👤 Ruotai Li

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Also published as: A Li, Ai-Jun Li, Ai-Qin Li, Ailing Li, Aimin Li, Aixin Li, Alexander H Li, Alexander Li, Amy Li, An-Qi Li, AnHai Li, Anan Li, Andrew C Li, Ang Li, Anna Fen-Yau Li, Annie Li, Anqi Li, Anyao Li, Ao Li, Aowen Li, Aoxi Li, Audrey Li, Bai-Qiang Li, Baichuan Li, Baiqiang Li, Baixing Li, Baizhou Li, Bang-Yan Li, Bao Li, Bao-Shan Li, Baoguang Li, Baoguo Li, Baohong Li, Baohua Li, Baolin Li, Baoqi Li, Baoqing Li, Baosheng Li, Baoting Li, Bei Li, Bei-Bei Li, Beibei Li, Beixu Li, Ben Li, Ben-Shang Li, Benyi Li, Biao Li, Bichun Li, Bin Li, Bin-Kui Li, Binbin Li, Bing Li, Bing-Heng Li, Bing-Hui Li, Bing-Mei Li, Bingbing Li, Binghu Li, Binghua Li, Bingjie Li, Bingjue Li, Bingkun Li, Binglan Li, Bingong Li, Bingshan Li, Bingsheng Li, Bingsong Li, Bingxin Li, Binjun Li, Binkui Li, Binru Li, Binxing Li, Biyu Li, Bizhi Li, Bo Li, BoWen Li, Bohao Li, Bohua Li, Bolun Li, Boru Li, Botao Li, Boxuan Li, Boya Li, Boyang Li, Bugao Li, C H Li, C Li, C X Li, C Y Li, Caesar Z Li, Cai Li, Cai-Hong Li, Caihong Li, Caili Li, Caixia Li, Caiyu Li, Caiyun Li, Can Li, Cang Li, Caolong Li, Chang Li, Chang-Da Li, Chang-Ping Li, Chang-Sheng Li, Chang-Yan Li, Chang-hai Li, Changcheng Li, Changgui Li, Changhong Li, Changhui Li, Changjiang Li, Changkai Li, Changqing Li, Changwei Li, Changxian Li, Changyan Li, Changyu Li, Changzheng Li, Chanjuan Li, Chanyuan Li, Chao Bo Li, Chao Li, Chaochen Li, Chaojie Li, Chaonan Li, Chaoqian Li, Chaowei Li, Chaoying Li, Chen Li, Chen-Chen Li, Chen-Lu Li, Chen-Xi Li, Chenfeng Li, Cheng Li, Cheng-Lin Li, Cheng-Tian Li, Cheng-Wei Li, Chengbin Li, Chengcheng Li, Chenghao Li, Chenghong Li, Chengjian Li, Chengjun Li, Chenglan Li, Chenglong Li, Chengnan Li, Chengping Li, Chengqian Li, Chengquan Li, Chengsi Li, Chenguang Li, Chengwen Li, Chengxin Li, Chengyun Li, Chenhao Li, Chenjie Li, Chenli Li, Chenlin Li, Chenlong Li, Chenlu Li, Chenmeng Li, Chenrui Li, Chensheng Li, Chenwen Li, Chenxi Li, Chenxiao Li, Chenxin Li, Chenxuan Li, Chenyang Li, Chenyao Li, Chenyu Li, Cheung Li, Chi-Ming Li, Chi-Yuan Li, Chia Li, Chia-Yang Li, Chien-Feng Li, Chien-Hsiu Li, Chien-Te Li, Chih-Chi Li, Chitao Li, Chiyang Li, Chong Li, Chongyang Li, Chongyi Li, Chris Li, Chu-Qiao Li, Chuan F Li, Chuan Li, Chuan-Hai Li, Chuan-Yun Li, Chuanbao Li, Chuanfang Li, Chuang Li, Chuangpeng Li, Chuanning Li, Chuanyin Li, Chumei Li, Chun Li, Chun-Bo Li, Chun-Lai Li, Chun-Mei Li, Chun-Quan Li, Chun-Xiao Li, Chun-Xu Li, Chung-Hao Li, Chung-I Li, Chunhong Li, Chunhui Li, Chunjie Li, Chunjun Li, Chunlan Li, Chunlian Li, Chunliang Li, Chunlin Li, Chunmei Li, Chunmiao Li, Chunqing Li, Chunqiong Li, Chunshan Li, Chunsheng Li, Chunting Li, Chunxia Li, Chunxiao Li, Chunxing Li, Chunxue Li, Chunya Li, Chunyan Li, Chunyi Li, Chunying Li, Chunyu Li, Chunzhu Li, Chuzhong Li, Cien Li, Cong Li, Congcong Li, Congfa Li, Conghui Li, Congjiao Li, Conglin Li, Congxin Li, Congye Li, Cui Li, Cui-lan Li, Cuicui Li, Cuiguang Li, Cuilan Li, Cuiling Li, Cun Li, Cunxi Li, Cyril Li, D C Li, Da Li, Da-Hong Li, Da-Jin Li, Da-Lei Li, Da-wei Li, DaZhuang Li, Dacheng Li, Dai Li, Daiyue Li, Dalei Li, Dali Li, Dalin Li, Dan C Li, Dan Li, Dan-Dan Li, Dan-Ni Li, Dandan Li, Daniel Tian Li, Danjie Li, Danni Li, Danxi Li, Danyang Li, Daoyuan Li, Dapei Li, Dawei Li, Dayong Li, Dazhi Li, De-Jun Li, De-Tao Li, Dechao Li, Defa Li, Defeng Li, Defu Li, Dehai Li, Deheng Li, Dehua Li, Dejun Li, Demin Li, Deming Li, Dengfeng Li, Dengke Li, Dengxiong Li, Deqiang Li, Desen Li, Desheng Li, Dexiong Li, Deyu Li, Dezhi Li, Di Li, Di-Jie Li, Dianjie Li, Dijie Li, Ding Li, Ding Yang Li, Ding-Biao Li, Ding-Jian Li, Dingchen Li, Dingshan Li, Diyan Li, Dong Li, Dong Sheng Li, Dong-Jie Li, Dong-Ling Li, Dong-Run Li, Dong-Yun Li, Dong-fei Li, Dongbiao Li, Dongdong Li, Dongfang Li, Dongfeng Li, Donghe Li, Donghua Li, Dongliang Li, Dongmei Li, Dongmin Li, Dongnan Li, Dongtao Li, Dongyang Li, Dongye Li, Duan Li, Duanbin Li, Duanxiang Li, Dujuan Li, Duo Li, Duoyun Li, Ellen Li, En Li, En-Min Li, Enhao Li, Enhong Li, Enxiao Li, F Li, Fa-Hong Li, Fa-Hui Li, Fadi Li, Fan Li, Fang Li, Fangqi Li, Fangyan Li, Fangyong Li, Fangyuan Li, Fangzhou Li, Fei Li, Fei-Lin Li, Fei-feng Li, Feifei Li, Feilong Li, Fen Li, Feng Li, Feng-Feng Li, Fengfeng Li, Fengjuan Li, Fengli Li, Fengqi Li, Fengqiao Li, Fengqing Li, Fengxia Li, Fengxiang Li, Fengyi Li, Fengyuan Li, Fu-Rong Li, Fugen Li, Fuhai Li, Fujun Li, Fulun Li, Fuping Li, Fusheng Li, Fuyu Li, Fuyuan Li, G Li, G-P Li, Gaijie Li, Gaizhen Li, Gaizhi Li, Gan Li, Gang Li, Ganggang Li, Gao-Fei Li, Gaoyuan Li, Ge Li, Gen Li, Gen-Lin Li, Gerard Li, Gong-Hua Li, Gongda Li, Guanbin Li, Guandu Li, Guang Li, Guang Y Li, Guang-Li Li, Guang-Xi Li, Guangda Li, Guangdi Li, Guanghua Li, Guanghui Li, Guangjin Li, Guangli Li, Guanglu Li, Guanglve Li, Guangming Li, Guangping Li, Guangpu Li, Guangqiang Li, Guangquan Li, Guangwen Li, Guangxi Li, Guangxiao Li, Guangyan Li, Guangzhao Li, Guangzhen Li, Guannan Li, Guanqiao Li, Guanyu Li, Gui Lin Li, Gui-Bo Li, Gui-Hua Li, Gui-Rong Li, Gui-xing Li, Guigang Li, Guihua Li, Guilan Li, Guisen Li, Guixia Li, Guixin Li, Guiyang Li, Guiying Li, Guiyuan Li, Guo Li, Guo-Chun Li, Guo-Jian Li, Guo-Li Li, Guo-Ping Li, Guo-Qiang Li, Guobin Li, Guoge Li, Guohong Li, Guohua Li, Guohui Li, Guojin Li, Guojun Li, Guoli Li, Guoping Li, Guoqin Li, Guoqing Li, Guowei Li, Guoxi Li, Guoxiang Li, Guoxing Li, Guoyan Li, Guoyin Li, H J Li, H Li, H-F Li, H-H Li, H-J Li, Hai Li, Hai-Yun Li, Haibin Li, Haibo Li, Haifeng Li, Haihong Li, Haihua Li, Haijun Li, Hailong Li, Haimin Li, Haiming Li, Hainan Li, Haipeng Li, Hairong Li, Haitao Li, Haitong Li, Haixia Li, Haiyan Li, Haiyang Li, Haiying Li, Haiyu Li, Han Li, Han-Bing Li, Han-Bo Li, Han-Ni Li, Han-Ru Li, Han-Wei Li, Hanbin Li, Hanbing Li, Hanbo Li, Handong Li, Hang Li, Hangwen Li, Hanjun Li, Hankun Li, Hanlu Li, Hanmei Li, Hanqi Li, Hanqin Li, Hansen Li, Hanting Li, Hanxiao Li, Hanxue Li, Hao Li, Hao-Fei Li, Haojing Li, Haolong Li, Haomiao Li, Haoqi Li, Haoran Li, Haotong Li, Haoxian Li, Haoyu Li, Haying Li, He Li, He-Zhen Li, Hecheng Li, Hegen Li, Hehua Li, Heng Li, Heng-Zhen Li, Hengguo Li, Hengtong Li, Hengyu Li, Hening Li, Hewei Li, Hexin Li, Heying Li, Hong Li, Hong-Chun Li, Hong-Lan Li, Hong-Lian Li, Hong-Mei Li, Hong-Tao Li, Hong-Wen Li, Hong-Yan Li, Hong-Yu Li, Hong-Zheng Li, Hongbo Li, Hongchang Li, Hongde Li, Honggang Li, Hongguo Li, Honghua Li, Honghui Li, Hongjia Li, Hongjiang Li, Hongjuan Li, Honglei Li, Hongli Li, Honglian Li, Hongliang Li, Honglin Li, Hongling Li, Honglong Li, Hongmei Li, Hongmin Li, Hongming Li, Hongqin Li, Hongquan Li, Hongru Li, Hongsen Li, Hongwei Li, Hongxia Li, Hongxin Li, Hongxing Li, Hongxue Li, Hongyan Li, Hongye Li, Hongyi Li, Hongyu Li, Hongyun Li, Hongzhe K Li, Hongzheng Li, Hongzhi Li, Hsiao-Fen Li, Hsiao-Hui Li, Hsin-Hua Li, Hsin-Yun Li, Hu Li, Hua Li, Hua-Zhong Li, Huabin Li, Huafang Li, Huafu Li, Huaixing Li, Huaiyuan Li, Hualian Li, Hualing Li, Huamao Li, Huan Li, Huanan Li, Huang Li, Huangbao Li, Huangyuan Li, Huanhuan Li, Huanjun Li, Huanqing Li, Huanqiu Li, Huaping Li, Huashun Li, Huawei Li, Huayao Li, Huayin Li, Huaying Li, Hui Li, Hui-Jun Li, Hui-Long Li, Hui-Ping Li, Huibo Li, Huifang Li, Huifeng Li, Huihuang Li, Huihui Li, Huijie Li, Huijuan Li, Huijun Li, Huilan Li, Huili Li, Huiliang Li, Huilin Li, Huilong Li, Huimin Li, Huiping Li, Huiqin Li, Huiqing Li, Huiqiong Li, Huiting Li, Huixia Li, Huixue Li, Huiying Li, Huiyou Li, Huiyuan Li, Huizi Li, Hujie Li, Hulun Li, Hung Li, Hung-Yuan Li, Ivan Li, J Li, J T Li, Jason Li, Jen-Ming Li, Jenny J Li, Ji Li, Ji Xia Li, Ji-Cheng Li, Ji-Feng Li, Ji-Liang Li, Ji-Lin Li, Ji-Min Li, Jia Li, Jia Li Li, Jia-Da Li, Jia-Huan Li, Jia-Peng Li, Jia-Ru Li, Jia-Xin Li, Jiabei Li, Jiachen Li, Jiacheng Li, Jiafang Li, Jiafei Li, Jiahao Li, Jiahui Li, Jiajia Li, Jiajie Li, Jiajing Li, Jiajun Li, Jiajv Li, Jiali Li, Jialin Li, Jialing Li, Jialun Li, Jiaming Li, Jian Li, Jian'an Li, Jian-Jun Li, Jian-Mei Li, Jian-Qiang Li, Jian-Shuang Li, Jianan Li, Jianang Li, Jianbin Li, Jianbo Li, Jianchun Li, Jiandong Li, Jianfang Li, Jianfeng Li, Jiang Li, Jiangan Li, Jiangbo Li, Jiangchao Li, Jiangfeng Li, Jianglin Li, Jianglong Li, Jiangtao Li, Jiangui Li, Jianguo Li, Jiangxia Li, Jiangya Li, Jianhai Li, Jianhua Li, Jiani Li, Jianing Li, Jianliang Li, Jianlin Li, Jianmin Li, Jiannan Li, Jianping Li, Jianrong Li, Jianrui Li, Jiansheng Li, Jianshuang Li, Jianwei Li, Jianxin Li, Jianxiong Li, Jianye Li, Jianyi Li, Jianyong Li, Jianyu Li, Jianzhong Li, Jiao Li, Jiao-Jiao Li, Jiaomei Li, Jiaping Li, Jiaqi Li, Jiawei Li, Jiaxi Li, Jiaxin Li, Jiaxuan Li, Jiayan Li, Jiayang Li, Jiayi Li, Jiaying Li, Jiayu Li, Jiayuan Li, Jiazhou Li, Jicheng Li, Jie Li, Jie-Pin Li, Jie-Shou Li, Jiehan Li, Jiejia Li, Jiejie Li, Jiejing Li, Jieming Li, Jiequn Li, Jieshou Li, Jiexi Li, Jiexin Li, Jiezhen Li, Jifang Li, Jihua Li, Jin Li, Jin-Jiang Li, Jin-Liang Li, Jin-Long Li, Jin-Mei Li, Jin-Ping Li, Jin-Qiu Li, Jin-Wei Li, Jin-Xiu Li, Jinchen Li, Jinfang Li, Jinfeng Li, Jing Li, Jing-Jing Li, Jing-Ming Li, Jing-Yao Li, Jing-Yi Li, Jing-gao Li, Jingcheng Li, Jingchun Li, Jingfeng Li, Jinghao Li, Jinghui Li, Jingjing Li, Jingke Li, Jinglin Li, Jingmei Li, Jingming Li, Jingping Li, Jingqi