👤 Ke Chen

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2981
Articles
1996
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Also published as: Ai-Qun Chen, Aiping Chen, Alex Chen, Alex F Chen, Alice P Chen, Alice Y Chen, Alice Ye A Chen, Allen Menglin Chen, Alon Chen, Alvin Chen, An Chen, Andrew Chen, Anqi Chen, Aoshuang Chen, Aozhou Chen, B Chen, B-S Chen, Baihua Chen, Ban Chen, Bang Chen, Bang-dang Chen, Bao-Bao Chen, Bao-Fu Chen, Bao-Sheng Chen, Bao-Ying Chen, Baofeng Chen, Baojiu Chen, Baolin Chen, Baosheng Chen, Baoxiang Chen, Beidong Chen, Beijian Chen, Ben-Kuen Chen, Benjamin Chen, Benjamin Jieming Chen, Benjamin P C Chen, Beth L Chen, Bihong T Chen, Bin Chen, Bing Chen, Bing-Bing Chen, Bing-Feng Chen, Bing-Huei Chen, Bingdi Chen, Bingqian Chen, Bingqing Chen, Bingyu Chen, Binlong Chen, Binzhen Chen, Bo Chen, Bo-Fang Chen, Bo-Jun Chen, Bo-Rui Chen, Bo-Sheng Chen, Bohe Chen, Bohong Chen, Bosong Chen, Bowang Chen, Bowei Chen, Bowen Chen, Boyu Chen, Brian Chen, C Chen, C Y Chen, C Z Chen, C-Y Chen, Cai-Long Chen, Caihong Chen, Can Chen, Cancan Chen, Canrong Chen, Canyu Chen, Caressa Chen, Carl Pc Chen, Carol Chen, Carol X-Q Chen, Catherine Qing Chen, Ceshi Chen, Chan Chen, Chang Chen, Chang-Lan Chen, Chang-Zheng Chen, Changjie Chen, Changya Chen, Changyan Chen, Chanjuan Chen, Chao Chen, Chao-Jung Chen, Chao-Wei Chen, Chaochao Chen, Chaojin Chen, Chaoli Chen, Chaoping Chen, Chaoqun Chen, Chaoran Chen, Chaoyi Chen, Chaoyue Chen, Chen Chen, Chen-Mei Chen, Chen-Sheng Chen, Chen-Yu Chen, Cheng Chen, Cheng-Fong Chen, Cheng-Sheng Chen, Cheng-Yi Chen, Cheng-Yu Chen, Chengchuan Chen, Chengchun Chen, Chengde Chen, Chengsheng Chen, Chengwei Chen, Chenyang Chen, Chi Chen, Chi-Chien Chen, Chi-Hua Chen, Chi-Long Chen, Chi-Yu Chen, Chi-Yuan Chen, Chi-Yun Chen, Chian-Feng Chen, Chider Chen, Chien-Hsiun Chen, Chien-Jen Chen, Chien-Lun Chen, Chien-Ting Chen, Chien-Yu Chen, Chih-Chieh Chen, Chih-Mei Chen, Chih-Ping Chen, Chih-Ta Chen, Chih-Wei Chen, Chih-Yi Chen, Chin-Chuan Chen, Ching Kit Chen, Ching-Hsuan Chen, Ching-Jung Chen, Ching-Wen Chen, Ching-Yi Chen, Ching-Yu Chen, Chiqi Chen, Chiung Mei Chen, Chiung-Mei Chen, Chixiang Chen, Chong Chen, Chongyang Chen, Christina Y Chen, Christina Yingxian Chen, Christopher S Chen, Chu Chen, Chu-Huang Chen, Chuanbing Chen, Chuannan Chen, Chuanzhi Chen, Chuck T Chen, Chueh-Tan Chen, Chujie Chen, Chun Chen, Chun-An Chen, Chun-Chi Chen, Chun-Fa Chen, Chun-Han Chen, Chun-Houh Chen, Chun-Wei Chen, Chun-Yuan Chen, Chung-Hao Chen, Chung-Hsing Chen, Chung-Hung Chen, Chung-Jen Chen, Chung-Yung Chen, Chunhai Chen, Chunhua Chen, Chunji Chen, Chunjie Chen, Chunlin Chen, Chunnuan Chen, Chunxiu Chen, Chuo Chen, Chuyu Chen, Cindi Chen, Constance Chen, Cuicui Chen, Cuie Chen, Cuilan Chen, Cuimin Chen, Cuncun Chen, D F Chen, D M Chen, D-F Chen, D. Chen, Dafang Chen, Daijie Chen, Daiwen Chen, Daiyu Chen, Dake Chen, Dali Chen, Dan Chen, Dan-Dan Chen, Dandan Chen, Danlei Chen, Danli Chen, Danmei Chen, Danna Chen, Danni Chen, Danxia Chen, Danxiang Chen, Danyang Chen, Danyu Chen, Daoyuan Chen, Dapeng Chen, Dawei Chen, Defang Chen, Dejuan Chen, Delong Chen, Denghui Chen, Dengpeng Chen, Deqian Chen, Dexi Chen, Dexiang Chen, Dexiong Chen, Deying Chen, Deyu Chen, Di Chen, Di-Long Chen, Dian Chen, Dianke Chen, Ding Chen, Diyun Chen, Dong Chen, Dong-Mei Chen, Dong-Yi Chen, Dongli Chen, Donglong Chen, Dongquan Chen, Dongrong Chen, Dongsheng Chen, Dongxue Chen, Dongyan Chen, Dongyin Chen, Du-Qun Chen, Duan-Yu Chen, Duo Chen, Duo-Xue Chen, Duoting Chen, E S Chen, Eleanor Y Chen, Elizabeth H Chen, Elizabeth S Chen, Elizabeth Suchi Chen, Emily Chen, En-Qiang Chen, Erbao Chen, Erfei Chen, Erqu Chen, Erzhen Chen, Everett H Chen, F Chen, F-K Chen, Fa Chen, Fa-Xi Chen, Fahui Chen, Fan Chen, Fang Chen, Fang-Pei Chen, Fang-Yu Chen, Fang-Zhi Chen, Fang-Zhou Chen, Fangfang Chen, Fangli Chen, Fangyan Chen, Fangyuan Chen, Faye H Chen, Fei Chen, Fei Xavier Chen, Feifan Chen, Feifeng Chen, Feilong Chen, Feixue Chen, Feiyang Chen, Feiyu Chen, Feiyue Chen, Feng Chen, Feng-Jung Chen, Feng-Ling Chen, Fenghua Chen, Fengju Chen, Fengling Chen, Fengming Chen, Fengrong Chen, Fengwu Chen, Fengyang Chen, Fred K Chen, Fu Chen, Fu-Shou Chen, Fumei Chen, Fusheng Chen, Fuxiang Chen, Gang Chen, Gao B Chen, Gao Chen, Gao-Feng Chen, Gaoyang Chen, Gaoyu Chen, Gaozhi Chen, Gary Chen, Gary K Chen, Ge Chen, Gen-Der Chen, Geng Chen, Gengsheng Chen, Ginny I Chen, Gong Chen, Gongbo Chen, Gonghai Chen, Gonglie Chen, Guan-Wei Chen, Guang Chen, Guang-Chao Chen, Guang-Yu Chen, Guangchun Chen, Guanghao Chen, Guanghong Chen, Guangjie Chen, Guangju Chen, Guangliang Chen, Guanglong Chen, Guangnan Chen, Guangping Chen, Guangquan Chen, Guangyao Chen, Guangyi Chen, Guangyong Chen, Guanjie Chen, Guanren Chen, Guanyu Chen, Guanzheng Chen, Gui Mei Chen, Gui-Hai Chen, Gui-Lai Chen, Guihao Chen, Guiqian Chen, Guiquan Chen, Guiying Chen, Guo Chen, Guo-Chong Chen, Guo-Jun Chen, Guo-Rong Chen, Guo-qing Chen, Guochao Chen, Guochong Chen, Guofang Chen, Guohong Chen, Guohua Chen, Guojun Chen, Guoliang Chen, Guopu Chen, Guoshun Chen, Guoxun Chen, Guozhong Chen, Guozhou Chen, H Chen, H Q Chen, H T Chen, Hai-Ning Chen, Haibing Chen, Haibo Chen, Haide Chen, Haifeng Chen, Haijiao Chen, Haimin Chen, Haiming Chen, Haining Chen, Haiqin Chen, Haiquan Chen, Haitao Chen, Haiyan Chen, Haiyang Chen, Haiyi Chen, Haiying Chen, Haiyu Chen, Haiyun Chen, Han Chen, Han-Bin Chen, Han-Chun Chen, Han-Hsiang Chen, Han-Min Chen, Hanbei Chen, Hang Chen, Hangang Chen, Hanjing Chen, Hanlin Chen, Hanqing Chen, Hanwen Chen, Hanxi Chen, Hanyong Chen, Hao Chen, Hao Yu Chen, Hao-Zhu Chen, Haobo Chen, Haodong Chen, Haojie Chen, Haoran Chen, Haotai Chen, Haotian Chen, Haoting Chen, Haoyun Chen, Haozhu Chen, Harn-Shen Chen, Haw-Wen Chen, He-Ping Chen, Hebing Chen, Hegang Chen, Hehe Chen, Hekai Chen, Heng Chen, Heng-Sheng Chen, Heng-Yu Chen, Hengsan Chen, Hengsheng Chen, Hengyu Chen, Heni Chen, Herbert Chen, Hetian Chen, Heye Chen, Hong Chen, Hong Yang Chen, Hong-Sheng Chen, Hongbin Chen, Hongbo Chen, Hongen Chen, Honghai Chen, Honghui Chen, Honglei Chen, Hongli Chen, Hongmei Chen, Hongmin Chen, Hongmou Chen, Hongqi Chen, Hongqiao Chen, Hongshan Chen, Hongxiang Chen, Hongxing Chen, Hongxu Chen, Hongyan Chen, Hongyu Chen, Hongyue Chen, Hongzhi Chen, Hou-Tsung Chen, Hou-Zao Chen, Hsi-Hsien Chen, Hsiang-Wen Chen, Hsiao-Jou Cortina Chen, Hsiao-Tan Chen, Hsiao-Wang Chen, Hsiao-Yun Chen, Hsin-Han Chen, Hsin-Hong Chen, Hsin-Hung Chen, Hsin-Yi Chen, Hsiu-Wen Chen, Hsuan-Yu Chen, Hsueh-Fen Chen, Hu Chen, Hua Chen, Hua-Pu Chen, Huachen Chen, Huafei Chen, Huaiyong Chen, Hualan Chen, Huali Chen, Hualin Chen, Huan Chen, Huan-Xin Chen, Huanchun Chen, Huang Chen, Huang-Pin Chen, Huangtao Chen, Huanhua Chen, Huanhuan Chen, Huanxiong Chen, Huaping Chen, Huapu Chen, Huaqiu Chen, Huatao Chen, Huaxin Chen, Huayu Chen, Huei-Rong Chen, Huei-Yan Chen, Huey-Miin Chen, Hui Chen, Hui Mei Chen, Hui-Chun Chen, Hui-Fen Chen, Hui-Jye Chen, Hui-Ru Chen, Hui-Wen Chen, Hui-Xiong Chen, Hui-Zhao Chen, Huichao Chen, Huijia Chen, Huijiao Chen, Huijie Chen, Huimei Chen, Huimin Chen, Huiqin Chen, Huiqun Chen, Huiru Chen, Huishan Chen, Huixi Chen, Huixian Chen, Huizhi Chen, Hung-Chang Chen, Hung-Chi Chen, Hung-Chun Chen, Hung-Po Chen, Hung-Sheng Chen, I-Chun Chen, I-M Chen, Ida Y-D Chen, Irwin Chen, Ivy Xiaoying Chen, J Chen, Jacinda Chen, Jack Chen, Jake Y Chen, Jason A Chen, Jeanne Chen, Jen-Hau Chen, Jen-Sue Chen, Jennifer F Chen, Jenny Chen, Jeremy J W Chen, Ji-ling Chen, Jia Chen, Jia Min Chen, Jia Wei Chen, Jia-De Chen, Jia-Feng Chen, Jia-Lin Chen, Jia-Mei Chen, Jia-Shun Chen, Jiabing Chen, Jiacai Chen, Jiacheng Chen, Jiade Chen, Jiahao Chen, Jiahua Chen, Jiahui Chen, Jiajia Chen, Jiajing Chen, Jiajun Chen, Jiakang Chen, Jiale Chen, Jiali Chen, Jialing Chen, Jiamiao Chen, Jiamin Chen, Jian Chen, Jian-Guo Chen, Jian-Hua Chen, Jian-Jun Chen, Jian-Kang Chen, Jian-Min Chen, Jian-Qiao Chen, Jian-Qing Chen, Jianan Chen, Jianfei Chen, Jiang Chen, Jiang Ye Chen, Jiang-hua Chen, Jianghua Chen, Jiangxia Chen, Jianhua Chen, Jianhui Chen, Jiani Chen, Jianjun Chen, Jiankui Chen, Jianlin Chen, Jianmin Chen, Jianping Chen, Jianshan Chen, Jiansu Chen, Jianxiong Chen, Jianzhong Chen, Jianzhou Chen, Jiao Chen, Jiao-Jiao Chen, Jiaohua Chen, Jiaping Chen, Jiaqi Chen, Jiaqing Chen, Jiaren Chen, Jiarou Chen, Jiawei Chen, Jiawen Chen, Jiaxin Chen, Jiaxu Chen, Jiaxuan Chen, Jiayao Chen, Jiaye Chen, Jiayi Chen, Jiayuan Chen, Jichong Chen, Jie Chen, Jie-Hua Chen, Jiejian Chen, Jiemei Chen, Jien-Jiun Chen, Jihai Chen, Jijun Chen, Jimei Chen, Jin Chen, Jin-An Chen, Jin-Ran Chen, Jin-Shuen Chen, Jin-Wu Chen, Jin-Xia Chen, Jina Chen, Jinbo Chen, Jindong Chen, Jing Chen, Jing-Hsien Chen, Jing-Wen Chen, Jing-Xian Chen, Jing-Yuan Chen, Jing-Zhou Chen, Jingde Chen, Jinghua Chen, Jingjing Chen, Jingli Chen, Jinglin Chen, Jingming Chen, Jingnan Chen, Jingqing Chen, Jingshen Chen, Jingteng Chen, Jinguo Chen, Jingxuan Chen, Jingyao Chen, Jingyi Chen, Jingyuan Chen, Jingzhao Chen, Jingzhou Chen, Jinhao Chen, Jinhuang Chen, Jinli Chen, Jinlun Chen, Jinquan Chen, Jinsong Chen, Jintian Chen, Jinxuan Chen, Jinyan Chen, Jinyong Chen, Jion Chen, Jiong Chen, Jiongyu Chen, Jishun Chen, Jiu-Chiuan Chen, Jiujiu Chen, Jiwei Chen, Jiyan Chen, Jiyuan Chen, Jonathan Chen, Joy J Chen, Juan Chen, Juan-Juan Chen, Juanjuan Chen, Juei-Suei Chen, Juhai Chen, Jui-Chang Chen, Jui-Yu Chen, Jun Chen, Jun-Long Chen, Junchen Chen, Junfei Chen, Jung-Sheng Chen, Junhong Chen, Junhui Chen, Junjie Chen, Junling Chen, Junmin Chen, Junming Chen, Junpan Chen, Junpeng Chen, Junqi Chen, Junqin Chen, Junsheng Chen, Junshi Chen, Junyang Chen, Junyi Chen, Junyu Chen, K C Chen, Kai Chen, Kai-En Chen, Kai-Ming Chen, Kai-Ting Chen, Kai-Yang Chen, Kaifu Chen, Kaijian Chen, Kailang Chen, Kaili Chen, Kaina Chen, Kaiquan Chen, Kan Chen, Kang Chen, Kang-Hua Chen, Kangyong Chen, Kangzhen Chen, Katharine Y Chen, Katherine C Chen, Kecai Chen, Kehua Chen, Kehui Chen, Kelin Chen, Ken Chen, Kenneth L Chen, Keping Chen, Kequan Chen, Kevin Chen, Kewei Chen, Kexin Chen, Keyan Chen, Keyang Chen, Keying Chen, Keyu Chen, Keyuan Chen, Kuan-Jen Chen, Kuan-Ling Chen, Kuan-Ting Chen, Kuan-Yu Chen, Kuangyang Chen, Kuey Chu Chen, Kui Chen, Kun Chen, Kun-Chieh Chen, Kunmei Chen, Kunpeng Chen, L B Chen, L F Chen, Lan Chen, Lang Chen, Lankai Chen, Lanlan Chen, Lanmei Chen, Le Chen, Le