👤 Yu-Ting 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, 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-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

SarcTrack.

Christopher N Toepfer, Arun Sharma, Marcelo Cicconet +13 more · 2019 · Circulation research · added 2026-04-24
Human induced pluripotent stem cell-derived cardiomyocytes (hiPSC-CMs) in combination with CRISPR/Cas9 genome editing provide unparalleled opportunities to study cardiac biology and disease. However, Show more
Human induced pluripotent stem cell-derived cardiomyocytes (hiPSC-CMs) in combination with CRISPR/Cas9 genome editing provide unparalleled opportunities to study cardiac biology and disease. However, sarcomeres, the fundamental units of myocyte contraction, are immature and nonlinear in hiPSC-CMs, which technically challenge accurate functional interrogation of contractile parameters in beating cells. Furthermore, existing analysis methods are relatively low-throughput, indirectly assess contractility, or only assess well-aligned sarcomeres found in mature cardiac tissues. We aimed to develop an analysis platform that directly, rapidly, and automatically tracks sarcomeres in beating cardiomyocytes. The platform should assess sarcomere content, contraction and relaxation parameters, and beat rate. We developed SarcTrack, a MatLab software that monitors fluorescently tagged sarcomeres in hiPSC-CMs. The algorithm determines sarcomere content, sarcomere length, and returns rates of sarcomere contraction and relaxation. By rapid measurement of hundreds of sarcomeres in each hiPSC-CM, SarcTrack provides large data sets for robust statistical analyses of multiple contractile parameters. We validated SarcTrack by analyzing drug-treated hiPSC-CMs, confirming the contractility effects of compounds that directly activate (CK-1827452) or inhibit (MYK-461) myosin molecules or indirectly alter contractility (verapamil and propranolol). SarcTrack analysis of hiPSC-CMs carrying a heterozygous truncation variant in the myosin-binding protein C ( MYBPC3) gene, which causes hypertrophic cardiomyopathy, recapitulated seminal disease phenotypes including cardiac hypercontractility and diminished relaxation, abnormalities that normalized with MYK-461 treatment. SarcTrack provides a direct and efficient method to quantitatively assess sarcomere function. By improving existing contractility analysis methods and overcoming technical challenges associated with functional evaluation of hiPSC-CMs, SarcTrack enhances translational prospects for sarcomere-regulating therapeutics and accelerates interrogation of human cardiac genetic variants. Show less
no PDF DOI: 10.1161/CIRCRESAHA.118.314505
MYBPC3
Hong-Li Guo, Xia Jing, Jie-Yu Sun +7 more · 2019 · Current pharmaceutical design · Bentham Science · added 2026-04-24
Valproic acid (VPA) as a widely used primary medication in the treatment of epilepsy is associated with reversible or irreversible hepatotoxicity. Long-term VPA therapy is also related to increased ri Show more
Valproic acid (VPA) as a widely used primary medication in the treatment of epilepsy is associated with reversible or irreversible hepatotoxicity. Long-term VPA therapy is also related to increased risk for the development of non-alcoholic fatty liver disease (NAFLD). In this review, metabolic elimination pathways of VPA in the liver and underlying mechanisms of VPA-induced hepatotoxicity are discussed. We searched in PubMed for manuscripts published in English, combining terms such as "Valproic acid", "hepatotoxicity", "liver injury", and "mechanisms". The data of screened papers were analyzed and summarized. The formation of VPA reactive metabolites, inhibition of fatty acid β-oxidation, excessive oxidative stress and genetic variants of some enzymes, such as CPS1, POLG, GSTs, SOD2, UGTs and CYPs genes, have been reported to be associated with VPA hepatotoxicity. Furthermore, carnitine supplementation and antioxidants administration proved to be positive treatment strategies for VPA-induced hepatotoxicity. Therapeutic drug monitoring (TDM) and routine liver biochemistry monitoring during VPA-therapy, as well as genotype screening for certain patients before VPA administration, could improve the safety profile of this antiepileptic drug. Show less
no PDF DOI: 10.2174/1381612825666190329145428
CPS1
Jared M Churko, Priyanka Garg, Barbara Treutlein +14 more · 2018 · Nature communications · Nature · added 2026-04-24
Human induced pluripotent stem cell-derived cardiomyocytes (hiPSC-CMs) have become a powerful tool for human disease modeling and therapeutic testing. However, their use remains limited by their immat Show more
Human induced pluripotent stem cell-derived cardiomyocytes (hiPSC-CMs) have become a powerful tool for human disease modeling and therapeutic testing. However, their use remains limited by their immaturity and heterogeneity. To characterize the source of this heterogeneity, we applied complementary single-cell RNA-seq and bulk RNA-seq technologies over time during hiPSC cardiac differentiation and in the adult heart. Using integrated transcriptomic and splicing analysis, more than half a dozen distinct single-cell populations were observed, several of which were coincident at a single time-point, day 30 of differentiation. To dissect the role of distinct cardiac transcriptional regulators associated with each cell population, we systematically tested the effect of a gain or loss of three transcription factors (NR2F2, TBX5, and HEY2), using CRISPR genome editing and ChIP-seq, in conjunction with patch clamp, calcium imaging, and CyTOF analysis. These targets, data, and integrative genomics analysis methods provide a powerful platform for understanding in vitro cellular heterogeneity. Show less
📄 PDF DOI: 10.1038/s41467-018-07333-4
HEY2
Valérie Turcot, Yingchang Lu, Heather M Highland +408 more · 2018 · Nature genetics · Nature · added 2026-04-24
Valérie Turcot, Yingchang Lu, Heather M Highland, Claudia Schurmann, Anne E Justice, Rebecca S Fine, Jonathan P Bradfield, Tõnu Esko, Ayush Giri, Mariaelisa Graff, Xiuqing Guo, Audrey E Hendricks, Tugce Karaderi, Adelheid Lempradl, Adam E Locke, Anubha Mahajan, Eirini Marouli, Suthesh Sivapalaratnam, Kristin L Young, Tamuno Alfred, Mary F Feitosa, Nicholas G D Masca, Alisa K Manning, Carolina Medina-Gomez, Poorva Mudgal, Maggie C Y Ng, Alex P Reiner, Sailaja Vedantam, Sara M Willems, Thomas W Winkler, Gonçalo Abecasis, Katja K Aben, Dewan S Alam, Sameer E Alharthi, Matthew Allison, Philippe Amouyel, Folkert W Asselbergs, Paul L Auer, Beverley Balkau, Lia E Bang, Inês Barroso, Lisa Bastarache, Marianne Benn, Sven Bergmann, Lawrence F Bielak, Matthias Blüher, Michael Boehnke, Heiner Boeing, Eric Boerwinkle, Carsten A Böger, Jette Bork-Jensen, Michiel L Bots, Erwin P Bottinger, Donald W Bowden, Ivan Brandslund, Gerome Breen, Murray H Brilliant, Linda Broer, Marco Brumat, Amber A Burt, Adam S Butterworth, Peter T Campbell, Stefania Cappellani, David J Carey, Eulalia Catamo, Mark J Caulfield, John C Chambers, Daniel I Chasman, Yii-Der I Chen, Rajiv Chowdhury, Cramer Christensen, Audrey Y