👤 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, Weilong Wang, Weimin Wang, Weina Wang, Weining Wang, Weipeng Wang, Weiqin Wang, Weiqing Wang, Weirong Wang, Weiwei Wang, Weiwen Wang, Weixiao Wang, Weixue Wang, Weiyan Wang, Weiyu Wang, Weiyuan Wang, Weizhen Wang, Weizhi Wang, Weizhong Wang, Wen Wang, Wen-Chang Wang, Wen-Der Wang, Wen-Fei Wang, Wen-Jie Wang, Wen-Jun Wang, Wen-Qing Wang, Wen-Xuan Wang, Wen-Yan Wang, Wen-Ying Wang, Wen-Yong Wang, Wen-mei Wang, Wenbin Wang, Wenbo Wang, Wence Wang, Wenchao Wang, Wencheng Wang, Wendong Wang, Wenfei Wang, Wengong Wang, Wenhan Wang, Wenhao Wang, Wenhe Wang, Wenhui Wang, Wenjie Wang, Wenjing Wang, Wenju Wang, Wenjuan Wang, Wenjun Wang, Wenkai Wang, Wenkang Wang, Wenke Wang, Wenming Wang, Wenqi Wang, Wenqiang Wang, Wenqing Wang, Wenran Wang, Wenrui Wang, Wentao Wang, Wentian Wang, Wenting Wang, Wenwen Wang, Wenxia Wang, Wenxian Wang, Wenxiang Wang, Wenxiu Wang, Wenxuan Wang, Wenya Wang, Wenyan Wang, Wenyi Wang, Wenying Wang, Wenyu Wang, Wenyuan Wang, Wenzhou Wang, William Wang, Won-Jing Wang, 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, 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 Wang, Yuxing Wang, Yuxuan Wang, Yuxue Wang, Yuyan Wang, Yuyang Wang, Yuyin Wang, Yuying Wang, Yuyong Wang, Yuzhong Wang, Yuzhou Wang, Yuzhuo Wang, Z P Wang, Z Wang, Z-Y Wang, Zai Wang, Zaihua Wang, Ze Wang, Zechen Wang, Zehao Wang, Zehua Wang, Zekun Wang, Zelin Wang, Zeneng Wang, Zengtao Wang, Zeping Wang, Zexin Wang, Zeying Wang, Zeyu Wang, Zeyuan Wang, Zezhou Wang, Zhan Wang, Zhang Wang, Zhanggui Wang, Zhangshun Wang, Zhangying Wang, Zhanju Wang, Zhao Wang, Zhao-Jun Wang, Zhaobo Wang, Zhaofeng Wang, Zhaofu Wang, Zhaohai Wang, Zhaohui Wang, Zhaojing Wang, Zhaojun Wang, Zhaoming Wang, Zhaoqing Wang, Zhaosong Wang, Zhaotong Wang, Zhaoxi Wang, Zhaoxia Wang, Zhaoyu Wang, Zhe Wang, Zhehai Wang, Zhehao Wang, Zhen Wang, ZhenXue Wang, Zhenbin Wang, Zhenchang Wang, Zhenda Wang, Zhendan Wang, Zhendong Wang, Zheng Wang, Zhengbing Wang, Zhengchun Wang, Zhengdong Wang, Zhenghui Wang, Zhengkun Wang, Zhenglong Wang, Zhenguo Wang, Zhengwei Wang, Zhengxuan Wang, Zhengyang Wang, Zhengyi Wang, Zhengyu Wang, Zhenhua Wang, Zhenning Wang, Zhenqian Wang, Zhenshan Wang, Zhentang Wang, Zhenwei Wang, Zhenxi Wang, Zhenyu Wang, Zhenze Wang, Zhenzhen Wang, Zheyi Wang, Zheyue Wang, Zhezhi Wang, Zhi Wang, Zhi Xiao Wang, Zhi-Gang Wang, Zhi-Guo Wang, Zhi-Hao Wang, Zhi-Hong Wang, Zhi-Hua Wang, Zhi-Jian Wang, Zhi-Long Wang, Zhi-Qin Wang, Zhi-Wei Wang, Zhi-Xiao Wang, Zhi-Xin Wang, Zhibo Wang, Zhichao Wang, Zhicheng Wang, Zhicun Wang, Zhidong Wang, Zhifang Wang, Zhifeng Wang, Zhifu Wang, Zhigang Wang, Zhige Wang, Zhiguo Wang, Zhihao Wang, Zhihong Wang, Zhihua Wang, Zhihui Wang, Zhiji Wang, Zhijian Wang, Zhijie Wang, Zhijun Wang, Zhilun Wang, Zhimei Wang, Zhimin Wang, Zhipeng Wang, Zhiping Wang, Zhiqi Wang, Zhiqian Wang, Zhiqiang Wang, Zhiqing Wang, Zhiren Wang, Zhiruo Wang, Zhisheng Wang, Zhitao Wang, Zhiting Wang, Zhiwu Wang, Zhixia Wang, Zhixiang Wang, Zhixiao Wang, Zhixin Wang, Zhixing Wang, Zhixiong Wang, Zhixiu Wang, Zhiying Wang, Zhiyong Wang, Zhiyou Wang, Zhiyu Wang, Zhiyuan Wang, Zhizheng Wang, Zhizhong Wang, Zhong Wang, Zhong-Hao Wang, Zhong-Hui Wang, Zhong-Ping Wang, Zhong-Yu Wang, ZhongXia Wang, Zhongfang Wang, Zhongjing Wang, Zhongli Wang, Zhonglin Wang, Zhongqun Wang, Zhongsu Wang, Zhongwei Wang, Zhongyi Wang, Zhongyu Wang, Zhongyuan Wang, Zhongzhi Wang, Zhou Wang, Zhou-Ping Wang, Zhoufeng Wang, Zhouguang Wang, Zhuangzhuang Wang, Zhugang Wang, Zhulin Wang, Zhulun Wang, Zhuo Wang, Zhuo-Hui Wang, Zhuo-Jue Wang, Zhuo-Xin Wang, Zhuowei Wang, Zhuoying Wang, Zhuozhong Wang, Zhuqing Wang, Zi Wang, Zi Xuan Wang, Zi-Hao Wang, Zi-Qi Wang, Zi-Yi Wang, Zicheng Wang, Zifeng Wang, Zihan Wang, Ziheng Wang, Zihua Wang, Zihuan Wang, Zijian Wang, Zijie Wang, Zijue Wang, Zijun Wang, Zikang Wang, Zikun Wang, Ziliang Wang, Zilin Wang, Ziling Wang, Zilong Wang, Zining Wang, Ziping Wang, Ziqi Wang, Ziqian Wang, Ziqiang Wang, Ziqing Wang, Ziqiu Wang, Zitao Wang, Ziwei Wang, Zixi Wang, Zixia Wang, Zixian Wang, Zixiang Wang, Zixu Wang, Zixuan Wang, Ziyi Wang, Ziying Wang, Ziyu Wang, Ziyun Wang, Zongbao Wang, Zonggui Wang, Zongji Wang, Zongkui Wang, Zongqi Wang, Zongwei Wang, Zou Wang, Zulong Wang, Zumin Wang, Zun Wang, Zunxian Wang, Zuo Wang, Zuoheng Wang, Zuoyan Wang, Zusen Wang
articles
Rui Zhang, Peijuan Cao, Zhongzhou Yang +4 more · 2015 · PloS one · PLOS · added 2026-04-24
Glycosaminoglycans are important regulators of multiple signaling pathways. As a major constituent of the heart extracellular matrix, glycosaminoglycans are implicated in cardiac morphogenesis through Show more
Glycosaminoglycans are important regulators of multiple signaling pathways. As a major constituent of the heart extracellular matrix, glycosaminoglycans are implicated in cardiac morphogenesis through interactions with different signaling morphogens. Ext1 is a glycosyltransferase responsible for heparan sulfate synthesis. Here, we evaluate the function of Ext1 in heart development by analyzing Ext1 hypomorphic mutant and conditional knockout mice. Outflow tract alignment is sensitive to the dosage of Ext1. Deletion of Ext1 in the mesoderm induces a cardiac phenotype similar to that of a mutant with conditional deletion of UDP-glucose dehydrogenase, a key enzyme responsible for synthesis of all glycosaminoglycans. The outflow tract defect in conditional Ext1 knockout(Ext1f/f:Mesp1Cre) mice is attributable to the reduced contribution of second heart field and neural crest cells. Ext1 deletion leads to downregulation of FGF signaling in the pharyngeal mesoderm. Exogenous FGF8 ameliorates the defects in the outflow tract and pharyngeal explants. In addition, Ext1 expression in second heart field and neural crest cells is required for outflow tract remodeling. Our results collectively indicate that Ext1 is crucial for outflow tract formation in distinct progenitor cells, and heparan sulfate modulates FGF signaling during early heart development. Show less
📄 PDF DOI: 10.1371/journal.pone.0136518
EXT1
Peiqiang Su, Ye Wang, David N Cooper +5 more · 2015 · Human mutation · Wiley · added 2026-04-24
The additional mutational complexity associated with copy number variation (CNV) can provide important clues as to the underlying mechanisms of CNV formation. Correct annotation of the additional muta Show more
The additional mutational complexity associated with copy number variation (CNV) can provide important clues as to the underlying mechanisms of CNV formation. Correct annotation of the additional mutational complexity is, however, a prerequisite for establishing the mutational mechanism. We illustrate this point through the characterization of a novel ∼230 kb EXT1 duplication CNV causing autosomal dominant hereditary multiple osteochondromas. Whole-genome sequencing initially identified the CNV as having a 22-bp insertion at the breakpoint junction and, unprecedentedly, multiple breakpoint-flanking micromutations on both sides of the duplication. Further investigation revealed that this genomic rearrangement had a duplication-inverted triplication-duplication structure, the inverted triplication being a 41-bp sequence synthesized from a nearby template. This permitted the identification of the sequence determinants of both the initiation (an inverted Alu repeat) and termination (a triplex-forming sequence) of break-induced replication and suggested a possible model for the repair of replication-associated double-strand breaks. Show less
no PDF DOI: 10.1002/humu.22815
EXT1
Aileen O'Hearn, Minxiu Wang, Han Cheng +6 more · 2015 · Journal of virology · added 2026-04-24
Filoviruses, including both Ebola virus (EBOV) and Marburg virus (MARV), can infect humans and other animals, causing hemorrhagic fever with a high mortality rate. Entry of these viruses into the host Show more
