz +7 more · 2024 · ACS medicinal chemistry letters · ACS Publications · added 2026-04-24
Elevated levels of the branched chain α-amino acids valine, leucine, and isoleucine are associated with heart disease and metabolic disorders. The kinase BDK, also known as branched-chain ketoacid deh Show more
Elevated levels of the branched chain α-amino acids valine, leucine, and isoleucine are associated with heart disease and metabolic disorders. The kinase BDK, also known as branched-chain ketoacid dehydrogenase kinase (BCKDK), is a negative regulator of branched-chain α-amino acid metabolism through deactivation of BCKDC, the branched-chain α-ketoacid dehydrogenase complex. Inhibitors of BDK increase the activity of BCKDC and could be useful therapeutic leads for cardiometabolic diseases. We describe a novel bicyclic carboxy amide as an inhibitor of BDK with in vivo activity. Show less
no PDF DOI: 10.1021/acsmedchemlett.4c00362
BCKDK
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
Yan Li, Yuxiang Lin, Yali Tang +16 more · 2024 · Cell death & disease · Nature · added 2026-04-24
Tumour metabolic reprogramming is pivotal for tumour survival and proliferation. Investigating potential molecular mechanisms within the heterogeneous and clinically aggressive triple-negative breast Show more
Tumour metabolic reprogramming is pivotal for tumour survival and proliferation. Investigating potential molecular mechanisms within the heterogeneous and clinically aggressive triple-negative breast cancer (TNBC) subtype is essential to identifying novel therapeutic targets. Accordingly, we investigated the role of branched-chain α-keto acid dehydrogenase kinase (BCKDK) in promoting tumorigenesis in TNBC. We analysed The Cancer Genome Atlas dataset and immunohistochemically stained surgical specimens to investigate BCKDK expression and its prognostic implications in TNBC. The effects of BCKDK on tumorigenesis were assessed using cell viability, colony formation, apoptosis, and cell cycle assays, and subsequently validated in vivo. Metabolomic screening was performed via isotope tracer studies. The downstream target was confirmed using mass spectrometry and a co-immunoprecipitation experiment coupled with immunofluorescence analysis. Upstream transcription factors were also examined using chromatin immunoprecipitation and luciferase assays. BCKDK was upregulated in TNBC tumour tissues and associated with poor prognosis. BCKDK depletion led to reduced cell proliferation both in vitro and vivo. MYC-associated zinc finger protein (MAZ) was confirmed as the major transcription factor directly regulating BCKDK expression in TNBC. Mechanistically, BCKDK interacted with glucose-6-phosphate dehydrogenase (G6PD), leading to increased flux in the pentose phosphate pathway for macromolecule synthesis and detoxification of reactive oxygen species. Forced expression of G6PD rescued the growth defect in BCKDK-deficient cells. Notably, the small-molecule inhibitor of BCKDK, 3,6-dichlorobenzo(b)thiophene-2-carboxylic acid, exhibited anti-tumour effects in a patient-derived tumour xenograft model. Our findings hold significant promise for developing targeted therapies aimed at disrupting the MAZ/BCKDK/G6PD signalling pathway, offering potential advancements in treating TNBC through metabolic reprogramming. Show less
📄 PDF DOI: 10.1038/s41419-024-06835-y
BCKDK