👤 M L 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, Ke 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, 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
Huimei Chen, Aida Moreno-Moral, Francesco Pesce +24 more · 2019 · Nature communications · Nature · added 2026-04-24
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
no PDF DOI: 10.1038/s41467-019-12060-5
WWP2
Guangxu Cao, Shuang Li, Hezhan Shi +6 more · 2019 · Toxicology and applied pharmacology · Elsevier · added 2026-04-24
Tubulointerstitial fibrosis (TIF) is the main pathologic feature of end-stage renal disease. Epithelial-mesenchymal transition (EMT) of proximal tubular cells (PTCs) is one of the most significant fea Show more
Tubulointerstitial fibrosis (TIF) is the main pathologic feature of end-stage renal disease. Epithelial-mesenchymal transition (EMT) of proximal tubular cells (PTCs) is one of the most significant features of TIF. MicroRNAs play critical roles during EMT in TIF. However, whether miRNAs can be used as therapeutic targets in TIF therapy remains undetermined. We found that miR-30e, a member of the miR-30 family, is deregulated in TGF-β1-induced PTCs, TIF mice and human fibrotic kidney tissues. Moreover, transcription factors that induce EMT, such as snail, slug, and Zeb2, were direct targets of miR-30e. Using a cell-based miR-30e promoter luciferase reporter system, Schisandrin B (Sch B) was selected for the enhancement of miR-30e transcriptional activity. Our results indicate that Sch B can decrease the expression of snail, slug, and Zeb2, thereby attenuating the EMT of PTCs during TIF by upregulating miR-30e, both in vivo and in vitro. This study shows that miR-30e can serve as a therapeutic target in the treatment of patients with TIF and that Sch B may potentially be used in therapy against renal fibrosis. Show less
no PDF DOI: 10.1016/j.taap.2019.114769
SNAI1
Yunqin Chen, Jibin Dong, Xiaojin Zhang +5 more · 2019 · Atherosclerosis · Elsevier · added 2026-04-24
Cholesteryl ester transfer protein (CETP) inhibitor-mediated induction of HDL-cholesterol has no effect on the protection from cardiovascular disease (CVD). However, the mechanism is still unknown. Da Show more
Cholesteryl ester transfer protein (CETP) inhibitor-mediated induction of HDL-cholesterol has no effect on the protection from cardiovascular disease (CVD). However, the mechanism is still unknown. Data on the effects of this class of drugs on subclasses of HDL are either limited or insufficient. In this study, we investigated the effect of evacetrapib, a CETP inhibitor, on subclasses of HDL in patients with atherosclerotic cardiovascular disease or diabetes. Baseline and 3-month post-treatment samples from atorvastatin 40 mg plus evacetrapib 130 mg (n = 70) and atorvastatin 40 mg plus placebo (n = 30) arms were used for this purpose. Four subclasses of HDL (large HDL, medium HDL, small HDL, and preβ-1 HDL) were separated according to their size and quantified by densitometry using a recently developed native polyacrylamide gel electrophoresis (PAGE) system. Relative to placebo, while evacetrapib treatment dramatically increased large HDL and medium HDL subclasses, it significantly reduced small HDL (27%) as well as preβ-1 HDL (36%) particles. Evacetrapib treatment reduced total LDL, but also resulted in polydisperse LDL with LDL particles larger and smaller than the LDL subclasses of the placebo group. Evacetrapib reduced preβ-1 HDL and small HDL in patients with ASCVD or diabetes on statin. Preβ-1 HDL and medium HDL are negatively interrelated. The results could give a clue to understand the effect of CETP inhibitors on cardiovascular outcomes. Show less
đź“„ PDF DOI: 10.1016/j.atherosclerosis.2019.04.211
CETP
Yue Wu, Ming-Jiang Xu, Zhiyou Cao +9 more · 2019 · International journal of molecular sciences · MDPI · added 2026-04-24
Proprotein convertase subtilisin/kexin type 9 (PCSK9) plays a key role in cholesterol homeostasis and atherogenesis. However, there are only limited rodent models, with a functional low-density lipopr Show more
Proprotein convertase subtilisin/kexin type 9 (PCSK9) plays a key role in cholesterol homeostasis and atherogenesis. However, there are only limited rodent models, with a functional low-density lipoprotein receptor (LDLR) pathway and cholesteryl ester transfer protein (CETP) to evaluate the drug candidates targeting the PCSK9/LDLR pathway, that are translatable to humans. Here, by using our recently generated LDLR heterozygote ( Show less
đź“„ PDF DOI: 10.3390/ijms20235936
CETP
Xiao-ping Chen, Xin Long, Wen-Long Jia +23 more · 2019 · Journal of experimental & clinical cancer research : CR · BioMed Central · added 2026-04-24
Although the prognosis of patients with occult hepatitis B virus (HBV) infection (OBI) is usually benign, a small portion may undergo cirrhosis and subsequently hepatocellular carcinoma (HCC). We stud Show more