Li, Jingshang Li, Jingshu Li, Jingtong Li, Jingui Li, Jingwen Li, Jingxia Li, Jingxiang Li, Jingxin Li, Jingya Li, Jingyi Li, Jingyong Li, Jingyu Li, Jingyun Li, Jinhua Li, Jinhui Li, Jinjie Li, Jinku Li, Jinlan Li, Jinliang Li, Jinlin Li, Jinman Li, Jinming Li, Jinping Li, Jinsong Li, Jinwei Li, Jinxia Li, Jinxin Li, Jinzhi Li, Jiong Li, Jiong-Ming Li, Jipeng Li, Jiqing Li, Jisen Li, Jisheng Li, Jiuke Li, Jiuyi Li, Jiwei Li, Jiwen Li, Jixi Li, Jixuan Li, Jiyang Li, Jiyuan Li, John Zhong Li, Jonathan Z Li, Joyce Li, Ju-Rong Li, Juan Li, Juan-Juan Li, Juanjuan Li, Juanling Li, Juanni Li, Jufang Li, Julia Li, Jun Li, Jun Z Li, Jun-Cheng Li, Jun-Jie Li, Jun-Ling Li, Jun-Ru Li, Jun-Yan Li, Jun-Ying Li, JunBo Li, Junfeng Li, Junhong Li, Junhui Li, Junjie Li, Junjun Li, Junming Li, Junping Li, Junqin Li, Junru Li, Junsheng Li, Juntong Li, Junxian Li, Junxin Li, Junxu Li, Junya Li, Junyi Li, Junying Li, Justin Li, Jutang Li, Juxue Li, K-L Li, Ka Li, Ka Wan Li, Kai Li, Kai-Wen Li, Kaibin Li, Kaibo Li, Kaifeng Li, Kailong Li, Kaimi Li, Kainan Li, Kaiwei Li, Kaixin Li, Kaiyi Li, Kaiyuan Li, Kang Li, Kangli Li, Kangyuan Li, Karen Li, Kathy H Li, Kawah Li, Ke Li, KeZhong Li, Keanning Li, Kecheng Li, Kechun Li, Keguo Li, Kejuan Li, Keke Li, Kening Li, Kenli Li, Kenneth Kai Wang Li, Keqing Li, Keshen Li, Keying Li, Keyuan Li, Kezhen Li, Kongdong Li, Kuan Li, Kui Li, Kuiliang Li, Kun Li, Kun-Peng Li, Kun-Ping Li, Kun-Xin Li, Kunlin Li, Kunlong Li, Kunlun Li, Kunpeng Li, L I Li, L K Li, L Li, L P Li, L-Y Li, Lai K Li, Laiqing Li, Lamei Li, Lan Li, Lan-Juan Li, Lan-Lan Li, Lanfang Li, Lang Li, Lanjuan Li, Lanlan Li, Lanzhou Li, Le Li, Le-Le Li, Le-Ying Li, Lei Li, Leilei Li, Leipeng Li, Letai Li, Leyao Li, Li Li, Li-Min Li, Li-Na Li, Lian Li, Lianbing Li, Liang Li, Liangdong Li, Liangji Li, Liangkui Li, Liangqian Li, Lianhong Li, Lianjian Li, Lianyong Li, Liao-Yuan Li, Lieyou Li, Liguo Li, Lihong Li, Lihua Li, Lijia Li, Lijuan Li, Lijun Li, Lili Li, Liliang Li, Liling Li, Liming Li, Lin Li, Lin-Feng Li, Linchuan Li, Linfeng Li, Ling Li, Ling-Jie Li, Ling-Ling Li, Ling-Zhi Li, Lingjiang Li, Lingjie Li, Lingjun Li, Lingling Li, Lingxi Li, Lingyan Li, Lingyi Li, Lingzhi Li, Linhong Li, Linke Li, Linlin Li, Linqi Li, Linqing Li, Linsheng Li, Linting Li, Linxin Li, Linyan Li, Linying Li, Lipeng Li, Liping Li, Liqin Li, Liqun Li, Lirong Li, Lisha Li, Litao Li, Liuzheng Li, Liwei Li, Lixi Li, Lixia Li, Lixiang Li, Liyan Li, Long Li, Long Shan Li, Long-Yan Li, Longhui Li, Longxuan Li, Longyu Li, Lu Li, Lu-Yun Li, Lucia M Li, Lucy Li, Luhan Li, Lujiao Li, Lujie Li, Lulu Li, Luquan Li, Luxuan Li, Luyao Li, Luying Li, M D Li, M Li, M V Li, M-J Li, Man Li, Man-Xiang Li, Man-Zhi Li, Mangmang Li, Manjiang Li, Manna Li, Manru Li, Manxia Li, Mao Li, Maogui Li, Maolin Li, Maoquan Li, Maosheng Li, Marilyn Li, Mei Li, Mei-Lan Li, Mei-Ya Li, Mei-Zhen Li, Meifang Li, Meifen Li, Meijia Li, Meilan Li, Meiqing Li, Meitao Li, Meiting Li, Meiyan Li, Meiying Li, Meiyue Li, Meizi Li, Melody M H Li, Meng Li, Meng-Hua Li, Meng-Jun Li, Meng-Meng Li, Meng-Miao Li, Meng-Yang Li, Meng-Yao Li, Meng-Yue Li, MengGe Li, Mengfan Li, Menghua Li, Mengjiao Li, Mengjuan Li, Mengling Li, Menglu Li, Mengmeng Li, Mengqing Li, Mengqiu Li, Mengsen Li, Mengshi Li, Mengxi Li, Mengxia Li, Mengxuan Li, Mengyang Li, Mengyao Li, Mengying Li, Mengyuan Li, Mengyun Li, Mengze Li, Mi Li, Mian Li, Miao Li, Miao X Li, Miaoxin Li, Michelle Li, Mimi Li, Min Li, Min-Dian Li, Min-Rui Li, Min-jun Li, Minerva X Li, Ming D Li, Ming Li, Ming V Li, Ming Xing Li, Ming Zhou Li, Ming-Han Li, Ming-Hao Li, Ming-Jiang Li, Ming-Kai Li, Ming-Qing Li, Ming-Wei Li, Ming-Xing Li, Ming-Yang Li, Mingdan Li, Mingfang Li, Mingfei Li, Minghao Li, Minghua Li, Minghui Li, Mingjiang Li, Mingjie Li, Mingjun Li, Mingke Li, Mingkun Li, Mingli Li, Minglong Li, Minglun Li, Mingna Li, Mingqiang Li, Mingquan Li, Mingrui Li, Mingwei Li, Mingxi Li, Mingxia Li, Mingxing Li, Mingxu Li, Mingxuan Li, Mingyang Li, Mingyao Li, Mingyue Li, Mingzhe Li, Mingzhou Li, Minhui Li, Minle Li, Minmin Li, Minqi Li, Minyue Li, Minze Li, Minzhe Li, Miyang Li, Mo Li, Mohan Li, Monica M Li, Moyi Li, Mufan Li, Mulin Jun Li, Muzi Li, N Li, Na Li, Naishi Li, Nan Li, Nan-Nan Li, Nana Li, Nanjun Li, Nanlong Li, Nanxing Li, Nanzhen Li, Ni Li, Nianfu Li, Nianyu Li, Nien Li, Nien-Chen Li, Nien-Chi Li, Ning Li, Ningyan Li, Ningyang Li, Niu Li, Nuomin Li, O Li, P H Li, P Li, Pan Li, Panlong Li, Panyuan Li, Pei Li, Pei-Lin Li, Pei-Qin Li, Pei-Shan Li, Pei-Ying Li, Pei-Zhi Li, PeiQi Li, Peibo Li, Peifen Li, Peifeng Li, Peihong Li, Peihua Li, Peilin Li, Peilong Li, Peining Li, Peipei Li, Peiqin Li, Peiran Li, Peiwu Li, Peixin Li, Peiyu Li, Peiyuan Li, Peiyun Li, Peng Li, Peng Peng Li, Peng-li Li, Pengcui Li, Penghui Li, Pengjie Li, Pengju Li, Pengsong Li, Pengyang Li, Pengyu Li, Pengyun Li, Pik Yi Li, Pilong Li, Pindong Li, Ping Li, Ping'an Li, Pinghua Li, Pingping Li, Pu Li, Pu-Yu Li, Q Li, Qi Li, Qi-Fu Li, Qi-Jing Li, Qian Li, Qian-Qian Li, Qiang Li, Qiang-Ming Li, Qiankun Li, Qianqian Li, Qiao Li, Qiao-Xin Li, Qiaolian Li, Qiaoqiao Li, Qibing Li, Qifang Li, Qihang Li, Qihua Li, Qiji Li, Qijun Li, Qilan Li, Qilong Li, Qin Li, Qiner Li, Qing Li, Qing Run Li, Qing-Chang Li, Qing-Fang Li, Qing-Min Li, Qing-Wei Li, Qingchao Li, Qingfang Li, Qingfeng Li, Qinggang Li, Qinghe Li, Qinghong Li, Qinghua Li, Qingjie Li, Qinglan Li, Qingli Li, Qinglin Li, Qingling Li, Qingqin S Li, Qingrun Li, Qingshang Li, Qingsheng Li, Qingxian Li, Qingyang Li, Qingyu Li, Qingyuan Li, Qingyun Li, Qinqin Li, Qinrui Li, Qintong Li, Qiong Li, Qionghua Li, Qipei Li, Qiqiong Li, Qiu Li, Qiufeng Li, Qiuhong Li, Qiusheng Li, Qiuxuan Li, Qiuya Li, Qiuyan Li, Qiwei Li, Qiyong Li, Qizhai Li, Quan Li, Quan-Zhong Li, Quanpeng Li, Quanshun Li, Quanzhang Li, Qun Li, R H L Li, R Li, Ran Li, Ranchang Li, Ranran Li, Ranwei Li, Ren Li, Ren-Ke Li, Rena Li, Roger Li, Ronald Li, Rong Li, Rong-Bing Li, Ronggui Li, Rongkai Li, Rongling Li, Rongqing Li, Rongsong Li, Rongxia Li, Rongyao Li, Rosa J W Li, Ru Li, Ru-Hao Li, Rui Li, Rui-Fang Li, Rui-Han Li, Rui-Jún Eveline Li, Ruibing Li, Ruidong Li, Ruifang Li, Ruihuan Li, Ruijia Li, Ruijin Li, Ruikai Li, Ruitong Li, Ruiwen Li, Ruixi Li, Ruixia Li, Ruixue Li, Ruiyang Li, Rujia Li, Rulin Li, Rumei Li, Runbing Li, Runwen Li, Runzhao Li, Runzhen Li, Runzhi Li, Ruobing Li, Ruolin Li, Ruonan Li, Ruotian Li, Ruotong Li, Ruyi Li, Ruyue Li, S A Li, S E Li, S L Li, S Li, S S Li, S-C Li, Sai Li, Saijuan Li, Sainan Li, San-Feng Li, Sanqiang Li, Senlin Li, Senmao Li, Sha Li, Sha-Sha Li, Shan Li, Shan-Shan Li, Shangjia Li, Shanglai Li, Shangming Li, Shanhang Li, Shanpeng Li, Shanshan Li, Shanyi Li, Shao-Dan Li, Shaobin Li, Shaodan Li, Shaofei Li, Shaoguang Li, Shaojian Li, Shaojing Li, Shaoliang Li, Shaomin Li, Shaoqi Li, Shaoyong Li, Shasha Li, Shawn S C Li, Shawn Shun-Cheng Li, Shen Li, Sheng Li, Sheng-Fu Li, Sheng-Jie Li, Sheng-Qing Li, Sheng-Tien Li, Shengbiao Li, Shengbin Li, Shengchao A Li, Shenghao Li, Shengjie Li, Shengli Li, Shengliang Li, Shengsheng Li, Shengwen Li, Shengxian Li, Shengxu Li, Shengze Li, Sherly X Li, Shi Li, Shi-Fang Li, Shi-Guang Li, Shi-Hong Li, Shi-Ying Li, Shibao Li, Shibo Li, Shichao Li, Shigang Li, Shihao Li, Shiheng Li, Shihong Li, Shijie Li, Shijun Li, Shikang Li, Shilan Li, Shili Li, Shiliang Li, Shilin Li, Shilun Li, Shiqi Li, Shiquan Li, Shisheng Li, Shishi Li, Shitao Li, Shiya Li, Shiyan Li, Shiyang Li, Shiyi Li, Shiying Li, Shiyu Li, Shiyue Li, Shiyun Li, Shu Li, Shu-Fang Li, Shu-Fen Li, Shu-Feng Li, Shu-Hong Li, Shu-Qi Li, Shu-Xin Li, Shuai Li, Shuaicheng Li, Shuang Li, Shuang-Ling Li, Shuangding Li, Shuangfei Li, Shuanglong Li, Shuangmei Li, Shuangshuang Li, Shuangxiu Li, Shubo Li, Shude Li, Shufen Li, Shugang Li, Shuguang Li, Shuhao Li, Shuhua Li, Shuhui Li, Shujiao Li, Shujie Li, Shujin Li, Shujing Li, Shulin Li, Shun Li, Shunhua Li, Shunle Li, Shunqin Li, Shunqing Li, Shunwang Li, Shuo Li, Shupeng Li, Shuqiang Li, Shuwei Li, Shuwen Li, Shuying Li, Shuyu D Li, Shuyu Dan Li, Shuyuan Li, Shuyue Li, Si Li, Si-Wei Li, Si-Xing Li, Si-Ying Li, Si-Yuan Li, Sibing Li, Sichen Li, Sichong Li, Side Li, Siguang Li, Sijie Li, Simin Li, Siming Li, Sin-Lun Li, Siqi Li, Sitao Li, Siting Li, Siwen Li, Siyi Li, Siyu Li, Siyue Li, Song Li, Song-Chao Li, Songhan Li, Songlin Li, Songtao Li, Songyu Li, Songyun Li, Stephen Li, Su Li, SuYun Li, Suchun Li, Suheng Li, Suhong Li, Suiyan Li, Sujing Li, Suk-Yee Li, Sumei Li, Sunan Li, Sung-Chou Li, Supeng Li, Suping Li, Suran Li, Suwei Li, Suwen Li, Suyan Li, T Li, Taibo Li, Taiwen Li, Taixu Li, Tao Li, Taoyingnan Li, Teng Li, Tengyan Li, Thomas Li, Tian Li, Tian-Yi Li, Tian-chang Li, Tian-wang Li, Tianchang Li, Tiandong Li, Tianfeng Li, Tiange Li, Tianjiao Li, Tianjun Li, Tianming Li, Tiansen Li, Tiantian Li, Tianxiang Li, Tianyao Li, Tianye Li, Tianyi Li, Tianyou Li, Tie Li, Tiegang Li, Tiehua Li, Tiewei Li, Timmy Li, Ting Li, Tingguang Li, Tinghao Li, Tinghua Li, Tingsong Li, Tingting Li, Tong Li, Tong-Ruei Li, Tongyao Li, Tongzheng Li, Tsai-Kun Li, Tuojian Li, Tuoping Li, Vivian Li, Vivian S W Li, W H Li, W J Li, W Li, W W Li, W Y Li, W-B Li, Wan Jie Li, Wan Li, Wan-Hong Li, Wan-Shan Li, Wan-Xin Li, Wang Li, Wanling Li, Wanni Li, Wanqian Li, Wanru Li, Wanshi Li, Wanshun Li, Wanting