👤 Xiuyuan Hugh 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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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, 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, 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 Wang, YueJiao Wang, Yuebing Wang, Yuecong Wang, Yuegang Wang, Yuehan Wang, Yuehong Wang, Yuehu Wang, Yuehua Wang, Yuelong Wang, Yuemiao Wang, Yueshen Wang, Yueting Wang, Yuewei Wang, Yuexiang Wang, Yuexin Wang, Yueying Wang, Yueze Wang, Yufei Wang, Yufeng Wang, Yugang Wang, Yuh-Hwa Wang, Yuhan Wang, Yuhang Wang, Yuhua Wang, Yuhuai Wang, Yuhuan Wang, Yuhui Wang, Yujia Wang, Yujiao Wang, Yujie Wang, Yujiong Wang, Yulai Wang, Yulei Wang, Yuli Wang, Yuliang Wang, Yulin Wang, Yuling Wang, Yulong Wang, Yumei Wang, Yumeng Wang, Yumin Wang, Yuming Wang, Yun Wang, Yun Yong Wang, Yun-Hui Wang, Yun-Jin Wang, Yun-Xing Wang, Yunbing Wang, Yunce Wang, Yunchao Wang, Yuncong Wang, Yunduan Wang, Yunfang Wang, Yunfei Wang, Yunhan Wang, Yunhe Wang, Yunong Wang, Yunpeng Wang, Yunqiong Wang, Yuntai Wang, Yunzhang Wang, Yunzhe Wang, Yunzhi Wang, Yupeng Wang, Yuping Wang, Yuqi Wang, Yuqian Wang, Yuqiang Wang, Yuqin Wang, Yusha Wang, Yushe Wang, Yusheng Wang, Yutao Wang, Yuting Wang, Yuwei Wang, Yuwen Wang, Yuxiang 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articles
Fei Wang, Alison B Kohan, Chun-Min Lo +3 more · 2015 · Journal of lipid research · added 2026-04-24
The purpose of this review is to summarize our current understanding of the physiological roles of apoA-IV in metabolism, and to underscore the potential for apoA-IV to be a focus for new therapies ai Show more
The purpose of this review is to summarize our current understanding of the physiological roles of apoA-IV in metabolism, and to underscore the potential for apoA-IV to be a focus for new therapies aimed at the treatment of diabetes and obesity-related disorders. ApoA-IV is primarily synthesized by the small intestine, attached to chylomicrons by enterocytes, and secreted into intestinal lymph during fat absorption. In circulation, apoA-IV is associated with HDL and chylomicron remnants, but a large portion is lipoprotein free. Due to its anti-oxidative and anti-inflammatory properties, and because it can mediate reverse-cholesterol transport, proposed functions of circulating apoA-IV have been related to protection from cardiovascular disease. This review, however, focuses primarily on several properties of apoA-IV that impact other metabolic functions related to food intake, obesity, and diabetes. In addition to participating in triglyceride absorption, apoA-IV can act as an acute satiation factor through both peripheral and central routes of action. It also modulates glucose homeostasis through incretin-like effects on insulin secretion, and by moderating hepatic glucose production. While apoA-IV receptors remain to be conclusively identified, the latter modes of action suggest that this protein holds therapeutic promise for treating metabolic disease. Show less
no PDF DOI: 10.1194/jlr.R052753
APOA4
Alison B Kohan, Fei Wang, Chun-Min Lo +2 more · 2015 · American journal of physiology. Gastrointestinal and liver physiology · added 2026-04-24
Apolipoprotein A-IV (apoA-IV) is secreted by the small intestine on chylomicrons into intestinal lymph in response to fat absorption. Many physiological functions have been ascribed to apoA-IV, includ Show more
Apolipoprotein A-IV (apoA-IV) is secreted by the small intestine on chylomicrons into intestinal lymph in response to fat absorption. Many physiological functions have been ascribed to apoA-IV, including a role in chylomicron assembly and lipid metabolism, a mediator of reverse-cholesterol transport, an acute satiety factor, a regulator of gastric function, and, finally, a modulator of blood glucose homeostasis. The purpose of this review is to update our current view of intestinal apoA-IV synthesis and secretion and the physiological roles of apoA-IV in lipid metabolism and energy homeostasis, and to underscore the potential for intestinal apoA-IV to serve as a therapeutic target for the treatment of diabetes and obesity-related disease. Show less
no PDF DOI: 10.1152/ajpgi.00098.2014
APOA4
Wensheng Lu, Yu-Ching Cheng, Keping Chen +13 more · 2015 · Human molecular genetics · Oxford University Press · added 2026-04-24
Lipoprotein (a) [Lp(a)] is an independent risk factor for atherosclerosis-related events that is under strong genetic control (heritability = 0.68-0.98). However, causal mutations and functional valid Show more
Lipoprotein (a) [Lp(a)] is an independent risk factor for atherosclerosis-related events that is under strong genetic control (heritability = 0.68-0.98). However, causal mutations and functional validation of biological pathways modulating Lp(a) metabolism are lacking. We performed a genome-wide association scan to identify genetic variants associated with Lp(a)-cholesterol levels in the Old Order Amish. We confirmed a previously known locus on chromosome 6q25-26 and found Lp(a) levels also to be significantly associated with a SNP near the APOA5-APOA4-APOC3-APOA1 gene cluster on chromosome 11q23 linked in the Amish to the APOC3 R19X null mutation. On 6q locus, we detected associations of Lp(a)-cholesterol with 118 common variants (P = 5 × 10(-8) to 3.91 × 10(-19)) spanning a ∼5.3 Mb region that included the LPA gene. To further elucidate variation within LPA, we sequenced LPA and identified two variants most strongly associated with Lp(a)-cholesterol, rs3798220 (P = 1.07 × 10(-14)) and rs10455872 (P = 1.85 × 10(-12)). We also measured copy numbers of kringle IV-2 (KIV-2) in LPA using qPCR. KIV-2 numbers were significantly associated with Lp(a)-cholesterol (P = 2.28 × 10(-9)). Conditional analyses revealed that rs3798220 and rs10455872 were associated with Lp(a)-cholesterol levels independent of each other and KIV-2 copy number. Furthermore, we determined for the first time that levels of LPA mRNA were higher in the carriers than non-carriers of rs10455872 (P = 0.0001) and were not different between carriers and non-carriers of rs3798220. Protein levels of apo(a) were higher in the carriers than non-carriers of both rs10455872 and rs3798220. In summary, we identified multiple independent genetic determinants for Lp(a)-cholesterol. These findings provide new insights into Lp(a) regulation. Show less
no PDF DOI: 10.1093/hmg/ddu731
APOA4
Josh W Pressler, April Haller, Joyce Sorrell +4 more · 2015 · Diabetes · added 2026-04-24
Bariatric surgery is the most successful strategy for treating obesity, yet the mechanisms for this success are not clearly understood. Clinical literature suggests that plasma levels of apolipoprotei Show more