Qi Chen, Lei Chen, Lei-Chin Chen, Lei-Lei Chen, Leijie Chen, Lena W Chen, Leqi Chen, Letian Chen, Lexia Chen, Li Chen, Li Jia Chen, Li-Chieh Chen, Li-Hsien Chen, Li-Hsin Chen, Li-Hua Chen, Li-Jhen Chen, Li-Juan Chen, Li-Mien Chen, Li-Nan Chen, Li-Tzong Chen, Li-Zhen Chen, Li-hong Chen, Lian Chen, Lianfeng Chen, Liang Chen, Liang-Kung Chen, Liangkai Chen, Liangsheng Chen, Liangwan Chen, Lianmin Chen, Liaobin Chen, Lichang Chen, Lichun Chen, Lidian Chen, Lie Chen, Liechun Chen, Lifang Chen, Lifen Chen, Lifeng Chen, Ligang Chen, Lihong Chen, Lihua Chen, Lijin Chen, Lijuan Chen, Lili Chen, Limei Chen, Limin Chen, Liming Chen, Lin Chen, Lina Chen, Linbo Chen, Ling Chen, Ling-Yan Chen, Lingfeng Chen, Lingjun Chen, Lingli Chen, Lingxia Chen, Lingxue Chen, Lingyi Chen, Linjie Chen, Linlin Chen, Linna Chen, Linxi Chen, Linyi Chen, Liping Chen, Liqiang Chen, Liugui Chen, Liujun Chen, Liutao Chen, Lixia Chen, Lixian Chen, Liyun Chen, Lizhen Chen, Lizhu Chen, Lo-Yun Chen, Long Chen, Long-Jiang Chen, Longqing Chen, Longyun Chen, Lu Chen, Lu Hua Chen, Lu-Biao Chen, Lu-Zhu Chen, Lulu Chen, Luming Chen, Luyi Chen, Luzhu Chen, M Chen, M L Chen, Man Chen, Man-Hua Chen, Mao Chen, Mao-Yuan Chen, Maochong Chen, Maorong Chen, Marcus Y Chen, Mark I-Cheng Chen, Max Jl Chen, Mechi Chen, Mei Chen, Mei-Chi Chen, Mei-Chih Chen, Mei-Hsiu Chen, Mei-Hua Chen, Mei-Jie Chen, Mei-Ling Chen, Mei-Ru Chen, Meilan Chen, Meilin Chen, Meiling Chen, Meimei Chen, Meiting Chen, Meiyang Chen, Meiyu Chen, Meizhen Chen, Meng Chen, Meng Xuan Chen, Meng-Lin Chen, Meng-Ping Chen, Mengdi Chen, Menglan Chen, Mengling Chen, Mengping Chen, Mengqing Chen, Mengting Chen, Mengxia Chen, Mengyan Chen, Mengying Chen, Mian-Mian Chen, Miao Chen, Miao-Der Chen, Miao-Hsueh Chen, Miao-Yu Chen, Miaomiao Chen, Miaoran Chen, Michael C Chen, Michelle Chen, Mien-Cheng Chen, Min Chen, Min-Hsuan Chen, Min-Hu Chen, Min-Jie Chen, Ming Chen, Ming-Fong Chen, Ming-Han Chen, Ming-Hong Chen, Ming-Huang Chen, Ming-Huei Chen, Ming-Yu Chen, Mingcong Chen, Mingfeng Chen, Minghong Chen, Minghua Chen, Minglang Chen, Mingling Chen, Mingmei Chen, Mingxia Chen, Mingxing Chen, Mingyang Chen, Mingyi Chen, Mingyue Chen, Minjian Chen, Minjiang Chen, Minjie Chen, Minyan Chen, Mo Chen, Mu-Hong Chen, Muh-Shy Chen, Mulan Chen, Mystie X Chen, Na Chen, Naifei Chen, Naisong Chen, Nan Chen, Ni Chen, Nian-Ping Chen, Ning Chen, Ning-Bo Chen, Ning-Hung Chen, Ning-Yuan Chen, Ningbo Chen, Ningning Chen, Nuan Chen, On Chen, Ou Chen, Ouyang Chen, P P Chen, Pan Chen, Paul Chih-Hsueh Chen, Pei Chen, Pei-Chen Chen, Pei-Chun Chen, Pei-Lung Chen, Pei-Yi Chen, Pei-Yin Chen, Pei-zhan Chen, Peihong Chen, Peipei Chen, Peiqin Chen, Peixian Chen, Peiyou Chen, Peiyu Chen, Peize Chen, Peizhan Chen, Peng Chen, Peng-Cheng Chen, Pengxiang Chen, Ping Chen, Ping-Chung Chen, Ping-Kun Chen, Pingguo Chen, Po-Han Chen, Po-Ju Chen, Po-Min Chen, Po-See Chen, Po-Sheng Chen, Po-Yu Chen, Qi Chen, Qi-An Chen, Qian Chen, Qianbo Chen, Qianfen Chen, Qiang Chen, Qiangpu Chen, Qiankun Chen, Qianling Chen, Qianming Chen, Qianping Chen, Qianqian Chen, Qianxue Chen, Qianyi Chen, Qianyu Chen, Qianyun Chen, Qianzhi Chen, Qiao Chen, Qiao-Yi Chen, Qiaoli Chen, Qiaoling Chen, Qichen Chen, Qifang Chen, Qihui Chen, Qili Chen, Qinfen Chen, Qing Chen, Qing-Hui Chen, Qing-Juan Chen, Qing-Wei Chen, Qingao Chen, Qingchao Chen, Qingchuan Chen, Qingguang Chen, Qinghao Chen, Qinghua Chen, Qingjiang Chen, Qingjie Chen, Qingliang Chen, Qingmei Chen, Qingqing Chen, Qingqiu Chen, Qingshi Chen, Qingxing Chen, Qingyang Chen, Qingyi Chen, Qinian Chen, Qinsheng Chen, Qinying Chen, Qiong Chen, Qiongyun Chen, Qiqi Chen, Qitong Chen, Qiu Jing Chen, Qiu-Jing Chen, Qiu-Sheng Chen, Qiuchi Chen, Qiuhong Chen, Qiujing Chen, Qiuli Chen, Qiuwen Chen, Qiuxia Chen, Qiuxiang Chen, Qiuxuan Chen, Qiuyun Chen, Qiwei Chen, Qixian Chen, Qu Chen, Quan Chen, Quanjiao Chen, Quanwei Chen, Qunxiang Chen, R Chen, Ran Chen, Ranyun Chen, Ray-Jade Chen, Ren-Hui Chen, Renjin Chen, Renwei Chen, Renyu Chen, Robert Chen, Roger Chen, Rong Chen, Rong-Hua Chen, Rongfang Chen, Rongfeng Chen, Rongrong Chen, Rongsheng Chen, Rongyuan Chen, Roufen Chen, Rouxi Chen, Ru Chen, Rucheng Chen, Ruey-Hwa Chen, Rui Chen, Rui-Fang Chen, Rui-Min Chen, Rui-Pei Chen, Rui-Zhen Chen, Ruiai Chen, Ruibing Chen, Ruijing Chen, Ruijuan Chen, Ruilin Chen, Ruimin Chen, Ruiming Chen, Ruiqi Chen, Ruisen Chen, Ruixiang Chen, Ruixue Chen, Ruiying Chen, Rujun Chen, Runfeng Chen, Runsen Chen, Runsheng Chen, Ruofan Chen, Ruohong Chen, Ruonan Chen, Ruoyan Chen, Ruoying Chen, S Chen, S N Chen, S Pl Chen, S-D Chen, Sai Chen, San-Yuan Chen, Sean Chen, Sen Chen, Shali Chen, Shan Chen, Shanchun Chen, Shang-Chih Chen, Shang-Hung Chen, Shangduo Chen, Shangsi Chen, Shangwu Chen, Shangzhong Chen, Shanshan Chen, Shanyuan Chen, Shao-Ke Chen, Shao-Peng Chen, Shao-Wei Chen, Shao-Yu Chen, Shao-long Chen, Shaofei Chen, Shaohong Chen, Shaohua Chen, Shaokang Chen, Shaokun Chen, Shaoliang Chen, Shaotao Chen, Shaoxing Chen, Shaoze Chen, Shasha Chen, She Chen, Shen Chen, Shen-Ming Chen, Sheng Chen, Sheng-Xi Chen, Sheng-Yi Chen, Shengdi Chen, Shenghui Chen, Shenglan Chen, Shengnan Chen, Shengpan Chen, Shengyu Chen, Shengzhi Chen, Shi Chen, Shi-Qing Chen, Shi-Sheng Chen, Shi-Yi Chen, Shi-You Chen, Shibo Chen, Shih-Jen Chen, Shih-Pin Chen, Shih-Yin Chen, Shih-Yu Chen, Shilan Chen, Shiming Chen, Shin-Wen Chen, Shin-Yu Chen, Shipeng Chen, Shiqian Chen, Shiqun Chen, Shirui Chen, Shiuhwei Chen, Shiwei Chen, Shixuan Chen, Shiyan Chen, Shiyao Chen, Shiyi Chen, Shiyu Chen, Shou-Tung Chen, Shoudeng Chen, Shoujun Chen, Shouzhen Chen, Shu Chen, Shu-Fen Chen, Shu-Gang Chen, Shu-Hua Chen, Shu-Jen Chen, Shuai Chen, Shuai-Bing Chen, Shuai-Ming Chen, Shuaijie Chen, Shuaijun Chen, Shuaiyin Chen, Shuaiyu Chen, Shuang Chen, Shuangfeng Chen, Shuanghui Chen, Shuchun Chen, Shuen-Ei Chen, Shufang Chen, Shufeng Chen, Shuhai Chen, Shuhong Chen, Shuhuang Chen, Shuhui Chen, Shujuan Chen, Shuliang Chen, Shuming Chen, Shunde Chen, Shuntai Chen, Shunyou Chen, Shuo Chen, Shuo-Bin Chen, Shuoni Chen, Shuqin Chen, Shuqiu Chen, Shuting Chen, Shuwen Chen, Shuyi Chen, Shuying Chen, Si Chen, Si-Ru Chen, Si-Yuan Chen, Si-Yue Chen, Si-guo Chen, Sien-Tsong Chen, Sifeng Chen, Sihui Chen, Sijia Chen, Sijuan Chen, Sili Chen, Silian Chen, Siping Chen, Siqi Chen, Siqin Chen, Sisi Chen, Siteng Chen, Siting Chen, Siyi Chen, Siyu Chen, Siyu S Chen, Siyuan Chen, Siyue Chen, Size Chen, Song Chen, Song-Mei Chen, Songfeng Chen, Suet N Chen, Suet Nee Chen, Sufang Chen, Suipeng Chen, Sulian Chen, Suming Chen, Sun Chen, Sung-Fang Chen, Suning Chen, Sunny Chen, Sy-Jou Chen, Syue-Ting Chen, Szu-Chi Chen, Szu-Chia Chen, Szu-Chieh Chen, Szu-Han Chen, Szu-Yun Chen, T Chen, Tai-Heng Chen, Tai-Tzung Chen, Tailai Chen, Tan-Huan Chen, Tan-Zhou Chen, Tania Chen, Tao Chen, Tian Chen, Tianfeng Chen, Tianhang Chen, Tianhong Chen, Tianhua Chen, Tianpeng Chen, Tianran Chen, Tianrui Chen, Tiantian Chen, Tianzhen Chen, Tielin Chen, Tien-Hsing Chen, Ting Chen, Ting-Huan Chen, Ting-Tao Chen, Ting-Ting Chen, Tingen Chen, Tingtao Chen, Tingting Chen, Tom Wei-Wu Chen, Tong Chen, Tongsheng Chen, Tse-Ching Chen, Tse-Wei Chen, TsungYen Chen, Tuantuan Chen, Tzu-An Chen, Tzu-Chieh Chen, Tzu-Ju Chen, Tzu-Ting Chen, Tzu-Yu Chen, Tzy-Yen Chen, Valerie Chen, W Chen, Wai Chen, Wan Jun Chen, Wan-Tzu Chen, Wan-Yan Chen, Wan-Yi Chen, Wanbiao Chen, Wanjia Chen, Wanjun Chen, Wanling Chen, Wantao Chen, Wanting Chen, Wanyin Chen, Wei Chen, Wei J Chen, Wei Ning Chen, Wei-Cheng Chen, Wei-Cong Chen, Wei-Fei Chen, Wei-Hao Chen, Wei-Hui Chen, Wei-Kai Chen, Wei-Kung Chen, Wei-Lun Chen, Wei-Min Chen, Wei-Peng Chen, Wei-Ting Chen, Wei-Wei Chen, Wei-Yu Chen, Wei-xian Chen, Weibo Chen, Weican Chen, Weichan Chen, Weicong Chen, Weihao Chen, Weihong Chen, Weihua Chen, Weijia Chen, Weijie Chen, Weili Chen, Weilun Chen, Weina Chen, Weineng Chen, Weiping Chen, Weiqin Chen, Weiqing Chen, Weirui Chen, Weisan Chen, Weitao Chen, Weitian Chen, Weiwei Chen, Weixian Chen, Weixin Chen, Weiyi Chen, Weiyong Chen, Wen Chen, Wen-Chau Chen, Wen-Jie Chen, Wen-Pin Chen, Wen-Qi Chen, Wen-Tsung Chen, Wen-Yi Chen, Wenbiao Chen, Wenbing Chen, Wenfan Chen, Wenfang Chen, Wenhao Chen, Wenhua Chen, Wenjie Chen, Wenjun Chen, Wenlong Chen, Wenqin Chen, Wensheng Chen, Wenshuo Chen, Wentao Chen, Wenting Chen, Wentong Chen, Wenwen Chen, Wenwu Chen, Wenxi Chen, Wenxing Chen, Wenxu Chen, Willian Tzu-Liang Chen, Wu-Jun Chen, Wu-Xian Chen, Wuyan Chen, X Chen, X R Chen, X Steven Chen, Xi Chen, Xia Chen, Xia-Fei Chen, Xiaguang Chen, Xiameng Chen, Xian Chen, Xian-Kai Chen, Xianbo Chen, Xiancheng Chen, Xianfeng Chen, Xiang Chen, Xiang-Bin Chen, Xiang-Mei Chen, XiangFan Chen, Xiangding Chen, Xiangjun Chen, Xiangli Chen, Xiangliu Chen, Xiangmei Chen, Xiangna Chen, Xiangning Chen, Xiangqiu Chen, Xiangyu Chen, Xiankai Chen, Xianmei Chen, Xianqiang Chen, Xianxiong Chen, Xianyue Chen, Xianze Chen, Xianzhen Chen, Xiao Chen, Xiao-Chen Chen, Xiao-Hui Chen, Xiao-Jun Chen, Xiao-Lin Chen, Xiao-Qing Chen, Xiao-Quan Chen, Xiao-Wei Chen, Xiao-Yang Chen, Xiao-Ying Chen, Xiao-chun Chen, Xiao-he Chen, Xiao-ping Chen, Xiaobin Chen, Xiaobo Chen, Xiaochang Chen, Xiaochun Chen, Xiaodong Chen, Xiaofang Chen, Xiaofen Chen, Xiaofeng Chen, Xiaohan Chen, Xiaohong Chen, Xiaohua Chen, Xiaohui Chen, Xiaojiang S Chen, Xiaojie Chen, Xiaojing Chen, Xiaojuan Chen, Xiaojun Chen, Xiaokai Chen, Xiaolan Chen, Xiaole L Chen, Xiaolei Chen, Xiaoli Chen, Xiaolin Chen, Xiaoling Chen, Xiaolong Chen, Xiaolu Chen, Xiaomeng Chen, Xiaomin Chen, Xiaona Chen, Xiaonan Chen, Xiaopeng Chen, Xiaoping Chen, Xiaoqian Chen, Xiaoqing Chen, Xiaorong Chen, Xiaoshan Chen, Xiaotao Chen, Xiaoting Chen, Xiaowan Chen, Xiaowei Chen, Xiaowen Chen, Xiaoxiang Chen, Xiaoxiao Chen, Xiaoyan Chen, Xiaoyang Chen, Xiaoyin Chen, Xiaoyong Chen, Xiaoyu Chen, Xiaoyuan Chen, Xiaoyun Chen, Xiatian Chen, Xihui Chen, Xijun Chen, Xikun Chen, Ximei Chen, Xin Chen, Xin-Jie Chen, Xin-Ming Chen, Xin-Qi Chen, Xinan Chen, Xing Chen, Xing-Lin Chen, Xing-Long Chen, Xing-Zhen Chen, Xingdong Chen, Xinghai Chen, Xingxing Chen, Xingyi Chen, Xingyong Chen, Xingyu Chen, Xinji Chen, Xinlin Chen, Xinpu Chen, Xinqiao Chen, Xinwei Chen, Xinyan Chen, Xinyang Chen, Xinyi Chen, Xinyu Chen, Xinyuan Chen, Xinyue Chen, Xinzhuo Chen, Xiong Chen, Xiqun Chen, Xiu Chen, Xiu-Juan Chen, Xiuhui Chen, Xiujuan Chen, Xiuli Chen, Xiuping Chen, Xiuxiu Chen, Xiuyan Chen, Xixi