Li, Wanwan Li, Wanxin Li, Wanyan Li, Wanyi Li, Wei Li, Wei-Bo Li, Wei-Dong Li, Wei-Jun Li, Wei-Li Li, Wei-Ming Li, Wei-Na Li, Wei-Ping Li, Wei-Qin Li, Wei-Yang Li, Weidong Li, Weifeng Li, Weiguang Li, Weiguo Li, Weihai Li, Weiheng Li, Weihua Li, Weijian Li, Weijie Li, Weijun Li, Weike Li, Weiling Li, Weimin Li, Weina Li, Weining Li, Weiping Li, Weiqin Li, Weirong Li, Weisong Li, Weiyang Li, Weiye Li, Weiyong Li, Weizu Li, Wen Lan Li, Wen Li, Wen-Chao Li, Wen-Jie Li, Wen-Ting Li, Wen-Wen Li, Wen-Xi Li, Wen-Xing Li, Wen-Ya Li, Wen-Ying Li, Wen-juan Li, Wenbo Li, Wenchao Li, Wende Li, Wendeng Li, Wenfang Li, Wenfeng Li, Wenge Li, Wenguo Li, Wenhao Li, Wenhong Li, Wenhua Li, Wenhui Li, Wenjia Li, Wenjian Li, Wenjie Li, Wenjing Li, Wenjuan Li, Wenjun Li, Wenke Li, Wenlei Li, Wenli Li, Wenlong Li, Wenming Li, Wenqi Li, Wenqiang Li, Wenqing Li, Wenqun Li, Wenrui Li, Wensheng Li, Wentao Li, Wenwen Li, Wenxi Li, Wenxia Li, Wenxiang Li, Wenxin Li, Wenxiu Li, Wenxue Li, Wenyan Li, Wenyang Li, Wenyi Li, Wenying Li, Wenyong Li, Wenyu Li, Wenzhe Li, Wenzhuo Li, Wu-Jun Li, Wuguo Li, Wulan Li, Wuyan Li, X B Li, X L Li, X Li, X Y Li, X-H Li, X-L Li, Xi Li, Xi-Hai Li, Xi-Xi Li, Xia Li, Xian Li, Xiancheng Li, Xiang Li, Xiang-Dong Li, Xiang-Jun Li, Xiang-Ping Li, Xiang-Yu Li, Xiangcheng Li, Xiangchun Li, Xiangdong Li, Xiangfei Li, Xiangjun Li, Xiangling Li, Xianglong Li, Xiangnan Li, Xiangpan Li, Xiangping Li, Xiangqi Li, Xiangrui Li, Xiangwei Li, Xiangyan Li, Xiangyang Li, Xiangyun Li, Xiangzhe Li, Xiankai Li, Xiankun Li, Xianlin Li, Xianlong Li, Xianlu Li, Xianlun Li, Xianrui Li, Xianyong Li, Xiao Li, Xiao-Cheng Li, Xiao-Dong Li, Xiao-Feng Li, Xiao-Gang Li, Xiao-Guang Li, Xiao-Hong Li, Xiao-Hui Li, Xiao-Jiao Li, Xiao-Jing Li, Xiao-Jun Li, Xiao-Kang Li, Xiao-Li Li, Xiao-Lin Li, Xiao-Long Li, Xiao-Min Li, Xiao-Na Li, Xiao-Qiang Li, Xiao-Qin Li, Xiao-Qiu Li, Xiao-Sa Li, Xiao-Tong Li, Xiao-Yao Li, Xiao-Yun Li, Xiao-kun Li, Xiao-mei Li, Xiao-xu Li, Xiao-yu Li, XiaoQiu Li, Xiaobai Li, Xiaobin Li, Xiaobing Li, Xiaobo Li, Xiaochen Li, Xiaochun Li, Xiaocun Li, Xiaodong Li, Xiaofang Li, Xiaofei Li, Xiaofeng Li, Xiaoguang Li, Xiaohan Li, Xiaoheng Li, Xiaohong Li, Xiaohu Li, Xiaohua Li, Xiaohuan Li, Xiaohui Li, Xiaojiao Li, Xiaojiaoyang Li, Xiaojing Li, Xiaoju Li, Xiaojuan Li, Xiaokun Li, Xiaolei Li, Xiaoli Li, Xiaolian Li, Xiaoliang Li, Xiaolin Li, Xiaoling Li, Xiaolong Li, Xiaoman Li, Xiaomei Li, Xiaomeng Li, Xiaomin Li, Xiaoming Li, Xiaona Li, Xiaonan Li, Xiaoning Li, Xiaopeng Li, Xiaoping Li, Xiaoqi Li, Xiaoqiang Li, Xiaoqin Li, Xiaoqing Li, Xiaoqiong Li, Xiaoquan Li, Xiaoran Li, Xiaorong Li, Xiaotian Li, Xiaoting Li, Xiaotong Li, Xiaowei Li, Xiaoxia Li, Xiaoxiao Li, Xiaoxiong Li, Xiaoxuan Li, Xiaoya Li, Xiaoyan Li, Xiaoyao Li, Xiaoyi Li, Xiaoying Li, Xiaoyong Li, Xiaoyu Li, Xiaoyuan Li, Xiaoyun Li, Xiaozhao Li, Xiaozhen Li, Xiaozheng Li, Xiatian Li, Xiawei Li, Xiaxia Li, Xiayu Li, Xidan Li, Xihao Li, Xihe Li, Xijing Li, Xikun Li, Xiliang Li, Ximei Li, Xin Li, Xin-Chang Li, Xin-Jian Li, Xin-Ping Li, Xin-Tao Li, Xin-Ya Li, Xin-Yu Li, Xin-Yue Li, Xin-Zhu Li, Xinbin Li, Xing Li, Xing-Wang Li, Xingchen Li, Xingcheng Li, Xingfang Li, Xinghuan Li, Xinghui Li, Xingli Li, Xinglong Li, Xingwang Li, Xingxing Li, Xingya Li, Xingye Li, Xingyu Li, Xingyuan Li, Xinhai Li, Xinhua Li, Xinhui Li, Xining Li, Xinjia Li, Xinjian Li, Xinke Li, Xinle Li, Xinli Li, Xinlin Li, Xinmei Li, Xinmiao Li, Xinmin Li, Xinming Li, Xinpeng Li, Xinping Li, Xinrong Li, Xinrui Li, Xinsheng Li, Xinwei Li, Xinxin Li, Xinxiu Li, Xinyan Li, Xinyang Li, Xinyao Li, Xinye Li, Xinyi Li, Xinyu Li, Xinyuan Li, Xinzhi Li, Xinzhong Li, Xiong Bing Li, Xiong Li, Xiongfeng Li, Xionghao Li, Xionghui Li, Xiu-Ling Li, Xiucui Li, Xiufeng Li, Xiujuan Li, Xiuli Li, Xiuling Li, Xiumei Li, Xiuqi Li, Xiurong Li, Xiushen Li, Xiushi Li, Xiuzhen Li, Xixi Li, Xiying Li, Xiyue Li, Xiyun Li, Xu Li, Xu-Bo Li, Xu-Wei Li, Xu-Zhao Li, Xuan Li, Xuan-Ling Li, Xuanfei Li, Xuanxuan Li, Xuanzheng Li, Xudong Li, Xue Cheng Li, Xue Li, Xue-Er Li, Xue-Fei Li, Xue-Hua Li, Xue-Lian Li, Xue-Min Li, Xue-Nan Li, Xue-Peng Li, Xue-Yan Li, Xue-Ying Li, Xue-jing Li, Xue-zhi Li, Xuebiao Li, Xueer Li, Xuefei Li, Xuefeng Li, Xuehua Li, Xuejie Li, Xuejun Li, Xuekun Li, Xuelian Li, Xuelin Li, Xueling Li, Xuemei Li, Xuemin Li, Xuening Li, Xuepeng Li, Xueqin Li, Xueren Li, Xueshan Li, Xuesong Li, Xueting Li, Xuewang Li, Xuewei Li, Xuewen Li, Xueyang Li, Xueyi Li, Xueying Li, Xuezhong Li, Xuhang Li, Xuhong Li, Xuhua Li, Xujun Li, Xun Li, Xunjia Li, Xuri Li, Xutong Li, Xuyi Li, Xuze Li, Y H Li, Y L Li, Y Li, Y M Li, Y X Li, Y-Y Li, Ya Li, Ya-Feng Li, Ya-Ge Li, Ya-Jun Li, Ya-Li Li, Ya-Pei Li, Ya-Qiang Li, Ya-Ting Li, Ya-Zhou Li, YaJie Li, Yadong Li, Yahui Li, Yajiao Li, Yajing Li, Yajuan Li, Yajun Li, Yakui Li, Yalan Li, Yali Li, Yalin Li, Yan Bing Li, Yan Li, Yan Ning Li, Yan-Chun Li, Yan-Guang Li, Yan-Hong Li, Yan-Hua Li, Yan-Li Li, Yan-Nan Li, Yan-Xue Li, Yan-Yan Li, Yan-Yu Li, Yanan Li, Yanbin Li, Yanbing Li, Yanbo Li, Yanchang Li, Yanchuan Li, Yanchun Li, Yandong Li, Yanfeng Li, Yang Li, Yangxue Li, Yangyang Li, Yanhui Li, Yani Li, Yanjiao Li, Yanjie Li, Yanjing Li, Yanjun Li, Yanli Li, Yanlin Li, Yanling Li, Yanlong Li, Yanmei Li, Yanmin Li, Yanming Li, Yanni Li, Yanping Li, Yanqing Li, Yansen Li, Yanshu Li, Yansong Li, Yantao Li, Yanwei Li, Yanwu Li, Yanxi Li, Yanxiang Li, Yanxin Li, Yanyan Li, Yanying Li, Yanze Li, Yanzhong Li, Yao Li, Yaobo Li, Yaochen Li, Yaodong Li, Yaofu Li, Yaojia Li, Yaokun Li, Yaoqi Li, Yaoyao Li, Yaqi Li, Yaqiang Li, Yaqiao Li, Yaqin Li, Yaqing Li, Yaqiong Li, Yarong Li, Yawei Li, Yaxi Li, Yaxian Li, Yaxiong Li, Yaxuan Li, Yaying Li, Yayu Li, Yazhou Li, Ye Li, Yehong Li, Yeshan Li, Yetian Li, Yi Li, Yi-Heng Li, Yi-Ling Li, Yi-Ning Li, Yi-Shuan J Li, Yi-Ting Li, Yi-Wen Li, Yi-Yang Li, Yi-Ying Li, Yi-Yun Li, YiPing Li, YiQing Li, Yibo Li, Yiche Li, Yicun Li, Yifan Li, Yifei Li, Yifeng Li, Yige Li, Yihan Li, Yihao Li, Yiheng Li, Yihong Li, Yijian Li, Yijie Li, Yijing Li, Yiju Li, Yikang Li, Yike Li, Yilang Li, Yiliang Li, Yilong Li, Yimei Li, Yimeng Li, Yiming Li, Yin Li, Yinan Li, Ying Li, Ying-Bo Li, Ying-Lan Li, Ying-Qin Li, Ying-Qing Li, Ying-na Li, Yinggao Li, Yinghao Li, Yinghua Li, Yinghui Li, Yingjian Li, Yingjie Li, Yingjun Li, Yinglin Li, Yingnan Li, Yingpu Li, Yingqin Li, Yingrui Li, Yingshuo Li, Yingxi Li, Yingxia Li, Yingyi Li, Yingying Li, Yinhao Li, Yining Li, Yinliang Li, Yinxiong Li, Yinyan Li, Yinzhen Li, Yipeng Li, Yiqiang Li, Yirun Li, Yitong Li, Yiwei Li, Yiwen Li, Yixi Li, Yixiang Li, Yixiao Li, Yixin Li, Yixing Li, Yixuan Li, Yixue Li, Yiyang Li, Yizhe Li, Yong Li, Yong-Jian Li, Yong-Jun Li, Yong-Liang Li, Yongchao Li, Yonghao Li, Yonghe Li, Yongjia Li, Yongjiang Li, Yongjin Li, Yongjing Li, Yongjun Li, Yongkai Li, Yongle Li, Yongli Li, Yongmei Li, Yongnan Li, Yongpeng Li, Yongping Li, Yongqi Li, Yongqiang Li, Yongqiu Li, Yongsen Li, Yongsheng Li, Yongting Li, Yongxiang Li, Yongxin Li, Yongxue Li, Yongze Li, Yongzhe Li, Yongzhen Li, Yongzheng Li, You Li, You Ran Li, You-Mei Li, Youchen Li, Youjun Li, Youming Li, Youran Li, Yousheng Li, Youwei Li, Yu Li, Yu-Cheng Li, Yu-Chia Li, Yu-Hang Li, Yu-Hao Li, Yu-He Li, Yu-Hui Li, Yu-I Li, Yu-Jin Li, Yu-Jui Li, Yu-Kun Li, Yu-Lin Li, Yu-Sheng Li, Yu-Xiang Li, Yu-Ye Li, Yu-Ying Li, Yu-quan Li, Yuan Hao Li, Yuan Li, Yuan-Hai Li, Yuan-Jing Li, Yuan-Tao Li, Yuan-Yuan Li, Yuan-hao Li, Yuanchang Li, Yuanchuang Li, Yuancong Li, Yuandong Li, Yuanfang Li, Yuanfei Li, Yuanhao Li, Yuanhe Li, Yuanheng Li, Yuanhong Li, Yuanhua Li, Yuanjing Li, Yuanmei Li, Yuanyou Li, Yuanyuan Li, Yuanze Li, Yubin Li, Yubo Li, Yuchan Li, Yuchao Li, Yucheng Li, Yuchuan Li, Yuchun Li, Yudong Li, Yue Li, Yue-Chun Li, Yue-Jia Li, Yue-Ming Li, Yue-Rui Li, Yue-Ting Li, Yue-Ying Li, YueQiang Li, Yuefei Li, Yuefeng Li, Yueguo Li, Yuehua Li, Yuemei Li, Yueping Li, Yueqi Li, Yueting Li, Yuezheng Li, Yufan Li, Yufen Li, Yufeng Li, Yuguang Li, Yuhan Li, Yuhang Li, Yuhong Li, Yuhua Li, Yuhuang Li, Yuhui Li, Yujie Li, Yujun Li, Yukun Li, Yuli Li, Yulin Li, Yuling Li, Yulong Li, Yumao Li, Yumei Li, Yumiao Li, Yumin Li, Yun Li, Yun-Da Li, Yun-Lin Li, Yun-Peng Li, Yun-tian Li, Yuna Li, Yunan Li, Yunchu Li, Yunfeng Li, Yunjiu Li, Yunlong Li, Yunlun Li, Yunman Li, Yunmin Li, Yunpeng Li, Yunqi Li, Yunrui Li, Yunshen Li, Yunsheng Li, Yunting Li, Yunxi Li, Yunxiao Li, Yunxu Li, Yunyun Li, Yunze Li, Yuping Li, Yuqi Li, Yuqian Li, Yuqing Li, Yuqiu Li, Yuquan Li, Yushan Li, Yutang Li, Yutian 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articles
Weiling Li, Liang Song, Ann-Marie Ritchie +1 more · 2012 · Pigment cell & melanoma research · Blackwell Publishing · added 2026-04-24
The mitogen-activated protein kinase (MAPK) pathway is important in melanoma. In this pathway, DUSP6 phosphatase negatively controls the activation of extracellular signal-regulated (ERK) kinase. Thro Show more