Bariatric surgery is the most successful strategy for treating obesity, yet the mechanisms for this success are not clearly understood. Clinical literature suggests that plasma levels of apolipoprotein A-IV (apoA-IV) rise with Roux-en-Y gastric bypass (RYGB). apoA-IV is secreted from the intestine postprandially and has demonstrated benefits for both glucose and lipid homeostasis. Because of the parallels in the metabolic improvements seen with surgery and the rise in apoA-IV levels, we hypothesized that apoA-IV was necessary for obtaining the metabolic benefits of bariatric surgery. To test this hypothesis, we performed vertical sleeve gastrectomy (VSG), a surgery with clinical efficacy very similar to that for RYGB, in whole-body apoA-IV knockout (KO) mice. We found that VSG reduced body mass and improved both glucose and lipid homeostasis similarly in wild-type mice compared with apoA-IV KO mice. In fact, VSG normalized the impairment in glucose tolerance and caused a significantly greater improvement in hepatic triglyceride storage in the apoA-IV KO mice. Last, independent of surgery, apoA-IV KO mice had a significantly reduced preference for a high-fat diet. Altogether, these data suggest that apoA-IV is not necessary for the metabolic improvements shown with VSG, but also suggest an interesting role for apoA-IV in regulating macronutrient preference and hepatic triglyceride levels. Future studies are necessary to determine whether this is the case for RYGB as well. Show less
📄 PDF DOI: 10.2337/db14-0825
APOA4
Linda S Zhang, Hirokazu Sato, Qing Yang +4 more · 2015 · American journal of physiology. Gastrointestinal and liver physiology · added 2026-04-24
Apolipoprotein (apo) A-V is a protein synthesized only in the liver that dramatically modulates plasma triglyceride levels. Recent studies suggest a novel role for hepatic apoA-V in regulating the abs Show more
Apolipoprotein (apo) A-V is a protein synthesized only in the liver that dramatically modulates plasma triglyceride levels. Recent studies suggest a novel role for hepatic apoA-V in regulating the absorption of dietary triglycerides, but its mode of action on the gut remains unknown. The aim of this study was to test for apoA-V in bile and to determine whether its secretion is regulated by dietary lipids. After an overnight recovery, adult male Sprague-Dawley bile fistula rats indeed secreted apoA-V into bile at a constant rate under fasting conditions. An intraduodenal bolus of intralipid (n = 12) increased the biliary secretion of apoA-V but not of other apolipoproteins, such as A-I, A-IV, B, and E. The lipid-induced increase of biliary apoA-V was abolished under conditions of poor lymphatic lipid transport, suggesting that the stimulation is regulated by the magnitude of lipids associated with chylomicrons transported into lymph. We also studied the secretion of apoA-V into bile immediately following bile duct cannulation. Biliary apoA-V increased over time (∼6-fold increase at hour 16, n = 8) but the secretions of other apolipoproteins remained constant. Replenishing luminal phosphatidylcholine and taurocholate (n = 9) only enhanced apoA-V secretion in bile, suggesting that the increase was not due to depletion of phospholipids or bile salts. This is the first study to demonstrate that apoA-V is secreted into bile, introducing a potential route of delivery of hepatic apoA-V to the gut lumen. Our study also reveals the uniqueness of apoA-V secretion into bile that is regulated by mechanisms different from other apolipoproteins. Show less
no PDF DOI: 10.1152/ajpgi.00227.2015
APOA5
Huadan Ye, Annan Zhou, Qiangxiao Hong +8 more · 2015 · PloS one · PLOS · added 2026-04-24
Apolipoprotein A5 (APOA5) is associated with plasma triglyceride (TG) levels, a risk factor for coronary heart disease (CHD). This study explored the association between CHD and the APOA5 rs662799 pol Show more
Apolipoprotein A5 (APOA5) is associated with plasma triglyceride (TG) levels, a risk factor for coronary heart disease (CHD). This study explored the association between CHD and the APOA5 rs662799 polymorphism. We collected 1,521 samples (783 CHD patients and 738 controls) for this case-control study. Meta-analysis was performed using Review Manager Software and Stata Software. Significant differences were observed between CHD cases and controls at the level of both genotype (χ2 = 8.964, df = 2, P = 0.011) and allele (χ2 = 9.180, df = 1, P = 0.002, OR = 1.275, 95% CI = 1.089-1.492). A breakdown analysis by gender showed a significant association of APOA5 rs662799 with CHD in males (χ2 = 7.770, df = 1, P = 0.005; OR = 1.331, 95% CI = 1.088-1.628). An additional meta-analysis using 21378 cases and 28428 controls established that rs662799 is significantly associated with CHD (P < 0.00001). Both our case-control study and meta-analysis confirm a significant association between APOA5 rs662799 and CHD. In addition, our results suggest a male-specific association between the APOA5 rs662799 polymorphism and CHD. Show less
📄 PDF DOI: 10.1371/journal.pone.0135683
APOA5
Yin Cai, Fan Ying, Erfei Song +4 more · 2015 · FASEB journal : official publication of the Federation of American Societies for Experimental Biology · added 2026-04-24
Upon high-fat feeding, prostaglandin E receptor subtype 4 (EP4)-knockout mice gain less body weight than their EP4(+/+) littermates. We investigated the cause of the lean phenotype. The mice showed a Show more
Upon high-fat feeding, prostaglandin E receptor subtype 4 (EP4)-knockout mice gain less body weight than their EP4(+/+) littermates. We investigated the cause of the lean phenotype. The mice showed a 68.8% reduction in weight gain with diminished fat mass that was not attributable to reduced food intake, fat malabsorption, or increased energy expenditure. Plasma triglycerides in the mice were elevated by 244.9%. The increase in plasma triglycerides was independent of changes in hepatic very low density lipoprotein (VLDL)-triglyceride production or intestinal chylomicron-triglyceride synthesis. However, VLDL-triglyceride clearance was drastically impaired in the EP4-knockout mice. The absence of EP4 in mice compromised the activation of lipoprotein lipase (LPL), the key enzyme responsible for trafficking of plasma triglycerides into peripheral tissues. Deficiency in EP4 reduced hepatic mRNA expression of the transcriptional factor cAMP response element binding protein H (by 36.8%) and LPL activators, including apolipoprotein (Apo)a5 (by 40.2%) and Apoc2 (by 61.3%). In summary, the lean phenotype of EP4-deficient mice resulted from reduction in adipose tissue and accretion of other peripheral organs caused by impaired triglyceride clearance. The findings identify a new metabolic dimension in the physiologic role played by endogenous EP4. Show less
no PDF DOI: 10.1096/fj.15-274597
APOA5
Ron Do, Nathan O Stitziel, Hong-Hee Won +91 more · 2015 · Nature · Nature · added 2026-04-24