Chen, Xiyao Chen, Xiyu Chen, Xu Chen, Xuan Chen, Xuancai Chen, Xuanjing Chen, Xuanli Chen, Xuanmao Chen, Xuanwei Chen, Xuanxu Chen, Xuanyi Chen, Xue Chen, Xue-Mei Chen, Xue-Qing Chen, Xue-Xin Chen, Xue-Yan Chen, Xue-Ying Chen, XueShu Chen, Xuechun Chen, Xuefei Chen, Xuehua Chen, Xuejiao Chen, Xuejun Chen, Xueli Chen, Xueling Chen, Xuemei Chen, Xuemin Chen, Xueqin Chen, Xueqing Chen, Xuerong Chen, Xuesong Chen, Xueting Chen, Xueyan Chen, Xueying Chen, Xufeng Chen, Xuhui Chen, Xujia Chen, Xun Chen, Xuxiang Chen, Xuxin Chen, Xuzhuo Chen, Y Chen, Y D I Chen, Y Eugene Chen, Y M Chen, Y P Chen, Y S Chen, Y U Chen, Y-D I Chen, Y-D Ida Chen, Ya Chen, Ya-Chun Chen, Ya-Nan Chen, Ya-Peng Chen, Ya-Ting Chen, Ya-xi Chen, Yafang Chen, Yafei Chen, Yahong Chen, Yajie Chen, Yajing Chen, Yajun Chen, Yalan Chen, Yali Chen, Yan Chen, Yan Jie Chen, Yan Q Chen, Yan-Gui Chen, Yan-Jun Chen, Yan-Ming Chen, Yan-Qiong Chen, Yan-yan Chen, Yanan Chen, Yananlan Chen, Yanbin Chen, Yanfei Chen, Yanfen Chen, Yang Chen, Yang-Ching Chen, Yang-Yang Chen, Yangchao Chen, Yanghui Chen, Yangxin Chen, Yanhan Chen, Yanhua Chen, Yanjie Chen, Yanjing Chen, Yanli Chen, Yanlin Chen, Yanling Chen, Yanming Chen, Yann-Jang Chen, Yanping Chen, Yanqiu Chen, Yanrong Chen, Yanru Chen, Yanting Chen, Yanyan Chen, Yanyun Chen, Yanzhu Chen, Yanzi Chen, Yao Chen, Yao-Shen Chen, Yaodong Chen, Yaosheng Chen, Yaowu Chen, Yau-Hung Chen, Yaxi Chen, Yayun Chen, Yazhuo Chen, Ye Chen, Ye-Guang Chen, Yeh Chen, Yelin Chen, Yen-Chang Chen, Yen-Chen Chen, Yen-Cheng Chen, Yen-Ching Chen, Yen-Fu Chen, Yen-Hao Chen, Yen-Hsieh Chen, Yen-Jen Chen, Yen-Ju Chen, Yen-Lin Chen, Yen-Ling Chen, Yen-Ni Chen, Yen-Rong Chen, Yen-Teen Chen, Yewei Chen, Yi Chen, Yi Feng Chen, Yi-Bing Chen, Yi-Chun Chen, Yi-Chung Chen, Yi-Fei Chen, Yi-Guang Chen, Yi-Han Chen, Yi-Hau Chen, Yi-Heng Chen, Yi-Hong Chen, Yi-Hsuan Chen, Yi-Hui Chen, Yi-Jen Chen, Yi-Lin Chen, Yi-Ru Chen, Yi-Ting Chen, Yi-Wen Chen, Yi-Yung Chen, YiChung Chen, YiPing Chen, Yian Chen, Yibing Chen, Yibo Chen, Yidan Chen, Yiding Chen, Yidong Chen, Yiduo Chen, Yifa Chen, Yifan Chen, Yifang Chen, Yifei Chen, Yih-Chieh Chen, Yihao Chen, Yihong Chen, Yii-Der Chen, Yii-Der I Chen, Yii-Derr Chen, Yii-der Ida Chen, Yijiang Chen, Yijun Chen, Yike Chen, Yilan Chen, Yilei Chen, Yili Chen, Yilin Chen, Yiming Chen, Yin-Huai Chen, Ying Chen, Ying-Cheng Chen, Ying-Hsiang Chen, Ying-Jie Chen, Ying-Jung Chen, Ying-Lan Chen, Ying-Ying Chen, Yingchun Chen, Yingcong Chen, Yinghui Chen, Yingji Chen, Yingjie Chen, Yinglian Chen, Yingting Chen, Yingxi Chen, Yingying Chen, Yingyu Chen, Yinjuan Chen, Yintong Chen, Yinwei Chen, Yinzhu Chen, Yiru Chen, Yishan Chen, Yisheng Chen, Yitong Chen, Yixin Chen, Yiyin Chen, Yiyun Chen, Yizhi Chen, Yong Chen, Yong-Jun Chen, Yong-Ping Chen, Yong-Syuan Chen, Yong-Zhong Chen, YongPing Chen, Yongbin Chen, Yongfa Chen, Yongfang Chen, Yongheng Chen, Yonghui Chen, Yongke Chen, Yonglu Chen, Yongmei Chen, Yongming Chen, Yongning Chen, Yongqi Chen, Yongshen Chen, Yongshuo Chen, Yongxing Chen, Yongxun Chen, You-Ming Chen, You-Xin Chen, You-Yue Chen, Youhu Chen, Youjia Chen, Youmeng Chen, Youran Chen, Youwei Chen, Yu Chen, Yu-Bing Chen, Yu-Cheng Chen, Yu-Chi Chen, Yu-Chia Chen, Yu-Chuan Chen, Yu-Fan Chen, Yu-Fen Chen, Yu-Fu Chen, Yu-Gen Chen, Yu-Han Chen, Yu-Hui Chen, Yu-Ling Chen, Yu-Ming Chen, Yu-Pei Chen, Yu-San Chen, Yu-Si Chen, Yu-Ting Chen, Yu-Tung Chen, Yu-Xia Chen, Yu-Xin Chen, Yu-Yang Chen, Yu-Ying Chen, Yuan Chen, Yuan-Hua Chen, Yuan-Shen Chen, Yuan-Tsong Chen, Yuan-Yuan Chen, Yuan-Zhen Chen, Yuanbin Chen, Yuanhao Chen, Yuanjia Chen, Yuanjian Chen, Yuanli Chen, Yuanqi Chen, Yuanwei Chen, Yuanwen Chen, Yuanyu Chen, Yuanyuan Chen, Yubin Chen, Yucheng Chen, Yue Chen, Yue-Lai Chen, Yuebing Chen, Yueh-Peng Chen, Yuelei Chen, Yuewen Chen, Yuewu Chen, Yuexin Chen, Yuexuan Chen, Yufei Chen, Yufeng Chen, Yuh-Lien Chen, Yuh-Ling Chen, Yuh-Min Chen, Yuhan Chen, Yuhang Chen, Yuhao Chen, Yuhong Chen, Yuhui Chen, Yujie Chen, Yule Chen, Yuli Chen, Yulian Chen, Yulin Chen, Yuling Chen, Yulong Chen, Yulu Chen, Yumei Chen, Yun Chen, Yun-Ju Chen, Yun-Tzu Chen, Yun-Yu Chen, Yundai Chen, Yunfei Chen, Yunfeng Chen, Yung-Hsiang Chen, Yung-Wu Chen, Yunjia Chen, Yunlin Chen, Yunn-Yi Chen, Yunqin Chen, Yunshun Chen, Yunwei Chen, Yunyun Chen, Yunzhong Chen, Yunzhu Chen, Yupei Chen, Yupeng Chen, Yuping Chen, Yuqi Chen, Yuqin Chen, Yuqing Chen, Yuquan Chen, Yurong Chen, Yushan Chen, Yusheng Chen, Yusi Chen, Yuting Chen, Yutong Chen, Yuxi Chen, Yuxian Chen, Yuxiang Chen, Yuxin Chen, Yuxing Chen, Yuyan Chen, Yuyang Chen, Yuyao Chen, Z Chen, Zan Chen, Zaozao Chen, Ze-Hui Chen, Ze-Xu Chen, Zechuan Chen, Zemin Chen, Zetian Chen, Zexiao Chen, Zeyu Chen, Zhanfei Chen, Zhang-Liang Chen, Zhang-Yuan Chen, Zhangcheng Chen, Zhanghua Chen, Zhangliang Chen, Zhanglin Chen, Zhangxin Chen, Zhanjuan Chen, Zhao Chen, Zhao-Xia Chen, ZhaoHui Chen, Zhaojun Chen, Zhaoli Chen, Zhaolin Chen, Zhaoran Chen, Zhaowei Chen, Zhaoyao Chen, Zhe Chen, Zhe-Ling Chen, Zhe-Sheng Chen, Zhe-Yu Chen, Zhebin Chen, Zhehui Chen, Zhelin Chen, Zhen Bouman Chen, Zhen Chen, Zhen-Hua Chen, Zhen-Yu Chen, Zhencong Chen, Zhenfeng Chen, Zheng Chen, Zheng-Zhen Chen, Zhenghong Chen, Zhengjun Chen, Zhengling Chen, Zhengming Chen, Zhenguo Chen, Zhengwei Chen, Zhengzhi Chen, Zhenlei Chen, Zhenyi Chen, Zhenyue Chen, Zheping Chen, Zheren Chen, Zhesheng Chen, Zheyi Chen, Zhezhe Chen, Zhi Bin Chen, Zhi Chen, Zhi-Hao Chen, Zhi-bin Chen, Zhi-zhe Chen, Zhiang Chen, Zhichuan Chen, Zhifeng Chen, Zhigang Chen, Zhigeng Chen, Zhiguo Chen, Zhihai Chen, Zhihang Chen, Zhihao Chen, Zhiheng Chen, Zhihong Chen, Zhijian Chen, Zhijian J Chen, Zhijing Chen, Zhijun Chen, Zhimin Chen, Zhinan Chen, Zhiping Chen, Zhiqiang Chen, Zhiquan Chen, Zhishi Chen, Zhitao Chen, Zhiting Chen, Zhiwei Chen, Zhixin Chen, Zhixuan Chen, Zhixue Chen, Zhiyong Chen, Zhiyu Chen, Zhiyuan Chen, Zhiyun Chen, Zhizhong Chen, Zhong Chen, Zhongbo Chen, Zhonghua Chen, Zhongjian Chen, Zhongliang Chen, Zhongxiu Chen, Zhongzhu Chen, Zhou Chen, Zhouji Chen, Zhouliang Chen, Zhoulong Chen, Zhouqing Chen, Zhuchu Chen, Zhujun Chen, Zhuo Chen, Zhuo-Yuan Chen, ZhuoYu Chen, Zhuohui Chen, Zhuojia Chen, Zi-Jiang Chen, Zi-Qing Chen, Zi-Yang Chen, Zi-Yue Chen, Zi-Yun Chen, Zian Chen, Zifan Chen, Zihan Chen, Zihang Chen, Zihao Chen, Zihe Chen, Zihua Chen, Zijie Chen, Zike Chen, Zilin Chen, Zilong Chen, Ziming Chen, Zinan Chen, Ziqi Chen, Ziqing Chen, Zitao Chen, Zixi Chen, Zixin Chen, Zixuan Chen, Ziying Chen, Ziyuan Chen, Zoe Chen, Zongming E Chen, Zongnan Chen, Zongyou Chen, Zongzheng Chen, Zugen Chen, Zuolong Chen
articles
Chih-Ping Chen, Chen-Yu Chen, Schu-Rern Chern +6 more · 2017 · Taiwanese journal of obstetrics & gynecology · Elsevier · added 2026-04-24
We present molecular cytogenetic characterization of a duplication of 15q24.2-q26.2 associated with anencephaly and neural tube defect (NTD). A 35-year-old pregnant woman was found to have a fetus wit Show more
We present molecular cytogenetic characterization of a duplication of 15q24.2-q26.2 associated with anencephaly and neural tube defect (NTD). A 35-year-old pregnant woman was found to have a fetus with anencephaly by prenatal ultrasound at 12 weeks of gestation. The pregnancy was subsequently terminated, and a malformed fetus was delivered with anencephaly. Cytogenetic analysis of the cultured placental tissues revealed a karyotype of 46,XX,dup(15) (q24.2q26.2). Parental karyotypes were normal. Array comparative genomic hybridization analysis of the placental tissues revealed a 20.36-Mb duplication of 15q24.2-q26.2 encompassing 100 Online Mendelian Inheritance of in Man (OMIM) genes including LINGO1, MTHFS, KIF7 and CHD2. Metaphase fluorescence in situ hybridization analysis using 15q25.1-specidic probe confirmed a duplication of 15q25.1. Polymorphic DNA marker analysis showed a maternal origin of the duplication. A duplication of chromosome 15q24.2-q26.2 can be associated with NTD. Show less
no PDF DOI: 10.1016/j.tjog.2017.06.003
LINGO1
Hanbei Chen, Yakui Li, Yemin Zhu +8 more · 2017 · Medicine · added 2026-04-24
The aim of the study was to elucidate the mechanism by which advanced glycation end products (AGEs) promote cell proliferation in liver cancer cells.We treated liver cancer HepG2 cells with 200 mg/L A Show more
The aim of the study was to elucidate the mechanism by which advanced glycation end products (AGEs) promote cell proliferation in liver cancer cells.We treated liver cancer HepG2 cells with 200 mg/L AGEs or bovine serum albumin (BSA) and assayed for cell viability, cell cycle, and apoptosis. We performed real-time PCR and Western blot analysis for RNA and protein levels of carbohydrate responsive element-binding protein (ChREBP) in AGEs- or BSA-treated HepG2 cells. We analyzed the level of reactive oxygen species (ROS) in HepG2 cells treated with AGEs or BSA.We found that increased S-phase cell percentage and decreased apoptosis contributed to AGEs-induced liver cancer cell proliferation. Real-time PCR and Western blot analysis showed that AGEs stimulated RNA and protein levels of ChREBP, a transcription factor promoting glycolysis and maintaining cell proliferation in liver cancer cells. Intriguingly, the level of ROS was higher in AGEs-treated liver cancer cells. Treating liver cancer cells with antioxidant N-acetyl cystein (NAC) partly blocked AGEs-induced ChREBP expression and cell proliferation.Our results suggest that the AGEs-ROS-ChREBP pathway plays a critical role in promoting ChREBP expression and liver cancer cell proliferation. Show less
📄 PDF DOI: 10.1097/MD.0000000000007456
MLXIPL
Yanlei Ma, Jiping Yue, Yao Zhang +14 more · 2017 · Nature communications · Nature · added 2026-04-24
In the intestinal epithelium, the aberrant regulation of cell/cell junctions leads to intestinal barrier defects, which may promote the onset and enhance the severity of inflammatory bowel disease (IB Show more