The mitogen-activated protein kinase (MAPK) pathway is important in melanoma. In this pathway, DUSP6 phosphatase negatively controls the activation of extracellular signal-regulated (ERK) kinase. Through comparison of melanoma signalling pathways between immortal mouse melanocytes and their tumourigenic derivatives, retrieved from mouse xenografts, we identified a molecularly distinct subtype of melanoma, characterized by reduced ERK activity and increased DUSP6 expression. Overexpression of DUSP6 enhanced anchorage-independent growth and invasive ability of immortal mouse melanocytes, suggesting that increased DUSP6 expression contributes to melanoma formation in the mouse xenografts. In contrast, reduced tumourigenicity was observed after DUSP6 overexpression in human melanoma cells. A minority of thick human primary melanomas had high DUSP6 expression and the same poor melanoma-specific survival as the majority of thick primaries with low DUSP6 levels. We have demonstrated that DUSP6 is important in melanoma and that it plays a different role in our distinct subtype of mouse melanoma compared with that in classic human melanoma. Show less
no PDF DOI: 10.1111/j.1755-148X.2011.00949.x
DUSP6
W Li, D W Melton · 2012 · Oncogene · Nature · added 2026-04-24
The incidence of malignant melanoma is growing rapidly worldwide and there is still no effective therapy for metastatic disease. Melanoma is the second most common cancer among young adults in the UK, Show more
The incidence of malignant melanoma is growing rapidly worldwide and there is still no effective therapy for metastatic disease. Melanoma is the second most common cancer among young adults in the UK, where incidence rates have more than quadrupled since the 1970s. Increased expression of a number of DNA repair genes has been reported in melanoma and this likely contributes to its extreme resistance to conventional DNA-damaging chemotherapeutics. One such chemotherapeutic that is effective against a range of other cancers, but not melanoma, is cisplatin. The DNA repair proteins ERCC1 and XPF are needed to remove cisplatin-induced DNA damage and we have investigated the response of these proteins to cisplatin in melanoma. The expression of both genes is induced by cisplatin. Use of a MEK inhibitor showed that ERCC1, but not XPF induction was regulated by the mitogen-activated protein kinase (MAPK) pathway, with reduction in expression of DUSP6, the phosphatase that inactivates the extracellular signal-regulated kinase (ERK), being particularly important. DUSP6 overexpression prevented cisplatin induction of both ERCC1 and XPF, resulting in increased sensitivity to cisplatin. A novel ERCC1 mRNA was found that initiated upstream of the normal transcription initiation site, and was strongly regulated by both cisplatin and the MAPK pathway and its role in cisplatin resistance merits further study. The cisplatin induction of ERCC1 and XPF provides important insights into the resistance of melanoma to DNA-damaging chemotherapeutics, which is one of the major obstacles to melanoma treatment. Show less
no PDF DOI: 10.1038/onc.2011.426
DUSP6
Shaojing Li, Chuanhong Wu, Li Zhu +8 more · 2012 · Molecules (Basel, Switzerland) · MDPI · added 2026-04-24
Ischemic stroke is a devastating disease with a complex pathophysiology. Galangin is a natural flavonoid isolated from the rhizome of Alpina officinarum Hance, which has been widely used as an antioxi Show more
Ischemic stroke is a devastating disease with a complex pathophysiology. Galangin is a natural flavonoid isolated from the rhizome of Alpina officinarum Hance, which has been widely used as an antioxidant agent. However, its effects against ischemic stroke have not been reported and its related neuroprotective mechanism has not really been explored. In this study, neurological behavior, cerebral infarct volumes and the improvement of the regional cortical blood flow (rCBF) were used to evaluate the therapeutic effect of galangin in rats impaired by middle cerebral artery occlusion (MCAO)-induced focal cerebral ischemia. Furthermore, the determination of mitochondrial function and Western blot of apoptosis-related proteins were performed to interpret the neuroprotective mechanism of galangin. The results showed that galangin alleviated the neurologic impairments, reduced cerebral infarct at 24 h after MCAO and exerted a protective effect on the mitochondria with decreased production of mitochondrial reactive oxygen species (ROS). These effects were consistent with improvements in the membrane potential level (Dym), membrane fluidity, and degree of mitochondrial swelling in a dose-dependent manner. Moreover, galangin significantly improved the reduced rCBF after MCAO. Western blot analysis revealed that galangin also inhibited apoptosis in a dose-dependent manner concomitant with the up-regulation of Bcl-2 expression, down-regulation of Bax expression and the Bax/Bcl-2 ratio, a reduction in cytochrome c release from the mitochondria to the cytosol, the reduced expression of activated caspase-3 and the cleavage of poly(ADP-ribose) polymerase (PARP). All these data in this study demonstrated that galangin might have therapeutic potential for ischemic stroke and play its protective role through the improvement in rCBF, mitochondrial protection and inhibiting caspase-dependent mitochondrial cell death pathway for the first time. Show less
📄 PDF DOI: 10.3390/molecules171113403
DYM
Yechun Xu, Min-jun Li, Harry Greenblatt +10 more · 2012 · Acta crystallographica. Section D, Biological crystallography · added 2026-04-24
β-Secretase (β-site amyloid precursor protein-cleaving enzyme 1; BACE1) is a transmembrane aspartic protease that cleaves the β-amyloid precursor protein en route to generation of the amyloid β-peptid Show more
β-Secretase (β-site amyloid precursor protein-cleaving enzyme 1; BACE1) is a transmembrane aspartic protease that cleaves the β-amyloid precursor protein en route to generation of the amyloid β-peptide (Aβ) that is believed to be responsible for the Alzheimer's disease amyloid cascade. It is thus a prime target for the development of inhibitors which may serve as drugs in the treatment and/or prevention of Alzheimer's disease. In the following determination of the crystal structures of both apo and complexed BACE1, structural analysis of all crystal structures of BACE1 deposited in the PDB and molecular dynamics (MD) simulations of monomeric and `dimeric' BACE1 were used to study conformational changes in the active-site region of the enzyme. It was observed that a flap able to cover the active site is the most flexible region, adopting multiple conformational states in the various crystal structures. Both the presence or absence of an inhibitor within the active site and the crystal packing are shown to influence the flap's conformation. An open conformation of the flap is mostly observed in the apo structures, while direct hydrogen-bonding interaction between main-chain atoms of the flap and the inhibitor is a prerequisite for the flap to adopt a closed conformation in the crystal structures of complexes. Thus, a systematic study of the conformational flexibility of the enzyme may not only contribute to structure-based drug design of BACE1 inhibitors and of other targets with flexible conformations, but may also help to better understand the mechanistic events associated with the binding of substrates and inhibitors to the enzyme. Show less
no PDF DOI: 10.1107/S0907444911047251
DYM
Xue Wang, Lin Li, Jiangxia Li +4 more · 2012 · Genetic testing and molecular biomarkers · added 2026-04-24
Multiple osteochondroma (MO) is an autosomal dominant disease characterized by abnormal skeleton development: one or more exostoses localized mainly at the end of long bones. Three pathogenic gene loc Show more
Multiple osteochondroma (MO) is an autosomal dominant disease characterized by abnormal skeleton development: one or more exostoses localized mainly at the end of long bones. Three pathogenic gene loci have been identified and cloned: EXT1, 2, and 3. Only EXT1 and 2 mutations were reported to cause MO. Here, we report on a large Chinese family with MO and a disease-causing mutation in EXT. We extracted DNA from peripheral blood samples of 25 family members, 9 with MO. Polymerase chain reaction and direct DNA sequencing of the entire coding regions of EXT1 and 2 for the nine patients revealed a novel pathogenic mutation, insertion of a T in exon 2 (c.72-73 insT) of EXT2. Our results extend the mutational spectrum of MO and can help with genetic counseling and prenatal diagnosis for this family. Show less
no PDF DOI: 10.1089/gtmb.2011.0276
EXT1
Meng Guo, Hua Zhang, Fenghua Bian +7 more · 2012 · Frontiers in bioscience (Elite edition) · added 2026-04-24
Nest breakdown and primordial folliculogenesis of the mouse ovary can be inhibited by progesterone (P4) and Notch signaling inhibitors. However, the relationship between these two signals during this Show more
Nest breakdown and primordial folliculogenesis of the mouse ovary can be inhibited by progesterone (P4) and Notch signaling inhibitors. However, the relationship between these two signals during this process remains unknown. In the present study, transcript levels of Jagged2, Notch1, and their target, Hey2, increased markedly in ovaries during the beginning stage of folliculogenesis (17.5 days post coitus (dpc) to birth). Maternal P4 levels decreased simultaneously. We found that maternal midpregnancy P4 levels significantly inhibited Jagged2, Notch1, and Hey2 expression, and follicle formation in vitro. Maintaining high maternal P4 levels by daily injection also significantly suppressed the expression of Jagged2, Notch1, and Hey2, and follicle formation during late pregnancy. Based on immunohistochemistry, Jagged2 was localized in oocytes and Notch1 was strongly stained in pre-granulosa cells in 19.5 dpc ovaries. Suppression of their function by antibody addition and RNAi markedly inhibited nest breakdown and follicle formation. Taken together, these results demonstrate that maternal P4 levels during midpregnancy can inhibit the expression of Jagged2 and Notch1, which are involved in primordial folliculogenesis, in the mouse fetal ovary. Show less