Ron Do, Nathan O Stitziel, Hong-Hee Won, Anders Berg Jørgensen, Stefano Duga, Pier Angelica Merlini, Adam Kiezun, Martin Farrall, Anuj Goel, Or Zuk, Illaria Guella, Rosanna Asselta, Leslie A Lange, Gina M Peloso, Paul L Auer, NHLBI Exome Sequencing Project, Domenico Girelli, Nicola Martinelli, Deborah N Farlow, Mark A DePristo, Robert Roberts, Alexander F R Stewart, Danish Saleheen, John Danesh, Stephen E Epstein, Suthesh Sivapalaratnam, G Kees Hovingh, John J Kastelein, Nilesh J Samani, Heribert Schunkert, Jeanette Erdmann, Svati H Shah, William E Kraus, Robert Davies, Majid Nikpay, Christopher T Johansen, Jian Wang, Robert A Hegele, Eliana Hechter, Winfried Marz, Marcus E Kleber, Jie Huang, Andrew D Johnson, Mingyao Li, Greg L Burke, Myron Gross, Yongmei Liu, Themistocles L Assimes, Gerardo Heiss, Ethan M Lange, Aaron R Folsom, Herman A Taylor, Oliviero Olivieri, Anders Hamsten, Robert Clarke, Dermot F Reilly, Wu Yin, Manuel A Rivas, Peter Donnelly, Jacques E Rossouw, Bruce M Psaty, David M Herrington, James G Wilson, Stephen S Rich, Michael J Bamshad, Russell P Tracy, L Adrienne Cupples, Daniel J Rader, Muredach P Reilly, John A Spertus, Sharon Cresci, Jaana Hartiala, W H Wilson Tang, Stanley L Hazen, Hooman Allayee, Alex P Reiner, Christopher S Carlson, Charles Kooperberg, Rebecca D Jackson, Eric Boerwinkle, Eric S Lander, Stephen M Schwartz, David S Siscovick, Ruth McPherson, Anne Tybjaerg-Hansen, Goncalo R Abecasis, Hugh Watkins, Deborah A Nickerson, Diego Ardissino, Shamil R Sunyaev, Christopher J O'Donnell, David Altshuler, Stacey Gabriel, Sekar Kathiresan Show less
Myocardial infarction (MI), a leading cause of death around the world, displays a complex pattern of inheritance. When MI occurs early in life, genetic inheritance is a major component to risk. Previo Show more
Myocardial infarction (MI), a leading cause of death around the world, displays a complex pattern of inheritance. When MI occurs early in life, genetic inheritance is a major component to risk. Previously, rare mutations in low-density lipoprotein (LDL) genes have been shown to contribute to MI risk in individual families, whereas common variants at more than 45 loci have been associated with MI risk in the population. Here we evaluate how rare mutations contribute to early-onset MI risk in the population. We sequenced the protein-coding regions of 9,793 genomes from patients with MI at an early age (≤50 years in males and ≤60 years in females) along with MI-free controls. We identified two genes in which rare coding-sequence mutations were more frequent in MI cases versus controls at exome-wide significance. At low-density lipoprotein receptor (LDLR), carriers of rare non-synonymous mutations were at 4.2-fold increased risk for MI; carriers of null alleles at LDLR were at even higher risk (13-fold difference). Approximately 2% of early MI cases harbour a rare, damaging mutation in LDLR; this estimate is similar to one made more than 40 years ago using an analysis of total cholesterol. Among controls, about 1 in 217 carried an LDLR coding-sequence mutation and had plasma LDL cholesterol > 190 mg dl(-1). At apolipoprotein A-V (APOA5), carriers of rare non-synonymous mutations were at 2.2-fold increased risk for MI. When compared with non-carriers, LDLR mutation carriers had higher plasma LDL cholesterol, whereas APOA5 mutation carriers had higher plasma triglycerides. Recent evidence has connected MI risk with coding-sequence mutations at two genes functionally related to APOA5, namely lipoprotein lipase and apolipoprotein C-III (refs 18, 19). Combined, these observations suggest that, as well as LDL cholesterol, disordered metabolism of triglyceride-rich lipoproteins contributes to MI risk. Show less
📄 PDF DOI: 10.1038/nature13917
APOA5
Huihua Wang, Li Zhang, Jiaxve Cao +7 more · 2015 · PloS one · PLOS · added 2026-04-24
Commercial sheep raised for mutton grow faster than traditional Chinese sheep breeds. Here, we aimed to evaluate genetic selection among three different types of sheep breed: two well-known commercial Show more
Commercial sheep raised for mutton grow faster than traditional Chinese sheep breeds. Here, we aimed to evaluate genetic selection among three different types of sheep breed: two well-known commercial mutton breeds and one indigenous Chinese breed. We first combined locus-specific branch lengths and di statistical methods to detect candidate regions targeted by selection in the three different populations. The results showed that the genetic distances reached at least medium divergence for each pairwise combination. We found these two methods were highly correlated, and identified many growth-related candidate genes undergoing artificial selection. For production traits, APOBR and FTO are associated with body mass index. For meat traits, ALDOA, STK32B and FAM190A are related to marbling. For reproduction traits, CCNB2 and SLC8A3 affect oocyte development. We also found two well-known genes, GHR (which affects meat production and quality) and EDAR (associated with hair thickness) were associated with German mutton merino sheep. Furthermore, four genes (POL, RPL7, MSL1 and SHISA9) were associated with pre-weaning gain in our previous genome-wide association study. Our results indicated that combine locus-specific branch lengths and di statistical approaches can reduce the searching ranges for specific selection. And we got many credible candidate genes which not only confirm the results of previous reports, but also provide a suite of novel candidate genes in defined breeds to guide hybridization breeding. Show less
📄 PDF DOI: 10.1371/journal.pone.0128688
APOBR
Anna-Lena Volckmar, Jie-Yun Song, Ivonne Jarick +12 more · 2015 · PloS one · PLOS · added 2026-04-24
Large-scale genome-wide association studies (GWASs) have identified 97 chromosomal loci associated with increased body mass index in population-based studies on adults. One of these SNPs, rs7359397, t Show more
Large-scale genome-wide association studies (GWASs) have identified 97 chromosomal loci associated with increased body mass index in population-based studies on adults. One of these SNPs, rs7359397, tags a large region (approx. 1MB) with high linkage disequilibrium (r2>0.7), which comprises five genes (SH2B1, APOBR, sulfotransferases: SULT1A1 and SULT1A2, TUFM). We had previously described a rare mutation in SH2B1 solely identified in extremely obese individuals but not in lean controls. The coding regions of the genes APOBR, SULT1A1, SULT1A2, and TUFM were screened for mutations (dHPLC, SSCP, Sanger re-sequencing) in 95 extremely obese children and adolescents. Detected non-synonymous variants were genotyped (TaqMan SNP Genotyping, MALDI TOF, PCR-RFLP) in independent large study groups (up to 3,210 extremely obese/overweight cases, 485 lean controls and 615 obesity trios). In silico tools were used for the prediction of potential functional effects of detected variants. Except for TUFM we detected non-synonymous variants in all screened genes. Two polymorphisms rs180743 (APOBR p.Pro428Ala) and rs3833080 (APOBR p.Gly369_Asp370del9) showed nominal association to (extreme) obesity (uncorrected p = 0.003 and p = 0.002, respectively). In silico analyses predicted a functional implication for rs180743 (APOBR p.Pro428Ala). Both APOBR variants are located in the repetitive region with unknown function. Variants in APOBR contributed as strongly as variants in SH2B1 to the association with extreme obesity in the chromosomal region chr16p11.2. In silico analyses implied no functional effect of several of the detected variants. Further in vitro or in vivo analyses on the functional implications of the obesity associated variants are warranted. Show less