In the intestinal epithelium, the aberrant regulation of cell/cell junctions leads to intestinal barrier defects, which may promote the onset and enhance the severity of inflammatory bowel disease (IBD). However, it remains unclear how the coordinated behaviour of cytoskeletal network may contribute to cell junctional dynamics. In this report, we identified ACF7, a crosslinker of microtubules and F-actin, as an essential player in this process. Loss of ACF7 leads to aberrant microtubule organization, tight junction stabilization and impaired wound closure in vitro. With the mouse genetics approach, we show that ablation of ACF7 inhibits intestinal wound healing and greatly increases susceptibility to experimental colitis in mice. ACF7 level is also correlated with development and progression of ulcerative colitis (UC) in human patients. Together, our results reveal an important molecular mechanism whereby coordinated cytoskeletal dynamics contributes to cell adhesion regulation during intestinal wound repair and the development of IBD. Show less
📄 PDF DOI: 10.1038/ncomms15375
MACF1
Zhiping Miao, Arshad Ali, Lifang Hu +5 more · 2017 · Cancer science · Blackwell Publishing · added 2026-04-24
Cancer is a polygenic disease characterized by uncontrolled growth of normal body cells, deregulation of the cell cycle as well as resistance to apoptosis. The spectraplakin protein microtubule actin Show more
Cancer is a polygenic disease characterized by uncontrolled growth of normal body cells, deregulation of the cell cycle as well as resistance to apoptosis. The spectraplakin protein microtubule actin cross-linking factor 1 (MACF1) plays an essential function in various cellular processes, including cell proliferation, migration, signaling transduction and embryo development. MACF1 is also involved in processes such as metastatic invasion in which cytoskeleton organization is a critical element that contributes to tumor progression in various human cancers. Aberrant expression of MACF1 initiates the tumor cell proliferation, and migration and metastasis in numerous cancers, such as breast cancer, colon cancer, lung cancer and glioblastoma. In this review, we summarized the current knowledge of MACF1 and its critical role in different human cancers. This will be helpful for researchers to investigate the novel functional role of MACF1 in human cancers and as a potential target to enhance the efficacy of therapeutic treatment modalities. Show less
📄 PDF DOI: 10.1111/cas.13344
MACF1
Pei-Wen Wang, Yu-Ching Hung, Tung-Ho Wu +3 more · 2017 · Oncotarget · Impact Journals · added 2026-04-24
Hepatic fibrosis may ultimately result in organ failure and death, a reality compounded by the fact that most drugs for liver fibrosis appear to be effective only if given as a prophylactic or early t Show more
Hepatic fibrosis may ultimately result in organ failure and death, a reality compounded by the fact that most drugs for liver fibrosis appear to be effective only if given as a prophylactic or early treatment. In a dimethylnitrosamine-induced liver fibrotic model, aspartate aminotransferase/alanine aminotransferase levels could not precisely distinguish the differences between the initial stage of liver fibrosis and normal control, whereas histological examination indicated that dimethylnitrosamine treatment for two weeks has resulted in hepatic fibrogenesis. Comprehensive proteomics identified 12 proteins mainly associated with the interleukin 6-stimulated inflammatory pathway. Coordinately, cytokine profiles showed that dimethylnitrosamine administration would stimulate various signaling pathways leading to liver fibrosis. Of note, apolipoprotein A4 in serum samples obtained from patients in the early stage of liver fibrosis were significantly increased compared to the healthy controls ( Show less
📄 PDF DOI: 10.18632/oncotarget.21627
APOA4
Zhanfei Chen, Nanhong Tang, Xiaoqian Wang +1 more · 2017 · Journal of cellular and molecular medicine · Blackwell Publishing · added 2026-04-24
Carbamoyl phosphate synthase 1 (CPS1) is the rate-limiting enzyme in the first step of the urea cycle and an indispensable enzyme in the metabolism of human liver. However, CPS1 epigenetic regulation Show more
Carbamoyl phosphate synthase 1 (CPS1) is the rate-limiting enzyme in the first step of the urea cycle and an indispensable enzyme in the metabolism of human liver. However, CPS1 epigenetic regulation involves promoter analysis and the role of liver-enriched transcription factors (LETFs), which is not fully elucidated. In this work, the promoter region of hCPS1 gene was cloned, and its activity was investigated. An LETF, hepatocyte nuclear factor 3-beta (HNF3β), was found to promote the transcriptional expression of CPS1 in liver-derived cell lines. In addition, dual-luciferase reporter assay shows that the essential binding sites of the HNF3β may exist in the oligonucleotide -70 nt to +73 nt. Two putative binding sites are available for HNF3β. Mutation analysis results show that the binding site 2 of HNF3β was effective, and the transcriptional activity of CPS1 promoter significantly decreased after mutation. Electrophoretic mobile shift assay (EMSA) and ChIP assay confirmed that HNF3β can interact with the binding site in the CPS1 promoter region of -70 nt to +73 nt promoter region in vivo and in vitro to regulate the transcription of CPS1. Moreover, HNF3β overexpression enhanced the transcription of CPS1 and consequently improved the mRNA and protein levels of CPS1, whereas the knockdown of HNF3β showed the opposite effects. Finally, urea production in cells was measured, and ammonia detoxification improved significantly in cells after transfection with HNF3β. HNF3β plays a vital role in regulation of CPS1 gene and could promote the metabolism of ammonia by regulating CPS1 expression. Show less
📄 PDF DOI: 10.1111/jcmm.13123
CPS1
D J Luessen, H Sun, M M McGinnis +2 more · 2017 · Brain research · Elsevier · added 2026-04-24
Chronic alcohol exposure induces pronounced changes in GPCR-mediated G-protein signaling. Recent microarray and RNA-seq analyses suggest associations between alcohol abuse and the expression of genes Show more
Chronic alcohol exposure induces pronounced changes in GPCR-mediated G-protein signaling. Recent microarray and RNA-seq analyses suggest associations between alcohol abuse and the expression of genes involved in G-protein signaling. The activity of G-proteins (e.g. Gαi/o and Gαq) is negatively modulated by regulator of G-protein signaling (RGS) proteins which are implicated in drugs of abuse including alcohol. The present study used 7days of chronic intermittent ethanol exposure followed by 24h withdrawal (CIE) to investigate changes in mRNA and protein levels of G-protein subunit isoforms and RGS protein subtypes in rat prefrontal cortex, a region associated with cognitive deficit attributed to excessive alcohol drinking. We found that this ethanol paradigm induced differential expression of Gα subunits and RGS subtypes. For example, there were increased mRNA and protein levels of Gαi1/3 subunits and no changes in the expression of Gαs and Gαq subunits in ethanol-treated animals. Moreover, CIE increased the mRNA but not the protein levels of Gαo. Additionally, a modest increase in Gαi2 mRNA level by CIE was accompanied by a pronounced increase in its protein level. Interestingly, we found that CIE increased mRNA and protein levels of RGS2, RGS4, RGS7 and RGS19 but had no effect on the expression of RGS5, RGS6, RGS8, RGS12 or RGS17. Changes in the expression of Gα subunits and RGS subtypes could contribute to the functional alterations of certain GPCRs following chronic ethanol exposure. The present study suggests that RGS proteins may be potential new targets for intervention of alcohol abuse via modification of Gα-mediated GPCR function. Show less
no PDF DOI: 10.1016/j.brainres.2017.07.014
RGS17
HPS3/TIMI55–REVEAL Collaborative Group, Louise Bowman, Jemma C Hopewell +9 more · 2017 · The New England journal of medicine · added 2026-04-24
Patients with atherosclerotic vascular disease remain at high risk for cardiovascular events despite effective statin-based treatment of low-density lipoprotein (LDL) cholesterol levels. The inhibitio Show more
Patients with atherosclerotic vascular disease remain at high risk for cardiovascular events despite effective statin-based treatment of low-density lipoprotein (LDL) cholesterol levels. The inhibition of cholesteryl ester transfer protein (CETP) by anacetrapib reduces LDL cholesterol levels and increases high-density lipoprotein (HDL) cholesterol levels. However, trials of other CETP inhibitors have shown neutral or adverse effects on cardiovascular outcomes. We conducted a randomized, double-blind, placebo-controlled trial involving 30,449 adults with atherosclerotic vascular disease who were receiving intensive atorvastatin therapy and who had a mean LDL cholesterol level of 61 mg per deciliter (1.58 mmol per liter), a mean non-HDL cholesterol level of 92 mg per deciliter (2.38 mmol per liter), and a mean HDL cholesterol level of 40 mg per deciliter (1.03 mmol per liter). The patients were assigned to receive either 100 mg of anacetrapib once daily (15,225 patients) or matching placebo (15,224 patients). The primary outcome was the first major coronary event, a composite of coronary death, myocardial infarction, or coronary revascularization. During the median follow-up period of 4.1 years, the primary outcome occurred in significantly fewer patients in the anacetrapib group than in the placebo group (1640 of 15,225 patients [10.8%] vs. 1803 of 15,224 patients [11.8%]; rate ratio, 0.91; 95% confidence interval, 0.85 to 0.97; P=0.004). The relative difference in risk was similar across multiple prespecified subgroups. At the trial midpoint, the mean level of HDL cholesterol was higher by 43 mg per deciliter (1.12 mmol per liter) in the anacetrapib group than in the placebo group (a relative difference of 104%), and the mean level of non-HDL cholesterol was lower by 17 mg per deciliter (0.44 mmol per liter), a relative difference of -18%. There were no significant between-group differences in the risk of death, cancer, or other serious adverse events. Among patients with atherosclerotic vascular disease who were receiving intensive statin therapy, the use of anacetrapib resulted in a lower incidence of major coronary events than the use of placebo. (Funded by Merck and others; Current Controlled Trials number, ISRCTN48678192 ; ClinicalTrials.gov number, NCT01252953 ; and EudraCT number, 2010-023467-18 .). Show less
no PDF DOI: 10.1056/NEJMoa1706444
CETP
Tao Yang, Kai Zhao, Haifeng Shu +6 more · 2017 · Neuroreport · added 2026-04-24