no PDF DOI: 10.2741/e579
HEY2
Huiqing Li, Sheila Cherry, Donna Klinedinst +7 more · 2012 · Circulation. Cardiovascular genetics · added 2026-04-24
About half of people with Down syndrome (DS) exhibit some form of congenital heart disease (CHD); however, trisomy for human chromosome 21 (Hsa21) alone is insufficient to cause CHD, as half of all pe Show more
About half of people with Down syndrome (DS) exhibit some form of congenital heart disease (CHD); however, trisomy for human chromosome 21 (Hsa21) alone is insufficient to cause CHD, as half of all people with DS have a normal heart, suggesting that genetic modifiers interact with dosage-sensitive gene(s) on Hsa21 to result in CHD. We hypothesize that a threshold exists in both DS and euploid populations for the number of genetic perturbations that can be tolerated before CHD results. We ascertained a group of individuals with DS and complete atrioventricular septal defect and sequenced 2 candidate genes for CHD: CRELD1, which is associated with atrioventricular septal defect in people with or without DS, and HEY2, whose mouse ortholog (Hey2) produces septal defects when mutated. Several deleterious variants were identified, but the frequency of these potential modifiers was low. We crossed mice with mutant forms of these potential modifiers to the Ts65Dn mouse model of DS. Crossing loss-of-function alleles of either Creld1 or Hey2 onto the trisomic background caused a significant increase in the frequency of CHD, demonstrating an interaction between the modifiers and trisomic genes. We showed further that, although each of these mutant modifiers is benign by itself, they interact to affect heart development when inherited together. Using mouse models of Down syndrome and of genes associated with congenital heart disease, we demonstrate a biological basis for an interaction that supports a threshold hypothesis for additive effects of genetic modifiers in the sensitized trisomic population. Show less
📄 PDF DOI: 10.1161/CIRCGENETICS.111.960872
HEY2
Kaiming Yuan, Binghai Zhao, Xing-Wang Li +6 more · 2012 · Chemico-biological interactions · Elsevier · added 2026-04-24
The 3β-hydroxysteroid dehydrogenase (3β-HSD) and 17β-hydroxysteroid dehydrogenase 3 (17β-HSD3) are involved in the reactions that culminate in androgen biosynthesis in Leydig cells. Human and rat test Show more
The 3β-hydroxysteroid dehydrogenase (3β-HSD) and 17β-hydroxysteroid dehydrogenase 3 (17β-HSD3) are involved in the reactions that culminate in androgen biosynthesis in Leydig cells. Human and rat testis microsomes were used to investigate the inhibitory potencies on 3β-HSD and 17β-HSD3 activities of 14 different phthalates with various carbon numbers in the ethanol moiety. The results demonstrated that the half-maximal inhibitory concentrations (IC(50)s) of dipropyl (DPrP), dibutyl (DBP), dipentyl (DPP), bis(2-butoxyethyl) (BBOP) and dicyclohexyl (DCHP) phthalate were 123.0, 24.1, 25.5, 50.3 and 25.5μM for human 3β-HSD activity, and 62.7, 30.3, 33.8, 82.6 and 24.7μM for rat 3β-HSD activity, respectively. However, only BBOP and DCHP potently inhibited human (IC(50)s, 23.3 and 8.2μM) and rat (IC(50)s, 30.24 and 9.1μM) 17β-HSD3 activity. Phthalates with 1-2 or 7-8 carbon atoms in ethanol moieties had no effects on both enzyme activities even at concentrations up to 1mM. The mode of action of DCHP on 3β-HSD activity was competitive with the substrate pregnenolone but noncompetitive with the cofactor NAD+. The mode of action of DCHP on 17β-HSD3 activity was competitive with the substrate androstenedione but noncompetitive with the cofactor NADPH. In summary, our results showed that there are clear structure-activity responses for phthalates in the inhibition of both 3β-HSD and 17β-HSD3 activities. The length of carbon chains in the ethanol moieties of phthalates may determine the potency to inhibit these two enzymes. Show less
no PDF DOI: 10.1016/j.cbi.2011.12.008
HSD17B12
Si-Xun Yu, Song Li, Hai-Feng Shu +3 more · 2012 · Journal of neuropathology and experimental neurology · added 2026-04-24
The reticulon protein Nogo-A is an important regulator of neurite growth, axonal plasticity, and cell migration in the central nervous system. Previous studies have shown markedly elevated levels of N Show more
The reticulon protein Nogo-A is an important regulator of neurite growth, axonal plasticity, and cell migration in the central nervous system. Previous studies have shown markedly elevated levels of Nogo-A in human temporal lobe epilepsy. In the present study, we examined the expression pattern of the Nogo-A system in cortical lesions of pediatric patients with tuberous sclerosis complex and focal cortical dysplasia type IIb. These disorders are characterized by malformations of cortical development and are frequently associated with intractable epilepsy. We found that the messenger RNA and protein levels of the Nogo-A receptor (NgR) and the downstream targets of Nogo-A, LINGO-1, TROY, and RhoA but not P75 were upregulated in the cortices of patients compared with autopsy control samples. Immunohistochemical analyses indicated that Nogo-A and NgR were strongly expressed in misshapen cells, particularly dysmorphic neurons, balloon cells, and giant cells. TROY was diffusely expressed in the malformations of cortical development. Most of theNogo-A/NgR-positive misshapen cells were colabeled with neuronal rather than astrocytic markers. Taken together, our results suggestthat the activation of Nogo-A via the NgR/LINGO-1/TROY signal transduction pathways, but not NgR/LINGO-1/P75, may be involved in the development and/or seizure activity of cortical lesions in tuberous sclerosis complex and focal cortical dysplasia type IIb. Show less
no PDF DOI: 10.1097/NEN.0b013e31825d6585
LINGO1
Miguel A Lanaspa, Laura G Sanchez-Lozada, Christina Cicerchi +13 more · 2012 · PloS one · PLOS · added 2026-04-24
Excessive dietary fructose intake may have an important role in the current epidemics of fatty liver, obesity and diabetes as its intake parallels the development of these syndromes and because it can Show more
Excessive dietary fructose intake may have an important role in the current epidemics of fatty liver, obesity and diabetes as its intake parallels the development of these syndromes and because it can induce features of metabolic syndrome. The effects of fructose to induce fatty liver, hypertriglyceridemia and insulin resistance, however, vary dramatically among individuals. The first step in fructose metabolism is mediated by fructokinase (KHK), which phosphorylates fructose to fructose-1-phosphate; intracellular uric acid is also generated as a consequence of the transient ATP depletion that occurs during this reaction. Here we show in human hepatocytes that uric acid up-regulates KHK expression thus leading to the amplification of the lipogenic effects of fructose. Inhibition of uric acid production markedly blocked fructose-induced triglyceride accumulation in hepatocytes in vitro and in vivo. The mechanism whereby uric acid stimulates KHK expression involves the activation of the transcription factor ChREBP, which, in turn, results in the transcriptional activation of KHK by binding to a specific sequence within its promoter. Since subjects sensitive to fructose often develop phenotypes associated with hyperuricemia, uric acid may be an underlying factor in sensitizing hepatocytes to fructose metabolism during the development of fatty liver. Show less
📄 PDF DOI: 10.1371/journal.pone.0047948
MLXIPL
Qiang Ge, Nian Huang, R Max Wynn +5 more · 2012 · The Journal of biological chemistry · American Society for Biochemistry and Molecular Biology · added 2026-04-24
Carbohydrate response element-binding protein (ChREBP) is an insulin-independent, glucose-responsive transcription factor that is expressed at high levels in liver hepatocytes where it plays a critica Show more
Carbohydrate response element-binding protein (ChREBP) is an insulin-independent, glucose-responsive transcription factor that is expressed at high levels in liver hepatocytes where it plays a critical role in converting excess carbohydrates to fat for storage. In response to fluctuating glucose levels, hepatic ChREBP activity is regulated in large part by nucleocytoplasmic shuttling of ChREBP protein via interactions with 14-3-3 proteins. The N-terminal ChREBP regulatory region is necessary and sufficient for glucose-responsive ChREBP nuclear import and export. Here, we report the crystal structure of a complex of 14-3-3β bound to the N-terminal regulatory region of ChREBP at 2.4 Å resolution. The crystal structure revealed that the α2 helix of ChREBP (residues 117-137) adopts a well defined α-helical conformation and binds 14-3-3 in a phosphorylation-independent manner that is different from all previously characterized 14-3-3 and target protein-binding modes. ChREBP α2 interacts with 14-3-3 through both electrostatic and van der Waals interactions, and the binding is partially mediated by a free sulfate or phosphate. Structure-based mutagenesis and binding assays indicated that disrupting the observed 14-3-3 and ChREBP α2 interface resulted in a loss of complex formation, thus validating the novel protein interaction mode in the 14-3-3β·ChREBP α2 complex. Show less