Although the prognosis of patients with occult hepatitis B virus (HBV) infection (OBI) is usually benign, a small portion may undergo cirrhosis and subsequently hepatocellular carcinoma (HCC). We studied the mechanism of life-long Integration of virus DNA into OBI host's genome, of which may induce hepatocyte transformation. We applied HBV capture sequencing on single cells from an OBI patient who, developed multiple HCC tumors and underwent liver resection in May 2013 at Tongji Hospital in China. Despite with the undetectable virus DNA in serum, we determined the pattern of viral integration in tumor cells and adjacent non-tumor cells and obtained the details of the viral arrangement in host genome, and furthermore the HBV integrated region in cancer genome. HBV captured sequencing of tissues and individual cells revealed that samples from multiple tumors shared two viral integration sites that could affect three host genes, including CSMD2 on chr1 and MED30/EXT1 on chr8. Whole genome sequencing further indicated one hybrid chromosome formed by HBV integrations between chr1 and chr8 that was shared by multiple tumors. Additional 50 poorly differentiated liver tumors and the paired adjacent non-tumors were evaluated and functional studies suggested up-regulated EXT1 expression promoted HCC growth. We further observed that the most somatic mutations within the tumor cell genome were common among the multiple tumors, suggesting that HBV associated, multifocal HCC is monoclonal in origin. Through analyzing the HBV integration sites in multifocal HCC, our data suggested that the tumor cells were monoclonal in origin and formed in the absence of active viral replication, whereas the affected host genes may subsequently contribute to carcinogenesis. Show less
đź“„ PDF DOI: 10.1186/s13046-019-1273-1
EXT1
Ying-Zhu Rao, Rong Chen, Yong Zhang +1 more · 2019 · General and comparative endocrinology · Elsevier · added 2026-04-24
Melanocortin-4 receptor (MC4R) and melanocortin receptor accessory protein 2 (MRAP2) play important roles in the melanocortin system, and interaction of MC4R and MRAP2 is suggested to play pivotal rol Show more
Melanocortin-4 receptor (MC4R) and melanocortin receptor accessory protein 2 (MRAP2) play important roles in the melanocortin system, and interaction of MC4R and MRAP2 is suggested to play pivotal role in energy balance of vertebrates. Orange-spotted grouper (Epinephelus coioides) is a widely cultured marine fish with high economic value in Asia. To explore potential interaction between grouper MC4R and MRAP2, herein we cloned grouper mc4r and mrap2. Grouper mc4r consisted of a 981 bp ORF encoding a putative protein of 327 amino acids, while the grouper mrap2 consisted of a 696 bp ORF encoding a putative protein of 232 amino acids. Sequence and phylogenetic analysis revealed that the grouper MC4R and MRAP2 were highly homologous at amino acid levels to several teleost MC4Rs and MRAP2s, respectively. qRT-PCR results showed that both mc4r and mrap2 were expressed primarily in the central nervous system. In the periphery, these genes were expressed more widely in male fish. The cloned grouper MC4R was functional, exhibiting high constitutive activity in cAMP pathway, capable of binding to three peptide agonists and increasing intracellular cAMP production dose-dependently. MRAP2 significantly decreased basal and agonist-stimulated cAMP signaling. MRAP2 also increased basal ERK1/2 activation but decreased ligand-induced stimulation when expressed at high levels. These data will facilitate future investigation of these molecules in regulating diverse physiological processes in orange-spotted grouper. Show less
no PDF DOI: 10.1016/j.ygcen.2019.113234
MC4R
Meiyi Zhou, Jing Shao, Cheng-Yang Wu +17 more · 2019 · Diabetes · added 2026-04-24
Recent studies implicate a strong association between elevated plasma branched-chain amino acids (BCAAs) and insulin resistance (IR). However, a causal relationship and whether interrupted BCAA homeos Show more
Recent studies implicate a strong association between elevated plasma branched-chain amino acids (BCAAs) and insulin resistance (IR). However, a causal relationship and whether interrupted BCAA homeostasis can serve as a therapeutic target for diabetes remain to be established experimentally. In this study, unbiased integrative pathway analyses identified a unique genetic link between obesity-associated IR and BCAA catabolic gene expression at the pathway level in human and mouse populations. In genetically obese ( Show less
đź“„ PDF DOI: 10.2337/db18-0927
BCKDK
Yan Chen, Angela C Estampador, Maria Keller +7 more · 2019 · International journal of obesity (2005) · Nature · added 2026-04-24
Recent analyses in Greenlandic Inuit identified six genetic polymorphisms (rs74771917, rs3168072, rs12577276, rs7115739, rs174602 and rs174570) in the fatty acid desaturase gene cluster (FADS1-FADS2-F Show more
Recent analyses in Greenlandic Inuit identified six genetic polymorphisms (rs74771917, rs3168072, rs12577276, rs7115739, rs174602 and rs174570) in the fatty acid desaturase gene cluster (FADS1-FADS2-FADS3) that are associated with multiple metabolic and anthropometric traits. Our objectives were to systematically assess whether dietary polyunsaturated fatty acid (PUFA) intake modifies the associations between genetic variants in the FADS gene cluster and cardiometabolic traits, and to functionally annotate top-ranking candidates to estimate their regulatory potential. Data analyses consisted of the following: interaction analyses between the 6 candidate genetic variants and dietary PUFA intake; gene-centric joint analyses to detect interaction signals in the FADS region; haplotype-centric joint tests across 30 haplotype blocks in the FADS region to refine interaction signals; and functional annotation of top-ranking loci from the previous steps. These analyses were undertaken in Swedish adults from the GLACIER Study (N = 5,160); data on genetic variation and eight cardiometabolic traits were used. Interactions were observed between rs174570 and n-6 PUFA intake on fasting glucose (P The association between FADS variants and triglycerides may be modified by PUFA intake. The intronic FADS2 rs5792235 variant is a potential causal variant in the region, having the highest regulatory potential. However, our results suggest that multiple haplotypes may harbour functional variants in a region, rather than a single causal variant. Show less
đź“„ PDF DOI: 10.1038/s41366-018-0112-3
FADS1
Timon Seeger, Rajani Shrestha, Chi Keung Lam +16 more · 2019 · Circulation · added 2026-04-24