Chu, Massimiliano Cocca, Francis S Collins, James P Cook, Janie Corley, Jordi Corominas Galbany, Amanda J Cox, David S Crosslin, Gabriel Cuellar-Partida, Angela D'Eustacchio, John Danesh, Gail Davies, Paul I W Bakker, Mark C H Groot, Renée Mutsert, Ian J Deary, George Dedoussis, Ellen W Demerath, Martin Heijer, Anneke I Hollander, Hester M Ruijter, Joe G Dennis, Josh C Denny, Emanuele Di Angelantonio, Fotios Drenos, Mengmeng Du, Marie-Pierre Dubé, Alison M Dunning, Douglas F Easton, Todd L Edwards, David Ellinghaus, Patrick T Ellinor, Paul Elliott, Evangelos Evangelou, Aliki-Eleni Farmaki, I Sadaf Farooqi, Jessica D Faul, Sascha Fauser, Shuang Feng, Ele Ferrannini, Jean Ferrieres, Jose C Florez, Ian Ford, Myriam Fornage, Oscar H Franco, Andre Franke, Paul W Franks, Nele Friedrich, Ruth Frikke-Schmidt, Tessel E Galesloot, Wei Gan, Ilaria Gandin, Paolo Gasparini, Jane Gibson, Vilmantas Giedraitis, Anette P Gjesing, Penny Gordon-Larsen, Mathias Gorski, Hans-Jörgen Grabe, Struan F A Grant, Niels Grarup, Helen L Griffiths, Megan L Grove, Vilmundur Gudnason, Stefan Gustafsson, Jeff Haessler, Hakon Hakonarson, Anke R Hammerschlag, Torben Hansen, Kathleen Mullan Harris, Tamara B Harris, Andrew T Hattersley, Christian T Have, Caroline Hayward, Liang He, Nancy L Heard-Costa, Andrew C Heath, Iris M Heid, Øyvind Helgeland, Jussi Hernesniemi, Alex W Hewitt, Oddgeir L Holmen, G Kees Hovingh, Joanna M M Howson, Yao Hu, Paul L Huang, Jennifer E Huffman, M Arfan Ikram, Erik Ingelsson, Anne U Jackson, Jan-Håkan Jansson, Gail P Jarvik, Gorm B Jensen, Yucheng Jia, Stefan Johansson, Marit E Jørgensen, Torben Jørgensen, J Wouter Jukema, Bratati Kahali, René S Kahn, Mika Kähönen, Pia R Kamstrup, Stavroula Kanoni, Jaakko Kaprio, Maria Karaleftheri, Sharon L R Kardia, Fredrik Karpe, Sekar Kathiresan, Frank Kee, Lambertus A Kiemeney, Eric Kim, Hidetoshi Kitajima, Pirjo Komulainen, Jaspal S Kooner, Charles Kooperberg, Tellervo Korhonen, Peter Kovacs, Helena Kuivaniemi, Zoltán Kutalik, Kari Kuulasmaa, Johanna Kuusisto, Markku Laakso, Timo A Lakka, David Lamparter, Ethan M Lange, Leslie A Lange, Claudia Langenberg, Eric B Larson, Nanette R Lee, Terho Lehtimäki, Cora E Lewis, Huaixing Li, Jin Li, Ruifang Li-Gao, Honghuang Lin, Keng-Hung Lin, Li-An Lin, Xu Lin, Lars Lind, Jaana Lindström, Allan Linneberg, Ching-Ti Liu, Dajiang J Liu, Yongmei Liu, Ken S Lo, Artitaya Lophatananon, Andrew J Lotery, Anu Loukola, Jian'an Luan, Steven A Lubitz, Leo-Pekka Lyytikäinen, Satu Männistö, Gaëlle Marenne, Angela L Mazul, Mark I McCarthy, Roberta McKean-Cowdin, Sarah E Medland, Karina Meidtner, Lili Milani, Vanisha Mistry, Paul Mitchell, Karen L Mohlke, Leena Moilanen, Marie Moitry, Grant W Montgomery, Dennis O Mook-Kanamori, Carmel Moore, Trevor A Mori, Andrew D Morris, Andrew P Morris, Martina Müller-Nurasyid, Patricia B Munroe, Mike A Nalls, Narisu Narisu, Christopher P Nelson, Matt Neville, Sune F Nielsen, Kjell Nikus, Pål R Njølstad, Børge G Nordestgaard, Dale R Nyholt, Jeffrey R O'Connel, Michelle L O'Donoghue, Loes M Olde Loohuis, Roel A Ophoff, Katharine R Owen, Chris J Packard, Sandosh Padmanabhan, Colin N A Palmer, Nicholette D Palmer, Gerard Pasterkamp, Aniruddh P Patel, Alison Pattie, Oluf Pedersen, Peggy L Peissig, Gina M Peloso, Craig E Pennell, Markus Perola, James A Perry, John R B Perry, Tune H Pers, Thomas N Person, Annette Peters, Eva R B Petersen, Patricia A Peyser, Ailith Pirie, Ozren Polasek, Tinca J Polderman, Hannu Puolijoki, Olli T Raitakari, Asif Rasheed, Rainer Rauramaa, Dermot F Reilly, Frida Renström, Myriam Rheinberger, Paul M Ridker, John D Rioux, Manuel A Rivas, David J Roberts, Neil R Robertson, Antonietta Robino, Olov Rolandsson, Igor Rudan, Katherine S Ruth, Danish Saleheen, Veikko Salomaa, Nilesh J Samani, Yadav Sapkota, Naveed Sattar, Robert E Schoen, Pamela J Schreiner, Matthias B Schulze, Robert A Scott, Marcelo P Segura-Lepe, Svati H Shah, Wayne H-H Sheu, Xueling Sim, Andrew J Slater, Kerrin S Small, Albert V Smith, Lorraine Southam, Timothy D Spector, Elizabeth K Speliotes, John M Starr, Kari Stefansson, Valgerdur Steinthorsdottir, Kathleen E Stirrups, Konstantin Strauch, Heather M Stringham, Michael Stumvoll, Liang Sun, Praveen Surendran, Amy J Swift, Hayato Tada, Katherine E Tansey, Jean-Claude Tardif, Kent D Taylor, Alexander Teumer, Deborah J Thompson, Gudmar Thorleifsson, Unnur Thorsteinsdottir, Betina H Thuesen, Anke Tönjes, Gerard Tromp, Stella Trompet, Emmanouil Tsafantakis, Jaakko Tuomilehto, Anne Tybjaerg-Hansen, Jonathan P Tyrer, Rudolf Uher, André G Uitterlinden, Matti Uusitupa, Sander W Laan, Cornelia M Duijn, Nienke Leeuwen, Jessica van Setten, Mauno Vanhala, Anette Varbo, Tibor V Varga, Rohit Varma, Digna R Velez Edwards, Sita H Vermeulen, Giovanni Veronesi, Henrik Vestergaard, Veronique Vitart, Thomas F Vogt, Uwe Völker, Dragana Vuckovic, Lynne E Wagenknecht, Mark Walker, Lars Wallentin, Feijie Wang, Carol A Wang, Shuai Wang, Yiqin Wang, Erin B Ware, Nicholas J Wareham, Helen R Warren, Dawn M Waterworth, Jennifer Wessel, Harvey D White, Cristen J Willer, James G Wilson, Daniel R Witte, Andrew R Wood, Ying Wu, Hanieh Yaghootkar, Jie Yao, Pang Yao, Laura M Yerges-Armstrong, Robin Young, Eleftheria Zeggini, Xiaowei Zhan, Weihua Zhang, Jing Hua Zhao, Wei Zhao, Wei Zhou, Krina T Zondervan, CHD Exome+ Consortium, EPIC-CVD Consortium, ExomeBP Consortium, Global Lipids Genetic Consortium, GoT2D Genes Consortium, EPIC InterAct Consortium, INTERVAL Study, ReproGen Consortium, T2D-Genes Consortium, MAGIC Investigators, Understanding Society Scientific Group, Jerome I Rotter, John A Pospisilik, Fernando Rivadeneira, Ingrid B Borecki, Panos Deloukas, Timothy M Frayling, Guillaume Lettre, Kari E North, Cecilia M Lindgren, Joel N Hirschhorn, Ruth J F Loos Show less
Genome-wide association studies (GWAS) have identified >250 loci for body mass index (BMI), implicating pathways related to neuronal biology. Most GWAS loci represent clusters of common, noncoding var Show more
Genome-wide association studies (GWAS) have identified >250 loci for body mass index (BMI), implicating pathways related to neuronal biology. Most GWAS loci represent clusters of common, noncoding variants from which pinpointing causal genes remains challenging. Here we combined data from 718,734 individuals to discover rare and low-frequency (minor allele frequency (MAF) < 5%) coding variants associated with BMI. We identified 14 coding variants in 13 genes, of which 8 variants were in genes (ZBTB7B, ACHE, RAPGEF3, RAB21, ZFHX3, ENTPD6, ZFR2 and ZNF169) newly implicated in human obesity, 2 variants were in genes (MC4R and KSR2) previously observed to be mutated in extreme obesity and 2 variants were in GIPR. The effect sizes of rare variants are ~10 times larger than those of common variants, with the largest effect observed in carriers of an MC4R mutation introducing a stop codon (p.Tyr35Ter, MAF = 0.01%), who weighed ~7 kg more than non-carriers. Pathway analyses based on the variants associated with BMI confirm enrichment of neuronal genes and provide new evidence for adipocyte and energy expenditure biology, widening the potential of genetically supported therapeutic targets in obesity. Show less