no PDF DOI: 10.1074/jbc.M112.418855
MLXIPL
N Poungvarin, J K Lee, V K Yechoor +7 more · 2012 · Diabetologia · Springer · added 2026-04-24
This study was aimed at the elucidation of the pathogenesis of glucotoxicity, i.e. the mechanism whereby hyperglycaemia damages pancreatic beta cells. The identification of pathways in the process may Show more
This study was aimed at the elucidation of the pathogenesis of glucotoxicity, i.e. the mechanism whereby hyperglycaemia damages pancreatic beta cells. The identification of pathways in the process may help identify targets for beta cell-protective therapy. Carbohydrate response element-binding protein (ChREBP), a transcription factor that regulates the expression of multiple hyperglycaemia-induced genes, is produced in abundance in pancreatic beta cells. We hypothesise that ChREBP plays a pivotal role in mediating beta cell glucotoxicity. We assessed the role of ChREBP in glucotoxicity in 832/13 beta cells, isolated mouse islets and human pancreas tissue sections using multiple complementary approaches under control and high-glucose-challenge conditions as well as in adeno-associated virus-induced beta cell-specific overexpression of Chrebp (also known as Mlxipl) in mice. Under both in vitro and in vivo conditions, ChREBP activates downstream target genes, including fatty acid synthase and thioredoxin-interacting protein, leading to lipid accumulation, increased oxidative stress, reduced insulin gene transcription/secretion and enhanced caspase activity and apoptosis, processes that collectively define glucotoxicity. Immunoreactive ChREBP is enriched in the nucleuses of beta cells in pancreatic tissue sections from diabetic individuals compared with non-diabetic individuals. Finally, we demonstrate that induced beta cell-specific Chrebp overexpression is sufficient to phenocopy the glucotoxicity manifestations of hyperglycaemia in mice in vivo. These data indicate that ChREBP is a key transcription factor that mediates many of the hyperglycaemia-induced activations in a gene expression programme that underlies beta cell glucotoxicity at the molecular, cellular and whole animal levels. Show less
📄 PDF DOI: 10.1007/s00125-012-2506-4
MLXIPL
Cristian Pattaro, Anna Köttgen, Alexander Teumer +167 more · 2012 · PLoS genetics · PLOS · added 2026-04-24
Cristian Pattaro, Anna Köttgen, Alexander Teumer, Maija Garnaas, Carsten A Böger, Christian Fuchsberger, Matthias Olden, Ming-Huei Chen, Adrienne Tin, Daniel Taliun, Man Li, Xiaoyi Gao, Mathias Gorski, Qiong Yang, Claudia Hundertmark, Meredith C Foster, Conall M O'Seaghdha, Nicole Glazer, Aaron Isaacs, Ching-Ti Liu, Albert V Smith, Jeffrey R O'Connell, Maksim Struchalin, Toshiko Tanaka, Guo Li, Andrew D Johnson, Hinco J Gierman, Mary Feitosa, Shih-Jen Hwang, Elizabeth J Atkinson, Kurt Lohman, Marilyn C Cornelis, Åsa Johansson, Anke Tönjes, Abbas Dehghan, Vincent Chouraki, Elizabeth G Holliday, Rossella Sorice, Zoltan Kutalik, Terho Lehtimäki, Tõnu Esko, Harshal Deshmukh, Sheila Ulivi, Audrey Y Chu, Federico Murgia, Stella Trompet, Medea Imboden, Barbara Kollerits, Giorgio Pistis, CARDIoGRAM Consortium, ICBP Consortium, CARe Consortium, Wellcome Trust Case Control Consortium 2 (WTCCC2), Tamara B Harris, Lenore J Launer, Thor Aspelund, Gudny Eiriksdottir, Braxton D Mitchell, Eric Boerwinkle, Helena Schmidt, Margherita Cavalieri, Madhumathi Rao, Frank B Hu, Ayse Demirkan, Ben A Oostra, Mariza de Andrade, Stephen T Turner, Jingzhong Ding, Jeanette S Andrews, Barry I Freedman, Wolfgang Koenig, Thomas Illig, Angela Döring, H-Erich Wichmann, Ivana Kolcic, Tatijana Zemunik, Mladen Boban, Cosetta Minelli, Heather E Wheeler, Wilmar Igl, Ghazal Zaboli, Sarah H Wild, Alan F Wright, Harry Campbell, David Ellinghaus, Ute Nöthlings, Gunnar Jacobs, Reiner Biffar, Karlhans Endlich, Florian Ernst, Georg Homuth, Heyo K Kroemer, Matthias Nauck, Sylvia Stracke, Uwe Völker, Henry Völzke, Peter Kovacs, Michael Stumvoll, Reedik Mägi, Albert Hofman, Andre G Uitterlinden, Fernando Rivadeneira, Yurii S Aulchenko, Ozren Polasek, Nick Hastie, Veronique Vitart, Catherine Helmer, Jie Jin Wang, Daniela Ruggiero, Sven Bergmann, Mika Kähönen, Jorma Viikari, Tiit Nikopensius, Michael Province, Shamika Ketkar, Helen Colhoun, Alex Doney, Antonietta Robino, Franco Giulianini, Bernhard K Krämer, Laura Portas, Ian Ford, Brendan M Buckley, Martin Adam, Gian-Andri Thun, Bernhard Paulweber, Margot Haun, Cinzia Sala, Marie Metzger, Paul Mitchell, Marina Ciullo, Stuart K Kim, Peter Vollenweider, Olli Raitakari, Andres Metspalu, Colin Palmer, Paolo Gasparini, Mario Pirastu, J Wouter Jukema, Nicole M Probst-Hensch, Florian Kronenberg, Daniela Toniolo, Vilmundur Gudnason, Alan R Shuldiner, Josef Coresh, Reinhold Schmidt, Luigi Ferrucci, David S Siscovick, Cornelia M Van Duijn, Ingrid Borecki, Sharon L R Kardia, Yongmei Liu, Gary C Curhan, Igor Rudan, Ulf Gyllensten, James F Wilson, Andre Franke, Peter P Pramstaller, Rainer Rettig, Inga Prokopenko, Jacqueline C M Witteman, Caroline Hayward, Paul Ridker, Afshin Parsa, Murielle Bochud, Iris M Heid, Wolfram Goessling, Daniel I Chasman, W H Linda Kao, Caroline S Fox Show less
Chronic kidney disease (CKD) is an important public health problem with a genetic component. We performed genome-wide association studies in up to 130,600 European ancestry participants overall, and s Show more
Chronic kidney disease (CKD) is an important public health problem with a genetic component. We performed genome-wide association studies in up to 130,600 European ancestry participants overall, and stratified for key CKD risk factors. We uncovered 6 new loci in association with estimated glomerular filtration rate (eGFR), the primary clinical measure of CKD, in or near MPPED2, DDX1, SLC47A1, CDK12, CASP9, and INO80. Morpholino knockdown of mpped2 and casp9 in zebrafish embryos revealed podocyte and tubular abnormalities with altered dextran clearance, suggesting a role for these genes in renal function. By providing new insights into genes that regulate renal function, these results could further our understanding of the pathogenesis of CKD. Show less
📄 PDF DOI: 10.1371/journal.pgen.1002584
MPPED2
Sugata Hazra, Adil Rasheed, Ashay Bhatwadekar +14 more · 2012 · Diabetes · added 2026-04-24
Endothelial progenitor cells (EPCs), critical for mediating vascular repair, are dysfunctional in a hyperglycemic and/or hypercholesterolemic environment. Their dysfunction contributes to the progress Show more
Endothelial progenitor cells (EPCs), critical for mediating vascular repair, are dysfunctional in a hyperglycemic and/or hypercholesterolemic environment. Their dysfunction contributes to the progression of diabetic macro- and microvascular complications. Activation of "cholesterol-sensing" nuclear receptors, the liver X receptors (LXRα/LXRβ), protects against atherosclerosis by transcriptional regulation of genes important in promoting cholesterol efflux and inhibiting inflammation. We hypothesized that LXR activation with a synthetic ligand would correct diabetes-induced EPC dysfunction and improve diabetic retinopathy. Studies were performed in streptozotocin (STZ)-injected DBA/2J mice fed a high-fat Western diet (DBA/STZ/WD) and treated with the LXR agonist GW3965 and in LXRα(-/-), LXRβ(-/-), and LXRα/β(-/-) mice. Retinas were evaluated for number of acellular capillaries and glial fibrillary acidic protein (GFAP) immunoreactivity. Bone marrow EPCs were analyzed for migratory function and gene expression. Compared with vehicle-treated DBA/STZ/WD mice, GW3965 treated mice showed fewer acellular capillaries and reduced GFAP expression. These mice also exhibited enhanced EPC migration and restoration of inflammatory and oxidative stress genes toward nondiabetic levels. LXRα(-/-), LXRβ(-/-), and LXRα/β(-/-) mice developed acellular capillaries and EPC dysfunction similar to the DBA/STZ/WD mice. These studies support a key role for LXR in retinal and bone marrow progenitor dysfunction associated with type 1 diabetes. LXR agonists may represent promising pharmacologic targets for correcting retinopathy and EPC dysfunction. Show less
no PDF DOI: 10.2337/db11-1596
NR1H3
Ji-Shan Fan, Dan-Ning Liu, Gang Huang +5 more · 2012 · Journal of ethnopharmacology · Elsevier · added 2026-04-24
Panax notoginseng (Burk.) F.H. Chen has been used as a health product and natural remedy in traditional medicine for cardiovascular diseases for more than 1000 years in Asia, including China, Japan, a Show more