📄 PDF DOI: 10.1371/journal.pone.0125660
APOBR
Qian Wang, Andrew T Grainger, Ani Manichaikul +3 more · 2015 · BMC genetics · BioMed Central · added 2026-04-24
Individuals with dyslipidemia often develop type 2 diabetes, and diabetic patients often have dyslipidemia. It remains to be determined whether there are genetic connections between the 2 disorders. A Show more
Individuals with dyslipidemia often develop type 2 diabetes, and diabetic patients often have dyslipidemia. It remains to be determined whether there are genetic connections between the 2 disorders. A female F2 cohort, generated from BALB/cJ (BALB) and SM/J (SM) Apoe-deficient (Apoe(-/-)) strains, was started on a Western diet at 6 weeks of age and maintained on the diet for 12 weeks. Fasting plasma glucose and lipid levels were measured before and after 12 weeks of Western diet. 144 genetic markers across the entire genome were used for quantitative trait locus (QTL) analysis. One significant QTL on chromosome 9, named Bglu17 [26.4 cM, logarithm of odds ratio (LOD): 5.4], and 3 suggestive QTLs were identified for fasting glucose levels. The suggestive QTL near the proximal end of chromosome 9 (2.4 cM, LOD: 3.12) was replicated at both time points and named Bglu16. Bglu17 coincided with a significant QTL for HDL (high-density lipoprotein) and a suggestive QTL for non-HDL cholesterol levels. Plasma glucose levels were inversely correlated with HDL but positively correlated with non-HDL cholesterol levels in F2 mice on either chow or Western diet. A significant correlation between fasting glucose and triglyceride levels was also observed on the Western diet. Haplotype analysis revealed that "lipid genes" Sik3, Apoa1, and Apoc3 were probable candidates for Bglu17. We have identified multiple QTLs for fasting glucose and lipid levels. The colocalization of QTLs for both phenotypes and the sharing of potential candidate genes demonstrate genetic connections between dyslipidemia and type 2 diabetes. Show less
📄 PDF DOI: 10.1186/s12863-015-0292-y
APOC3
Hui Li, Shun Jiao, Xin Li +3 more · 2015 · Biochemical and biophysical research communications · Elsevier · added 2026-04-24
Aberrant activation of the Wnt/β-catenin signaling pathway is common in human cervical cancers and has great potential therapeutic value. We show that tigecycline, a FDA-approved antibiotic drug, targ Show more
Aberrant activation of the Wnt/β-catenin signaling pathway is common in human cervical cancers and has great potential therapeutic value. We show that tigecycline, a FDA-approved antibiotic drug, targets cervical squamous cell carcinoma through inhibiting Wnt/β-catenin signaling pathway. Tigecycline is effective in inducing apoptosis, inhibiting proliferation and anchorage-independent colony formation of Hela cells. The inhibitory effects of tigecycline are further enhanced upon combination with paclitaxel, a most commonly used chemotherapeutic drug for cervical cancer. In a cervical xenograft model, tigecycline inhibits tumor growth as a single agent and its combination with paclitaxel significantly inhibits more tumor growth throughout the duration of treatment. We further show that tigecycline decreases level of both cytoplasmic and nuclear β-catenin and suppressed Wnt/β-catenin-mediated transcription through increasing levels of Axin 1 in Hela cells. In addition, stabilization or overexpression of β-catenin using pharmacological and genetic approaches abolished the effects of tigecycline in inhibiting proliferation and inducing apoptosis of Hela cells. Our study suggests that tigecycline is a useful addition to the treatment armamentarium for cervical cancer and targeting Wnt/β-catenin represents a potential therapeutic strategy in cervical cancer. Show less
no PDF DOI: 10.1016/j.bbrc.2015.09.140
AXIN1
Li Ma, Xiaolin Wang, Tao Jia +3 more · 2015 · Oncotarget · Impact Journals · added 2026-04-24
Deregulated WNT/β-catenin signaling contributes to the development of a subgroup of hepatocellular carcinoma (HCC), the second leading cause of cancer deaths worldwide. Within this pathway, the tankyr Show more
Deregulated WNT/β-catenin signaling contributes to the development of a subgroup of hepatocellular carcinoma (HCC), the second leading cause of cancer deaths worldwide. Within this pathway, the tankyrase enzymes (TNKS1 and TNKS2) degrade AXIN and thereby enhance β-catenin activity. We evaluate TNKS enzymes as potential therapeutic targets in HCC, and the anti-tumor efficacy of tankyrase inhibitors (XAV939, and its novel nitro-substituted derivative WXL-8) in HCC cells. Using semi-quantitative RT-PCR, we found significantly elevated levels of TNKS1/2 mRNA in tumor liver tissues compared to adjacent non-tumor livers, at protein levels only TNKS1 is increased. In HepG2, Huh7cells, siRNA-mediated knockdown suppression of endogenous TNKS1 and TNKS2 reduced cell proliferation, together with decreased nuclear β-catenin levels. XAV939 and WXL-8 inhibited cell proliferation and colony formation in HepG2, Huh7, and Hep40 cells (p < 0.05), with stabilization of AXIN1 and AXIN2, and decreased β-catenin protein levels. XAV939 and WXL-8 also attenuated rhWNT3A-induced TOPflash luciferase reporter activity in HCC cells, indicating reduced β-catenin transcriptional activity, consistent with decreased nuclear β-catenin levels. In vivo, intra-tumor injections of XAV939 or WXL-8 significantly inhibited the growth of subcutaneous HepG2 xenografts (P < 0.05). We suggest that tankyrase inhibition is a potential therapeutic approach for treating a subgroup HCC with aberrant WNT/β-catenin signaling pathway. Show less
📄 PDF DOI: 10.18632/oncotarget.4455
AXIN1
Shan-Long Ding, Zi-Wei Yang, Jie Wang +3 more · 2015 · World journal of gastroenterology · added 2026-04-24
To comprehensively understand the underlying molecular events accounting for aberrant Wnt signaling activation in hepatocellular carcinoma (HCC). This study was retrospective. The HCC tissue specimens Show more