Filoviruses, including both Ebola virus (EBOV) and Marburg virus (MARV), can infect humans and other animals, causing hemorrhagic fever with a high mortality rate. Entry of these viruses into the host is mediated by a single filoviral glycoprotein (GP). GP is composed of two subunits: GP1, which is responsible for attachment and binding to receptor(s) on susceptible cells, and GP2, which mediates viral and cell membrane fusion. Although numerous host factors have been implicated in the entry process, the initial attachment receptor(s) has not been well defined. In this report, we demonstrate that exostosin 1 (EXT1), which is involved in biosynthesis of heparan sulfate (HS), plays a role in filovirus entry. Expression knockdown of EXT1 by small interfering RNAs (siRNAs) impairs GP-mediated pseudoviral entry and that of infectious EBOV and MARV in tissue cultured cells. Furthermore, HS, heparin, and other related glycosaminoglycans (GAGs), to different extents, can bind to and block GP-mediated viral entry and that of infectious filoviruses. These results strongly suggest that HS and other related GAGs are attachment receptors that are utilized by filoviruses for entry and infection. These GAGs may have therapeutic potential in treating EBOV- and MARV-infected patients. Infection by Ebola virus and Marburg virus can cause severe illness in humans, with a high mortality rate, and currently there is no FDA-approved vaccine or therapeutic treatment available. The ongoing 2014 outbreak in West Africa underscores a lack of our understanding in the infection and pathogenesis of these viruses and the urgency of drug discovery and development. In this study, we provide several pieces of evidence that demonstrate that heparan sulfate and other closely related glycosaminoglycans are the molecules that are used by filoviruses for initial attachment. Furthermore, we demonstrate that these glycosaminoglycans can block entry of and infection by filoviruses. Thus, this work provides mechanistic insights on the early step of filoviral infection and suggests a possible therapeutic option for diseases caused by filovirus infection. Show less
no PDF DOI: 10.1128/JVI.03689-14
EXT1
Hongjie Liu, Song Wu, Li Duan +16 more · 2015 · Oncology reports · added 2026-04-24
Hereditary multiple exostosis (HME) is an autosomal inherited skeletal disease whose etiology is not fully understood. To further understand the genetic spectrum of the disease, we analyzed a five-gen Show more
Hereditary multiple exostosis (HME) is an autosomal inherited skeletal disease whose etiology is not fully understood. To further understand the genetic spectrum of the disease, we analyzed a five-generation Chinese family with HME that have observable inheritance. Exome sequencing was performed on three HME individuals and three unaffected individuals from the family. A downstream study confirmed a new C deletion at codon 442 on exon 5 of the exostosin-1 (EXT1) gene as the only pathogenic site which generated a stop codon and caused the truncation of the protein. We rediscovered the deletion in other affected individuals but not in the unaffected individuals from the family. Upon immunohistochemistry assay, we found that the EXT1 protein level of the patients with the novel mutation in our study was less than the level in the patients without the EXT1 mutation from another unrelated family. For a deeper understanding, we analyzed the mutation spectrum of the EXT1 gene. The present study should facilitate a further understanding of HME. Show less
📄 PDF DOI: 10.3892/or.2014.3610
EXT1
Yantao Lv, Wutai Guan, Hanzhen Qiao +4 more · 2015 · Omics : a journal of integrative biology · added 2026-04-24
Mammalian milk is a key source of lipids, providing not only important calories but also essential fatty acids. Veterinary medicine and omics systems sciences intersection, termed as "veterinomics" he Show more
Mammalian milk is a key source of lipids, providing not only important calories but also essential fatty acids. Veterinary medicine and omics systems sciences intersection, termed as "veterinomics" here, has received little attention to date but stands to offer much promise for building bridges between human and animal health. We determined the changes in porcine mammary genes and proteomics expression associated with milk triacylglycerol (TAG) synthesis and secretion from late pregnancy to lactation. TAG content and fatty acid (FA) composition were determined in porcine colostrum (the 1st day of lactation) and milk (the 17th day of lactation). The mammary transcriptome for 70 genes and 13 proteins involved in TAG synthesis and secretion from six sows, each at d -17(late pregnancy), d 1(early lactation), and d 17 (peak lactation) relative to parturition were analyzed using quantitative real-time PCR and Western blot analyses. The TAG content and the concentrations of de novo synthesized FAs, saturated FAs, and monounsaturated FAs were higher in milk than in colostrum (p<0.05). Robust upregulation with high relative mRNA abundance was evident during lactation for genes associated with FA uptake (VLDLR, LPL, CD36), FA activation (ACSS2, ACSL3), and intracellar transport (FABP3), de novo FA synthesis (ACACA, FASN), FA elongation (ELOVL1), FA desaturation (SCD, FADS1), TAG synthesis (GPAM, AGPAT1, LPIN1, DGAT1), lipid droplet formation (BTN2A1, XDH, PLIN2), and transcription factors and nuclear receptors (SREBP1, SCAP, INSIG1/2). In conclusion, a wide variety of lipogenic genes and proteins regulate the channeling of FAs towards milk TAG synthesis and secretion in porcine mammary gland tissue. These findings inform future omics strategies to increase milk fat production and lipid profile and attest to the rise of both veterinomics and lipidomics in postgenomics life sciences. Show less
no PDF DOI: 10.1089/omi.2015.0102
FADS1
Jwu Jin Khong, Lynn Yuning Wang, Gordon K Smyth +9 more · 2015 · Investigative ophthalmology & visual science · added 2026-04-24
We aimed to determine differentially expressed genes relevant to orbital inflammation and orbital fat expansion in thyroid orbitopathy (TO) using microarray gene profiling in a case-control study. Hum Show more
We aimed to determine differentially expressed genes relevant to orbital inflammation and orbital fat expansion in thyroid orbitopathy (TO) using microarray gene profiling in a case-control study. Human orbital adipose samples were obtained from individuals with active TO (n = 12), inactive TO (n = 21), and normal controls (n = 21). Gene expression profiles were examined using microarray analysis and were compared between active and inactive TO, and between active TO and normal controls. Top ranked differentially expressed genes were validated by real-time RT-PCR in an additional eight active TO, 13 inactive TO, and 11 normal controls and correlated with gene set enrichment analysis (GSEA) and molecular pathways analysis. Seven hundred twenty-one probes (683 genes) and 806 probes (735 genes) were significantly differentially expressed in comparing active to inactive TO and in comparing active TO to healthy controls, respectively. All selected genes were confirmed to be differentially expressed by real-time RT-PCR. Multiple top ranked genes in active versus inactive TO comparison are overrepresented by immune and inflammatory response genes. They include defensins (DEFA1, DEFA1B, DEFA3), which were overexpressed by 3.05- to 4.14-fold and TIMD4 by 4.20-fold. Markers for adipogenesis were overexpressed including SCD, FADS1, and SCDP1. Gene set enrichment analysis revealed dysregulation of epigenetic signatures, T-cell activation, Th1 differentiation, defensin pathway, cell adhesion, cytoskeleton organization, apoptosis, cell cycling, and lipid metabolism in active TO. Active TO is characterized by upregulation of genes involved in cell-mediated immune, innate immune, and inflammatory response and enhanced orbital adipogenesis. TIMD4, DEFA1, DEFA1B, and DEFA3 genes may be involved in the innate immune-mediated orbital inflammation in TO. Epigenetic mechanisms may play a role in the pathogenesis of TO. Show less
no PDF DOI: 10.1167/iovs.15-17185
FADS1
Fang Wang, Zhongkai Zhou, Xiaochong Ren +4 more · 2015 · Lipids in health and disease · BioMed Central · added 2026-04-24
The fruiting body of Ganoderma lucidum has been used as a traditional herbal medicine for many years. However, to the date, there is no detailed study for describing the effect of G. lucidum spores on Show more