Hypertrophic cardiomyopathy (HCM) is frequently caused by mutations in myosin-binding protein C3 ( MYBPC3) resulting in a premature termination codon (PTC). The underlying mechanisms of how PTC mutati Show more
Hypertrophic cardiomyopathy (HCM) is frequently caused by mutations in myosin-binding protein C3 ( MYBPC3) resulting in a premature termination codon (PTC). The underlying mechanisms of how PTC mutations in MYBPC3 lead to the onset and progression of HCM are poorly understood. This study's aim was to investigate the molecular mechanisms underlying the pathogenesis of HCM associated with MYBPC3 PTC mutations by utilizing human isogenic induced pluripotent stem cell-derived cardiomyocytes (iPSC-CMs). Isogenic iPSC lines were generated from HCM patients harboring MYBPC3 PTC mutations (p.R943x; p.R1073P_Fsx4) using genome editing. Comprehensive phenotypic and transcriptome analyses were performed in the iPSC-CMs. We observed aberrant calcium handling properties with prolonged decay kinetics and elevated diastolic calcium levels in the absence of structural abnormalities or contracile dysfunction in HCM iPSC-CMs as compared to isogenic controls. The mRNA expression levels of MYBPC3 were significantly reduced in mutant iPSC-CMs, but the protein levels were comparable among isogenic iPSC-CMs, suggesting that haploinsufficiency of MYBPC3 does not contribute to the pathogenesis of HCM in vitro. Furthermore, truncated MYBPC3 peptides were not detected. At the molecular level, the nonsense-mediated decay pathway was activated, and a set of genes involved in major cardiac signaling pathways was dysregulated in HCM iPSC-CMs, indicating an HCM gene signature in vitro. Specific inhibition of the nonsense-mediated decay pathway in mutant iPSC-CMs resulted in reversal of the molecular phenotype and normalization of calcium-handling abnormalities. iPSC-CMs carrying MYBPC3 PTC mutations displayed aberrant calcium signaling and molecular dysregulations in the absence of significant haploinsufficiency of MYBPC3 protein. Here we provided the first evidence of the direct connection between the chronically activated nonsense-mediated decay pathway and HCM disease development. Show less
no PDF DOI: 10.1161/CIRCULATIONAHA.118.034624
MYBPC3
Cheng Qin, Xin-Lan Bian, Cheng-Yun Cai +8 more · 2019 · Biochemical and biophysical research communications · Elsevier · added 2026-04-24
A typical feature of the contextual fear memory is increased fear generalization with time. Though much attention has been given to the neural structures that underlie the long-term consolidation of a Show more
A typical feature of the contextual fear memory is increased fear generalization with time. Though much attention has been given to the neural structures that underlie the long-term consolidation of a contextual fear memory, the molecular mechanisms regulating fear generalization remain unclear. We observed that retrieval of contextual fear in a novel context at a remote time point increased coupling of neuronal nitric oxide synthase (nNOS) with postsynaptic density-95 (PSD-95) and c-Fos expression in the anterior cingulate cortex (ACC). Disrupting nNOS-PSD-95 coupling in the ACC decreased the expression of Histone deacetylase 2 (HDAC Show less
no PDF DOI: 10.1016/j.bbrc.2019.03.184
DLG2
Yanjun Li, Yingyu Chen · 2019 · Advances in experimental medicine and biology · Springer · added 2026-04-24
AMPK is an evolutionarily conserved serine/threonine-protein kinase that acts as an energy sensor in cells and plays a key role in the upregulation of catabolism and inactivation of anabolism. Under v Show more
AMPK is an evolutionarily conserved serine/threonine-protein kinase that acts as an energy sensor in cells and plays a key role in the upregulation of catabolism and inactivation of anabolism. Under various physiological and pathological conditions, AMPK can be phosphorylated by an upstream kinase and bind to AMP or ADP rather than ATP, leading to its activation. Activated AMPK regulates a variety of metabolic processes, including autophagy. AMPK promotes autophagy directly by phosphorylating autophagy-related proteins in the mTORC1, ULK1, and PIK3C3/VPS34 complexes or indirectly by regulating the expression of autophagy-related genes downstream of transcription factors such as FOXO3, TFEB, and BRD4. AMPK can also upregulate the autophagic degradation of mitochondria (mitophagy), as it can induce fragmentation of damaged mitochondria in the network and promote the translocation of the autophagy machinery to damaged mitochondria. In this section, we will detail the molecular structure of AMPK, how its activity is regulated, and its pivotal role in regulating autophagy and mitophagy. Show less
no PDF DOI: 10.1007/978-981-15-0602-4_4
PIK3C3
Huiling Tang, Wenbing Nie, Jinna Xiao +3 more · 2019 · RSC advances · Royal Society of Chemistry · added 2026-04-24
The galactoglucan ACP2 was isolated from cultured
đź“„ PDF DOI: 10.1039/c8ra10347j
ACP2
Brandon Eilertson, Liang Chen, Audrey Li +3 more · 2019 · The Journal of antimicrobial chemotherapy · Oxford University Press · added 2026-04-24
To examine the epidemiology of β-lactam resistance in 'clonal group 258' (CG258), a successful KPC clonal group, over 14 years. Isolates were collected from 1999 to 2013 for a study of antibiotic resi Show more