📄 PDF DOI: 10.1038/s41588-017-0011-x
GIPR
Jie Chen, Pei Huang, Yachao He +6 more · 2018 · Parkinsonism & related disorders · Elsevier · added 2026-04-24
no PDF DOI: 10.1016/j.parkreldis.2018.05.017
MAP2K5
Weiwei Ruan, Li Cao, Zhonghua Chen +2 more · 2018 · Oncology letters · added 2026-04-24
Hereditary multiple osteochondroma (HMO) is an autosomal dominant genetic disorder characterized by multiple outgrowing bony tumors capped by cartilage, generally affecting the metaphyses. The disease Show more
Hereditary multiple osteochondroma (HMO) is an autosomal dominant genetic disorder characterized by multiple outgrowing bony tumors capped by cartilage, generally affecting the metaphyses. The disease is known as hereditary multiple exostoses, familial exostosis, multiple cartilaginous exostoses or hereditary malformation of cartilage. The prevalence of HMO in Europe and the Unites States is ~1:100,000, although it has not been reported in China. The disease is often accompanied by pain, asymmetry and skeletal malformations, including forearm and leg bending deformities, limb length discrepancies, and knee internal and external rotation abnormalities. Mutations to exostosin-1 ( Show less
📄 PDF DOI: 10.3892/ol.2018.7838
EXT1
Ji-Young Youn, Wade H Dunham, Seo Jung Hong +12 more · 2018 · Molecular cell · Elsevier · added 2026-04-24
mRNA processing, transport, translation, and ultimately degradation involve a series of dedicated protein complexes that often assemble into large membraneless structures such as stress granules (SGs) Show more
mRNA processing, transport, translation, and ultimately degradation involve a series of dedicated protein complexes that often assemble into large membraneless structures such as stress granules (SGs) and processing bodies (PBs). Here, systematic in vivo proximity-dependent biotinylation (BioID) analysis of 119 human proteins associated with different aspects of mRNA biology uncovers 7424 unique proximity interactions with 1,792 proteins. Classical bait-prey analysis reveals connections of hundreds of proteins to distinct mRNA-associated processes or complexes, including the splicing and transcriptional elongation machineries (protein phosphatase 4) and the CCR4-NOT deadenylase complex (CEP85, RNF219, and KIAA0355). Analysis of correlated patterns between endogenous preys uncovers the spatial organization of RNA regulatory structures and enables the definition of 144 core components of SGs and PBs. We report preexisting contacts between most core SG proteins under normal growth conditions and demonstrate that several core SG proteins (UBAP2L, CSDE1, and PRRC2C) are critical for the formation of microscopically visible SGs. Show less
no PDF DOI: 10.1016/j.molcel.2017.12.020
PRRC2C
Eriko Negishi, Noboru Fukuda, Tomoyasu Otsuki +11 more · 2018 · American journal of physiology. Renal physiology · added 2026-04-24
We previously showed that complement 3 (C3) is highly expressed in mesenchymal tissues in spontaneously hypertensive rats (SHR). We targeted C3 gene by zinc-finger nuclease (ZFN) gene-editing technolo Show more
We previously showed that complement 3 (C3) is highly expressed in mesenchymal tissues in spontaneously hypertensive rats (SHR). We targeted C3 gene by zinc-finger nuclease (ZFN) gene-editing technology and investigated blood pressure and phenotype in SHR. Blood pressure was measured by tail-cuff and telemetry methods. Histology and expression of liver X receptor α (LXRα), renin, Krüppel-like factor 5 (KLF5), and E-cadherin were evaluated in kidneys. Mesangial cells (MCs) were removed from glomeruli from three strains, and we evaluated the phenotype in vitro. SHR showed the salt-sensitive hypertension that was abolished in C3 knockout (KO) SHR. Proliferation of MCs from SHR was higher than that from Wistar-Kyoto (WKY) rats and showed a synthetic phenotype. Renal injury scores were higher in SHR than in WKY rats and C3 KO SHR. Expression of E-cadherin was lower, and expression of renin was higher in the nephrotubulus from SHR than WKY rats and C3 KO SHR. Expression of C3 α-chain protein and α-smooth muscle actin protein was significantly higher in renal medulla from SHR than from WKY rats. Expression of angiotensinogen, LXRα, renin, and KLF5 mRNA was increased in kidney from SHR compared with C3 KO SHR. Intrarenal angiotensin II levels were significantly higher in kidney from SHR than WKY rats and C3 KO SHR. Urinary epinephrine and norepinephrine excretions were significantly higher in SHR than in WKY rats and C3 KO SHR. These findings showed that increased C3 induces salt-sensitive hypertension with increases in urinary catecholamine excretion and intrarenal activation of the renin-angiotensin system by the dedifferentiation of mesenchymal tissues in kidney from SHR. Show less
no PDF DOI: 10.1152/ajprenal.00370.2018
NR1H3
Wenyan Fu, Hefen Sun, Yang Zhao +4 more · 2018 · Molecular immunology · Elsevier · added 2026-04-24
The overexpression of EGFR often occurs in TNBC, and the anti-EGFR receptor antibody cetuximab is used widely to treat metastatic cancer in the clinic. However, EGFR-targeted therapies have been devel Show more
The overexpression of EGFR often occurs in TNBC, and the anti-EGFR receptor antibody cetuximab is used widely to treat metastatic cancer in the clinic. However, EGFR-targeted therapies have been developed for TNBC without clinical success. In this study, we show that impaired EGFR degradation is crucial for resistance to cetuximab, which depends on the cell surface molecule CD44. To further investigate the role of CD44 in EGFR signaling and its treatment potential, we developed a targeting fusion protein composed of an anti-EGFR scFv generated from cetuximab and truncated protamine, called Ce-tP. CD44 siRNA can be specifically delivered into EGFR-positive TNBC cells by Ce-tP. Efficient knockdown of CD44 and suppression of both EGFR and downstream signaling by the Ce-tP/siRNA complex were observed in EGFR-positive TNBC cells. More importantly, our results also showed that targeted delivery of siRNA specific for CD44 can efficiently overcome resistance to EGFR targeting in TNBC cells both in vitro and in vivo. Overall, our results establish a new principle to achieve EGFR inhibition in TNBC and limit drug resistance. Show less
no PDF DOI: 10.1016/j.molimm.2018.05.010
CETP
Ning Ma, Joe Z Zhang, Ilanit Itzhaki +11 more · 2018 · Circulation · added 2026-04-24
The progression toward low-cost and rapid next-generation sequencing has uncovered a multitude of variants of uncertain significance (VUS) in both patients and asymptomatic "healthy" individuals. A VU Show more