Neuronal regeneration and axonal regrowth mechanisms in the injured mammalian central nervous system are largely unknown. As part of a major pathway for inhibiting axonal regeneration, activated neuro Show more
Neuronal regeneration and axonal regrowth mechanisms in the injured mammalian central nervous system are largely unknown. As part of a major pathway for inhibiting axonal regeneration, activated neuronal glycosylphosphatidylinositol-anchored Nogo receptor (NgR) interacts with LINGO-1 and p75NTR to form a complex at the cell surface. However, it was found in our previous report that upregulation of NgR stimulated by injury plays a key role in neuronal regeneration in the neonatal cortex freeze-lesion model, but its downstream signalling remains elusive. In the present study, the novel regulatory role of NgR in a serine-threonine kinase WNK1 was identified. NgR's transcriptional regulation of WNK1 was identified by RT-qPCR and semiquantitative western blot after the overexpression or knockdown of NgR, and the regulation is specific to WNK1, which is not the same for its family members, WNK2, WNK3 and WNK4. Furthermore, NgR inhibition by NEP fails to affect WNK1, which indicates that WNK1 functions outside of the Nogo-A/NgR pathway. By performing a proliferation, migration and axonal extension assay, we also identified that overexpressed NgR critically regulated these processes and impairment by overexpressing NgR was rescued with coexpression of WNK1, indicating the partial role of WNK1 in NgR-mediated morphological regulation. Our study identifies a separation of functions for the NgR-regulated WNK1 in mediating proliferation, migration and axonal extension in PC12 cells as well as a specific regulatory role between NgR and WNK1 that is important for recovery from central nervous system injury. Show less
no PDF DOI: 10.1097/WNR.0000000000000800
LINGO1
Hongxiang Zeng, Hao Gu, Chiqi Chen +9 more · 2016 · Oncotarget · Impact Journals · added 2026-04-24
Targeting leukemia-initiating cells (LICs) is the key to eradicating leukemia and preventing its relapse. Recent studies have indicated that metabolic regulation may play a critical role in the mainte Show more
Targeting leukemia-initiating cells (LICs) is the key to eradicating leukemia and preventing its relapse. Recent studies have indicated that metabolic regulation may play a critical role in the maintenance of stemness in LICs, although the detailed mechanisms are poorly understood. Herein, we provide intriguing evidence showing that a glucose-responsive transcription factor, carbohydrate responsive element binding protein (ChREBP), served as a tumor suppressor rather than an oncogene, as previously described, to inhibit the development of acute myeloid leukemia by promoting the differentiation of LICs. Using an MLL-AF9-induced murine leukemia model, we demonstrated that the deletion of ChREBP resulted in the blockage of the differentiation of LICs and significantly reduced survival in ChREBP-null leukemic mice. However, ChREBP was not required for the normal repopulation abilities of hematopoietic stem cells. ChREBP promoted leukemia cell differentiation through the direct inhibition of RUNX1 or the transactivation of TXNIP to downregulate the RUNX1 level and ROS generation. Moreover, knockdown of ChREBP in human leukemia THP1 cells led to markedly enhanced proliferation and decreased differentiation upon PMA treatment. Collectively, we unraveled an unexpected role of ChREBP in leukemogenesis, which may provide valuable clues for developing novel metabolic strategies for leukemia treatment. Show less
📄 PDF DOI: 10.18632/oncotarget.9520
MLXIPL
Aihui Fan, Qian Wang, Yongjun Yuan +7 more · 2016 · American journal of physiology. Cell physiology · added 2026-04-24
Recent studies have shown that activation of liver X receptors (LXRs) attenuates the development of atherosclerosis, not only by regulating lipid metabolism but also by suppressing inflammatory signal Show more
Recent studies have shown that activation of liver X receptors (LXRs) attenuates the development of atherosclerosis, not only by regulating lipid metabolism but also by suppressing inflammatory signaling. Sphingosine 1-phosphate receptor 2 (S1PR2), an important inflammatory gene product, plays a role in the development of various inflammatory diseases. It was proposed that S1PR2 might be regulated by LXR-α. In the present study, the effect of LXR-α on tumor necrosis factor-α (TNF-α)-induced S1PR2 expression in human umbilical vein endothelial cells (HUVECs) was investigated and the underlying mechanism was explored. The results demonstrated that TNF-α led to an increase in S1PR2 expression and triggered a downregulation of LXR-α expression in HUVECs as well. Downregulation of LXR-α with specific small interfering RNA (siRNA) remarkably enhanced the primary as well as TNF-α-induced expression of S1PR2 in HUVECs. Activation of LXR-α by agonist GW3965 inhibited both primary and TNF-α-induced S1PR2 expression. GW3965 also attenuated S1PR2-induced endothelial barrier dysfunction. The data further showed that TNF-α induced a significant decrease in miR-130a-3p expression. Overexpression of miR-130a-3p with mimic product reduced S1PR2 protein expression, and inhibition of miR-130a-3p by specific inhibitor resulted in an increase in S1PR2 protein expression. Furthermore, activation of LXRs with agonist enhanced the expression of miR-130a-3p, and knockdown of LXR-α by siRNA suppressed miR-130a-3p expression. These results suggest that LXR-α might downregulate S1PR2 expression via miR-130a-3p in quiescent HUVECs. Stimulation of TNF-α attenuates the activity of LXR-α and results in enhanced S1PR2 expression. Show less
no PDF DOI: 10.1152/ajpcell.00102.2015
NR1H3
Lucas Goedert, Cristiano G Pereira, Jason Roszik +8 more · 2016 · Oncotarget · Impact Journals · added 2026-04-24
Previous work identified RMEL3 as a lncRNA with enriched expression in melanoma. Analysis of The Cancer Genome Atlas (TCGA) data confirmed RMEL3 enriched expression in melanoma and demonstrated its as Show more
Previous work identified RMEL3 as a lncRNA with enriched expression in melanoma. Analysis of The Cancer Genome Atlas (TCGA) data confirmed RMEL3 enriched expression in melanoma and demonstrated its association with the presence of BRAFV600E. RMEL3 siRNA-mediated silencing markedly reduced (95%) colony formation in different BRAFV600E melanoma cell lines. Multiple genes of the MAPK and PI3K pathways found to be correlated with RMEL3 in TCGA samples were experimentally confirmed. RMEL3 knockdown led to downregulation of activators or effectors of these pathways, including FGF2, FGF3, DUSP6, ITGB3 and GNG2. RMEL3 knockdown induces gain of protein levels of tumor suppressor PTEN and the G1/S cyclin-Cdk inhibitors p21 and p27, as well as a decrease of pAKT (T308), BRAF, pRB (S807, S811) and cyclin B1. Consistently, knockdown resulted in an accumulation of cells in G1 phase and subG0/G1 in an asynchronously growing population. Thus, TCGA data and functional experiments demonstrate that RMEL3 is required for MAPK and PI3K signaling, and its knockdown decrease BRAFV600E melanoma cell survival and proliferation. Show less
📄 PDF DOI: 10.18632/oncotarget.9164
DUSP6
Tze-Kiong Er, Yu-Fa Su, Chun-Chieh Wu +9 more · 2016 · Journal of molecular medicine (Berlin, Germany) · Springer · added 2026-04-24
Recent molecular and pathological studies suggest that endometriosis may serve as a precursor of ovarian cancer (endometriosis-associated ovarian cancer, EAOC), especially of the endometrioid and clea Show more
Recent molecular and pathological studies suggest that endometriosis may serve as a precursor of ovarian cancer (endometriosis-associated ovarian cancer, EAOC), especially of the endometrioid and clear cell subtypes. Accordingly, this study had two cardinal aims: first, to obtain mutation profiles of EAOC from Taiwanese patients; and second, to determine whether somatic mutations present in EAOC can be detected in preneoplastic lesions. Formalin-fixed paraffin-embedded (FFPE) tissues were obtained from ten endometriosis patients with malignant transformation. Macrodissection was performed to separate four different types of cells from FFPE sections in six patients. The four types of samples included normal endometrium, ectopic endometriotic lesion, atypical endometriosis, and carcinoma. Ultra-deep (>1000×) targeted sequencing was performed on 409 cancer-related genes to identify pathogenic mutations associated with EAOC. The most frequently mutated genes were PIK3CA (6/10) and ARID1A (5/10). Other recurrently mutated genes included ETS1, MLH1, PRKDC (3/10 each), and AMER1, ARID2, BCL11A, CREBBP, ERBB2, EXT1, FANCD2, MSH6, NF1, NOTCH1, NUMA1, PDE4DIP, PPP2R1A, RNF213, and SYNE1 (2/10 each). Importantly, in five of the six patients, identical somatic mutations were detected in atypical endometriosis and tumor lesions. In two patients, genetic alterations were also detected in ectopic endometriotic lesions, indicating the presence of genetic alterations in preneoplastic lesion. Genetic analysis in preneoplastic lesions may help to identify high-risk patients at early stage of malignant transformation and also shed new light on fundamental aspects of the molecular pathogenesis of EAOC. Molecular characterization of endometriosis-associated ovarian cancer genes by targeted NGS. Candidate genes predictive of malignant transformation were identified. Chromatin remodeling, PI3K-AKT-mTOR, Notch signaling, and Wnt/β-catenin pathway may promote cell malignant transformation. Show less
no PDF DOI: 10.1007/s00109-016-1395-2
EXT1
Jing Qu, Min Song, Jian Xie +9 more · 2016 · Molecular and cellular biochemistry · Springer · added 2026-04-24
Many studies have explored whether the Notch signaling pathway has a tumor-suppressive or an oncogenic role in various tumors; however, the role of the Notch signaling pathway in salivary adenoid cyst Show more