To examine the epidemiology of β-lactam resistance in 'clonal group 258' (CG258), a successful KPC clonal group, over 14 years. Isolates were collected from 1999 to 2013 for a study of antibiotic resistance in Enterobacteriaceae in New York City; 515 bloodstream isolates had antibiotic susceptibility data available and 436 were available for a CG258 PCR assay. The 56 resulting CG258 isolates were characterized by MLST, capsular type and ESBL and KPC carriage. KPC-positive isolates were assessed for common KPC plasmid types, KPC subtype and Tn4401 isoform. RT-PCR revealed 56 isolates were CG258. Seventeen of the 56 CG258 isolates were phenotypically susceptible to all carbapenems (all KPC negative). Five out of 17 susceptible isolates were of the cps-2 (wzi154) capsule type; none was cps-1 (wzi29). Nineteen out of 28 KPC-2 isolates were cps-1 (wzi29) and 8/10 KPC-3 isolates carried cps-2 (wzi154); however, cps-2 (wzi154) predominated among KPC-2-positive isolates in 2003 and 2004. KPC-2 was first detected in 2003 and KPC-3 was first detected in 2006. KPC-harbouring plasmids pKpQIL (all Tn4401a) and pBK30683 (all Tn4401d) were detected in 16/38 and 6/38 carbapenem-resistant isolates, respectively. CG258-lineage Klebsiella pneumoniae isolates were completely absent in 1999, but common in 2003. Twenty-one percent of CG258 isolates were susceptible to carbapenems in addition to lacking both common ESBL and blaKPC-mediated resistance. The cps-2 (wzi154) capsule type was common in both these susceptible isolates and in early KPC-2-harbouring isolates, suggesting it was the initial capsule type in CG258. Carbapenem-resistant isolates carried common KPC-harbouring plasmids with the same KPC and Tn4401 isoforms, suggesting frequent clonal spread. Show less
no PDF DOI: 10.1093/jac/dky394
CPS1
Ke Liu, Li Ma, Timothy Y Y Lai +5 more · 2019 · Eye and vision (London, England) · BioMed Central · added 2026-04-24
Neovascular age-related macular degeneration (AMD) and polypoidal choroidal vasculopathy (PCV) are sight-threatening maculopathies with both environmental and genetic risk factors. We have previously Show more
Neovascular age-related macular degeneration (AMD) and polypoidal choroidal vasculopathy (PCV) are sight-threatening maculopathies with both environmental and genetic risk factors. We have previously shown relative risks posed by genes of the complement pathways to neovascular AMD and PCV. In this study, we investigated the haplotype-tagging single nucleotide polymorphisms (SNPs) in the The results revealed none of the six tagging SNPs of the This study showed no statistical significance in the genetic association of Show less
đź“„ PDF DOI: 10.1186/s40662-019-0161-2
CETP
Linyuan Ma, Lydia Jang, Jian Chen +5 more · 2019 · Journal of visualized experiments : JoVE · added 2026-04-24
Gene editing nucleases, represented by CRISPR-associated protein 9 (Cas9), are becoming mainstream tools in biomedical research. Successful delivery of CRISPR/Cas9 elements into the target cells by tr Show more
Gene editing nucleases, represented by CRISPR-associated protein 9 (Cas9), are becoming mainstream tools in biomedical research. Successful delivery of CRISPR/Cas9 elements into the target cells by transfection is a prerequisite for efficient gene editing. This protocol demonstrates that tube electroporation (TE) machine-mediated delivery of CRISPR/Cas9 ribonucleoprotein (RNP), along with single-stranded oligodeoxynucleotide (ssODN) donor templates to different types of mammalian cells, leads to robust precise gene editing events. First, TE was applied to deliver CRISPR/Cas9 RNP and ssODNs to induce disease-causing mutations in the interleukin 2 receptor subunit gamma (IL2RG) gene and sepiapterin reductase (SPR) gene in rabbit fibroblast cells. Precise mutation rates of 3.57%-20% were achieved as determined by bacterial TA cloning sequencing. The same strategy was then used in human iPSCs on several clinically relevant genes including epidermal growth factor receptor (EGFR), myosin binding protein C, cardiac (Mybpc3), and hemoglobin subunit beta (HBB). Consistently, highly precise mutation rates were achieved (11.65%-37.92%) as determined by deep sequencing (DeepSeq). The present work demonstrates that tube electroporation of CRISPR/Cas9 RNP represents an efficient transfection protocol for gene editing in mammalian cells. Show less
no PDF DOI: 10.3791/59512
MYBPC3
Xu Chen, Jun Jiang, Weiliang Zhu +2 more · 2019 · Medicine · added 2026-04-24
Hypertrophic cardiomyopathy (HCM) is mainly caused by mutations in genes encoding sarcomeric proteins. One of the most commonly mutated HCM genes is the MYBPC3 gene. Mutations in this gene lead mainly Show more
Hypertrophic cardiomyopathy (HCM) is mainly caused by mutations in genes encoding sarcomeric proteins. One of the most commonly mutated HCM genes is the MYBPC3 gene. Mutations in this gene lead mainly to truncation of the protein, which gives rise to a relatively severe phenotype. Analyses of gene mutations associated with HCM are valuable for molecular diagnosis, genetic counseling, and management of familial HCM. A 12-year-old boy presented with palpitations and dyspnea after exercise for 1 year. Echocardiography showed myocardial asymmetric hypertrophy of the ventricular septum, the anterior wall, and the lateral wall of the left ventricle. The thickness of the interventricular septum was estimated to be 33 mm. ECG showed left ventricular high voltage and ST-T changes. He had been diagnosed with HCM 3 months previously. Due to his clinical presentation, he was determined to have HCM via a molecular analysis, revealing compound heterozygotes (p.R597W and p.Q1012Sfs*8) in the MYBPC3 gene. The patient was prescribed metoprolol to slow the heart rate and increase diastolic filling time. The boy was treated with metoprolol 6.75 mg b.i.d. Approximately 3 months later, review of the echocardiography showed that the peak velocity across the LVOT dropped to 2.3 m/seconds and that the pressure gradient dropped to 21 mm Hg. A custom next-generation sequencing (NGS) technology for the HCM panel allowed us to identify compound heterozygous mutations in the MYBPC3 gene, confirming NGS as a molecular diagnostic tool. Show less