The fruiting body of Ganoderma lucidum has been used as a traditional herbal medicine for many years. However, to the date, there is no detailed study for describing the effect of G. lucidum spores on oxidative stress, blood glucose level and lipid compositions in animal models of type 2 diabetic rats, in particular the effect on the gene expression profiles associated with glucose and lipid metabolisms. G. lucidum spores powder (GLSP) with a shell-broken rate >99.9 % was used. Adult male Sprague-Dawley rats were randomly divided into three groups (n = 8/group). Group 1: Normal control, normal rats with ordinary feed; Group 2: Model control, diabetic rats with ordinary feed without intervention; Group 3: GLSP, diabetic rats with ordinary feed, an intervention group utilizing GLSP of 1 g per day by oral gavages for 4 consecutive weeks. Type 2 diabetic rats were obtained by streptozocin (STZ) injection. The changes in the levels of glucose, triglycerides, total cholesterol and HDL-cholesterol in blood samples were analyzed after GLSP intervention. Meanwhile, gene expressions associated with the possible molecular mechanism of GLSP regulation were also investigated using a quantitative RT-PCR. The reduction of blood glucose level occurred within the first 2 weeks of GLSP intervention and the lipid synthesis in the diabetic rats of GLSP group was significantly decreased at 4 weeks compared to the model control group. Furthermore, it was also found that GLSP intervention greatly attenuated the level of oxidative stress in the diabetic rats. Quantitative RT-PCR analysis showed up-regulation of lipid metabolism related genes (Acox1, ACC, Insig-1 and Insig-2) and glycogen synthesis related genes (GS2 and GYG1) in GLSP group compared to model control group. Additionally, there were no significant changes in the expression of other genes, such as SREBP-1, Acly, Fas, Fads1, Gpam, Dgat1, PEPCK and G6PC1. This study might indicate that GLSP consumption could provide a beneficial effect in terms of lowering the blood glucose levels by promoting glycogen synthesis and inhibiting gluconeogenesis. Meanwhile, GLSP treatment was also associated with the improvement of blood lipid compositions through the regulation of cholesterol homeostasis in the type 2 diabetic rats. Show less
📄 PDF DOI: 10.1186/s12944-015-0045-y
FADS1
Min Yao, Jing Li, Tian Xie +7 more · 2015 · Diabetes research and clinical practice · Elsevier · added 2026-04-24
Several studies have shown associations between the composition of polyunsaturated fatty acids (PUFAs) in various tissues and type 2 diabetes mellitus (T2DM) development in European populations. Genet Show more
Several studies have shown associations between the composition of polyunsaturated fatty acids (PUFAs) in various tissues and type 2 diabetes mellitus (T2DM) development in European populations. Genetic variants of fatty acid desaturase (FADS) contribute to the variations of PUFA composition. Here we have explored whether similar correlations are also true among Chinese Han people. A case-control study was employed to examine this correlation in Han Chinese people. The study included 421 healthy adults and 331 T2DM patients. The ratio of arachidonic acid/linoleic acid (AA/LA), which reflects Δ6 desaturase activity, was significantly increased in T2DM patients. Furthermore, the ratio of eicosapentaenoic acid/α-linolenic acid (EPA/ALA), which reflects Δ5 desaturase activity, was markedly decreased in T2DM patients. Importantly, among four single nucleotide polymorphisms (rs174545, rs2072114, rs174602 and rs174616) in the FADS1-FADS2 gene cluster, only minor allele (T) of rs174616 was associated with decreased risk of T2DM in both codominant and dominant models after adjustment for age, gender and BMI. Furthermore, the ratio of AA/LA in both controls and T2DM was reduced in T carriers while an increased proportion of LA was seen in T2DM patients compared with control patients. These data suggest that in northern Han Chinese people, the minor allele (T) of rs174616 in the FADS1-FADS2 gene cluster is associated with a decreased conversion rate of LA to AA, which may contribute to decreased reduced risk of developing T2DM. Show less
no PDF DOI: 10.1016/j.diabres.2015.03.009
FADS1
Zhongkai Zhou, Fang Wang, Xiaochong Ren +2 more · 2015 · International journal of biological macromolecules · Elsevier · added 2026-04-24
The effect of resistant starch (RS) administration on biological parameters including blood glucose, lipids composition and oxidative stress of type 2 diabetic rats was investigated. The results showe Show more
The effect of resistant starch (RS) administration on biological parameters including blood glucose, lipids composition and oxidative stress of type 2 diabetic rats was investigated. The results showed blood glucose level, total cholesterol and triglycerides concentrations significantly reduced, and high-density lipoprotein cholesterol concentration was doubly increased in the rats of RS administration group compared to model control group (P<0.01). The analyses of genes involved in glucose and lipid metabolism pathways demonstrated that the expression levels of lipid oxidation gene Acox1, glycogen synthesis genes, GS2 and GYG1, and insulin-induced genes, Insig-1 and Insig-2, were significantly up-regulated (P<0.01). In contrast, fatty acids and triglycerides synthesis and metabolism-related gene SREBP-1, fatty acid synthesis gene Fads1 and gluconeogenesis gene G6PC1 were greatly down-regulated. The mechanism study shows that the lowering of blood glucose level in diabetic rats by feeding RS is regulated through promoting glycogen synthesis and inhibiting gluconeogenesis, and the increased lipid metabolism is modulated through promoting lipid oxidation and cholesterol homeostasis. Our study revealed for the first time that the regulation of hepatic genes expression involved in glucose and lipids metabolisms in diabetic rats could be achieved even at a moderate level of RS consumption. Show less
no PDF DOI: 10.1016/j.ijbiomac.2015.01.052
FADS1
Dariush Mozaffarian, Edmond K Kabagambe, Catherine O Johnson +26 more · 2015 · The American journal of clinical nutrition · added 2026-04-24
Circulating trans fatty acids (TFAs), which cannot be synthesized by humans, are linked to adverse health outcomes. Although TFAs are obtained from diet, little is known about subsequent influences (e Show more
Circulating trans fatty acids (TFAs), which cannot be synthesized by humans, are linked to adverse health outcomes. Although TFAs are obtained from diet, little is known about subsequent influences (e.g., relating to incorporation, metabolism, or intercompetition with other fatty acids) that could alter circulating concentrations and possibly modulate or mediate impacts on health. The objective was to elucidate novel biologic pathways that may influence circulating TFAs by evaluating associations between common genetic variation and TFA biomarkers. We performed meta-analyses using 7 cohorts of European-ancestry participants (n = 8013) having measured genome-wide variation in single-nucleotide polymorphisms (SNPs) and circulating TFA biomarkers (erythrocyte or plasma phospholipids), including trans-16:1n-7, total trans-18:1, trans/cis-18:2, cis/trans-18:2, and trans/trans-18:2. We further evaluated SNPs with genome-wide significant associations among African Americans (n = 1082), Chinese Americans (n = 669), and Hispanic Americans (n = 657) from 2 of these cohorts. Among European-ancestry participants, 31 SNPs in or near the fatty acid desaturase (FADS) 1 and 2 cluster were associated with cis/trans-18:2; a top hit was rs174548 (β = 0.0035, P = 4.90 × 10(-15)), an SNP previously associated with circulating n-3 and n-6 polyunsaturated fatty acid concentrations. No significant association was identified for other TFAs. rs174548 in FADS1/2 was also associated with cis/trans-18:2 in Hispanic Americans (β = 0.0053, P = 1.05 × 10(-6)) and Chinese Americans (β = 0.0028, P = 0.002) but not African Americans (β = 0.0009, P = 0.34); however, in African Americans, fine mapping identified a top hit in FADS2 associated with cis/trans-18:2 (rs174579: β = 0.0118, P = 4.05 × 10(-5)). The association between rs174548 and cis/trans-18:2 remained significant after further adjustment for individual circulating n-3 and n-6 fatty acids, except arachidonic acid. After adjustment for arachidonic acid concentrations, the association between rs174548 and cis/trans-18:2 was nearly eliminated in European-ancestry participants (β-coefficient reduced by 86%), with similar reductions in Hispanic Americans and Chinese Americans. Our findings provide novel evidence for genetic regulation of cis/trans-18:2 by the FADS1/2 cluster and suggest that this regulation may be influenced/mediated by concentrations of arachidonic acid, an n-6 polyunsaturated fat. Show less