Panax notoginseng (Burk.) F.H. Chen has been used as a health product and natural remedy in traditional medicine for cardiovascular diseases for more than 1000 years in Asia, including China, Japan, and Korea. Panax notoginseng saponins (PNS) are the major effective ingredients extracted from Panax notoginseng. The purpose of this study was to investigate whether Panax notoginseng saponins (PNS) attenuated atherosclerosis by inducing liver X receptor alpha (LXRα) expression and to elucidate the mechanisms responsible for the effects. The AS rats were treated once daily with PNS (100 mg/kg, i.p.), and pathological changes in the aorta were observed using Sudan IV staining. The expression of LXRα in the aortic wall was measured by Western blot analysis. THP-1 macrophages were cultured with PNS in the presence or absence of geranylgeranyl pyrophosphate ammonium salt (GGPP), an LXRα antagonist. The expression of LXRα and its target genes ATP-binding cassette A1 and G1 (ABCA1, ABCG1) were determined by qRT-PCR. The transcriptional activation of the LXRα gene promoter was analyzed by a reporter assay. The NF-κB DNA binding activity and the expression of interleukin (IL)-6, monocyte chemotactic protein-1 (MCP-1) was evaluated respectively by Trans-AM NF-κB ELISA and ELISA in THP-1 macrophages that were stimulated with LPS after treatment with PNS and GGPP. PNS treatment alleviated the typical pathological changes associated with atherosclerosis in rats. The expression of LXRα was increased in rat aortas after treatment with PNS. In vitro, PNS increased LXRα mRNA levels in THP-1 macrophages. The reporter assays showed that PNS enhanced transcriptional activation of the LXRα gene promoter and led to the upregulation of ABCA1 and ABCG1 expression. This upregulation could be reversed by treatment with GGPP. Additionally, PNS inhibited NF-κB DNA binding activity and reduced secretion of IL-6 and MCP-1 in LPS-stimulated THP-1 macrophages. These effects could be reversed by GGPP. The results indicated that the PNS-mediated attenuation of AS may, at least partly, due to LXRα uprergulation. The mechanisms of action included enhancement transcriptional activation of the LXRα gene promoter by PNS and subsequent upregulation of ABCA1 and ABCG1 and inhibition of NF-κB DNA binding activity. Show less
no PDF DOI: 10.1016/j.jep.2012.05.053
NR1H3
Wei Wang, Jun Luo, Yu Zhong +6 more · 2012 · Gene · Elsevier · added 2026-04-24
The liver X receptor α (LXRα) is a nuclear receptor of the transcription factor and is known to play a crucial role in lipid metabolism processes such as bile acid and fatty acid synthesis in humans a Show more
The liver X receptor α (LXRα) is a nuclear receptor of the transcription factor and is known to play a crucial role in lipid metabolism processes such as bile acid and fatty acid synthesis in humans and rodents. However, very little information is available on the role of LXRα in the regulation of fatty acid synthesis in the goat mammary gland. In this investigation, a cDNA was isolated from the mammary gland of Xinong Saanen dairy goats and designated as goat LXRα. RT-PCR and RACE gave rise to the full-length cDNA of LXRα, which was comprised of 1654 bp and characterized by an ORF of 1344 bp and 5'- and 3'-UTR regions of 150 and 160 bp, respectively. The deduced amino acid sequence encodes 477 amino acids with a predicted molecular weight (MW) of 50.4kDa and a theoretical isoelectric point (pI) of 6.3. Additionally, homology search and sequence multi-alignment indicated that the putative goat LXRα amino acid sequence is very similar to those of cattle, mice, rats, swine, and humans. Bioinformatic predictions demonstrated that the LXRα protein is located in the nucleus, containing characteristic signatures of a nuclear receptor with DNA-binding domain (DBD) and ligand-binding domain (LBD). Real-time quantitative PCR suggested that LXRα was predominantly expressed in the small intestine, liver, spleen and mammary gland. Treatment of goat mammary gland epithelial cells (GMEC) with different concentrations (i.e., 0.01, 0.1, 1 μM) of T0901317, a synthetic agonist of LXRα, resulted in elevated sterol regulatory element binding protein 1 (SREBP1) and fatty acid synthase (FASN) mRNA levels in response to LXRα activation. The association between different T0901317 concentrations and fatty acid composition in GMEC also was examined using gas chromatography (GC). The results showed that activation of LXRα significantly increased GMEC C18:1 and C18:2 contents, but did not affect levels of saturated fatty acids (SFA). These discoveries are consistent with the notion that LXRα plays a key role in controlling lipogenesis and regulating synthesis of unsaturated fatty acids (UFA) in the mammary gland of goats, which may prove useful in regulation of milk fat production. Show less
no PDF DOI: 10.1016/j.gene.2012.05.028
NR1H3
Dongliang Wang, Min Xia, Song Gao +4 more · 2012 · Molecular nutrition & food research · Wiley · added 2026-04-24
Although previous studies have shown that consumption of anthocyanin extract from plant foods reduces hypercholesterolemia and the severity of atherosclerosis in different animal models, the mechanism Show more
Although previous studies have shown that consumption of anthocyanin extract from plant foods reduces hypercholesterolemia and the severity of atherosclerosis in different animal models, the mechanisms of these actions remained unclear. This study investigated whether pure anthocyanin inhibit atherosclerosis development and reduce hypercholesterolemia in the apolipoprotein E (ApoE)-deficient mice through enhancement of fecal bile acid excretion, a critical pathway for eliminating circulation cholesterol from the body. Five-week-old male ApoE-deficient mice were fed the AIN-93G diet supplemented with or without cyanidin-3-O-β-glucoside (0.06% w/w) for 12 weeks. Results showed that cyanidin-3-O-β-glucoside consumption inhibited the formation of aortic sinus plaque and reduced hypercholesterolemia, along with promoted fecal bile acid excretion and upregulated hepatic cholesterol 7a-hydroxylase expression (CYP7A1). In mouse primary hepatocytes, cyanidin-3-O-β-glucoside treatment increased bile acid synthesis and CYP7A1 expression in a liver X receptor alpha (LXRα)-)-dependent manner. Scintillation proximity and time-resolved fluorescence resonance energy transfer assays revealed that cyanidin-3-O-β-glucoside functions as an agonist of LXRα. Our results indicate that the hypocholesterolemic activity of cyanidin-3-O-β-glucoside was, at least in part, mediated by activating the potential LXRα-CYP7A1-bile acid excretion pathway, thus contributing to the antiatherogenic effect of cyanidin-3-O-β-glucoside. Importantly, cyanidin-3-O-β-glucoside could activate LXRα in an agonist-dependent manner. Show less
no PDF DOI: 10.1002/mnfr.201100659
NR1H3
Jiang Li, Chun Deng, Wen-juan Gu +3 more · 2012 · Zhonghua xin xue guan bing za zhi · added 2026-04-24
To investigate the role of liver X receptors (LXRs) on endothelin-1 (ET-1) induced murine HL-1 cardiomyocytes hypertrophy. Cultured murine HL-1 cardiomyocytes were divided into four experiment groups: Show more
To investigate the role of liver X receptors (LXRs) on endothelin-1 (ET-1) induced murine HL-1 cardiomyocytes hypertrophy. Cultured murine HL-1 cardiomyocytes were divided into four experiment groups: (1) CONTROL GROUP:treated with DMSO; (2) T0901317 group:treated with LXRs agonist T0901317 (1 µmol/L); (3) ET-1 group:treated with ET-1 (1 nmol/L); (4) T0901317 + ET-1 group:treated with T0901317 (1 µmol/L) for 8 hours, then treated with ET-1 (1 nmol/L). Twenty-four hours later, immunofluorescent staining was performed on HL-1 cells, the surface area of HL-1 cells was analyzed with NIH Image J software, and the synthetic rate of protein in HL-1 cells was detected by (3)H-leucine incorporation. The mRNA level of atrial natriuretic peptide (ANP) and β-myosin heavy chain (β-MyHC) was measured by quantitative realtime PCR. The effect of T0901317 on mRNA expression of ANP was also detected after LXRs gene silencing. The surface area of HL-1 cells, mRNA expression of ANP and β-MyHC, and (3)H-leucine incorporation in ET-1 group were 2.00 ± 0.29, 1.98 ± 0.47, 2.13 ± 0.39 and 1.79 ± 0.17, respectively, which were significantly higher than those of control group (1.00 ± 0.26, 1.00 ± 0.21, 1.00 ± 0.31 and 1.00 ± 0.03, respectively, all P < 0.05). Compared with ET-1 group, the surface area of HL-1 cells, mRNA expression of ANP and β-MyHC, and (3)H-leucine incorporation were significantly decreased in T0901317 + ET-1 group (1.24 ± 0.25, 1.19 ± 0.21, 1.48 ± 0.27 and 1.15 ± 0.11, respectively, all P < 0.05). After inhibition of LXRα/β expression in HL-1 cardiomyocytes using the specific siRNAs, the mRNA expression of ANP in T0901317 + ET-1 group was 1.78 ± 0.05, which was similar as that in ET-1 group (1.94 ± 0.17, P > 0.05). T0901317, an agonist of LXRs, could inhibit ET-1 induced cardiac hypertrophy in vitro, and LXR ligand-mediated inhibition on ANP mRNA expression by T0901317 is receptor dependent. Show less
no PDF
NR1H3
Yuyang Chen, Yao Chen, Lei Zhao +7 more · 2012 · Journal of gastroenterology and hepatology · Blackwell Publishing · added 2026-04-24