no PDF DOI: 10.1097/MD.0000000000014676
MYBPC3
Andy H Vo, Kayleigh A Swaggart, Anna Woo +11 more · 2019 · Human molecular genetics · Oxford University Press · added 2026-04-24
Like other single-gene disorders, muscular dystrophy displays a range of phenotypic heterogeneity even with the same primary mutation. Identifying genetic modifiers capable of altering the course of m Show more
Like other single-gene disorders, muscular dystrophy displays a range of phenotypic heterogeneity even with the same primary mutation. Identifying genetic modifiers capable of altering the course of muscular dystrophy is one approach to deciphering gene-gene interactions that can be exploited for therapy development. To this end, we used an intercross strategy in mice to map modifiers of muscular dystrophy. We interrogated genes of interest in an interval on mouse chromosome 10 associated with body mass in muscular dystrophy as skeletal muscle contributes significantly to total body mass. Using whole-genome sequencing of the two parental mouse strains combined with deep RNA sequencing, we identified the Met62Ile substitution in the dual-specificity phosphatase 6 (Dusp6) gene from the DBA/2 J (D2) mouse strain. DUSP6 is a broadly expressed dual-specificity phosphatase protein, which binds and dephosphorylates extracellular-signal-regulated kinase (ERK), leading to decreased ERK activity. We found that the Met62Ile substitution reduced the interaction between DUSP6 and ERK resulting in increased ERK phosphorylation and ERK activity. In dystrophic muscle, DUSP6 Met62Ile is strongly upregulated to counteract its reduced activity. We found that myoblasts from the D2 background were insensitive to a specific small molecule inhibitor of DUSP6, while myoblasts expressing the canonical DUSP6 displayed enhanced proliferation after exposure to DUSP6 inhibition. These data identify DUSP6 as an important regulator of ERK activity in the setting of muscle growth and muscular dystrophy. Show less
no PDF DOI: 10.1093/hmg/ddy349
DUSP6
Xia Hu, Zhenghao Tang, Siyuan Ma +3 more · 2019 · Biochemical and biophysical research communications · Elsevier · added 2026-04-24
Tripartite motif-containing protein 7 (TRIM7), which is involved in the biosynthesis of glycogen, has been reported to drive lung tumorigenesis. In the present study, we aimed to examine the expressio Show more
Tripartite motif-containing protein 7 (TRIM7), which is involved in the biosynthesis of glycogen, has been reported to drive lung tumorigenesis. In the present study, we aimed to examine the expression, roles and underlying molecular mechanisms of TRIM7 in hepatocellular carcinoma (HCC) development. Real-time PCR and immunohistochemical staining were performed to test the expression of TRIM7 in HCC tissues. Cell proliferation, cell cycle and tumorigenicity experiments were conducted to determine the function of TRIM7. The results showed that TRIM7 expression was elevated in human HCC tissues and that TRIM7 expression was significantly associated with tumor size, pTNM stage, serum α-fetoprotein (AFP) concentration, serum hepatitis B virus (HBV) DNA copy number and overall survival (OS) of HCC patients. TRIM7 knockdown inhibited the proliferation of HCC cells in vitro and in vivo. TRIM7 knockdown also induced a G1/S checkpoint in HCC cell lines. Additionally, TRIM7 knockdown led to decreased phosphorylated p38 (p-p38) and increased expression of p53 and p21. Ectopic expression of TRIM7 promoted HCC cell proliferation, cell cycle progression and p38 activation, but not in the presence of the p38 inhibitor SB203580. Moreover, TRIM7 overexpression enhanced the polyubiquitination and degradation of dual specificity phosphatase 6 (DUSP6). DUSP6 overexpression abolished the promotional effect of TRIM7 overexpression on HCC cell proliferation and the activation of p38. Furthermore, HBV X protein (HBx), a protein coded by HBV, was demonstrated to upregulate TRIM7 expression. Collectively, TRIM7 overexpression may contribute to the highly proliferative characteristics of HCC cells, and targeting TRIM7 might be a potential strategy for HCC treatment. Show less
no PDF DOI: 10.1016/j.bbrc.2019.02.001
DUSP6
Yuanfang Li, Yi Chen, Wenjiao Jin +9 more · 2019 · Frontiers in genetics · Frontiers · added 2026-04-24
There is a lack of understanding surrounding the molecular mechanisms involved in the development of chicken skeletal muscle in the late postnatal stage, especially in the regulation of breast muscle Show more
There is a lack of understanding surrounding the molecular mechanisms involved in the development of chicken skeletal muscle in the late postnatal stage, especially in the regulation of breast muscle development related genes, pathways, miRNAs and other factors. In this study, 12 cDNA libraries and 4 small RNA libraries were constructed from Gushi chicken breast muscle samples from 6, 14, 22, and 30 weeks. A total of 15,508 known transcripts, 25,718 novel transcripts, 388 known miRNAs and 31 novel miRNAs were identified by RNA-seq in breast muscle at the four developmental stages. Through correlation analysis of miRNA and mRNA expression profiles, it was found that 417, 370, 240, 1,418, 496, and 363 negatively correlated miRNA-mRNA pairs of Show less
no PDF DOI: 10.3389/fgene.2019.00197
MYBPC3
J Kalervo Hiltunen, Alexander J Kastaniotis, Kaija J Autio +3 more · 2019 · Molecular and cellular endocrinology · Elsevier · added 2026-04-24
17β-Hydroxysteroid dehydrogenases (HSD17B) catalyze the oxidation/reduction of 17β-hydroxy/keto group in position C17 in C18- and C19 steroids. Most HSD17Bs are also catalytically active with substrat Show more