To comprehensively understand the underlying molecular events accounting for aberrant Wnt signaling activation in hepatocellular carcinoma (HCC). This study was retrospective. The HCC tissue specimens used in this research were obtained from patients who underwent liver surgery. The Catalogue of Somatic Mutations in Cancer (COSMIC) database was searched for the mutation statuses of CTNNB1, TP53, and protein degradation regulator genes of CTNNB1. Dual-luciferase reporter assay was performed with TOP/FOP reporters to detect whether TP53 gain-of-function (GOF) mutations could enhance the transcriptional activity of Wnt signaling. Methylation sensitive restriction enzyme-quantitative PCR was used to explore the methylation status of CpG islands located in the promoters of APC, SFRP1, and SFRP5 in HCCs with different risk factors. Finally, nested-reverse transcription PCR was performed to examine the integration of HBx in front of LINE1 element and the existence of HBx-LINE1 chimeric transcript in Hepatitis B virus-related HCC. All results in this article were analyzed with the software SPSS version 19.0 for Windows, and different groups were compared by χ(2) test as appropriate. Based on the data from COSMIC database, compared with other solid tumors, mutation frequency of CTNNB1 was significantly higher in HCC (P < 0.01). The rate of CTNNB1 mutation was significantly less frequent in Hepatitis B virus-related HCC than in other etiologies (P < 0.01). Dual-luciferase reporter system and TOP/FOP reporter assays confirmed that TP53 GOF mutants were able to enhance the transcriptional ability of Wnt signaling. An exclusive relationship between the status of TP53 and CTNNB1 mutations was observed. However, according to the COSMIC database, TP53 GOF mutation is rare in HCC, which indicates that TP53 GOF mutation is not a reason for the aberrant activation of Wnt signaling in HCC. APC and AXIN1 were mutated in HCC. By using methylation sensitive restriction enzyme-quantitative PCR, hypermethylation of APC was detected in HCC with different risk factors, whereas SFRP1 and SFRP5 were not hypermethylated in any of the HCC etiologies, which indicates that the mutation of APC and AXIN1, together with the methylation of APC could take part in the overactivation of Wnt signaling. Nested-reverse transcription PCR failed to detect the integration of HBx before the LINE1 element, or the existence of an HBx-LINE1 chimeric transcript, suggesting that integration could not play a role in the aberrant activation of Wnt signaling in HCC. In HCC, genetic/epigenetic aberration of CTNNB1 and its protein degradation regulators are the major cause of Wnt signaling overactivation. Show less
no PDF DOI: 10.3748/wjg.v21.i20.6317
AXIN1
Yun Zhou, Maryta Sztukowska, Qian Wang +5 more · 2015 · Infection and immunity · added 2026-04-24
Porphyromonas gingivalis is an established pathogen in periodontal disease and an emerging pathogen in serious systemic conditions, including some forms of cancer. We investigated the effect of P. gin Show more
Porphyromonas gingivalis is an established pathogen in periodontal disease and an emerging pathogen in serious systemic conditions, including some forms of cancer. We investigated the effect of P. gingivalis on β-catenin signaling, a major pathway in the control of cell proliferation and tumorigenesis. Infection of gingival epithelial cells with P. gingivalis did not influence the phosphorylation status of β-catenin but resulted in proteolytic processing. The use of mutants deficient in gingipain production, along with gingipain-specific inhibitors, revealed that gingipain proteolytic activity was required for β-catenin processing. The β-catenin destruction complex components Axin1, adenomatous polyposis coli (APC), and GSK3β were also proteolytically processed by P. gingivalis gingipains. Cell fractionation and Western blotting demonstrated that β-catenin fragments were translocated to the nucleus. The accumulation of β-catenin in the nucleus following P. gingivalis infection was confirmed by immunofluorescence microscopy. A luciferase reporter assay showed that P. gingivalis increased the activity of the β-catenin-dependent TCF/LEF promoter. P. gingivalis did not increase Wnt3a mRNA levels, a finding consistent with P. gingivalis-induced proteolytic processing causing the increase in TCF/LEF promoter activity. Thus, our data indicate that P. gingivalis can induce the noncanonical activation of β-catenin and disassociation of the β-catenin destruction complex by gingipain-dependent proteolytic processing. β-Catenin activation in epithelial cells by P. gingivalis may contribute to a proliferative phenotype. Show less
no PDF DOI: 10.1128/IAI.00302-15
AXIN1
Ming-Zhu Zhang, Olivier Ferrigno, Zhe Wang +10 more · 2015 · Cancer cell · Elsevier · added 2026-04-24
Many types of human cancers having hyperactivated Wnt signaling display no causative alterations in known effectors of this pathway. Here, we report a function of TGIF in Wnt signaling. TGIF associate Show more
Many types of human cancers having hyperactivated Wnt signaling display no causative alterations in known effectors of this pathway. Here, we report a function of TGIF in Wnt signaling. TGIF associates with and diverts Axin1 and Axin2 from the β-catenin destruction complex, therefore allowing β-catenin accrual. Intriguingly, activation of Wnt signaling induces the expression of TGIF, which unveils a feed-forward loop that ensures effective integration of Wnt signaling. In triple-negative breast cancers (TNBC), elevated levels of TGIF correlate with high Wnt signaling and poor survival of patients. Moreover, genetic experiments revealed that Tgif1 ablation impeded mammary tumor development in MMTV-Wnt1 mice, further underscoring a requirement of TGIF for oncogenic Wnt signaling. Show less
📄 PDF DOI: 10.1016/j.ccell.2015.03.002
AXIN1
Weiling Wang, Fei Li, Yi Sun +6 more · 2015 · FASEB journal : official publication of the Federation of American Societies for Experimental Biology · added 2026-04-24
Water channel aquaporin-1 (AQP1) is expressed at epithelial cell plasma membranes in renal proximal tubules and thin descending limb of Henle. Recently, AQP1 was reported to interact with β-catenin. H Show more
Water channel aquaporin-1 (AQP1) is expressed at epithelial cell plasma membranes in renal proximal tubules and thin descending limb of Henle. Recently, AQP1 was reported to interact with β-catenin. Here we investigated the relationship between AQP1 and Wnt signaling in in vitro and in vivo models of autosomal dominant polycystic kidney disease (PKD). AQP1 overexpression decreased β-catenin and cyclinD1 expression, suggesting down-regulation of Wnt signaling, and coimmunoprecipitation showed AQP1 interaction with β-catenin, glycogen synthase kinase 3β, LRP6, and Axin1. AQP1 inhibited cyst development and promoted branching in matrix-grown MDCK cells. In embryonic kidney cultures, AQP1 deletion increased cyst development by up to ∼ 40%. Kidney size and cyst number were significantly greater in AQP1-null PKD mice than in AQP1-expressing PKD mice, with the difference mainly attributed to a greater number of proximal tubule cysts. Biochemical analysis revealed decreased β-catenin phosphorylation and increased β-catenin expression in AQP1-null PKD mice, suggesting enhanced Wnt signaling. These results implicate AQP1 as a novel determinant in renal cyst development that may involve inhibition of Wnt signaling by an AQP1-macromolecular signaling complex. Show less
no PDF DOI: 10.1096/fj.14-260828
AXIN1
Zesong Li, Yi Huang, Honggang Li +29 more · 2015 · Scientific reports · Nature · added 2026-04-24