Many studies have explored whether the Notch signaling pathway has a tumor-suppressive or an oncogenic role in various tumors; however, the role of the Notch signaling pathway in salivary adenoid cystic carcinoma (SACC) is still unknown. In this study, we attempt to define the role of Notch2 signaling in cell growth, invasion, and migration in SACC. We compared Notch2 expression in clinical SACC samples with that of normal samples by using immunohistochemical staining. Then, we down-regulated Notch2 expression to observe the effect of Notch2 on proliferation, invasion, migration, and the expression of known target genes of Notch signal pathway. According to our results, Notch2 expression was higher in SACC tissues compared with normal tissues. Knockdown of Notch2 inhibited cell proliferation, invasion, and migration in vitro and down-regulated the expression of HEY2 and CCND1. The results of this study suggest that Notch2 has an essential role in the cell growth, invasion, and migration of SACC. Notch2 may therefore be a potential target gene for the treatment of SACC by interfering with cell growth and metastasis. Show less
no PDF DOI: 10.1007/s11010-015-2575-z
HEY2
Jia Hu, Ge Li, Liujing Qu +10 more · 2016 · Cell death & disease · Nature · added 2026-04-24
The formation of the autophagosome is controlled by an orderly action of ATG proteins. However, how these proteins are recruited to autophagic membranes remain poorly clarified. In this study, we have Show more
The formation of the autophagosome is controlled by an orderly action of ATG proteins. However, how these proteins are recruited to autophagic membranes remain poorly clarified. In this study, we have provided a line of evidence confirming that EVA1A (eva-1 homolog A)/TMEM166 (transmembrane protein 166) is associated with autophagosomal membrane development. This notion is based on dotted EVA1A structures that colocalize with ZFYVE1, ATG9, LC3B, ATG16L1, ATG5, STX17, RAB7 and LAMP1, which represent different stages of the autophagic process. It is required for autophagosome formation as this phenotype was significantly decreased in EVA1A-silenced cells and Eva1a KO MEFs. EVA1A-induced autophagy is independent of the BECN1-PIK3C3 (phosphatidylinositol 3-kinase, catalytic subunit type 3) complex but requires ATG7 activity and the ATG12-ATG5/ATG16L1 complex. Here, we present a molecular mechanism by which EVA1A interacts with the WD repeats of ATG16L1 through its C-terminal and promotes ATG12-ATG5/ATG16L1 complex recruitment to the autophagic membrane and enhances the formation of the autophagosome. We also found that both autophagic and apoptotic mechanisms contributed to EVA1A-induced cell death while inhibition of autophagy and apoptosis attenuated EVA1A-induced cell death. Overall, these findings provide a comprehensive view to our understanding of the pathways involved in the role of EVA1A in autophagy and programmed cell death. Show less
no PDF DOI: 10.1038/cddis.2016.230
PIK3C3
Xiao-Jun Chen, Hong Zhang, Zhi-Ping Tan +2 more · 2016 · Molecular medicine reports · added 2026-04-24
Multiple osteochondromas (MO), also known as hereditary multiple exostoses, is an autosomal dominant bone disorder. Mutations in exostosin glycosyl transferase‑1 (EXT1) and exostosin glycosyl transfer Show more
Multiple osteochondromas (MO), also known as hereditary multiple exostoses, is an autosomal dominant bone disorder. Mutations in exostosin glycosyl transferase‑1 (EXT1) and exostosin glycosyl transferase‑2 (EXT2), including missense, nonsense, frameshift and splice‑site mutations, account for up to 80% of reported cases. The proteins EXT1 and EXT2 form a hetero‑oligomeric complex that functions in heparan sulfate proteoglycan biosynthesis. A heterozygous EXT2 mutation, c.939+1G>T, was identified in a five‑generation 33‑member MO family, and was present in all 13 affected members. The mutation results in deletion of exon 5 in the mRNA, producing a frameshift that leads to a premature termination codon. The present study extends the mutational spectrum of EXT2. Show less
📄 PDF DOI: 10.3892/mmr.2016.5814
EXT1
Rong Li, Lu-Zhu Chen, Wang ZHAO +2 more · 2016 · Biochemical and biophysical research communications · Elsevier · added 2026-04-24
Apolipoprotein A5 (apoA5) is a key regulator of triglyceride (TG) metabolism. This study is to investigate the role of apoA5 in obesity-associated hypertriglyceridemia and metformin-related hypotrigly Show more
Apolipoprotein A5 (apoA5) is a key regulator of triglyceride (TG) metabolism. This study is to investigate the role of apoA5 in obesity-associated hypertriglyceridemia and metformin-related hypotriglyceridemic actions. Two obese mouse models, including high-fat diet-induced obese mice and ob/ob obese mice, were adopted. The effects of low- and high-dose metformin were determined on plasma and hepatic TG and apoA5 of these obese mice. Besides, the effects of metformin on TG and apoA5 were also detected in mouse and human hepatocytes in vitro. (1) Plasma apoA5 levels in the obese mice were markedly elevated and positively correlated with TG. Hepatic TG contents and apoA5 expressions were also remarkably increased in the obese mice. (2) Metformin dose-dependently decreased hepatic and plasma TG and apoA5 in the obese mice. Similarly, metformin dose-dependently reduced cellular TG contents and apoA5 expressions in hepatocytes in vitro. Compared to APOA5 knock-down (KD), metformin plus APOA5 KD resulted in more TG reduction of hepatocytes. Increased hepatic and plasma apoA5 could be a result of obesity-associated hypertriglyceridemia, and metformin displays hypotriglyceridemic effects on obese mice partly via the apoA5 pathway. Show less
no PDF DOI: 10.1016/j.bbrc.2016.08.087
APOA5
Jue Wang, Zhizhong Ye, Shuhui Zheng +4 more · 2016 · Brain research · Elsevier · added 2026-04-24
Determination of the exogenous factors that regulate differentiation of neural stem/progenitor cells into neurons, oligodendrocytes and astrocytes is an important step in the clinical therapy of spina Show more
Determination of the exogenous factors that regulate differentiation of neural stem/progenitor cells into neurons, oligodendrocytes and astrocytes is an important step in the clinical therapy of spinal cord injury (SCI). The Notch pathway inhibits the differentiation of neural stem/progenitor cells and Lingo-1 is a strong negative regulator for myelination and axon growth. While Lingo-1 shRNA and N-[N-(3, 5-difluorophenacetyl)-1-alanyl]-S-Phenylglycinet-butylester (DAPT), a Notch pathway inhibitor, have been used separately to help repair SCI, the results have been unsatisfactory. Here we investigated and elucidated the preliminary mechanism for the effect of Lingo-1 shRNA and DAPT on neural stem/progenitor cells differentiation. We found that neural stem/progenitor cells from E14 rat embryos expressed Nestin, Sox-2 and Lingo-1, and we optimized the transduction of neural stem/progenitor cells using lentiviral vectors encoding Lingo-1 shRNA. The addition of DAPT decreased the expression of Notch intracellular domain (NICD) as well as the downstream genes Hes1 and Hes5. Expression of NeuN, CNPase and GFAP in DAPT treated cells and expression of NeuN in Lingo-1 shRNA treated cells confirmed differentiation of neural stem/progenitor cells into neurons, oligodendrocytes and astrocytes. These results revealed that while Lingo-1 shRNA and Notch signaling inhibitor DAPT both promoted differentiation of neural stem cells into neurons, only DAPT was capable of driving neural stem/progenitor cells differentiation into oligodendrocytes and astrocytes. Since we were able to show that both Lingo-1 shRNA and DAPT could drive neural stem/progenitor cells differentiation, our data might aid the development of more effective SCI therapies using Lingo-1 shRNA and DAPT. Show less
no PDF DOI: 10.1016/j.brainres.2015.11.029
LINGO1
Haiying Chen, Hongli Yang, Chong Xu +8 more · 2016 · Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · Elsevier · added 2026-04-24
Pulmonary arterial hypertension (PAH) is associated with sustained vasoconstriction, inflammation and suppressed apoptosis of smooth muscle cells. Our previous studies have found that rat bone marrow- Show more
Pulmonary arterial hypertension (PAH) is associated with sustained vasoconstriction, inflammation and suppressed apoptosis of smooth muscle cells. Our previous studies have found that rat bone marrow-derived mesenchymal stem cells (rBMSCs) transduced with a mutant caveolin-1(F92A-Cav1) could enhance endothelial nitric oxide synthase (eNOS) activity and improve pulmonary vascular remodeling, but the potential mechanism is not yet fully explored. The present study was to investigate the gene expression profile upon rBMSCs/F92A-Cav1delivered to PAH rat to evaluate the role of F92A-Cav1 in its regulation. PAH was induced with monocrotaline (MCT, 60mg/kg) prior to delivery of lentiviral vector transduced rBMSCs expressing Cav1 or F92A-Cav1. Gene expression profiling was performed using Rat Signal Transduction PathwayFinder array. The expression changes of 84 key genes representing 10 signal transduction pathways in rat following rBMSCs/F92A-Cav1 treatment was examined. Screening with the Rat Signal Transduction PathwayFinder R rBMSCs/F92A-Cav1 inhibits inflammation and cell proliferation by regulating signaling pathways that related to inflammation, proliferation, cell cycle and oxidative stress. Show less
no PDF DOI: 10.1016/j.biopha.2016.06.028
HEY2
Deyi Zhang, Wei Wang, Xiujie Sun +8 more · 2016 · Autophagy · Taylor & Francis · added 2026-04-24
Macroautophagy/autophagy is a conserved catabolic process that recycles cytoplasmic material during low energy conditions. BECN1/Beclin1 (Beclin 1, autophagy related) is an essential protein for funct Show more
Macroautophagy/autophagy is a conserved catabolic process that recycles cytoplasmic material during low energy conditions. BECN1/Beclin1 (Beclin 1, autophagy related) is an essential protein for function of the class 3 phosphatidylinositol 3-kinase (PtdIns3K) complexes that play a key role in autophagy nucleation and elongation. Here, we show that AMP-activated protein kinase (AMPK) regulates autophagy by phosphorylating BECN1 at Thr388. Phosphorylation of BECN1 is required for autophagy upon glucose withdrawal. BECN1(T388A), a phosphorylation defective mutant, suppresses autophagy through decreasing the interaction between PIK3C3 (phosphatidylinositol 3-kinase catalytic subunit type 3) and ATG14 (autophagy-related 14). The BECN1(T388A) mutant has a higher affinity for BCL2 than its wild-type counterpart; the mutant is more prone to dimer formation. Conversely, a BECN1 phosphorylation mimic mutant, T388D, has stronger binding to PIK3C3 and ATG14, and promotes higher autophagy activity than the wild-type control. These findings uncover a novel mechanism of autophagy regulation. Show less