The progression toward low-cost and rapid next-generation sequencing has uncovered a multitude of variants of uncertain significance (VUS) in both patients and asymptomatic "healthy" individuals. A VUS is a rare or novel variant for which disease pathogenicity has not been conclusively demonstrated or excluded, and thus cannot be definitively annotated. VUS, therefore, pose critical clinical interpretation and risk-assessment challenges, and new methods are urgently needed to better characterize their pathogenicity. To address this challenge and showcase the uncertainty surrounding genomic variant interpretation, we recruited a "healthy" asymptomatic individual, lacking cardiac-disease clinical history, carrying a hypertrophic cardiomyopathy (HCM)-associated genetic variant (NM₀₀₀₂₅₈.2:c.170C>A, NP₀₀₀₂₄₉.1:p.Ala57Asp) in the sarcomeric gene MYL3, reported by the ClinVar database to be "likely pathogenic." Human-induced pluripotent stem cells (iPSCs) were derived from the heterozygous VUS MYL3 The heterozygous VUS MYL3 Our study illustrates the ability of clustered regularly interspaced short palindromic repeats/Cas9 genome-editing of carrier-specific iPSCs to elucidate both benign and pathogenic HCM functional phenotypes in a carrier-specific manner in a dish. As such, this platform represents a promising VUS risk-assessment tool that can be used for assessing HCM-associated VUS specifically, and VUS in general, and thus significantly contribute to the arsenal of precision medicine tools available in this emerging field. Show less
no PDF DOI: 10.1161/CIRCULATIONAHA.117.032273
MYBPC3
Qiu Peng, Ling Chen, Wei Wu +9 more · 2018 · Cell death & disease · Nature · added 2026-04-24
The erythropoietin-producing hepatoma (EPH) receptor A2 (EphA2) belongs to the Eph family of receptor tyrosine kinases. EphA2 is highly correlated with the formation of many solid tumors and has been Show more
The erythropoietin-producing hepatoma (EPH) receptor A2 (EphA2) belongs to the Eph family of receptor tyrosine kinases. EphA2 is highly correlated with the formation of many solid tumors and has been linked to the dysregulation of signaling pathways that promote tumor cell proliferation, migration, and invasion as well as angiogenesis. Deregulation of Wnt signaling is implicated in many forms of human disease including gastric cancer. We previously reported that EphA2 promotes the epithelial-mesenchymal transition through Wnt/β-catenin signaling in gastric cancer. Herein, we present a novel mechanism by which EphA2 regulates Wnt/β-catenin signaling. EphA2 acts as a receptor for Wnt ligands and recruits Axin1 to the plasma membrane by directly binding Dvl2. The EphA2-Dvl2/Axin1 interaction was enhanced by Wnt3a treatment, suggesting that EphA2 acts as a functional receptor for the Wnt/β-catenin pathway and plays a vital role in downstream signaling. We showed that Dvl2 mediates the EphA2-Axin1 interaction by binding to the tyrosine kinase domain of EphA2. We propose that EphA2/Dvl2/Axin1 forms a complex that destabilizes the β-catenin destruction complex and allows β-catenin to translocate to the nucleus and initiate the transcription of c-MYC, the primary Wnt signaling target gene. Intriguingly, c-MYC could bind directly to the EphA2 and Wnt1 promoter to enhance their transcription. The entire process formed an EphA2-mediated feed-forward loop. A small molecular inhibitor of EphA2 potently inhibited the proliferation of gastric cancer in vitro and in vivo, including gastric cancer patient-derived xenografts. Thus, our data identify EphA2 as an excellent candidate for gastric cancer therapy. Show less
📄 PDF DOI: 10.1038/s41419-018-1164-y
AXIN1
Wei-Chan Hsu, Ming-Yu Chen, Shu-Ching Hsu +10 more · 2018 · Proceedings of the National Academy of Sciences of the United States of America · National Academy of Sciences · added 2026-04-24
Activated T cells undergo metabolic reprogramming and effector-cell differentiation but the factors involved are unclear. Utilizing mice lacking DUSP6 (DUSP6
no PDF DOI: 10.1073/pnas.1800076115
DUSP6
Brandon Podyma, Hui Sun, Eric A Wilson +5 more · 2018 · The Journal of biological chemistry · American Society for Biochemistry and Molecular Biology · added 2026-04-24
Central melanocortin 4 receptors (MC4Rs) stimulate energy expenditure and inhibit food intake. MC4Rs activate the G protein G
no PDF DOI: 10.1074/jbc.RA118.003450
MC4R
Jun Jiang, Shulin Tang, Jianhong Xia +5 more · 2018 · Oncogene · Nature · added 2026-04-24
Wnt/β-catenin signaling activity is maintained in homeostasis by an expanding list of molecular determinants. However, the molecular components and the regulatory mechanisms involved in its fine-tunin Show more
Wnt/β-catenin signaling activity is maintained in homeostasis by an expanding list of molecular determinants. However, the molecular components and the regulatory mechanisms involved in its fine-tuning remain to be determined. Here, we identified C9orf140, a tumor-specific protein, as a novel Axin1-interacting protein by tandem-affinity purification and mass spectrometry. We further showed that C9orf140 is a negative regulator of Wnt/β-catenin signaling in cultured cells as well as in zebrafish embryos. It functions upstream of β-catenin, outcompetes PP2A for binding to Axin1, influences the balance between phosphorylation and de-phosphorylation of β-catenin, and ultimately compromises Wnt3A-induced β-catenin accumulation. Interestingly, Wnt-induced C9orf140 expression via β-catenin. We propose that C9orf140 mediates a negative feedback loop of Wnt/β-catenin signaling by interacting with Axin1. Our results advance the current understanding of the exquisite control of Wnt/β-catenin signaling cascade, and provide evidence of the new role of C9orf140. Show less
📄 PDF DOI: 10.1038/s41388-018-0166-7
AXIN1
Di Wu, Xiang Tang, Li-Hua Gu +7 more · 2018 · CNS neuroscience & therapeutics · Blackwell Publishing · added 2026-04-24
Multiple evidence has indicated that myelin injury is common in Alzheimer's disease (AD). However, whether myelin injury is an early event in AD and the relationship between it and cognitive function Show more
Multiple evidence has indicated that myelin injury is common in Alzheimer's disease (AD). However, whether myelin injury is an early event in AD and the relationship between it and cognitive function is still elusive. Spatial memory of 5XFAD mice was determined by Morris water maze at 1 and 3 months old. Meanwhile, the deposition of Aβ, the expression of myelin basic protein (MBP), LINGO-1, NgR, and myelin ultrastructure in many memory-associated brain regions were detected in one-month-old and three-month-old mice (before and after LINGO-1 antibody administration) using immunostaining, Western blot (WB), and transmission electron microscopy (TEM), respectively. No abnormal Aβ deposition was found in one-month-old 5XFAD mice. However, spatial memory deficits were proved in accordance with an obvious demyelination in memory-associated brain regions in one-month-old mice and both deteriorated with age. Administration of LINGO-1 antibody could obviously restore the myelin impairments in CA1 and DG region and partially ameliorate spatial memory deficits. Our results demonstrated that myelin injury was an early event in 5XFAD mice even prior to emergence of deposition of Aβ. Intervention with the LINGO-1 antibody could attenuate impaired spatial memory deficits by remyelination, which suggested that myelin injury was involved in spatial memory deficits and remyelination may be a potential therapeutic strategy in early stage of AD or mild cognitive impairments. Show less