no PDF DOI: 10.3945/ajcn.114.094557
FADS1
Caren E Smith, Jack L Follis, Jennifer A Nettleton +33 more · 2015 · Molecular nutrition & food research · Wiley · added 2026-04-24
Tissue concentrations of omega-3 fatty acids may reduce cardiovascular disease risk, and genetic variants are associated with circulating fatty acids concentrations. Whether dietary fatty acids intera Show more
Tissue concentrations of omega-3 fatty acids may reduce cardiovascular disease risk, and genetic variants are associated with circulating fatty acids concentrations. Whether dietary fatty acids interact with genetic variants to modify circulating omega-3 fatty acids is unclear. We evaluated interactions between genetic variants and fatty acid intakes for circulating alpha-linoleic acid, eicosapentaenoic acid, docosahexaenoic acid, and docosapentaenoic acid. We conducted meta-analyses (N = 11 668) evaluating interactions between dietary fatty acids and genetic variants (rs174538 and rs174548 in FADS1 (fatty acid desaturase 1), rs7435 in AGPAT3 (1-acyl-sn-glycerol-3-phosphate), rs4985167 in PDXDC1 (pyridoxal-dependent decarboxylase domain-containing 1), rs780094 in GCKR (glucokinase regulatory protein), and rs3734398 in ELOVL2 (fatty acid elongase 2)). Stratification by measurement compartment (plasma versus erthyrocyte) revealed compartment-specific interactions between FADS1 rs174538 and rs174548 and dietary alpha-linolenic acid and linoleic acid for docosahexaenoic acid and docosapentaenoic acid. Our findings reinforce earlier reports that genetically based differences in circulating fatty acids may be partially due to differences in the conversion of fatty acid precursors. Further, fatty acids measurement compartment may modify gene-diet relationships, and considering compartment may improve the detection of gene-fatty acids interactions for circulating fatty acid outcomes. Show less
📄 PDF DOI: 10.1002/mnfr.201400734
FADS1
Libo Wang, Shaminie Athinarayanan, Guanglong Jiang +3 more · 2015 · Hepatology (Baltimore, Md.) · Wiley · added 2026-04-24
Fatty acid desaturase (FADS) genes and their variants have been associated with multiple metabolic phenotypes, including liver enzymes and hepatic fat accumulation, but the detailed mechanism remains Show more
Fatty acid desaturase (FADS) genes and their variants have been associated with multiple metabolic phenotypes, including liver enzymes and hepatic fat accumulation, but the detailed mechanism remains unclear. We aimed to delineate the role of FADSs in modulating lipid composition in human liver. We performed a targeted lipidomic analysis of a variety of phospholipids, sphingolipids, and ceramides among 154 human liver tissue samples. The associations between previously genome-wide association studies (GWASs)-identified six FADS single-nucleotide polymorphisms (SNPs), and these lipid levels as well as total hepatic fat content (HFC) were tested. The potential function of these SNPs in regulating transcription of three FADS genes (FADS1, FADS2, and FADS3) in the locus was also investigated. We found that though these SNPs were in high linkage disequilibrium (r(2) > 0.8), the rare alleles of these SNPs were consistently and significantly associated with the accumulation of multiple long-chain fatty acids (LCFAs), with C47H85O13P (C36:4), a phosphatidylinositol (PI), and C43H80O8PN (C38:3), a phosphatidylethanolamine (PE), reached the Bonferroni corrected significance (P < 3 × 10(-4)). Meanwhile, these SNPs were significantly associated with increased ratios between the more saturated and relatively less saturated forms of LCFAs, especially between PEs, PIs, and phosphatidylcholines (PCs; P ≤ 3.5 × 10(-6)). These alleles were also associated with increased total HFC (P < 0.05). Further analyses revealed that these alleles were associated with decreased hepatic expression of FADS1 (P = 0.0018 for rs174556), but not FADS2 or FADS3 (P > 0.05). Our findings revealed critical insight into the mechanism underlying FADS1 and its polymorphisms in modulating hepatic lipid deposition by altering gene transcription and controlling lipid composition in human livers. Show less
📄 PDF DOI: 10.1002/hep.27373
FADS1
Xinming Zhou, Yongguang Xiao, Zhifu Mao +4 more · 2015 · Microvascular research · Elsevier · added 2026-04-24
The excessive proliferation of vascular smooth muscle cells was key factor in the restenosis of vein graft. And the Notch signaling was demonstrated to regulate vSMC proliferation and differentiation. Show more
The excessive proliferation of vascular smooth muscle cells was key factor in the restenosis of vein graft. And the Notch signaling was demonstrated to regulate vSMC proliferation and differentiation. Soluble Jagged-1 (sJag1) can inhibit Notch signaling in vitro and in vivo; however, its capacity to suppress restenosis of vein graft remains unknown. Under the microscope, the left jugular vein of these rats was interposed into the left common carotid artery, followed without any treatment (control), or with Ad-Jag1 (treatment) or placebo (DMSO) post operation. We showed that Ad-Jag1 can attenuate restenosis of vein graft by inducing decreased proliferation and increased apoptosis in vivo. Notch1-Hey2 signaling is critical for the development of intima thickening by controlling vSMC-fate determination. By blocking Notch signaling, Ad-Jag1 can significantly inhibit intima thickening. These studies identify that Ad-Jag1 can restore the vSMC phenotype and inhibit the vSMC proliferation by suppression of Notch1 signaling, and thus open a new avenue for the treatment of restenosis in vein graft. Show less
no PDF DOI: 10.1016/j.mvr.2015.01.009
HEY2
Hyojin Kim, Lan Huang, Paul J Critser +7 more · 2015 · Cytotherapy · Elsevier · added 2026-04-24
Human cord blood (CB) is enriched in circulating endothelial colony forming cells (ECFCs) that display high proliferative potential and in vivo vessel forming ability. Because Notch signaling is criti Show more
Human cord blood (CB) is enriched in circulating endothelial colony forming cells (ECFCs) that display high proliferative potential and in vivo vessel forming ability. Because Notch signaling is critical for embryonic blood vessel formation in utero, we hypothesized that Notch pathway activation may enhance cultured ECFC vasculogenic properties in vivo. In vitro ECFC stimulation with an immobilized chimeric Notch ligand (Delta-like1(ext-IgG)) led to significant increases in the mRNA and protein levels of Notch regulated Hey2 and EphrinB2 that were blocked by treatment with γ-secretase inhibitor addition. However, Notch stimulated preconditioning in vitro failed to enhance ECFC vasculogenesis in vivo. In contrast, in vivo co-implantation of ECFCs with OP9-Delta-like 1 stromal cells that constitutively expressed the Notch ligand delta-like 1 resulted in enhanced Notch activated ECFC-derived increased vessel density and enlarged vessel area in vivo, an effect not induced by OP9 control stromal implantation. This Notch activation was associated with diminished apoptosis in the exposed ECFC. We conclude that Notch pathway activation in ECFC in vivo via co-implanted stromal cells expressing delta-like 1 promotes vasculogenesis and augments blood vessel formation via diminishing apoptosis of the implanted ECFC. Show less
📄 PDF DOI: 10.1016/j.jcyt.2014.12.003
HEY2
Hua-Cheng Liu, Danyan Zhu, Chan Wang +8 more · 2015 · PloS one · PLOS · added 2026-04-24
Etomidate is a rapid hypnotic intravenous anesthetic agent. The major side effect of etomidate is the reduced plasma concentration of corticosteroids, leading to the abnormal reaction of adrenals. Cor Show more