Non-obstructive azoospermia (NOA), a severe form of male infertility, is often suspected to be linked to currently undefined genetic abnormalities. To explore the genetic basis of this condition, we s Show more
Non-obstructive azoospermia (NOA), a severe form of male infertility, is often suspected to be linked to currently undefined genetic abnormalities. To explore the genetic basis of this condition, we successfully sequenced ~650 infertility-related genes in 757 NOA patients and 709 fertile males. We evaluated the contributions of rare variants to the etiology of NOA by identifying individual genes showing nominal associations and testing the genetic burden of a given biological process as a whole. We found a significant excess of rare, non-silent variants in genes that are key epigenetic regulators of spermatogenesis, such as BRWD1, DNMT1, DNMT3B, RNF17, UBR2, USP1 and USP26, in NOA patients (P = 5.5 × 10(-7)), corresponding to a carrier frequency of 22.5% of patients and 13.7% of controls (P = 1.4 × 10(-5)). An accumulation of low-frequency variants was also identified in additional epigenetic genes (BRDT and MTHFR). Our study suggested the potential associations of genetic defects in genes that are epigenetic regulators with spermatogenic failure in human. Show less
📄 PDF DOI: 10.1038/srep08785
BRWD1
Hiroaki Fujimori, Akira Sato, Sota Kikuhara +6 more · 2015 · Scientific reports · Nature · added 2026-04-24
A comprehensive genome-wide screen of radiosensitization targets in HeLa cells was performed using a shRNA-library/functional cluster analysis and DNMT3B was identified as a candidate target. DNMT3B R Show more
A comprehensive genome-wide screen of radiosensitization targets in HeLa cells was performed using a shRNA-library/functional cluster analysis and DNMT3B was identified as a candidate target. DNMT3B RNAi increased the sensitivity of HeLa, A549 and HCT116 cells to both γ-irradiation and carbon-ion beam irradiation. DNMT3B RNAi reduced the activation of DNA damage responses induced by γ-irradiation, including HP1β-, γH2AX- and Rad51-foci formation. DNMT3B RNAi impaired damage-dependent H2AX accumulation and showed a reduced level of γH2AX induction after γ-irradiation. DNMT3B interacted with HP1β in non-irradiated conditions, whereas irradiation abrogated the DNMT3B/HP1β complex but induced interaction between DNMT3B and H2AX. Consistent with radiosensitization, TP63, BAX, PUMA and NOXA expression was induced after γ-irradiation in DNMT3B knockdown cells. Together with the observation that H2AX overexpression canceled radiosensitization by DNMT3B RNAi, these results suggest that DNMT3B RNAi induced radiosensitization through impairment of damage-dependent HP1β foci formation and efficient γH2AX-induction mechanisms including H2AX accumulation. Enhanced radiosensitivity by DNMT3B RNAi was also observed in a tumor xenograft model. Taken together, the current study implies that comprehensive screening accompanied by a cluster analysis enabled the identification of radiosensitization targets. Downregulation of DNMT3B, one of the targets identified using this method, radiosensitizes cancer cells by disturbing multiple DNA damage responses. Show less
📄 PDF DOI: 10.1038/srep18231
CBX1
Xili Liu, Xin Wang, Xiaojing Yang +6 more · 2015 · eLife · added 2026-04-24
Cell fate decisions are critical for life, yet little is known about how their reliability is achieved when signals are noisy and fluctuating with time. In this study, we show that in budding yeast, t Show more
Cell fate decisions are critical for life, yet little is known about how their reliability is achieved when signals are noisy and fluctuating with time. In this study, we show that in budding yeast, the decision of cell cycle commitment (Start) is determined by the time integration of its triggering signal Cln3. We further identify the Start repressor, Whi5, as the integrator. The instantaneous kinase activity of Cln3-Cdk1 is recorded over time on the phosphorylated Whi5, and the decision is made only when phosphorylated Whi5 reaches a threshold. Cells adjust the threshold by modulating Whi5 concentration in different nutrient conditions to coordinate growth and division. Our work shows that the strategy of signal integration, which was previously found in decision-making behaviors of animals, is adopted at the cellular level to reduce noise and minimize uncertainty. Show less
📄 PDF DOI: 10.7554/eLife.03977
CLN3
Kejun Wang, Dewu Liu, Jules Hernandez-Sanchez +5 more · 2015 · PloS one · PLOS · added 2026-04-24
In this study, 796 male Duroc pigs were used to identify genomic regions controlling growth traits. Three production traits were studied: food conversion ratio, days to 100 KG, and average daily gain, Show more
In this study, 796 male Duroc pigs were used to identify genomic regions controlling growth traits. Three production traits were studied: food conversion ratio, days to 100 KG, and average daily gain, using a panel of 39,436 single nucleotide polymorphisms. In total, we detected 11 genome-wide and 162 chromosome-wide single nucleotide polymorphism trait associations. The Gene ontology analysis identified 14 candidate genes close to significant single nucleotide polymorphisms, with growth-related functions: six for days to 100 KG (WT1, FBXO3, DOCK7, PPP3CA, AGPAT9, and NKX6-1), seven for food conversion ratio (MAP2, TBX15, IVL, ARL15, CPS1, VWC2L, and VAV3), and one for average daily gain (COL27A1). Gene ontology analysis indicated that most of the candidate genes are involved in muscle, fat, bone or nervous system development, nutrient absorption, and metabolism, which are all either directly or indirectly related to growth traits in pigs. Additionally, we found four haplotype blocks composed of suggestive single nucleotide polymorphisms located in the growth trait-related quantitative trait loci and further narrowed down the ranges, the largest of which decreased by ~60 Mb. Hence, our results could be used to improve pig production traits by increasing the frequency of favorable alleles via artificial selection. Show less
📄 PDF DOI: 10.1371/journal.pone.0139207
CPS1
Junwei Nie, Mingyang Jiang, Xiaotian Zhang +10 more · 2015 · Cell reports · Elsevier · added 2026-04-24
RNA G-quadruplexes (G4s) play important roles in RNA biology. However, the function and regulation of mRNA G-quadruplexes in embryonic development remain elusive. Previously, we identified RHAU (DHX36 Show more
RNA G-quadruplexes (G4s) play important roles in RNA biology. However, the function and regulation of mRNA G-quadruplexes in embryonic development remain elusive. Previously, we identified RHAU (DHX36, G4R1) as an RNA helicase that resolves mRNA G-quadruplexes. Here, we find that cardiac deletion of Rhau leads to heart defects and embryonic lethality in mice. Gene expression profiling identified Nkx2-5 mRNA as a target of RHAU that associates with its 5' and 3' UTRs and modulates its stability and translation. The 5' UTR of Nkx2-5 mRNA contains a G-quadruplex that requires RHAU for protein translation, while the 3' UTR of Nkx2-5 mRNA possesses an AU-rich element (ARE) that facilitates RHAU-mediated mRNA decay. Thus, we uncovered the mechanisms underlying Nkx2-5 post-transcriptional regulation during heart development. Meanwhile, this study demonstrates the function of mRNA 5' UTR G-quadruplex-mediated protein translation in organogenesis. Show less