no PDF DOI: 10.1111/cns.12809
LINGO1
Lifang Hu, Peihong Su, Chong Yin +10 more · 2018 · Journal of cellular physiology · Wiley · added 2026-04-24
Osteoblast differentiation is a multistep process delicately regulated by many factors, including cytoskeletal dynamics and signaling pathways. Microtubule actin crosslinking factor 1 (MACF1), a key c Show more
Osteoblast differentiation is a multistep process delicately regulated by many factors, including cytoskeletal dynamics and signaling pathways. Microtubule actin crosslinking factor 1 (MACF1), a key cytoskeletal linker, has been shown to play key roles in signal transduction and in diverse cellular processes; however, its role in regulating osteoblast differentiation is still needed to be elucidated. To further uncover the functions and mechanisms of action of MACF1 in osteoblast differentiation, we examined effects of MACF1 knockdown (MACF1-KD) in MC3T3-E1 osteoblastic cells on their osteoblast differentiation and associated molecular mechanisms. The results showed that knockdown of MACF1 significantly suppressed mineralization of MC3T3-E1 cells, down-regulated the expression of key osteogenic genes alkaline phosphatase (ALP), runt-related transcription factor 2 (Runx2) and type I collagen α1 (Col Iα1). Knockdown of MACF1 dramatically reduced the nuclear translocation of β-catenin, decreased the transcriptional activation of T cell factor 1 (TCF1), and down-regulated the expression of TCF1, lymphoid enhancer-binding factor 1 (LEF1), and Runx2, a target gene of β-catenin/TCF1. In addition, MACF1-KD increased the active level of glycogen synthase kinase-3β (GSK-3β), which is a key regulator for β-catenin signal transduction. Moreover, the reduction of nuclear β-catenin amount and decreased expression of TCF1 and Runx2 were significantly reversed in MACF1-KD cells when treated with lithium chloride, an agonist for β-catenin by inhibiting GSK-3β activity. Taken together, these findings suggest that knockdown of MACF1 in osteoblastic cells inhibits osteoblast differentiation through suppressing the β-catenin/TCF1-Runx2 axis. Thus, a novel role of MACF1 in and a new mechanistic insight of osteoblast differentiation are uncovered. Show less
no PDF DOI: 10.1002/jcp.26059
MACF1
Ming-Zhen Yuan, Ruo-An Han, Chen-Xi Zhang +1 more · 2018 · Journal of ophthalmology · added 2026-04-24
To assess the association of genes in the high-density lipoprotein metabolic pathway (HDLMP) with polypoidal choroidal vasculopathy (PCV) and the genetic difference in the HDLMP between PCV and age-re Show more
To assess the association of genes in the high-density lipoprotein metabolic pathway (HDLMP) with polypoidal choroidal vasculopathy (PCV) and the genetic difference in the HDLMP between PCV and age-related macular degeneration (AMD). We performed a literature search in EMBASE, PubMed, and Web of Science for genetic studies on 7 single nucleotide polymorphisms (SNPs) from 5 genes in the HDLMP including cholesteryl ester transfer protein (CETP), hepatic lipase (LIPC), lipoprotein lipase (LPL), ATP-binding cassette transporter A1 (ABCA1), and ATP-binding cassette transporter G1 (ABCG1) in PCV. All studies were published before September 30, 2017, without language restriction. Pooled odds ratios (ORs) and 95% confidence intervals (CIs) of each polymorphism were estimated. We also compared the association profiles between PCV and AMD and performed a sensitivity analysis. Our result is based on 43 articles. After excluding duplicates and articles without complete information, 7 studies were applicable to meta-analysis. 7 polymorphisms were meta-analyzed: CETP rs2303790/rs3764261, LIPC rs10468017/rs493258, LPL rs12678919, ABCA1 rs1883025, and ABCG1 rs57137919. We found that in Asian population, CETP rs3764261 (T allele; OR = 1.46; 95% CI: 1.28-1.665, Our study revealed 7 polymorphisms in 5 genes. Among them, CETP (rs3764261/rs2303790) and ABCG1 (rs57137919) were the major susceptibility genes for PCV in Asian population and ABCG1 (rs57137919) showed allelic diversity between PCV and AMD. Since the size for PCV and AMD was small, we need to study these genes genotyping in larger samples. Show less
📄 PDF DOI: 10.1155/2018/9538671
CETP
Olav B Smeland, Yunpeng Wang, Oleksandr Frei +10 more · 2018 · Schizophrenia bulletin · Oxford University Press · added 2026-04-24
Schizophrenia (SCZ) is associated with differences in subcortical brain volumes and intracranial volume (ICV). However, little is known about the underlying etiology of these brain alterations. Here, Show more
Schizophrenia (SCZ) is associated with differences in subcortical brain volumes and intracranial volume (ICV). However, little is known about the underlying etiology of these brain alterations. Here, we explored whether brain structure volumes and SCZ share genetic risk factors. Using conditional false discovery rate (FDR) analysis, we integrated genome-wide association study (GWAS) data on SCZ (n = 82315) and GWAS data on 7 subcortical brain volumes and ICV (n = 11840). By conditioning the FDR on overlapping associations, this statistical approach increases power to discover genetic loci. To assess the credibility of our approach, we studied the identified loci in larger GWAS samples on ICV (n = 26577) and hippocampal volume (n = 26814). We observed polygenic overlap between SCZ and volumes of hippocampus, putamen, and ICV. Based on conjunctional FDR < 0.05, we identified 2 loci shared between SCZ and ICV implicating genes FOXO3 (rs10457180) and ITIH4 (rs4687658), 2 loci shared between SCZ and hippocampal volume implicating SLC4A10 (rs4664442) and SPATS2L (rs1653290), and 2 loci shared between SCZ and volume of putamen implicating DCC (rs4632195) and DLG2 (rs11233632). The loci shared between SCZ and hippocampal volume or ICV had not reached significance in the primary GWAS on brain phenotypes. Proving our point of increased power, 2 loci did reach genome-wide significance with ICV (rs10457180) and hippocampal volume (rs4664442) in the larger GWAS. Three of the 6 identified loci are novel for SCZ. Altogether, the findings provide new insights into the relationship between SCZ and brain structure volumes, suggesting that their genetic architectures are not independent. Show less
no PDF DOI: 10.1093/schbul/sbx148
DLG2
Fan Wang, Isabel Z Wang, Stephen Ellis +6 more · 2018 · Annals of human genetics · Blackwell Publishing · added 2026-04-24
Apolipoprotein A5 (APOA5) regulates the metabolisms of triglyceride and HDL. APOA5 variants have been linked to coronary artery disease (CAD), but their causal roles are not well studied yet. This stu Show more