Etomidate is a rapid hypnotic intravenous anesthetic agent. The major side effect of etomidate is the reduced plasma concentration of corticosteroids, leading to the abnormal reaction of adrenals. Cortisol and testosterone biosynthesis has similar biosynthetic pathway, and shares several common steroidogenic enzymes, such as P450 side chain cleavage enzyme (CYP11A1) and 3β-hydroxysteroid dehydrogenase 1 (HSD3B1). The effect of etomidate on Leydig cell steroidogenesis during the cell maturation process is not well established. Immature Leydig cells isolated from 35 day-old rats were cultured with 30 μM etomidate for 3 hours in combination with LH, 8Br-cAMP, 25R-OH-cholesterol, pregnenolone, progesterone, androstenedione, testosterone and dihydrotestosterone, respectively. The concentrations of 5α-androstanediol and testosterone in the media were measured by radioimmunoassay. Leydig cells were cultured with various concentrations of etomidate (0.3-30 μM) for 3 hours, and total RNAs were extracted. Q-PCR was used to measure the mRNA levels of following genes: Lhcgr, Scarb1, Star, Cyp11a1, Hsd3b1, Cyp17a1, Hsd17b3, Srd5a1, and Akr1c14. The testis mitochondria and microsomes from 35-day-old rat testes were prepared and used to detect the direct action of etomidate on CYP11A1 and HSD3B1 activity. In intact Leydig cells, 30 μM etomidate significantly inhibited androgen synthesis. Further studies showed that etomidate also inhibited the LH- stimulated androgen production. On purified testicular mitochondria and ER fractions, etomidate competitively inhibited both CYP11A1 and HSD3B1 activities, with the half maximal inhibitory concentration (IC50) values of 12.62 and 2.75 μM, respectively. In addition, etomidate inhibited steroidogenesis-related gene expression. At about 0.3 μM, etomidate significantly inhibited the expression of Akr1C14. At the higher concentration (30 μM), it also reduced the expression levels of Cyp11a1, Hsd17b3 and Srd5a1. In conclusion, etomidate directly inhibits the activities of CYP11A1 and HSD3B1, and the expression levels of Cyp11a1 and Hsd17b3, leading to the lower production of androgen by Leydig cells. Show less
📄 PDF DOI: 10.1371/journal.pone.0139311
HSD17B12
Yi Ren, Xiao-guang Yang, Xue-zhi Li +3 more · 2015 · Zhen ci yan jiu = Acupuncture research · added 2026-04-24
To observe the effect of electroacupuncture (EA) intervention on expression of cytochrome P 450 side chain cleavage (P 450 scc) and 17 β-hydroxysteroid dehydrogenase 3 (17 β-HSD3) in the testis in par Show more
To observe the effect of electroacupuncture (EA) intervention on expression of cytochrome P 450 side chain cleavage (P 450 scc) and 17 β-hydroxysteroid dehydrogenase 3 (17 β-HSD3) in the testis in partial androgen deficiency of aging male (PADAM) rats so as to reveal its mechanism underlying improving PADAM. Thirty male SD rats were randomly and equally divided into control, model, and EA groups. The PADAM model was established by intraperitoneal injection of cyclophosphamide (20 mg · kg(-1) · d(-1)), once daily for 5 days. EA (20-30 Hz, 1-3 mA) was applied to bilateral "Shenshu" (BL 23) and "Guanyuan" (CV 4) for 15 min, once daily for 8 weeks. Serum total testosterone (TT) and free testosterone (FT) levels were measured using enzyme-linked immunosorbent assay (ELISA). The expression levels of P 450 scc/17 β-HSD3 proteins and mRNA in the testis tissue were assayed by immunohistochemistry, Western bolt (WB) and RT-polymerase chain reaction (RT-PCR), separately. Compared with the control group, both serum TT, FT levels and expression levels of P450 scc/17 β-HSD3 proteins and mRNA in the testis tissue in the model group were significantly down-regulated (P<0.01). After EA intervention, compared with the model group, the cyclophosphamide-induced decrease of serum TT, FT levels and the expression levels of P 450 scc/17 β-HSD3 proteins and mRNA in the testis was reversed in the EA group (P<0.01). EA intervention is effective in up-regulating serum TT and FT, testicular P 450 scc and 17 β-HSD3 proteins and mRNA levels in PADAM rats, which may be one of its mechanisms underlying improvement of PADAM. Show less
no PDF
HSD17B12
Chen-Yan Zhang, Wei-Qi Wang, Jiong Chen +1 more · 2015 · The Journal of steroid biochemistry and molecular biology · Elsevier · added 2026-04-24
The reductive 17β-hydroxysteroid dehydrogenases which catalyze the last step in estrogen activation for estrogen dependent breast cancer cells were studied. Their biological function and the effects o Show more
The reductive 17β-hydroxysteroid dehydrogenases which catalyze the last step in estrogen activation for estrogen dependent breast cancer cells were studied. Their biological function and the effects of their knockdown for cancer cell proliferation were demonstrated. The multidisciplinary study involves enzyme catalysis, sex-hormone and cell cycle regulation, as well as cell proliferation in breast cancer cells. Reductive 17β-HSD1, -7 and -12 were studied in the main breast cancer epithelial cells MCF-7 and T47D. Modification of estradiol and 5α-dihydrotestosterone concentrations was monitored by ELISA assay while corresponding cell viability measured by MTT assay. Cell cycle was determined by flow cytometry. Dual activity of estradiol activation and 5α-dihydrotestosterone reduction by 17β-HSD1 and -7 was critical for breast cancer cell (T47D and MCF-7) viability. Cell viability was decreased by 35.8% ± 1.6% in T47D cells after simultaneously knocking down 17β-HSD1 and -7. MCF-7 cell viability was decreased by 29.3% ± 4.2% using a combination of siRNAs and inhibitors. By knocking down 17β-HSD7, we have provided the first demonstration of the significant role of this enzyme in the stimulation of breast cancer cell viability as a result of its high activity on androgen reduction with positive feedback on estradiol production. A further decrease in cell viability was not observed with additional knockdown of 17β-HSD12 after 17β-HSD1 and 7. Breast cancer cell cycle progression was impeded to enter the S phase from G0-G1 after knocking down 17β-HSD1 and -7. In summary, this is the first demonstration that the dual activity in estrone activation and 5α-dihydrotestosterone reduction are the functional basis of reductive 17β-HSDs in breast cancer cells. 17β-HSD1 and -7 are principal reductive 17β-HSDs and major players in the viability of estrogen-dependent breast cancer cells. Combined targeting of these enzymes may be potential for molecular therapy of such cancer. Show less
no PDF DOI: 10.1016/j.jsbmb.2014.09.017
HSD17B12
C H Li, Y Gao, S Wang +7 more · 2015 · Genetics and molecular research : GMR · added 2026-04-24
Cell reprogramming mediated by histone methylation and demethylation is crucial for the activation of the embryonic genome in early embryonic development. In this study, we employed quantitative real- Show more
Cell reprogramming mediated by histone methylation and demethylation is crucial for the activation of the embryonic genome in early embryonic development. In this study, we employed quantitative real-time polymerase chain reaction (qRT-PCR) to detect mRNA levels and expression patterns of all known histone demethylases in early germinal vesicle stage and in vitro-matured metaphase II (MII) oocytes (which are commonly used as donor cells for nuclear transfer). On screening, the Jumonji domain containing 1C (JMJD1C) gene had the highest level of expression and hence was used for subsequent experiments. We also found that JMJD1C was primarily expressed in the nucleus and showed relatively high levels of expression at the 2-cell, 4-cell, 8-cell, 16-cell, morula, and blastocyst stages of embryos developed from MII oocytes fertilized in vitro. Further, we knocked down the JMJD1C gene in MII oocytes using siRNA and monitored the cleavage of zygotes and development of early embryos after in vitro fertilization. The results showed that the zygote cleavage and blastocyst rates of the transfection group were reduced by 57.1 ± 0.07 and 50 ± 0.01% respectively, which were significantly lower than those of the negative control group (P < 0.05). These data suggest that JMJD1C plays a key role in the normal development of early bovine embryos. Our results also provide a theoretical basis for the investigation of the role and molecular mechanism of histone demethylation in the early development of bovine embryos. Show less
no PDF DOI: 10.4238/2015.December.23.12
JMJD1C
Tingwei Guo, Jonathan H Chung, Tao Wang +7 more · 2015 · American journal of human genetics · Elsevier · added 2026-04-24
We performed whole exome sequence (WES) to identify genetic modifiers on 184 individuals with 22q11.2 deletion syndrome (22q11DS), of whom 89 case subjects had severe congenital heart disease (CHD) an Show more