no PDF DOI: 10.1016/j.celrep.2015.09.043
DHX36
Zheng Hu, Da Zhu, Wei Wang +33 more · 2015 · Nature genetics · Nature · added 2026-04-24
Human papillomavirus (HPV) integration is a key genetic event in cervical carcinogenesis. By conducting whole-genome sequencing and high-throughput viral integration detection, we identified 3,667 HPV Show more
Human papillomavirus (HPV) integration is a key genetic event in cervical carcinogenesis. By conducting whole-genome sequencing and high-throughput viral integration detection, we identified 3,667 HPV integration breakpoints in 26 cervical intraepithelial neoplasias, 104 cervical carcinomas and five cell lines. Beyond recalculating frequencies for the previously reported frequent integration sites POU5F1B (9.7%), FHIT (8.7%), KLF12 (7.8%), KLF5 (6.8%), LRP1B (5.8%) and LEPREL1 (4.9%), we discovered new hot spots HMGA2 (7.8%), DLG2 (4.9%) and SEMA3D (4.9%). Protein expression from FHIT and LRP1B was downregulated when HPV integrated in their introns. Protein expression from MYC and HMGA2 was elevated when HPV integrated into flanking regions. Moreover, microhomologous sequence between the human and HPV genomes was significantly enriched near integration breakpoints, indicating that fusion between viral and human DNA may have occurred by microhomology-mediated DNA repair pathways. Our data provide insights into HPV integration-driven cervical carcinogenesis. Show less
no PDF DOI: 10.1038/ng.3178
DLG2
Jupeng Diao, Hongxia Wang, Nannan Chang +4 more · 2015 · Developmental biology · Elsevier · added 2026-04-24
The remarkable regenerative capacity of the zebrafish has made it an important model organism for studying heart regeneration. However, current loss-of-function studies are limited by a lack of condit Show more
The remarkable regenerative capacity of the zebrafish has made it an important model organism for studying heart regeneration. However, current loss-of-function studies are limited by a lack of conditional-knockout and effective gene-knockdown methods for the adult heart. Here, we report a novel siRNA knockdown method facilitated by poly(ethylene glycol)-b-poly(D,L-lactide) (PEG-PLA) nanoparticles. The siRNA-encapsulated nanoparticles successfully entered cells and resulted in remarkable gene-specific knockdown in the adult heart. This effect was demonstrated by down-regulation of the Aldh1a2 and Dusp6 proteins after intrapleural delivery of nanoparticle-encapsulated siRNAs. Furthermore, siRNA-mediated knockdown of Aldh1a2 was sufficient to inhibit myocardial proliferation and decrease the numbers of Gata4-positive cardiomyocytes after ventricular resection. Therefore, the results of this work demonstrate that nanoparticle-facilitated siRNA delivery provides an alternative tool for loss-of-function studies of genes in the adult heart in particular and other organs in general in the adult zebrafish. Show less
no PDF DOI: 10.1016/j.ydbio.2015.08.020
DUSP6
Steven A Schaffert, Christina Loh, Song Wang +8 more · 2015 · Journal of immunology (Baltimore, Md. : 1950) · added 2026-04-24
Understanding the consequences of tuning TCR signaling on selection, peripheral T cell function, and tolerance in the context of native TCR repertoires may provide insight into the physiological contr Show more
Understanding the consequences of tuning TCR signaling on selection, peripheral T cell function, and tolerance in the context of native TCR repertoires may provide insight into the physiological control of tolerance. In this study, we show that genetic ablation of a natural tuner of TCR signaling, mir-181a-1/b-1, in double-positive thymocytes dampened TCR and Erk signaling and increased the threshold of positive selection. Whereas mir-181a-1/b-1 deletion in mice resulted in an increase in the intrinsic reactivity of naive T cells to self-antigens, it did not cause spontaneous autoimmunity. Loss of mir-181a-1/b-1 dampened the induction of experimental autoimmune encephalomyelitis and reduced basal TCR signaling in peripheral T cells and their migration from lymph nodes to pathogenic sites. Taken together, these results demonstrate that tolerance can be modulated by microRNA gene products through the control of opposing activities in T cell selection and peripheral T cell function. Show less
📄 PDF DOI: 10.4049/jimmunol.1401587
DUSP6
Yuanyuan Luo, Shuangshuang Li, Yinping Teng +4 more · 2015 · International journal of clinical and experimental pathology · added 2026-04-24
To describe the expression profiles of FOXA1, DUSP6, and HA117 in different portions of the colon of patients diagnosed with Hirschsprung's disease (HSCR). Colon specimens were collected from 34 HSCR Show more
To describe the expression profiles of FOXA1, DUSP6, and HA117 in different portions of the colon of patients diagnosed with Hirschsprung's disease (HSCR). Colon specimens were collected from 34 HSCR patients and grouped into 3 segments: proximal anastomosis, dilated segment and stenotic segment. Levels of FOXA1, DUSP6, and HA117 RNA were evaluated by real-time PCR. Levels of FOXA1 and DUSP6 protein were analyzed by immunohistochemistry and Western blotting. The levels of FOXA1 and DUSP6 RNA were significantly lower in the stenotic segment compared to proximal anastomosis (P < 0.05). The level of HA117 RNA was significantly higher in the stenotic segment compared to proximal anastomosis (P < 0.05). In proximal anastomosis, FOXA1 and DUSP6 were both expressed at the protein level in ganglion cells and nerve fibers between the circular and longitudinal muscles. In the stenotic segments, positive staining for FOXA1 and DUSP6 was diminished. The levels of FOXA1 and DUSP6 protein were significantly lower in the stenotic segment compared to proximal anastomosis (P < 0.05). Suppression of the FOXA1/DUSP6 signaling pathway may contribute to the development of HSCR. LncRNA HA117 may have an anti-differentiation function, and play a pivotal role in the progression of HSCR. Show less
no PDF
DUSP6
Xiuyan Feng, Yiqian Zhang, Ningjun Shao +10 more · 2015 · American journal of physiology. Renal physiology · added 2026-04-24
Thiazide-sensitive sodium chloride cotransporter (NCC) plays an important role in maintaining blood pressure. Aldosterone is known to modulate NCC abundance. Previous studies reported that dietary sal Show more