no PDF DOI: 10.1080/15548627.2016.1185576
PIK3C3
Tong-Hong Wang, Cheng-Chia Yu, Yong-Shiang Lin +6 more · 2016 · Oncotarget · Impact Journals · added 2026-04-24
Recently, increasing numbers of long noncoding RNAs (lncRNAs), with both oncogenic and tumor-suppressive potential, have been found to be aberrantly expressed in various human cancers. However, the fu Show more
Recently, increasing numbers of long noncoding RNAs (lncRNAs), with both oncogenic and tumor-suppressive potential, have been found to be aberrantly expressed in various human cancers. However, the function of lncRNAs in hepatocellular carcinoma (HCC) progression remains largely unknown. In this study, we performed a comprehensive microarray analysis of lncRNA expression using human HCC specimens. After validation in 119 human HCC tissues, we identified a novel tumor suppressor lncRNA, CPS1 intronic transcript 1 (CPS1-IT1). To elucidate the clinical significance of CPS1-IT1 in HCC, correlations between CPS1-IT1 levels, clinical parameters, and survival outcomes were analyzed. In vitro and in vivo functional assays were also performed to dissect the potential underlying mechanisms. Expression of CPS1-IT1 was significantly decreased in 73% of HCC tissues, and patients with low CPS1-IT1 expression had poor survival outcomes. Furthermore, in vitro functional assays indicated that CPS1-IT1 significantly reduced cell proliferation, migration and invasion capacities through reduced Hsp90 binding to and activation of HIF-1α, thereby suppressing the epithelial-mesenchymal transition (EMT). An in vivo animal model also demonstrated the tumor suppressor role of CPS1- IT1 via decreased tumor growth and metastasis. In conclusion, lncRNA CPS1-IT1 acts as a tumor suppressor in HCC by reducing HIF-1α activation and suppressing EMT. The findings of this study establish a function for CPS1-IT1 in HCC progression and suggest its potential as a new prognostic biomarker and target for HCC therapy. Show less
📄 PDF DOI: 10.18632/oncotarget.9635
CPS1
Wangshu Qin, Xinzhi Li, Liwei Xie +9 more · 2016 · Nucleic acids research · Oxford University Press · added 2026-04-24
Long non-coding RNAs (lncRNAs) have been shown to be critical biomarkers or therapeutic targets for human diseases. However, only a small number of lncRNAs were screened and characterized. Here, we id Show more
Long non-coding RNAs (lncRNAs) have been shown to be critical biomarkers or therapeutic targets for human diseases. However, only a small number of lncRNAs were screened and characterized. Here, we identified 15 lncRNAs, which are associated with fatty liver disease. Among them, APOA4-AS is shown to be a concordant regulator of Apolipoprotein A-IV (APOA4) expression. APOA4-AS has a similar expression pattern with APOA4 gene. The expressions of APOA4-AS and APOA4 are both abnormally elevated in the liver of ob/ob mice and patients with fatty liver disease. Knockdown of APOA4-AS reduces APOA4 expression both in vitro and in vivo and leads to decreased levels of plasma triglyceride and total cholesterol in ob/ob mice. Mechanistically, APOA4-AS directly interacts with mRNA stabilizing protein HuR and stabilizes APOA4 mRNA. Deletion of HuR dramatically reduces both APOA4-AS and APOA4 transcripts. This study uncovers an anti-sense lncRNA (APOA4-AS), which is co-expressed with APOA4, and concordantly and specifically regulates APOA4 expression both in vitro and in vivo with the involvement of HuR. Show less
📄 PDF DOI: 10.1093/nar/gkw341
APOA4
Rui Chen, Hao Wang, Beibei Liang +11 more · 2016 · Cell death & disease · Nature · added 2026-04-24
Autophagy is an important catabolic process, which sustains intracellular homeostasis and lengthens cell survival under stress. Here we identify the ankyrin-repeat-containing, SH3-domain-containing, a Show more
Autophagy is an important catabolic process, which sustains intracellular homeostasis and lengthens cell survival under stress. Here we identify the ankyrin-repeat-containing, SH3-domain-containing, and proline-rich region-containing protein 2 (ASPP2), a haploinsufficient tumor suppressor, as a molecular regulator of starvation-induced autophagy in hepatocellular carcinoma (HCC). ASPP2 expression is associated with an autophagic response upon nutrient deprivation and downregulation of ASPP2 facilitates autophagic flux, whereas overexpression of ASPP2 blocks this starvation-induced autophagy in HCC cells. Mechanistically, ASPP2 inhibits autophagy through regulating BECN1 transcription and formation of phosphatidylinositol 3-kinase catalytic subunit type 3 (PIK3C3) complex. Firstly, ASPP2 inhibits p65/RelA-induced transcription of BECN1, directly by an ASPP2-p65/RelA-IκBα complex which inhibits phosphorylation of IκBα and the translocation of p65/RelA into the nucleus. Secondly, ASPP2 binds to BECN1, leading to decreased binding of PIK3C3 and UV radiation resistance-associated gene (UVRAG), and increased binding of Rubicon in PIK3C3 complex. Downregulation of ASPP2 enhances the pro-survival and chemoresistant property via autophagy in HCC cells in vitro and in vivo. Decreased ASPP2 expression was associated with increased BECN1 and poor survival in HCC patients. Therefore, ASPP2 is a key regulator of BECN1-dependent autophagy, and decreased ASPP2 may contribute to tumor progression and chemoresistance via promoting autophagy. Show less
no PDF DOI: 10.1038/cddis.2016.407
PIK3C3
Tai-Heng Chen, Xia Tian, Pao-Lin Kuo +3 more · 2016 · Prenatal diagnosis · Wiley · added 2026-04-24
Fetal akinesia deformation sequence (FADS) refers to a broad spectrum of disorder with the absent fetal movement as the unifying feature. The etiology of FADS is heterogeneous, and the majority remain Show more
Fetal akinesia deformation sequence (FADS) refers to a broad spectrum of disorder with the absent fetal movement as the unifying feature. The etiology of FADS is heterogeneous, and the majority remains unknown. Prenatal diagnosis of FADS because of neuromuscular origin has relied on clinical features and fetal muscle pathology, which can be unrevealing. The recent advance of next-generation sequencing (NGS) can provide definitive molecular diagnosis effectively. An 18-week-old fetus presented with akinesia and multiple contractures of joints. The mother had two previously aborted similarly affected fetuses. Clinical diagnosis of FADS was made. Molecular diagnosis using cord blood by NGS of genes related to neuromuscular diseases revealed two compound heterozygous mutations; c.602G > A(p.W201*) and c.1516A > C(p.T506P), in the Kelch-like 40 (KLHL40) gene. Based on this information, prenatal diagnosis was performed on the CVS of the subsequent pregnancy that resulted in an unaffected female baby, heterozygous for the c.1516A > C(p.T506P) mutation. Identification of KLHL40 mutations in one of the aborted fetuses provided a confirmative diagnosis of FADS, facilitating the prenatal diagnosis of the subsequent pregnancy. This report underscores the importance of target NGS in providing FADS families with an affordable, precise molecular diagnosis for genetic counseling and options of prenatal diagnosis. © 2016 John Wiley & Sons, Ltd. Show less
no PDF DOI: 10.1002/pd.4949
FADS1
Yin-Feng Dong, Zheng-Zhen Chen, Zhan Zhao +4 more · 2016 · Journal of neuroinflammation · BioMed Central · added 2026-04-24
It is generally recognized that the inflammatory reaction in glia is one of the important pathological factors in brain ischemic injury. Our previous study has revealed that opening ATP-sensitive pota Show more
It is generally recognized that the inflammatory reaction in glia is one of the important pathological factors in brain ischemic injury. Our previous study has revealed that opening ATP-sensitive potassium (K-ATP) channels could attenuate glial inflammation induced by ischemic stroke. However, the detailed mechanisms are not well known. Primary cultured astrocytes separated from C57BL/6 mice were subjected to oxygen-glucose deprivation (OGD); cellular injuries were determined via observing the changes of cellular morphology and cell viability. MicroRNA (miR) and messenger RNA (mRNA) level was validated by real-time PCR. The interaction between microRNA and the target was confirmed via dual luciferase reporter gene assay. Expressions of proteins and inflammatory cytokines were respectively assessed by western blotting and enzyme-linked immunosorbent assay. OGD resulted in astrocytic damage, which was prevented by K-ATP channel opener nicorandil. Notably, we found that OGD significantly downregulated miR-7 and upregulated Herpud2. Our further study proved that miR-7 targeted Herpud2 3'UTR, which encoded endoplasmic reticulum (ER) stress protein-HERP2. Correspondingly, our results showed that OGD increased the levels of ER stress proteins along with significant elevations of pro-inflammatory cytokines, including tumor necrosis factor α (TNF-α) and interleukin 1β (IL-1β). Pretreatment with nicorandil could remarkably upregulate miR-7, depress the ER-related protein expressions including glucose-regulated protein 78 (GRP78), C/EBP-homologous protein (CHOP), and Caspase-12, and thereby attenuate inflammatory responses and astrocytic damages. These findings demonstrate that opening K-ATP channels protects astrocytes against OGD-mediated neuroinflammation. Potentially, miR-7-targeted ER stress acts as a key molecular brake on neuroinflammation. Show less
📄 PDF DOI: 10.1186/s12974-016-0527-5
HEY2
Sarwat Fatima, Xiaoke Shi, Zesi Lin +9 more · 2016 · Molecular oncology · Elsevier · added 2026-04-24
5-Hydroxytryptamine (5-HT), a neurotransmitter and vasoactive factor, has been reported to promote proliferation of serum-deprived hepatocellular carcinoma (HCC) cells but the detailed intracellular m Show more