We performed whole exome sequence (WES) to identify genetic modifiers on 184 individuals with 22q11.2 deletion syndrome (22q11DS), of whom 89 case subjects had severe congenital heart disease (CHD) and 95 control subjects had normal hearts. Three genes including JMJD1C (jumonji domain containing 1C), RREB1 (Ras responsive element binding protein 1), and SEC24C (SEC24 family member C) had rare (MAF < 0.001) predicted deleterious single-nucleotide variations (rdSNVs) in seven case subjects and no control subjects (p = 0.005; Fisher exact and permutation tests). Because JMJD1C and RREB1 are involved in chromatin modification, we investigated other histone modification genes. Eighteen case subjects (20%) had rdSNVs in four genes (JMJD1C, RREB1, MINA, KDM7A) all involved in demethylation of histones (H3K9, H3K27). Overall, rdSNVs were enriched in histone modifier genes that activate transcription (Fisher exact p = 0.0004, permutations, p = 0.0003, OR = 5.16); however, rdSNVs in control subjects were not enriched. This implicates histone modification genes as influencing risk for CHD in presence of the deletion. Show less
no PDF DOI: 10.1016/j.ajhg.2015.10.013
JMJD1C
Yongyue Wei, Zhaoxi Wang, Li Su +6 more · 2015 · Chest · added 2026-04-24
Platelets are believed to be critical in pulmonary-origin ARDS as mediators of endothelial damage through their interactions with fibrinogen and multiple signal transduction pathways. A prior meta-ana Show more
Platelets are believed to be critical in pulmonary-origin ARDS as mediators of endothelial damage through their interactions with fibrinogen and multiple signal transduction pathways. A prior meta-analysis identified five loci for platelet count (PLT): BAD, LRRC16A, CD36, JMJD1C, and SLMO2. This study aims to validate the quantitative trait loci (QTLs) of PLT within BAD, LRRC16A, CD36, JMJD1C, and SLMO2 among critically ill patients and to investigate the associations of these QTLs with ARDS risk that may be mediated through PLT. ARDS cases and at-risk control subjects were recruited from the intensive care unit of the Massachusetts General Hospital. Exome-wide genotyping data of 629 ARDS cases and 1,026 at-risk control subjects and genome-wide gene expression profiles of 18 at-risk control subjects were generated for analysis. Single-nucleotide polymorphism (SNP) rs7766874 within LRRC16A was a significant locus for PLT among at-risk control subjects (β = -13.00; 95% CI, -23.22 to -2.77; P = .013). This association was validated using LRRC16A gene expression data from at-risk control subjects (β = 77.03 per 1 SD increase of log2-transformed expression; 95% CI, 27.26-126.80; P = .005). Further, rs7766874 was associated with ARDS risk conditioned on PLT (OR = 0.68; 95% CI, 0.51-0.90; P = .007), interacting with PLT (OR = 1.15 per effect allele per 100 × 103/μL of PLT; 95% CI, 1.03-1.30; P = .015), and mediated through PLT (indirect OR = 1.045; 95% CI, 1.007-1.085; P = .021). Our findings support the role of LRRC16A in platelet formation and suggest the importance of LRRC16A in ARDS pathophysiology by interacting with, and being mediated through, platelets. Show less
no PDF DOI: 10.1378/chest.14-1246
JMJD1C
Chao Wang, Hongyang Wang, Yu Zhang +3 more · 2015 · Molecular ecology resources · Blackwell Publishing · added 2026-04-24
Pigs from Asia and Europe were independently domesticated from c. 9000 years ago. During this period, strong artificial selection has led to dramatic phenotypic changes in domestic pigs. However, the Show more
Pigs from Asia and Europe were independently domesticated from c. 9000 years ago. During this period, strong artificial selection has led to dramatic phenotypic changes in domestic pigs. However, the genetic basis underlying these morphological and behavioural adaptations is relatively unknown, particularly for indigenous Chinese pigs. Here, we performed a genome-wide analysis to screen 196 regions with selective sweep signals in Tongcheng pigs, which are a typical indigenous Chinese breed. Genes located in these regions have been found to be involved in lipid metabolism, melanocyte differentiation, neural development and other biological processes, which coincide with the evolutionary phenotypic changes in this breed. A synonymous substitution, c.669T>C, in ESR1, which colocalizes with a major quantitative trait locus for litter size, shows extreme differences in allele frequency between Tongcheng pigs and wild boars. Notably, the variant C allele in this locus exhibits high allele frequency in most Chinese populations, suggesting a consequence of positive selection. Five genes (PRM1, PRM2, TNP2, GPR149 and JMJD1C) related to reproductive traits were found to have high haplotype similarity in Chinese breeds. Two selected genes, MITF and EDNRB, are implied to shape the two-end black colour trait in Tongcheng pig. Subsequent SNP microarray studies of five Chinese white-spotted breeds displayed a concordant signature at both loci, suggesting that these two genes are responsible for colour variations in Chinese breeds. Utilizing massively parallel sequencing, we characterized the candidate sites that adapt to artificial and environmental selections during the Chinese pig domestication. This study provides fundamental proof for further research on the evolutionary adaptation of Chinese pigs. Show less
no PDF DOI: 10.1111/1755-0998.12311
JMJD1C
Shougang Guo, Jie Zhang, Chunjuan Wang +1 more · 2015 · Zhonghua yi xue za zhi · added 2026-04-24
To explore the effect of LINGO-1 silencing on movement function of experimental autoimmune encephalomyelitis (EAE) mice. EAE was established by induction of MOG35-55 in female C57/BL6 mice. Then femal Show more
To explore the effect of LINGO-1 silencing on movement function of experimental autoimmune encephalomyelitis (EAE) mice. EAE was established by induction of MOG35-55 in female C57/BL6 mice. Then female EAE mice (n=105) were completely randomly divided into 5 groups: group A (n=21): 5 µl 5×10(9) Tu/ml lentiviral vectors encoding LINGO-1shRNA (LV/LINGO-1-shRNA) by intracerebroventricular (ICV) injection, group B (n=21): 5 µl 5×10(8)Tu/ml LV/LINGO-1-shRNA by ICV injection, group C (n=21): 5 µl 5×10(7) Tu/ml LV/LINGO-1-shRNA by ICV injection, group D (n=21): 5 µl LVCON053 by ICV injection and group E (n=21): untreated.The movement function was scored and the expression of LINGO-1 protein was detected by Western blot on day 1, 3, 7, 14, 21, 30 after ICV among different groups. Luxol fast blue staining was performed to know about conditions of myelin sheath on day 30. The expression of LINGO-1 in EAE mouse was obviously downregulated ever since day 7 after LV/LINGO-1-shRNA implantation.Group B and C achieved the most reduction of LINGO-1 expression (1.99±0.13, 2.08±0.10, P<0.05, P<0.01). Simultaneously, the movement functional score of group A, B and C was lowered at different levels from day 7 (3.11±0.13, 2.42±0.13, 2.96±0.10 vs 3.56±0.15, 3.87±0.12, P<0.01, P<0.01, P<0.05), with the most marked decrease in group B. The densities of myelin sheaths in group A and B were higher than untreated group on day 30 (0.72±0.09, 0.83±0.11 vs 0.56±0.10, P<0.05, P<0.01). LV/LINGO-1shRNA by ICV injection is an effective method to silence LINGO-1 expression. LINGO-1 silencing could ameliorate motor function and promote formation of myelin sheaths. But the effects do not enhance with the increase of LV/LINGO-1-shRNA dose. Show less
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LINGO1
Wei Hua, He Wu, Min Zhou +7 more · 2015 · Zhonghua bing li xue za zhi = Chinese journal of pathology · added 2026-04-24
To study biological effect of recombinant human erythropoietin (RhEPO) on the expression of oligodendrocyte in the neuron glia antigen 2(NG2), Nogo receptor-interacting protein 1(LINGO-1), myelin basi Show more