Thiazide-sensitive sodium chloride cotransporter (NCC) plays an important role in maintaining blood pressure. Aldosterone is known to modulate NCC abundance. Previous studies reported that dietary salts modulated NCC abundance through either WNK4 [with no lysine (k) kinase 4]-SPAK (Ste20-related proline alanine-rich kinase) or WNK4-extracellular signal-regulated kinase-1 and -2 (ERK1/2) signaling pathways. To exclude the influence of SPAK signaling pathway on the role of the aldosterone-mediated ERK1/2 pathway in NCC regulation, we investigated the effects of dietary salt changes and aldosterone on NCC abundance in SPAK knockout (KO) mice. We found that in SPAK KO mice low-salt diet significantly increased total NCC abundance while reducing ERK1/2 phosphorylation, whereas high-salt diet decreased total NCC while increasing ERK1/2 phosphorylation. Importantly, exogenous aldosterone administration increased total NCC abundance in SPAK KO mice while increasing DUSP6 expression, an ERK1/2-specific phosphatase, and led to decreasing ERK1/2 phosphorylation without changing the ratio of phospho-T53-NCC/total NCC. In mouse distal convoluted tubule (mDCT) cells, aldosterone increased DUSP6 expression while reducing ERK1/2 phosphorylation. DUSP6 Knockdown increased ERK1/2 phosphorylation while reducing total NCC expression. Inhibition of DUSP6 by (E)-2-benzylidene-3-(cyclohexylamino)-2,3-dihydro-1H-inden-1-one increased ERK1/2 phosphorylation and reversed the aldosterone-mediated increments of NCC partly by increasing NCC ubiquitination. Therefore, these data suggest that aldosterone modulates NCC abundance via altering NCC ubiquitination through a DUSP6-dependent ERK1/2 signal pathway in SPAK KO mice and part of the effects of dietary salt changes may be mediated by aldosterone in the DCTs. Show less
no PDF DOI: 10.1152/ajprenal.00543.2014
DUSP6
Hui Zhang, Lei Yan, Yun Bai +5 more · 2015 · Gynecologic oncology · Elsevier · added 2026-04-24
We previously found that Dual-specificity phosphatase 6 (Dusp6) over-expression enhanced the growth-promoting effect of estrogen in endometrial adenocarcinoma cells. The aim of this study was to explo Show more
We previously found that Dual-specificity phosphatase 6 (Dusp6) over-expression enhanced the growth-promoting effect of estrogen in endometrial adenocarcinoma cells. The aim of this study was to explore the correlation of Dusp6 expression with progestin sensitivity in atypical endometrial hyperplasia (AEH) and earlier endometrial carcinomas (EC). Using immunohistochemistry study, we analyzed the expression of Dusp6 protein in AEH. We found that progestin treatment was effective in 89% of AEH and 50% of EC. Before treatment, Dusp6 expression was significantly higher in progestin-sensitive AEH groups compared with progestin-resistant groups. After treatment, Dusp6 expression was significantly upregulated in progestin-sensitive groups, but not in progestin-resistant groups. Moreover, a high-dose of Dusp6 transfection significantly enhanced progestin-induced growth-inhibition in Ishikawa cells. Dusp6 could be a predicting marker for deciding the effectiveness of progestin therapy in AEH. Show less
no PDF DOI: 10.1016/j.ygyno.2014.11.008
DUSP6
Chih-Ping Chen, Ming-Huei Lin, Yi-Yung Chen +6 more · 2015 · Taiwanese journal of obstetrics & gynecology · Elsevier · added 2026-04-24
The aim of this research was to present prenatal diagnosis of Langer-Giedion syndrome (LGS/TRPS type II) and Cornelia de Lange syndrome-4 (CDLS4). A 36-year-old woman underwent amniocentesis at 17 wee Show more
The aim of this research was to present prenatal diagnosis of Langer-Giedion syndrome (LGS/TRPS type II) and Cornelia de Lange syndrome-4 (CDLS4). A 36-year-old woman underwent amniocentesis at 17 weeks of gestation because of advanced maternal age. Conventional cytogenetic analysis of amniocentesis revealed an interstitial deletion of chromosome 8q or del(8)(q23.3q24.13). Level II prenatal ultrasound examination revealed craniofacial dysmorphism. The pregnancy was terminated, and a malformed fetus was delivered with characteristic craniofacial dysmorphism of LGS/TRPS type II and CDLS4. Whole-genome array comparative genomic hybridization (aCGH) on the DNA extracted from cultured amniocytes was performed. The analysis by aCGH revealed a result of arr 8q23.3q24.11 (116,087,006-118,969,399)×1, 8q24.13 (123,086,851-124,470,847)×1 (NCBI build 37) with a 2.88-Mb deletion of 8q23.3-q24.11 encompassing six OMIM genes, TRPS1, EIF3H, RAD21, SLC30A8, MED30, and EXT1, and a 1.383-Mb deletion of 8q24.13 encompassing four OMIM genes, ZHX2, DERL1, ZHX1, and ATAD2. In the present case, the conventional cytogenetic analysis of cultured amniocytes revealed del(8)(q23.3q24.13), whereas aCGH analysis of cultured amniocytes showed the deletions of 8q23.3-q24.11 and 8q24.13 with the presence of the segment 8q24.12. Therefore, aCGH provides the advantage of better understanding of the nature of interstitial deletion and genotype-phenotype correlation in this case. Show less
no PDF DOI: 10.1016/j.tjog.2015.08.013
EXT1
Y Xiong, S Wu, Q Du +2 more · 2015 · Cancer gene therapy · Nature · added 2026-04-24
Y Xiong, S Wu, Q Du, A Wang, Z Wang Show less
Cytogenetic analyses have revealed that complex karyotypes with numerous and highly variable genomic aberrations including single-nucleotide polymorphisms (SNPs) and copy number variants (CNVs), are o Show more
Cytogenetic analyses have revealed that complex karyotypes with numerous and highly variable genomic aberrations including single-nucleotide polymorphisms (SNPs) and copy number variants (CNVs), are observed in most of the conventional osteosarcomas (OSs). Several genome-wide studies have reported that the dysregulated expression of many genes is correlated with genomic aberrations in OS. We first compared OS gene expression in Gene Expression Omnibus (GEO) data sets and genomic aberrations in International Cancer Genome Consortium (ICGC) database to identify differentially expressed genes (DEGs) associated with SNPs or CNVs in OS. Then the function annotation of SNP- or CNV-associated DEGs was performed in terms of gene ontology analysis, pathway analysis and protein-protein interactions (PPIs). Finally, the expression of genes correlated with both SNPs and CNVs were confirmed by quantitative reverse-transcription PCR. Eight publicly available GEO data sets were obtained, and a set of 979 DEGs were identified (472 upregulated and 507 downregulated DEGs). Moreover, we obtained 1039 SNPs mapped in 938 genes, and 583 CNV sites mapped in 2915 genes. Comparing genomic aberrations and DGEs, we found 41 SNP-associated DEGs and 124 CNV-associated DEGs, in which 7 DGEs were associated with both SNPs and CNVs, including WWP1, EXT1, LDHB, C8orf59, PLEKHA5, CCT3 and VWF. The result of function annotation showed that ossification, bone development and skeletal system development were the significantly enriched terms of biological processes for DEGs. PPI network analysis showed that CCT3, COPS3 and WWP1 were the significant hub proteins. We conclude that these genes, including CCT3, COPS3 and WWP1 are candidate driver genes of importance in OS tumorigenesis. Show less
no PDF DOI: 10.1038/cgt.2015.48
EXT1