Apolipoprotein A5 (APOA5) regulates the metabolisms of triglyceride and HDL. APOA5 variants have been linked to coronary artery disease (CAD), but their causal roles are not well studied yet. This study aims to identify the causal effects of APOA5 variants on premature CAD. Sequencing analysis of APOA5 in 128 premature, familiar CAD patients from GeneQuest identified 11 genomic variants, including p.S19W (rs3135506). SKAT analysis showed that all sequenced variants, in aggregate, significantly increased the risk of premature CAD (P-skat = 0.037). Individually, the p.S19W variant was significantly associated with risk of premature CAD (OR = 2.30, P = 0.008) in an independent set of 342 premature CAD patients and 537 controls after adjusting for covariates of sex, age, hypertension, body mass index, triglycerides (TGs), and total, LDL-, and HDL-cholesterol levels. Meanwhile, p.S19W significantly correlated with HDL-C levels (P = 0.048) and TG levels (P = 0.025). Mediation analysis yielded a mediation effect of p.S19W on risk of premature CAD through HDL-C (OR = 0.98, P = 0.040) and TG (OR = 0.98, P = 0.042), suggesting a causal relationship between p.S19W and premature CAD partially through its effects on HDL-C and TG levels. These results suggest that APOA5 variation regulates TG and HDL levels, thus displaying a causal role in the development of CAD. Show less
📄 PDF DOI: 10.1111/ahg.12273
APOA5
Zhenzhen Sun, Yujie Xie, Yintong Chen +4 more · 2018 · Molecular neurobiology · Springer · added 2026-04-24
γ-Secretase has been a therapeutical target for its key role in cleaving APP to generate β-amyloid (Aβ), the primary constituents of senile plaques and a hallmark of Alzheimer's disease (AD) pathology Show more
γ-Secretase has been a therapeutical target for its key role in cleaving APP to generate β-amyloid (Aβ), the primary constituents of senile plaques and a hallmark of Alzheimer's disease (AD) pathology. Recently, γ-secretase-associating proteins showed promising role in specifically modulating APP processing while sparing Notch signaling; however, the underlying mechanism is still unclear. A co-immunoprecipitation (Co-IP) coupled with mass spectrometry proteomic assay for Presenilin1 (PS1, the catalytic subunit of γ-secretase) was firstly conducted to find more γ-secretase-associating proteins. Gene ontology analysis of these results identified Rab21 as a potential PS1 interacting protein, and the interaction between them was validated by reciprocal Co-IP and immunofluorescence assay. Then, molecular and biochemical methods were used to investigate the effect of Rab21 on APP processing. Results showed that overexpression of Rab21 enhanced Aβ generation, while silencing of Rab21 reduced the accumulation of Aβ, which resulted due to change in γ-secretase activity rather than α- or β-secretase. Finally, we demonstrated that Rab21 had no effect on γ-secretase complex synthesis or metabolism but enhanced PS1 endocytosis and translocation to late endosome/lysosome. In conclusion, we identified a novel γ-secretase-associating protein Rab21 and illustrate that Rab21 promotes γ-secretase internalization and translocation to late endosome/lysosome. Moreover, silencing of Rab21 decreases the γ-secretase activity in APP processing thus production of Aβ. All these results open new gateways towards the understanding of γ-secretase-associating proteins in APP processing and make inhibition of Rab21 a promising strategy for AD therapy. Show less
no PDF DOI: 10.1007/s12035-017-0606-3
RAB21
Kayla Thompson, Jonathan Chen, Qianyi Luo +3 more · 2018 · PloS one · PLOS · added 2026-04-24
Diabetic retinopathy (DR) is a major cause of adult blindness. Retinal Müller cells maintain water homeostasis and potassium concentration via inwardly rectifying Kir4.1 channels. Accumulation of adva Show more
Diabetic retinopathy (DR) is a major cause of adult blindness. Retinal Müller cells maintain water homeostasis and potassium concentration via inwardly rectifying Kir4.1 channels. Accumulation of advanced glycation end products (AGEs) is a major pathologic event in DR. While diabetes leads to a decrease in the Kir4.1 channels, it remains unknown whether AGEs-linked to the basement membrane (BM) affect normal Kir4.1 channels. For this study, we hypothesized that AGE-modification of laminin is detrimental to Kir4.1 channels, therefore, disrupting Müller cell function. The AGE-modified laminin-coated substrates were prepared by incubating Petri-dishes with laminin and methylglyoxal for seven days. The rat Müller cells (rMC-1) were propagated on AGE-modified laminin, and Kir4.1 expression and function were evaluated. Quantification of AGEs using ELISA revealed a dose-dependent increase in methylglyoxal-hydro-imidazolone adducts. The rMC-1 propagated on AGE-modified laminin demonstrated a decrease in Kir4.1 levels in immunofluorescence and western blot studies and a decrease in the Kir4.1 channel function. Kir4.1 decrease on AGE-modified laminin resulted in a disorganization of an actin cytoskeleton and disruption of α-dystroglycan-syntrophin-dystrophin complexes. Our studies suggest that AGE-modification of laminin is detrimental to Kir4.1 channels. By studying the role of AGEs in Kir4.1 channels we have identified a novel mechanism of Müller cell dysfunction and its subsequent involvement in DR. Show less
no PDF DOI: 10.1371/journal.pone.0193280
RMC1
Dawei Liu, Xiaoxing Kou, Chider Chen +8 more · 2018 · Cell research · Nature · added 2026-04-24
In the human body, 50-70 billion cells die every day, resulting in the generation of a large number of apoptotic bodies. However, the detailed biological role of apoptotic bodies in regulating tissue Show more
In the human body, 50-70 billion cells die every day, resulting in the generation of a large number of apoptotic bodies. However, the detailed biological role of apoptotic bodies in regulating tissue homeostasis remains unclear. In this study, we used Fas-deficient MRL/lpr and Caspase 3 Show less
no PDF DOI: 10.1038/s41422-018-0070-2
AXIN1
Jia Wang, Jianhua Gong, Li Li +7 more · 2018 · Autism research : official journal of the International Society for Autism Research · Wiley · added 2026-04-24
Increasing evidence suggests that abnormal synaptic function leads to neuronal developmental disorders and is an important component of the etiology of autism spectrum disorder (ASD). Neurexins are pr Show more
Increasing evidence suggests that abnormal synaptic function leads to neuronal developmental disorders and is an important component of the etiology of autism spectrum disorder (ASD). Neurexins are presynaptic cell-adhesion molecules that affect the function of synapses and mediate the conduction of nerve signals. Thus, neurexins are attractive candidate genes for autism. Since gene families have greater power to reveal genetic association than single genes, we designed this case-control study to investigate six genetic variants in three neurexin genes (NRXN1, NRXN2, and NRXN3) in a Chinese population including 529 ASD patients and 1,923 healthy controls. We found that two SNPs were significantly associated with ASD after false discovery rate (FDR) adjustment for multiple comparisons. The NRXN2 rs12273892 polymorphism T allele and AT genotype were significantly associated with increased risk of ASD (respectively: OR = 1.328, 95% CI = 1.133-1.557, P < 0.001; OR = 1.528; 95% CI = 1.249-1.868, P < 0.001). The dominant model showed the same association (OR = 1.495, 95% CI = 1.231-1.816, P < 0.001). The NRXN3 rs12879016 polymorphism played a significant role in ASD susceptibility under the dominant model (OR = 0.747, 95% CI= 0.615-0.908, P = 0.023), with the same trend detected for the G allele and GT genotype (respectively: OR = 0.811, 95% CI = 0.699-0.941, P = 0.036; OR = 0.755, 95% CI = 0.615-0.928, P = 0.035). In conclusion, this study supports the importance of two genetic variants in the neurexin gene family in ASD susceptibility in China. Autism Res 2018, 11: 37-43. © 2017 International Society for Autism Research, Wiley Periodicals, Inc. Autism spectrum disorder (ASD) is a neurodevelopmental disorder that is highly heritable, and studies have found a number of candidate genes that might contribute to ASD. Neurexins are presynaptic cell-adhesion molecules that affect the function of synapses and mediate the conduction of nerve signals, and they play an important role in normal brain development and become candidate genes for autism. The purpose of our study is to explore the association between variants of the neurexins gene family and ASD in a Chinese population through a case-control study. Show less