17β-Hydroxysteroid dehydrogenases (HSD17B) catalyze the oxidation/reduction of 17β-hydroxy/keto group in position C17 in C18- and C19 steroids. Most HSD17Bs are also catalytically active with substrates other than steroids. A subset of these enzymes is able to process thioesters of carboxylic acids. This group of enzymes includes HSD17B4, HSD17B8, HSD17B10 and HSD17B12, which execute reactions in intermediary metabolism, participating in peroxisomal β-oxidation of fatty acids, mitochondrial oxidation of 3R-hydroxyacyl-groups, breakdown of isoleucine and fatty acid chain elongation in endoplasmic reticulum. Divergent substrate acceptance capabilities exemplify acquirement of catalytic site adaptiveness during evolution. As an additional common feature these HSD17Bs are multifunctional enzymes that arose either via gene fusions (HSD17B4) or are incorporated as subunits into multifunctional protein complexes (HSD17B8 and HSD17B10). Crystal structures of HSD17B4, HSD17B8 and HSD17B10 give insight into their structure-function relationships. Thus far, deficiencies of HSD17B4 and HSD17B10 have been assigned to inborn errors in humans, underlining their significance as enzymes of metabolism. Show less
no PDF DOI: 10.1016/j.mce.2018.11.012
HSD17B12
Jae Young Lee, Shebli Mehrazarin, Abdullah Alshaikh +6 more · 2019 · FASEB journal : official publication of the Federation of American Societies for Experimental Biology · added 2026-04-24
Histone Lys-specific demethylases (KDMs) play a key role in many biological processes through epigenetic mechanisms. However, the role of KDMs in inflammatory responses to oral bacterial infection is Show more
Histone Lys-specific demethylases (KDMs) play a key role in many biological processes through epigenetic mechanisms. However, the role of KDMs in inflammatory responses to oral bacterial infection is poorly understood. Here, we show a novel regulatory role of KDM3C in inflammatory responses to oral bacterial infection. KDM3C expression is transiently suppressed in human and mouse macrophages exposed to LPS from Show less
no PDF DOI: 10.1096/fj.201900154RR
JMJD1C
Jiyeon Kim, Zeping Hu, Ling Cai +23 more · 2019 · Nature · Nature · added 2026-04-24
Further analysis has revealed that the signal reported in Extended Data Fig. 1c of this Letter is attributed to phosphorylethanolamine, not carbamoyl phosphate. A newly developed derivatization method Show more
Further analysis has revealed that the signal reported in Extended Data Fig. 1c of this Letter is attributed to phosphorylethanolamine, not carbamoyl phosphate. A newly developed derivatization method revealed that the level of carbamoyl phosphate in these NSCLC extracts is below the detection threshold of approximately 10 nanomoles. These findings do not alter the overall conclusions of the Letter; see associated Amendment for full details. The Letter has not been corrected online. Show less
no PDF DOI: 10.1038/s41586-019-1133-3
CPS1

Meningitic

Lu Liu, Jixuan Li, Dong Huo +7 more · 2019 · Pathogens (Basel, Switzerland) · MDPI · added 2026-04-24
Bacterial meningitis is currently recognized as one of the most important life-threatening infections of the central nervous system (CNS) with high morbidity and mortality, despite the advancements in Show more
Bacterial meningitis is currently recognized as one of the most important life-threatening infections of the central nervous system (CNS) with high morbidity and mortality, despite the advancements in antimicrobial treatment. The disruption of blood-brain barrier (BBB) induced by meningitis bacteria is crucial for the development of bacterial meningitis. However, the complete mechanisms involving in the BBB disruption remain to be elucidated. Here, we found meningitic Show less
đź“„ PDF DOI: 10.3390/pathogens8040254
ANGPTL4
Shipeng Gong, Yongning Chen, Fanliang Meng +4 more · 2019 · FASEB journal : official publication of the Federation of American Societies for Experimental Biology · added 2026-04-24
Currently, cisplatin (DDP) is the first-line chemotherapeutic agent used for treatment of ovarian cancer, but gradually acquired drug resistance minimizes its therapeutic outcomes. We aimed to identif Show more
Currently, cisplatin (DDP) is the first-line chemotherapeutic agent used for treatment of ovarian cancer, but gradually acquired drug resistance minimizes its therapeutic outcomes. We aimed to identify crucial genes associated with DDP resistance in ovarian cancer and uncover potential mechanisms. Two sets of gene expression data were downloaded from Gene Expression Omnibus, and bioinformatics analysis was conducted. In our study, the differentially expressed genes between DDP-sensitive and DDP-resistant ovarian cancer were screened in GSE15709 and GSE51373 database, and chromosome condensation 2 regulator (RCC2) and nucleoporin 160 were identified as 2 genes that significantly up-regulated in DDP-resistant ovarian cancer cell lines compared with DDP-sensitive cell lines. Moreover, RCC2, Ral small GTPase (RalA), and Ral binding protein-1 (RalBP1) expression was found to be significantly higher in DDP-resistant ovarian cancer tissues than in DDP-sensitive tissues. RCC2 plays a positive role in cell proliferation, apoptosis, and migration in DDP-resistant ovarian cancer cell lines in vitro and in vivo. Furthermore, RCC2 could interact with RalA, thus promoting its downstream effector RalBP1. RalA knockdown could reverse the effects of RCC2 overexpression on DDP-resistant ovarian cancer cell proliferation, apoptosis, and migration. Similarly, RalA overexpression could alleviate the effects of RCC2 knockdown in DDP-resistant ovarian cancer cells. Taken together, RCC2 may function as an oncogene, regulating the RalA signaling pathway, and intervention of RCC2 expression might be a promising therapeutic strategy for DDP-resistant ovarian cancer.-Gong, S., Chen, Y., Meng, F., Zhang, Y., Wu, H., Li, C., Zhang, G. RCC2, a regulator of the RalA signaling pathway, is identified as a novel therapeutic target in cisplatin-resistant ovarian cancer. Show less