5-Hydroxytryptamine (5-HT), a neurotransmitter and vasoactive factor, has been reported to promote proliferation of serum-deprived hepatocellular carcinoma (HCC) cells but the detailed intracellular mechanism is unknown. As Wnt/β-catenin signalling is highly dysregulated in a majority of HCC, this study explored the regulation of Wnt/β-catenin signalling by 5-HT. The expression of various 5-HT receptors was studied by quantitative real-time polymerase chain reaction (qPCR) in HCC cell lines as well as in 33 pairs of HCC tumours and corresponding adjacent non-tumour tissues. Receptors 5-HT1D (21/33, 63.6%), 5-HT2B (12/33, 36.4%) and 5-HT7 (15/33, 45.4%) were overexpressed whereas receptors 5-HT2A (17/33, 51.5%) and 5-HT5 (30/33, 90.1%) were reduced in HCC tumour tissues. In vitro data suggests 5-HT increased total β-catenin, active β-catenin and decreased phosphorylated β-catenin protein levels in serum deprived HuH-7 and HepG2 cells compared to control cells under serum free medium without 5-HT. Activation of Wnt/β-catenin signalling was evidenced by increased expression of β-catenin downstream target genes, Axin2, cyclin D1, dickoppf-1 (DKK1) and glutamine synthetase (GS) by qPCR in serum-deprived HCC cell lines treated with 5-HT. Additionally, biochemical analysis revealed 5-HT disrupted Axin1/β-catenin interaction, a critical step in β-catenin phosphorylation. Increased Wnt/β-catenin activity was attenuated by antagonist of receptor 5-HT7 (SB-258719) in HCC cell lines and patient-derived primary tumour tissues in the presence of 5-HT. SB-258719 also reduced tumour growth in vivo. This study provides evidence of Wnt/β-catenin signalling activation by 5-HT and may represent a potential therapeutic target for hepatocarcinogenesis. Show less
no PDF DOI: 10.1016/j.molonc.2015.09.008
AXIN1
Salman M Tajuddin, Ursula M Schick, John D Eicher +94 more · 2016 · American journal of human genetics · Elsevier · added 2026-04-24
Salman M Tajuddin, Ursula M Schick, John D Eicher, Nathalie Chami, Ayush Giri, Jennifer A Brody, W David Hill, Tim Kacprowski, Jin Li, Leo-Pekka Lyytikäinen, Ani Manichaikul, Evelin Mihailov, Michelle L O'Donoghue, Nathan Pankratz, Raha Pazoki, Linda M Polfus, Albert Vernon Smith, Claudia Schurmann, Caterina Vacchi-Suzzi, Dawn M Waterworth, Evangelos Evangelou, Lisa R Yanek, Amber Burt, Ming-Huei Chen, Frank J A van Rooij, James S Floyd, Andreas Greinacher, Tamara B Harris, Heather M Highland, Leslie A Lange, Yongmei Liu, Reedik Mägi, Mike A Nalls, Rasika A Mathias, Deborah A Nickerson, Kjell Nikus, John M Starr, Jean-Claude Tardif, Ioanna Tzoulaki, Digna R Velez Edwards, Lars Wallentin, Traci M Bartz, Lewis C Becker, Joshua C Denny, Laura M Raffield, John D Rioux, Nele Friedrich, Myriam Fornage, He Gao, Joel N Hirschhorn, David C M Liewald, Stephen S Rich, Andre Uitterlinden, Lisa Bastarache, Diane M Becker, Eric Boerwinkle, Simon de Denus, Erwin P Bottinger, Caroline Hayward, Albert Hofman, Georg Homuth, Ethan Lange, Lenore J Launer, Terho Lehtimäki, Yingchang Lu, Andres Metspalu, Chris J O'Donnell, Rakale C Quarells, Melissa Richard, Eric S Torstenson, Kent D Taylor, Anne-Claire Vergnaud, Alan B Zonderman, David R Crosslin, Ian J Deary, Marcus Dörr, Paul Elliott, Michele K Evans, Vilmundur Gudnason, Mika Kähönen, Bruce M Psaty, Jerome I Rotter, Andrew J Slater, Abbas Dehghan, Harvey D White, Santhi K Ganesh, Ruth J F Loos, Tõnu Esko, Nauder Faraday, James G Wilson, Mary Cushman, Andrew D Johnson, Todd L Edwards, Neil A Zakai, Guillaume Lettre, Alex P Reiner, Paul L Auer Show less
White blood cells play diverse roles in innate and adaptive immunity. Genetic association analyses of phenotypic variation in circulating white blood cell (WBC) counts from large samples of otherwise Show more
White blood cells play diverse roles in innate and adaptive immunity. Genetic association analyses of phenotypic variation in circulating white blood cell (WBC) counts from large samples of otherwise healthy individuals can provide insights into genes and biologic pathways involved in production, differentiation, or clearance of particular WBC lineages (myeloid, lymphoid) and also potentially inform the genetic basis of autoimmune, allergic, and blood diseases. We performed an exome array-based meta-analysis of total WBC and subtype counts (neutrophils, monocytes, lymphocytes, basophils, and eosinophils) in a multi-ancestry discovery and replication sample of ∼157,622 individuals from 25 studies. We identified 16 common variants (8 of which were coding variants) associated with one or more WBC traits, the majority of which are pleiotropically associated with autoimmune diseases. Based on functional annotation, these loci included genes encoding surface markers of myeloid, lymphoid, or hematopoietic stem cell differentiation (CD69, CD33, CD87), transcription factors regulating lineage specification during hematopoiesis (ASXL1, IRF8, IKZF1, JMJD1C, ETS2-PSMG1), and molecules involved in neutrophil clearance/apoptosis (C10orf54, LTA), adhesion (TNXB), or centrosome and microtubule structure/function (KIF9, TUBD1). Together with recent reports of somatic ASXL1 mutations among individuals with idiopathic cytopenias or clonal hematopoiesis of undetermined significance, the identification of a common regulatory 3' UTR variant of ASXL1 suggests that both germline and somatic ASXL1 mutations contribute to lower blood counts in otherwise asymptomatic individuals. These association results shed light on genetic mechanisms that regulate circulating WBC counts and suggest a prominent shared genetic architecture with inflammatory and autoimmune diseases. Show less
no PDF DOI: 10.1016/j.ajhg.2016.05.003
JMJD1C
Zong-Bo Wei, Ye-Feng Yuan, Florence Jaouen +8 more · 2016 · Autophagy · Taylor & Francis · added 2026-04-24
Searching for new regulators of autophagy involved in selective dopaminergic (DA) neuron loss is a hallmark in the pathogenesis of Parkinson disease (PD). We here report that an endoplasmic reticulum Show more
Searching for new regulators of autophagy involved in selective dopaminergic (DA) neuron loss is a hallmark in the pathogenesis of Parkinson disease (PD). We here report that an endoplasmic reticulum (ER)-associated transmembrane protein SLC35D3 is selectively expressed in subsets of midbrain DA neurons in about 10% TH (tyrosine hydroxylase)-positive neurons in the substantia nigra pars compacta (SNc) and in about 22% TH-positive neurons in the ventral tegmental area (VTA). Loss of SLC35D3 in ros (roswell mutant) mice showed a reduction of 11.9% DA neurons in the SNc and 15.5% DA neuron loss in the VTA with impaired autophagy. We determined that SLC35D3 enhanced the formation of the BECN1-ATG14-PIK3C3 complex to induce autophagy. These results suggest that SLC35D3 is a new regulator of tissue-specific autophagy and plays an important role in the increased autophagic activity required for the survival of subsets of DA neurons. Show less
no PDF DOI: 10.1080/15548627.2016.1179402
PIK3C3
Zan Chen, Stefani N Thomas, David M Bolduc +4 more · 2016 · Biochemistry · ACS Publications · added 2026-04-24
PTEN is a lipid phosphatase that converts phosphatidylinositol 3,4,5-phosphate (PIP3) to phosphatidylinositol 4,5-phosphate (PIP2) and plays a critical role in the regulation of tumor growth. PTEN is Show more
PTEN is a lipid phosphatase that converts phosphatidylinositol 3,4,5-phosphate (PIP3) to phosphatidylinositol 4,5-phosphate (PIP2) and plays a critical role in the regulation of tumor growth. PTEN is subject to regulation by a variety of post-translational modifications, including phosphorylation on a C-terminal cluster of four Ser/Thr residues (380, 382, 383, and 385) and ubiquitylation by various E3 ligases, including NEDD4-1 and WWP2. It has previously been shown that C-terminal phosphorylation of PTEN can increase its cellular half-life. Using in vitro ubiquitin transfer assays, we show that WWP2 is more active than NEDD4-1 in ubiquitylating unphosphorylated PTEN. The mapping of ubiquitylation sites in PTEN by mass spectrometry showed that both NEDD4-1 and WWP2 can target a broad range of Lys residues in PTEN, although NEDD4-1 versus WWP2 showed a stronger preference for ubiquitylating PTEN's C2 domain. Whereas tetraphosphorylation of PTEN did not significantly affect its ubiquitylation by NEDD4-1, it inhibited PTEN ubiquitylation by WWP2. Single-turnover and pull-down experiments suggested that tetraphosphorylation of PTEN appears to weaken its interaction with WWP2. These studies reveal how the PTEN E3 ligases WWP2 and NEDD4-1 exhibit distinctive properties in Lys selectivity and sensitivity to PTEN phosphorylation. Our findings also provide a molecular mechanism for the connection between PTEN Ser/Thr phosphorylation and PTEN's cellular stability. Show less
no PDF DOI: 10.1021/acs.biochem.6b00448
WWP2
Jian Meng, Ming Feng, Weibing Dong +11 more · 2016 · Scientific reports · Nature · added 2026-04-24
Transcription factor carbohydrate responsive element binding protein (ChREBP) promotes glycolysis and lipogenesis in metabolic tissues and cancer cells. ChREBP-α and ChREBP-β, two isoforms of ChREBP t Show more
Transcription factor carbohydrate responsive element binding protein (ChREBP) promotes glycolysis and lipogenesis in metabolic tissues and cancer cells. ChREBP-α and ChREBP-β, two isoforms of ChREBP transcribed from different promoters, are both transcriptionally induced by glucose. However, the mechanism by which glucose increases ChREBP mRNA levels remains unclear. Here we report that hepatocyte nuclear factor 4 alpha (HNF-4α) is a key transcription factor for glucose-induced ChREBP-α and ChREBP-β expression. Ectopic HNF-4α expression increased ChREBP transcription while knockdown of HNF-4α greatly reduced ChREBP mRNA levels in liver cancer cells and mouse primary hepatocytes. HNF-4α not only directly bound to an E-box-containing region in intron 12 of the ChREBP gene, but also promoted ChREBP-β transcription by directly binding to two DR1 sites and one E-box-containing site of the ChREBP-β promoter. Moreover, HNF-4α interacted with ChREBP-α and synergistically promoted ChREBP-β transcription. Functionally, HNF-4α suppression reduced glucose-dependent ChREBP induction. Increased nuclear abundance of HNF-4α and its binding to cis-elements of ChREBP gene in response to glucose contributed to glucose-responsive ChREBP transcription. Taken together, our results not only revealed the novel mechanism by which HNF-4α promoted ChREBP transcription in response to glucose, but also demonstrated that ChREBP-α and HNF-4α synergistically increased ChREBP-β transcription. Show less
📄 PDF DOI: 10.1038/srep23944
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