no PDF DOI: 10.1002/aur.1881
NRXN3
Mengshi Zhang, Youwei Chen, Hanqian Xu +7 more · 2018 · Developmental cell · Elsevier · added 2026-04-24
Melanocortin 4 receptor (Mc4r) plays a crucial role in the central control of energy homeostasis, but its role in peripheral organs has not been fully explored. We have investigated the roles of hypot Show more
Melanocortin 4 receptor (Mc4r) plays a crucial role in the central control of energy homeostasis, but its role in peripheral organs has not been fully explored. We have investigated the roles of hypothalamus-mediated energy metabolism during Xenopus limb regeneration. We report that hypothalamus injury inhibits Xenopus tadpole limb regeneration. By loss-of-function and gain-of-function studies, we show that Mc4r signaling is required for limb regeneration in regeneration-competent tadpoles and stimulates limb regeneration in later-stage regeneration-defective tadpoles. It regulates limb regeneration through modulating energy homeostasis and ROS production. Even more interestingly, our results demonstrate that Mc4r signaling is regulated by innervation and α-MSH substitutes for the effect of nerves in limb regeneration. Mc4r signaling is also required for mouse digit regeneration. Thus, our findings link vertebrate limb regeneration with Mc4r-mediated energy homeostasis and provide a new avenue for understanding Mc4r signaling in the peripheral organs. Show less
📄 PDF DOI: 10.1016/j.devcel.2018.07.021
MC4R
Jianhua Sun, Lizhi Sun, Weijie Chen +3 more · 2018 · Molecular medicine reports · added 2026-04-24
Hypothyroidism is a disease with a genetic component. The present study aimed to identify the potential causative gene mutation in a family with hypothyroidism and to investigate its potential patholo Show more
Hypothyroidism is a disease with a genetic component. The present study aimed to identify the potential causative gene mutation in a family with hypothyroidism and to investigate its potential pathology. DNA was extracted from the affected individual and his parents, maternal aunt and maternal grandmother. Whole exome sequencing was used to examine their exomes. The potential causative genes that may have an autosomal dominant mode of inheritance were selected after variant calling and filtering. Bioinformatics analysis was utilized to predict the deleteriousness of the identified variants, and multiple sequence alignment and conserved protein domain analyses were performed using online software. Finally, Sanger sequencing was used to validate the identified variants. In the present study, a total of 50 variants were screened based on the autosomal dominant mode of inheritance. Two variants, the fatty acid synthase (FASN) and apolipoprotein B receptor (APOBR) genes, were further analyzed, as they were highly associated with hypothyroidism. Genotyping results revealed that two mutations, c.G7192T (p.A2398S) in the FASN gene and c.C1883G (p.T628R) in the APOBR gene, were fully co‑segregated with established hypothyroidism phenotypes in the family. These mutations were located in the conserved α/β‑hydrolase fold and Na+/Ca2+ exchanger superfamily domain of FASN and APOBR, respectively. In conclusion, the present study demonstrated that the FASN c.G7192T and APOBR c.C1883G mutations may be the potential causative variants in this Chinese hypothyroidism pedigree. Show less
📄 PDF DOI: 10.3892/mmr.2018.9499
APOBR
Yi-Wen Li, Chung-Hsing Wang, Chao-Jung Chen +5 more · 2018 · Archives of toxicology · Springer · added 2026-04-24
To characterize the association between epilepsy, use of antiepileptic drugs (AEDs), and the risk of hyperlipidemia, we conducted a nationwide population-based cohort study with data obtained from the Show more
To characterize the association between epilepsy, use of antiepileptic drugs (AEDs), and the risk of hyperlipidemia, we conducted a nationwide population-based cohort study with data obtained from the National Health Insurance Research Database of Taiwan. The effects of AEDs on lipogenic gene expression were also examined in vitro. We identified 3617 cases involving patients, whose epilepsy was newly diagnosed between 2000 and 2011, and selected a comparison cohort comprising 14,468 patients without epilepsy. The Cox proportional hazards model was used to evaluate the association between epilepsy, AED use, and hyperlipidemia. The incidence rate of hyperlipidemia was higher in the epilepsy cohort than in the comparison cohort, with an adjusted hazard ratio (aHR) of 1.21 [95% confidence interval (CI): 1.06-1.38] after adjusting for comorbidities and medications. Epilepsy patients not taking AEDs had a higher risk of hyperlipidemia (aHR 1.65; 95% CI 1.35-2.03). Among AEDs, only valproate treatment showed a higher risk of hyperlipidemia (aHR 1.53; 95% CI 1.01-2.33), although the dose-dependent effect did not reach statistical significance. In vitro studies with two hepatic cell lines showed that valproate may exert its effects by activating the liver X receptor alpha (LXRα) signaling pathway, inducing the expression of lipogenesis-related genes and increasing cellular lipid contents. In silico calculations concluded that valproate can bind stably with the ligand-binding domain of LXRα. Thus, valproate-induced hepatic lipogenic gene expression may occur through LXRα activation. Predicting the 'off-target' effects of valproate may prove valuable in developing antiepileptic agents with fewer adverse reactions. Monitoring blood lipid levels throughout the course of treatment is recommended. Show less
no PDF DOI: 10.1007/s00204-018-2263-3
NR1H3
Cheng Chen, Maimaiti Aihemaiti, Xin Zhang +4 more · 2018 · American journal of cancer research · added 2026-04-24
Colorectal cancer (CRC) is one of the most common malignant gastrointestinal cancers. Metastasis is a major leading of death in patients with CRC and many patients have metastatic disease at diagnosis Show more