no PDF DOI: 10.1096/fj.201801529RR
NUP160
Fang-Zhou Chen, Ying Zhao, Hui-Zhao Chen · 2019 · International journal of molecular medicine · added 2026-04-24
Alzheimer's disease (AD) is a chronic neurodegenerative disease that often occurs at a slow pace yet deteriorates with time. MicroRNAs (miRs) have been demonstrated to offer novel therapeutic hope for Show more
Alzheimer's disease (AD) is a chronic neurodegenerative disease that often occurs at a slow pace yet deteriorates with time. MicroRNAs (miRs) have been demonstrated to offer novel therapeutic hope for disease treatment. The aim of the present study was to investigate the effect of miR‑98 on amyloid β (Aβ)‑protein production, oxidative stress and mitochondrial dysfunction through the Notch signaling pathway by targeting hairy and enhancer of split (Hes)‑related with YRPW motif protein 2 (HEY2) in mice with AD. A total of 70 Kunming mice were obtained and subjected to behavioral assessment. The levels of oxidative stress‑related proteins glutathione peroxidase, reduced glutathione, superoxide dismutase, malondialdehyde, acetylcholinesterase and Na+‑K+‑ATP were measured. Morphological changes in brain tissue, HEY2‑positivity levels, neuronal apoptotic index (AI) and neuron mitochondrial DNA (mtDNA) levels were also determined. Subsequently, the levels of miR‑98 and the mRNA and protein levels of HEY2, Jagged1, Notch1, Hes1, Hes5, β‑amyloid precursor protein, B‑cell lymphoma 2 (Bcl‑2) and Bcl‑2‑associated X protein in tissues and hippocampal neurons were determined by reverse transcription‑quantitative polymerase chain reaction and western blot analyses, respectively. Finally, hippocampal neuron viability and apoptosis were determined using an MTT assay and flow cytometry, respectively. The levels of miR‑98‑targeted HEY2 and miR‑98 were low and the levels of HEY2 were high in the AD mice. The AD mice exhibited poorer learning and memory abilities, oxidative stress function, and morphological changes of pyramidal cells in the hippocampal CA1 region. Furthermore, the AD mice exhibited increased protein levels of HEY2 and AI in the CA1 region of brain tissues with reduced mtDNA levels and dysfunctional neuronal mitochondria. miR‑98 suppressed hippocampal neuron apoptosis and promoted hippocampal neuron viability by inactivating the Notch signaling pathway via the inhibition of HEY2. In conclusion, the results demonstrated that miR‑98 reduced the production of Aβ and improved oxidative stress and mitochondrial dysfunction through activation of the Notch signaling pathway by binding to HEY2 in AD mice. Show less
đź“„ PDF DOI: 10.3892/ijmm.2018.3957
HEY2
Fred K Chen, Xiao Zhang, Jonathan Eintracht +10 more · 2019 · Documenta ophthalmologica. Advances in ophthalmology · Springer · added 2026-04-24
Mutation of the CLN3 gene, associated with juvenile neuronal ceroid lipofuscinosis, has recently been associated with late-onset, non-syndromic retinal dystrophy. Herein we describe the multimodal ima Show more
Mutation of the CLN3 gene, associated with juvenile neuronal ceroid lipofuscinosis, has recently been associated with late-onset, non-syndromic retinal dystrophy. Herein we describe the multimodal imaging, immunological and systemic features of an adult with compound heterozygous CLN3 mutations. A 50-year-old female with non-syndromic retinal dystrophy from the age of 36 years underwent multimodal retinal imaging, electroretinography, neuroimaging, immunological studies and genetic testing. CLN3 transcripts were amplified from patient leukocytes by reverse transcriptase polymerase chain reaction and characterized by Sanger sequencing. Visual acuity declined to 6/12 and 6/76 due to asymmetrical central scotoma. ERG responses became electronegative and patient's serum contained anti-retinal antibodies. Final visual acuity stabilized at 6/60 bilaterally 3 years after peri-ocular steroid and rituximab infusion. Genetic testing revealed compound heterozygous CLN3 mutations: the 1.02 kb deletion and a novel missense mutation (c.175G>A). In silico, analyses predicted the c.175G>A mutation disrupted an exonic splice enhancer site in exon 3. In patient leukocytes, CLN3 expression was reduced and novel CLN3 transcripts lacking exon 3 were detected. Our case study shows that (1) non-syndromic CLN3 disease leads to rod and delayed primary cone degeneration resulting in constricting peripheral field and enlarging central scotoma and, (2) the c.175G>A CLN3 mutation, altered splicing of the CLN3 gene. Overall, we provide comprehensive clinical characterization of a patient with non-syndromic CLN3 disease. Show less
no PDF DOI: 10.1007/s10633-018-9665-7
CLN3
Adam Karoutas, Witold Szymanski, Tobias Rausch +13 more · 2019 · Nature cell biology · Nature · added 2026-04-24
While nuclear lamina abnormalities are hallmarks of human diseases, their interplay with epigenetic regulators and precise epigenetic landscape remain poorly understood. Here, we show that loss of the Show more