To study biological effect of recombinant human erythropoietin (RhEPO) on the expression of oligodendrocyte in the neuron glia antigen 2(NG2), Nogo receptor-interacting protein 1(LINGO-1), myelin basic protein (MBP) and myelin associated glycoprotein (MAG), and to explore the protective mechanism of RhEPO for oligodendrocyte after cerebral infarction. Experimental rats were randomly divided into the treatment group (RhEPO at a dose of 3 000 U/kg) or saline control group. Both groups received intraperitoneal injection of RhEPO after cerebral ischemia in 30 min, 3 h, 6 h, 12 h and 24 h, which was administered daily for 7 days. The modified neurological severity score (mNSS) and histology were analyzed, and immunohistochemistry was used to detect the protein expression of NG2, MAG, MBP and LINGO-1. The overall mNSS of RhEPO treatment group significantly decreased compared with the saline control group on the seventh day after cerebral infarction (P<0.05). Such treatment effect was more obvious in the treatment group at 30 min and 3 h (P<0.01). Compared with the saline control group, the numbers of NG2 positive cells increased in RhEPO treatment group. In contrast, the expression of LINGO-1 protein significantly decreased (P<0.05), with a dramatic decrease observed at 30 min and 3 h (P<0.01). However, the expression of MBP protein decreased more significantly in saline control group, while the level of the MAG protein expression increased. The differences were statistically significant (P<0.05), especially at 30 min (P<0.01). After cerebral ischemia, RhEPO promotes the proliferation of NG2 positive cells, and inhibits the expression of LINGO-1 and MAG proteins. RhEPO improves the proliferation and differentiation of oligodendrocyte precursor cells, which in turn protects neuronal function, particularly at the early phase of ischemia. Show less
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LINGO1
Zhao-Huan Zhang, Jiao-Jiao Li, Qing-Jin Wang +4 more · 2015 · Molecular and cellular neurosciences · Elsevier · added 2026-04-24
LINGO-1 is a transmembrane receptor expressed primarily in the central nervous system (CNS) and plays an important role in myelination. Recent studies have indicated that it is also involved in oligod Show more
LINGO-1 is a transmembrane receptor expressed primarily in the central nervous system (CNS) and plays an important role in myelination. Recent studies have indicated that it is also involved in oligodendrocyte precursor cell (OPC) survival and differentiation; however, the downstream signaling pathway underlying OPC development is unknown. In our previous study, we found that LINGO-1 is associated with WNK1 in mediating Nogo-induced neurite extension inhibition by RhoA activation. In an effort to identify the role of LINGO-1-WNK1 in OPCs, we first confirmed that WNK1 is also expressed in OPCs and co-localized with LINGO-1, which suppresses WNK1 expression by RNA interference-attenuated Nogo66-induced inhibition of OPC differentiation. Furthermore, we mapped the WNK1 kinase domain using several fragmented peptides to identify the key region of interaction with LINGO-1. We found that a sequence corresponding to the D6 peptide is necessary for the interaction. Finally, we found that using the TAT-D6 peptide to introduce D6 peptide into primary cultured OPC inhibits the association between LINGO-1 and WNK1 and significantly attenuates Nogo66-induced inhibition of OPC differentiation. Taken together, our results show that WNK1, via a specific region on WNK1 kinase domain, interacts with LINGO-1, thus mediating Nogo66-inhibited OPC differentiation. Show less
no PDF DOI: 10.1016/j.mcn.2015.03.003
LINGO1
Qiang Wang, Miaoxin Li, Zhenxing Yang +14 more · 2015 · Scientific reports · Nature · added 2026-04-24
Schizophrenia is a heritable, heterogeneous common psychiatric disorder. In this study, we evaluated the hypothesis that de novo variants (DNVs) contribute to the pathogenesis of schizophrenia. We per Show more
Schizophrenia is a heritable, heterogeneous common psychiatric disorder. In this study, we evaluated the hypothesis that de novo variants (DNVs) contribute to the pathogenesis of schizophrenia. We performed exome sequencing in Chinese patients (N = 45) with schizophrenia and their unaffected parents (N = 90). Forty genes were found to contain DNVs. These genes had enriched transcriptional co-expression profile in prenatal frontal cortex (Bonferroni corrected p < 9.1 × 10(-3)), and in prenatal temporal and parietal regions (Bonferroni corrected p < 0.03). Also, four prenatal anatomical subregions (VCF, MFC, OFC and ITC) have shown significant enrichment of connectedness in co-expression networks. Moreover, four genes (LRP1, MACF1, DICER1 and ABCA2) harboring the damaging de novo mutations are strongly prioritized as susceptibility genes by multiple evidences. Our findings in Chinese schizophrenic patients indicate the pathogenic role of DNVs, supporting the hypothesis that schizophrenia is a neurodevelopmental disease. Show less
📄 PDF DOI: 10.1038/srep18209
MACF1
Duo Lv, Dan-Dan Zhang, Hao Wang +10 more · 2015 · Gene · Elsevier · added 2026-04-24
Both genetic predisposition and lifestyle factors are associated with the risk for obesity. Multiple obesity loci have been identified using genome-wide association studies mainly in European populati Show more
Both genetic predisposition and lifestyle factors are associated with the risk for obesity. Multiple obesity loci have been identified using genome-wide association studies mainly in European populations. The aims of this study were to examine the associations of these loci with obesity and gene×dietary behavior interactions among Chinese children and adolescents. Nineteen candidate SNPs were genotyped using Sequenom technology in the Chinese children (N=2977, 853 obese and 2124 controls, aged 7-17). Dietary behaviors were assessed using self-administered questionnaires. After adjusting for age, sex and multiple testing, MC4R rs17782313, SEC16B rs543874, MAP2K5 rs2241423 and KCTD15 rs11084753 were associated with obesity and obesity-related traits (all P<0.005), with odd ratios ranging from 1.22 to 2.15. Dose-response association was significant between genetic risk score, which was calculated by summing the risk alleles, and the risk of obesity (P<0.001). Multiplicative interaction was found between rs543874 and salt preference on obesity with an OR of 4.40 (95% CI, 1.12-17.30). Additive interactions with salt preference were found in rs17782313 and rs11084753. Our findings indicated that rs17782313, rs543874, rs2241423 and rs11084753 were associated with the risk for children obesity in China, and interaction of genetic variants with diet behaviors on obesity. Show less
no PDF DOI: 10.1016/j.gene.2015.01.054
MAP2K5
Yuhui Wang, Jose Viscarra, Sun-Joong Kim +1 more · 2015 · Nature reviews. Molecular cell biology · Nature · added 2026-04-24
Fatty acid and fat synthesis in the liver is a highly regulated metabolic pathway that is important for very low-density lipoprotein (VLDL) production and thus energy distribution to other tissues. Ha Show more
Fatty acid and fat synthesis in the liver is a highly regulated metabolic pathway that is important for very low-density lipoprotein (VLDL) production and thus energy distribution to other tissues. Having common features at their promoter regions, lipogenic genes are coordinately regulated at the transcriptional level. Transcription factors, such as upstream stimulatory factors (USFs), sterol regulatory element-binding protein 1C (SREBP1C), liver X receptors (LXRs) and carbohydrate-responsive element-binding protein (ChREBP) have crucial roles in this process. Recently, insights have been gained into the signalling pathways that regulate these transcription factors. After feeding, high blood glucose and insulin levels activate lipogenic genes through several pathways, including the DNA-dependent protein kinase (DNA-PK), atypical protein kinase C (aPKC) and AKT-mTOR pathways. These pathways control the post-translational modifications of transcription factors and co-regulators, such as phosphorylation, acetylation or ubiquitylation, that affect their function, stability and/or localization. Dysregulation of lipogenesis can contribute to hepatosteatosis, which is associated with obesity and insulin resistance. Show less
📄 PDF DOI: 10.1038/nrm4074
MLXIPL
Coffee and Caffeine Genetics Consortium, Marilyn C Cornelis, Enda M Byrne +155 more · 2015 · Molecular psychiatry · Nature · added 2026-04-24