Colorectal cancer (CRC) is one of the most common malignant gastrointestinal cancers. Metastasis is a major leading of death in patients with CRC and many patients have metastatic disease at diagnosis. However, the underlying molecular mechanisms are still elusive. Here, we showed that JMJD1C was overexpressed in colon cancer tissues compared to normal samples and was positively associated with metastasis and poor prognosis. Silencing JMJD1C strongly inhibits CRC migration and invasion both in vitro and in vivo. Further, we found that knockdown of JMJD1C decreased the protein and mRNA levels of ATF2, mechanistically, and JMJD1C regulated the expression of ATF2 by modulating the H3K9me2 but not H3K9me1 activity. In addition, we further performed some "rescues experiments". We found that overexpression of ATF2 could reverse the abrogated migration and invasion ability by knockdown of JMJD1C in CRC. Our results demonstrated that an increase of JMJD1C was observed in colon cancer and knockdown of JMJD1C regulated CRC metastasis by inactivation of the ATF2 pathway. This novel JMJD1C/ATF2 signaling pathway may be a promising therapeutic target for CRC metastasis. Show less
no PDF
JMJD1C
C M Mak, S Pl Chen, N S Mok +13 more · 2018 · Hong Kong medical journal = Xianggang yi xue za zhi · added 2026-04-24
Hereditary channelopathies and cardiomyopathies are potentially lethal and are clinically and genetically heterogeneous, involving at least 90 genes. Genetic testing can provide an accurate diagnosis, Show more
Hereditary channelopathies and cardiomyopathies are potentially lethal and are clinically and genetically heterogeneous, involving at least 90 genes. Genetic testing can provide an accurate diagnosis, guide treatment, and enable cascade screening. The genetic basis among the Hong Kong Chinese population is largely unknown. We aimed to report on 28 unrelated patients with positive genetic findings detected from January 2006 to December 2015. Sanger sequencing was performed for 28 unrelated patients with a clinical diagnosis of channelopathies or cardiomyopathies, testing for the following genes: There were 17 males and 11 females; their mean age at diagnosis was 39 years (range, 1-80 years). The major clinical presentations included syncope, palpitations, and abnormal electrocardiography findings. A family history was present in 13 (46%) patients. There were 26 different heterozygous mutations detected, of which six were novel-two in We have characterised the genetic heterogeneity in channelopathies and cardiomyopathies among Hong Kong Chinese patients in a 10-year case series. Correct interpretation of genetic findings is difficult and requires expertise and experience. Caution regarding issues of non-penetrance, variable expressivity, phenotype-genotype correlation, susceptibility risk, and digenic inheritance is necessary for genetic counselling and cascade screening. Show less
no PDF DOI: 10.12809/hkmj176870
MYBPC3
Chong Yin, Yan Zhang, Lifang Hu +11 more · 2018 · Journal of cellular physiology · Wiley · added 2026-04-24
Mechanical unloading was considered a major threat to bone homeostasis, and has been shown to decrease osteoblast proliferation although the underlying mechanism is unclear. Microtubule actin crosslin Show more
Mechanical unloading was considered a major threat to bone homeostasis, and has been shown to decrease osteoblast proliferation although the underlying mechanism is unclear. Microtubule actin crosslinking factor 1 (MACF1) is a cytoskeletal protein that regulates cellular processes and Wnt/β-catenin pathway, an essential signaling pathway for osteoblasts. However, the relationship between MACF1 expression and mechanical unloading, and the function and the associated mechanisms of MACF1 in regulating osteoblast proliferation are unclear. This study investigated effects of mechanical unloading on MACF1 expression levels in cultured MC3T3-E1 osteoblastic cells and in femurs of mice with hind limb unloading; and it also examined the role and potential action mechanisms of MACF1 in osteoblast proliferation in MACF1-knockdown, overexpressed or control MC3T3-E1 cells treated with or without the mechanical unloading condition. Results showed that the mechanical unloading condition inhibited osteoblast proliferation and MACF1 expression in MC3T3-E1 osteoblastic cells and mouse femurs. MACF1 knockdown decreased osteoblast proliferation, while MACF1 overexpression increased it. The inhibitory effect of mechanical unloading on osteoblast proliferation also changed with MACF1 expression levels. Furthermore, MACF1 was found to enhance β-catenin expression and activity, and mechanical unloading decreased β-catenin expression through MACF1. Moreover, β-catenin was found an important regulator of osteoblast proliferation, as its preservation by treatment with its agonist lithium attenuated the inhibitory effects of MACF1-knockdown or mechanical unloading on osteoblast proliferation. Taken together, mechanical unloading decreases MACF1 expression, and MACF1 up-regulates osteoblast proliferation through enhancing β-catenin signaling. This study has thus provided a mechanism for mechanical unloading-induced inhibited osteoblast proliferation. Show less
no PDF DOI: 10.1002/jcp.26374
MACF1
Fenghua Guo, Wenting Hong, Mingjie Yang +4 more · 2018 · Biochemical and biophysical research communications · Elsevier · added 2026-04-24
Gastric cancer (GC) is one of the most common cancers and is the second-leading cause of cancer-associated morbidity worldwide. Oxysterols are oxidized derivatives of cholesterol that may be important Show more
Gastric cancer (GC) is one of the most common cancers and is the second-leading cause of cancer-associated morbidity worldwide. Oxysterols are oxidized derivatives of cholesterol that may be important in many biological processes, but the levels and roles of oxysterols in gastric tumours remain to be elucidated. The levels of cholesterol, oxysterols and sulfated oxysterols in human gastric tumour tissues, adjacent normal mucosal tissues, cancerous gastric juice and gastric juice obtained from healthy subjects were detected by LC-MS. It was found that the levels of 24(R/S),25-EC and 27HC in human gastric tumour tissues and cancerous gastric juice were significantly increased compared with those of adjacent normal mucosal tissues and gastric juice from healthy subjects. Compared with normal gastric mucosal tissue, the levels of sulfated 25-hydroxycholesterol (25HC3S) and the ratio of 25HC3S/25HC were decreased in human gastric tumour tissues, which might be related to the dramatically decreased SULT2A1 expression in gastric tumour tissue. Both 24(R/S),25-EC and 27HC suppressed gastric cancer proliferation, which was not altered by LXRα-siRNA treatment. The suppression of cell proliferation induced by 27HC was attenuated by LXRβ-siRNA, but the suppression of cell proliferation induced by 24(R/S),25-EC was intensified by LXRβ-siRNA. Both 24(R/S),25-EC and 27HC dramatically inhibited HGC-27 cell migration, which was attenuated by the co-transfection of cells with LXRα-siRNA and LXRβ-siRNA, but not LXRα-siRNA or LXRβ-siRNA alone. In conclusion, the accumulated 24(R/S),25-EC and 27HC in human gastric tumour tissues might play important roles in gastric cancer development. Show less
no PDF DOI: 10.1016/j.bbrc.2018.09.058
NR1H3