While nuclear lamina abnormalities are hallmarks of human diseases, their interplay with epigenetic regulators and precise epigenetic landscape remain poorly understood. Here, we show that loss of the lysine acetyltransferase MOF or its associated NSL-complex members KANSL2 or KANSL3 leads to a stochastic accumulation of nuclear abnormalities with genomic instability patterns including chromothripsis. SILAC-based MOF and KANSL2 acetylomes identified lamin A/C as an acetylation target of MOF. HDAC inhibition or acetylation-mimicking lamin A derivatives rescue nuclear abnormalities observed in MOF-deficient cells. Mechanistically, loss of lamin A/C acetylation resulted in its increased solubility, defective phosphorylation dynamics and impaired nuclear mechanostability. We found that nuclear abnormalities include EZH2-dependent histone H3 Lys 27 trimethylation and loss of nascent transcription. We term this altered epigenetic landscape "heterochromatin enrichment in nuclear abnormalities" (HENA). Collectively, the NSL-complex-dependent lamin A/C acetylation provides a mechanism that maintains nuclear architecture and genome integrity. Show less
no PDF DOI: 10.1038/s41556-019-0397-z
KANSL1
Guanglin Xing, Hongyang Jing, Lei Zhang +9 more · 2019 · eLife · added 2026-04-24
Neuromuscular junction is a synapse between motoneurons and skeletal muscles, where acetylcholine receptors (AChRs) are concentrated to control muscle contraction. Studies of this synapse have contrib Show more
Neuromuscular junction is a synapse between motoneurons and skeletal muscles, where acetylcholine receptors (AChRs) are concentrated to control muscle contraction. Studies of this synapse have contributed to our understanding of synapse assembly and pathological mechanisms of neuromuscular disorders. Nevertheless, underlying mechanisms of NMJ formation was not well understood. To this end, we took a novel approach - studying mutant genes implicated in congenital myasthenic syndrome (CMS). We showed that knock-in mice carrying N88K, a prevalent CMS mutation of Rapsyn (Rapsn), died soon after birth with profound NMJ deficits. Rapsn is an adapter protein that bridges AChRs to the cytoskeleton and possesses E3 ligase activity. In investigating how N88K impairs the NMJ, we uncovered a novel signaling pathway by which Agrin-LRP4-MuSK induces tyrosine phosphorylation of Rapsn, which is required for its self-association and E3 ligase activity. Our results also provide insight into pathological mechanisms of CMS. Show less
no PDF DOI: 10.7554/eLife.49180
RAPSN
Xu Liu, Mei Mei, Xiang Chen +8 more · 2019 · Respiratory research · BioMed Central · added 2026-04-24
Persistent pulmonary hypertension of the newborn (PPHN) is a severe clinical problem among neonatal intensive care unit (NICU) patients. The genetic pathogenesis of PPHN is unclear. Only a few genetic Show more
Persistent pulmonary hypertension of the newborn (PPHN) is a severe clinical problem among neonatal intensive care unit (NICU) patients. The genetic pathogenesis of PPHN is unclear. Only a few genetic polymorphisms have been identified in infants with PPHN. Our study aimed to investigate the potential genetic etiology of PPHN. This study recruited PPHN patients admitted to the NICU of the Children's Hospital of Fudan University from Jan 2016 to Dec 2017. Exome sequencing was performed for all patients. Variants in reported PPHN/pulmonary arterial hypertension (PAH)-related genes were assessed. Single nucleotide polymorphism (SNP) association and gene-level analyses were carried out in 74 PPHN cases and 115 non-PPHN controls with matched baseline characteristics. Among the patient cohort, 74 (64.3%) patients were late preterm and term infants (≥ 34 weeks gestation) and 41 (35.7%) were preterm infants (< 34 weeks gestation). Preterm infants with PPHN exhibited low birth weight and a high frequency of bronchopulmonary dysplasia, respiratory distress syndrome (RDS) and mortality. Nine patients (only one preterm infant) were identified as harboring genetic variants, including three with pathogenic/likely pathogenic variants in TBX4 and BMPR2 and six with variants of unknown significance in BMPR2, SMAD9, TGFB1, KCNA5 and TRPC6. Three SNPs (rs192759073, rs1047883 and rs2229589) in CPS1 and one SNP (rs1044008) in NOTCH3 were significantly associated with PPHN (p < 0.05). CPS1 and SMAD9 were identified as risk genes for PPHN (p < 0.05). In this study, we identified genetic variants in PPHN patients, and we reported CPS1, NOTCH3 and SMAD9 as risk genes for late preterm and term PPHN in a single-center Chinese cohort. Our findings provide additional genetic evidence of the pathogenesis of PPHN and new insight into potential strategies for disease treatment. Show less
đź“„ PDF DOI: 10.1186/s12931-019-1148-1
CPS1
Ramreddy Tippana, Michael C Chen, Natalia A Demeshkina +2 more · 2019 · Nature communications · Nature · added 2026-04-24
DHX36 is a DEAH-box helicase that resolves parallel G-quadruplex structures formed in DNA and RNA. The recent co-crystal structure of DHX36 bound G4-DNA revealed an intimate contact, but did not addre Show more
DHX36 is a DEAH-box helicase that resolves parallel G-quadruplex structures formed in DNA and RNA. The recent co-crystal structure of DHX36 bound G4-DNA revealed an intimate contact, but did not address the role of ATP hydrolysis in G4 resolving activity. Here, we demonstrate that unlike on G4-DNA, DHX36 displays ATP-independent unfolding of G4-RNA followed by ATP-dependent refolding, generating a highly asymmetric pattern of activity. Interestingly, DHX36 refolds G4-RNA in several steps, reflecting the discrete steps in forming the G4 structure. We show that the ATP-dependent activity of DHX36 arises from the RNA tail rather than the G4. Mutations that perturb G4 contact result in quick dissociation of the protein from RNA upon ATP hydrolysis, while mutations that interfere with binding the RNA tail induce dysregulated activity. We propose that the ATP-dependent activity of DHX36 may be useful for dynamically resolving various G4-RNA structures in cells. Show less
đź“„ PDF DOI: 10.1038/s41467-019-09802-w
DHX36