Coffee and Caffeine Genetics Consortium, Marilyn C Cornelis, Enda M Byrne, Tõnu Esko, Michael A Nalls, Andrea Ganna, Nina Paynter, Keri L Monda, Najaf Amin, Krista Fischer, Frida Renstrom, Julius S Ngwa, Ville Huikari, Alana Cavadino, Ilja M Nolte, Alexander Teumer, Kai Yu, Pedro Marques-Vidal, Rajesh Rawal, Ani Manichaikul, Mary K Wojczynski, Jacqueline M Vink, Jing Hua Zhao, George Burlutsky, Jari Lahti, Vera Mikkilä, Rozenn N Lemaitre, Joel Eriksson, Solomon K Musani, Toshiko Tanaka, Frank Geller, Jian'an Luan, Jennie Hui, Reedik Mägi, Maria Dimitriou, Melissa E Garcia, Weang-Kee Ho, Margaret J Wright, Lynda M Rose, Patrik Ke Magnusson, Nancy L Pedersen, David Couper, Ben A Oostra, Albert Hofman, Mohammad Arfan Ikram, Henning W Tiemeier, Andre G Uitterlinden, Frank Ja van Rooij, Inês Barroso, Ingegerd Johansson, Luting Xue, Marika Kaakinen, Lili Milani, Chris Power, Harold Snieder, Ronald P Stolk, Sebastian E Baumeister, Reiner Biffar, Fangyi Gu, François Bastardot, Zoltán Kutalik, David R Jacobs, Nita G Forouhi, Evelin Mihailov, Lars Lind, Cecilia Lindgren, Karl Michaëlsson, Andrew Morris, Majken Jensen, Kay-Tee Khaw, Robert N Luben, Jie Jin Wang, Satu Männistö, Mia-Maria Perälä, Mika Kähönen, Terho Lehtimäki, Jorma Viikari, Dariush Mozaffarian, Kenneth Mukamal, Bruce M Psaty, Angela Döring, Andrew C Heath, Grant W Montgomery, Norbert Dahmen, Teresa Carithers, Katherine L Tucker, Luigi Ferrucci, Heather A Boyd, Mads Melbye, Jorien L Treur, Dan Mellström, Jouke Jan Hottenga, Inga Prokopenko, Anke Tönjes, Panos Deloukas, Stavroula Kanoni, Mattias Lorentzon, Denise K Houston, Yongmei Liu, John Danesh, Asif Rasheed, Marc A Mason, Alan B Zonderman, Lude Franke, Bruce S Kristal, International Parkinson’s Disease Genomics Consortium (IPDGC), North American Brain Expression Consortium (NABEC), UK Brain Expression Consortium (UKBEC), Juha Karjalainen, Danielle R Reed, Harm-Jan Westra, Michele K Evans, Danish Saleheen, Tamara B Harris, George Dedoussis, Gary Curhan, Michael Stumvoll, John Beilby, Louis R Pasquale, Bjarke Feenstra, Stefania Bandinelli, Jose M Ordovas, Andrew T Chan, Ulrike Peters, Claes Ohlsson, Christian Gieger, Nicholas G Martin, Melanie Waldenberger, David S Siscovick, Olli Raitakari, Johan G Eriksson, Paul Mitchell, David J Hunter, Peter Kraft, Eric B Rimm, Dorret I Boomsma, Ingrid B Borecki, Ruth Jf Loos, Nicholas J Wareham, Peter Vollenweider, Neil Caporaso, Hans Jörgen Grabe, Marian L Neuhouser, Bruce Hr Wolffenbuttel, Frank B Hu, Elina Hyppönen, Marjo-Riitta Järvelin, L Adrienne Cupples, Paul W Franks, Paul M Ridker, Cornelia M Van Duijn, Gerardo Heiss, Andres Metspalu, Kari E North, Erik Ingelsson, Jennifer A Nettleton, Rob M Van Dam, Daniel I Chasman Show less
Coffee, a major dietary source of caffeine, is among the most widely consumed beverages in the world and has received considerable attention regarding health risks and benefits. We conducted a genome- Show more
Coffee, a major dietary source of caffeine, is among the most widely consumed beverages in the world and has received considerable attention regarding health risks and benefits. We conducted a genome-wide (GW) meta-analysis of predominately regular-type coffee consumption (cups per day) among up to 91,462 coffee consumers of European ancestry with top single-nucleotide polymorphisms (SNPs) followed-up in ~30 062 and 7964 coffee consumers of European and African-American ancestry, respectively. Studies from both stages were combined in a trans-ethnic meta-analysis. Confirmed loci were examined for putative functional and biological relevance. Eight loci, including six novel loci, met GW significance (log10Bayes factor (BF)>5.64) with per-allele effect sizes of 0.03-0.14 cups per day. Six are located in or near genes potentially involved in pharmacokinetics (ABCG2, AHR, POR and CYP1A2) and pharmacodynamics (BDNF and SLC6A4) of caffeine. Two map to GCKR and MLXIPL genes related to metabolic traits but lacking known roles in coffee consumption. Enhancer and promoter histone marks populate the regions of many confirmed loci and several potential regulatory SNPs are highly correlated with the lead SNP of each. SNP alleles near GCKR, MLXIPL, BDNF and CYP1A2 that were associated with higher coffee consumption have previously been associated with smoking initiation, higher adiposity and fasting insulin and glucose but lower blood pressure and favorable lipid, inflammatory and liver enzyme profiles (P<5 × 10(-8)).Our genetic findings among European and African-American adults reinforce the role of caffeine in mediating habitual coffee consumption and may point to molecular mechanisms underlying inter-individual variability in pharmacological and health effects of coffee. Show less
📄 PDF DOI: 10.1038/mp.2014.107
MLXIPL
Wei Wu, Chao-Xia Lu, Yi-Ning Wang +7 more · 2015 · Journal of the American Heart Association · added 2026-04-24
MYBPC3 dysfunctions have been proven to induce dilated cardiomyopathy, hypertrophic cardiomyopathy, and/or left ventricular noncompaction; however, the genotype-phenotype correlation between MYBPC3 an Show more
MYBPC3 dysfunctions have been proven to induce dilated cardiomyopathy, hypertrophic cardiomyopathy, and/or left ventricular noncompaction; however, the genotype-phenotype correlation between MYBPC3 and restrictive cardiomyopathy (RCM) has not been established. The newly developed next-generation sequencing method is capable of broad genomic DNA sequencing with high throughput and can help explore novel correlations between genetic variants and cardiomyopathies. A proband from a multigenerational family with 3 live patients and 1 unrelated patient with clinical diagnoses of RCM underwent a next-generation sequencing workflow based on a custom AmpliSeq panel, including 64 candidate pathogenic genes for cardiomyopathies, on the Ion Personal Genome Machine high-throughput sequencing benchtop instrument. The selected panel contained a total of 64 genes that were reportedly associated with inherited cardiomyopathies. All patients fulfilled strict criteria for RCM with clinical characteristics, echocardiography, and/or cardiac magnetic resonance findings. The multigenerational family with 3 adult RCM patients carried an identical nonsense MYBPC3 mutation, and the unrelated patient carried a missense mutation in the MYBPC3 gene. All of these results were confirmed by the Sanger sequencing method. This study demonstrated that MYBPC3 gene mutations, revealed by next-generation sequencing, were associated with familial and sporadic RCM patients. It is suggested that the next-generation sequencing platform with a selected panel provides a highly efficient approach for molecular diagnosis of hereditary and idiopathic RCM and helps build new genotype-phenotype correlations. Show less
no PDF DOI: 10.1161/JAHA.115.001879
MYBPC3
Tao Tian, Jizheng Wang, Hu WANG +7 more · 2015 · Heart and vessels · Springer · added 2026-04-24
Left ventricular non-compaction (LVNC) is genetically heterogeneous. It has been previously shown that LVNC is associated with defects in TAZ, DNTA, LDB3, YWHAE, MIB1, PRDM16, and sarcomeric genes. Th Show more
Left ventricular non-compaction (LVNC) is genetically heterogeneous. It has been previously shown that LVNC is associated with defects in TAZ, DNTA, LDB3, YWHAE, MIB1, PRDM16, and sarcomeric genes. This study was aimed to investigate sarcomeric gene mutations in a Chinese population with LVNC. From 2004 to 2010, 57 unrelated Chinese patients with LVNC were recruited at Fuwai Hospital, Beijing, China. Detailed clinical evaluation was performed on the probands and available family members. DNA samples isolated from the peripheral blood of the index cases were screened for 10 sarcomeric genes, including MYH7, MYBPC3, MYL2, MYL3, MYH6, TNNC1, TNNT2, TNNI3, TPM1, and ACTC1. Seven heterozygous mutations (6 missense and 1 deletion) were identified in 7 (12 %) of the patients. These mutations were distributed among 4 genes, 4 in MYH7, and 1 each in ACTC1, TNNT2, and TPM1. Six of the mutations were novel and another one was reported previously. All mutations affected conserved amino acid residues and were predicted to alter the structure of the proteins by in silico analysis. No significant difference was observed between mutation-positive and mutation-negative patients with respect to clinical characteristics at baseline and mortality during follow-up. In conclusion, our study indicates that sarcomeric gene mutations are uncommon causes of LVNC in Chinese patients and genetic background of the disease may be divergent among the different races. Show less
no PDF DOI: 10.1007/s00380-014-0503-x
MYBPC3