Both inflammation and cholesterol accumulation play important roles in the development of non-alcoholic fatty liver disease. This study was undertaken to investigate whether inflammation aggravated ch Show more
Both inflammation and cholesterol accumulation play important roles in the development of non-alcoholic fatty liver disease. This study was undertaken to investigate whether inflammation aggravated cholesterol accumulation via disrupting hepatic cholesterol export and we explored the underlying mechanisms. We used casein injection in C57BL/6J mice, and tumor necrosis factor alpha (TNF-α) stimulation in human hepatoblastoma cell line (HepG2) cells to induce inflammation. Intracellular cholesterol level was examined by Oil Red O staining and quantitative analysis. Bile acid level was quantified by colorimetric analysis. (3)[H] cholesterol assay by scintillation counting was performed to evaluate the cholesterol efflux. The mRNA and protein expression was examined by real-time polymerase chain reaction and Western blot. Inflammation increased cholesterol accumulation in livers of C57BL/6J mice and in HepG2 cells. High-fat diet in mice and low-density lipoprotein (LDL) loading in HepG2 cells increased bile acid synthesis and cholesterol efflux, enhanced the mRNA and protein expression of liver X receptor α (LXRα), peroxisome proliferator-activated receptors (PPARα, γ), cholesterol 7α-hydroxylase (CYP7A1) and ATP-binding cassette transporter A1 (ABCA1). However, inflammation reduced bile acid synthesis and cholesterol efflux even in high-fat-diet-fed mice and HepG2 cells in the presence of LDL loading. The enhanced effects of these genes and proteins expression due to high-fat diet and LDL loading were inhibited by inflammation both in vivo and in vitro. Inflammation disrupted PPAR-LXR-CYP7A1/ABCA1-mediated bile acid synthesis and cholesterol efflux resulting in exacerbated cholesterol accumulation in livers of C57BL/6J mice and HepG2 cells. Show less
no PDF DOI: 10.1111/j.1440-1746.2011.06986.x
NR1H3
Marcel Wiermer, Yu Ti Cheng, Julia Imkampe +4 more · 2012 · The Plant journal : for cell and molecular biology · Blackwell Publishing · added 2026-04-24
In eukaryotic cells, transduction of external stimuli into the nucleus to induce transcription and export of mRNAs for translation in the cytoplasm is mediated by nuclear pore complexes (NPCs) compose Show more
In eukaryotic cells, transduction of external stimuli into the nucleus to induce transcription and export of mRNAs for translation in the cytoplasm is mediated by nuclear pore complexes (NPCs) composed of nucleoporin proteins (Nups). We previously reported that Arabidopsis MOS3, encoding the homolog of vertebrate Nup96, is required for plant immunity and constitutive resistance mediated by the de-regulated Toll interleukin 1 receptor/nucleotide-binding/leucine-rich repeat (TNL)-type R gene snc1. In vertebrates, Nup96 is a component of the conserved Nup107-160 nuclear pore sub-complex, and implicated in immunity-related mRNA export. Here, we used a reverse genetics approach to examine the requirement for additional subunits of the predicted Arabidopsis Nup107-160 complex in plant immunity. We show that, among eight putative complex members, beside MOS3, only plants with defects in Nup160 or Seh1 are impaired in basal resistance. Constitutive resistance in the snc1 mutant and immunity mediated by TNL-type R genes also depend on functional Nup160 and have a partial requirement for Seh1. Conversely, resistance conferred by coiled coil-type immune receptors operates largely independently of both genes, demonstrating specific contributions to plant defense signaling. Our functional analysis further revealed that defects in nup160 and seh1 result in nuclear accumulation of poly(A) mRNA, and, in the case of nup160, considerable depletion of EDS1, a key positive regulator of basal and TNL-triggered resistance. These findings suggest that Nup160 is required for nuclear mRNA export and full expression of EDS1-conditioned resistance pathways in Arabidopsis. Show less
no PDF DOI: 10.1111/j.1365-313X.2012.04928.x
NUP160
Dan Liu, Bin Yin, Qiang Wang +6 more · 2012 · Journal of genetics and genomics = Yi chuan xue bao · Elsevier · added 2026-04-24
Cytoplasmic poly(A) binding protein 4 (PABPC4) is an RNA-processing protein that plays an important role in the regulation of gene expression. The aim of this study was to investigate the expression p Show more
Cytoplasmic poly(A) binding protein 4 (PABPC4) is an RNA-processing protein that plays an important role in the regulation of gene expression. The aim of this study was to investigate the expression pattern and identify the potential clinical significance of PABPC4 in colorectal cancer. Immunohistochemical analysis revealed that 26.7% (27/101 patients) of primary colorectal tumors and 60.5% (23/38 patients) of corresponding adjacent, normal tissues showed high cytoplasmic expression of PABPC4, whereas expression was absent in 98% (43/44 patients) of distant, normal tissues. Using Kaplan-Meier analysis, we observed that the expression of PABPC4 was significantly correlated with disease-free survival and overall survival in patients with stage II and stage III colorectal cancer (P=0.022 and P=0.020, respectively). PABPC4 expression was positively associated with survival outcome, and may have predictive value in the prognosis of patients with colorectal cancer. Taken together, our findings indicate that PABPC4 may play a role in the pathogenesis of colorectal cancer. Show less
no PDF DOI: 10.1016/j.jgg.2012.05.007
PABPC4
Xi Yang, Yanquan Zhang, Shan Li +5 more · 2012 · Biochemical and biophysical research communications · Elsevier · added 2026-04-24
Epidermal growth factor (EGF) receptor (EGFR) signal transduction is regulated by endocytosis where many Rab proteins play an important role in the determination of the receptor recycle or degradation Show more
Epidermal growth factor (EGF) receptor (EGFR) signal transduction is regulated by endocytosis where many Rab proteins play an important role in the determination of the receptor recycle or degradation. In an effort to better understand how EGF signaling is regulated, we examined the role of Rab21 in regulation of the degradation and signal transduction of the EGFR. Using a transient expression protocol in HEK293T and HeLa cells, we found that Rab21 enhanced the degradation of EGFR through accelerating its internalization in both EGF-independent and EGF-dependent manners. We further demonstrated that Rab21 interacted with EGFR by immunoprecipitation experiments. Interestingly, we observed that overexpression of Rab21 attenuated EGF-mediated mitogen-activated protein kinase (MAPK) signaling by inducing EGFR degradation. Taken together, these data suggest that Rab21 plays a negative role in the EGF-mediated MAPK signaling pathway. Show less
no PDF DOI: 10.1016/j.bbrc.2012.04.049
RAB21
Samil Jung, Soonduck Lee, Jayhee Lee +9 more · 2012 · Oncology letters · added 2026-04-24
Breast cancer is one of the most common types of cancer in women and is highly treatable by radiotherapy. However, repeated exposure to radiation results in tumor cell resistance. Understanding the mo Show more
Breast cancer is one of the most common types of cancer in women and is highly treatable by radiotherapy. However, repeated exposure to radiation results in tumor cell resistance. Understanding the molecular mechanisms involved in the response of tumors to γ-irradiation is important for improving radiotherapy. For this reason, we aimed to identify radiation-responsive genes at the protein level. In the present study, we observed differentially expressed proteins using 2D-PAGE and MALDI-TOF-MS for the global analysis of protein expression patterns in response to ionizing radiation (IR). When the expression patterns of proteins were compared to a control gel, numerous spots were found that differed greatly. Among them, 11 spots were found to be significantly different. One set of proteins (GH2, RGS17, BAK1, CCNH, TSG6, RAD51B, IGFBP1 and CASP14) was upregulated and another set of proteins (C1QRF, PLSCR2 and p34(SE1-1)) was downregulated after exposure to γ-rays. These proteins are known to be related to cell cycle control, apoptosis, DNA repair, cell proliferation and other signaling pathways. Show less
no PDF DOI: 10.3892/ol.2011.444
RGS17
Dankyu Yoon, Young-Jin Kim, Wen-Yan Cui +7 more · 2012 · Human genetics · Springer · added 2026-04-24
Diseases related to smoking are the second leading cause of death in the world. Cigarette smoking is a risk factor for several diseases such as cancer and cardiovascular and respiratory disorders. Des Show more
Diseases related to smoking are the second leading cause of death in the world. Cigarette smoking is a risk factor for several diseases such as cancer and cardiovascular and respiratory disorders. Despite increasing evidence of genetic determination, the susceptibility genes and loci underlying various aspects of smoking behavior are largely unknown. Moreover, almost all reported genome-wide association studies (GWASs) have been performed on samples of European origin, limiting the applicability of the results to other ethnic populations. In this first GWAS on smoking behavior in an Asian population, after analyzing 8,842 DNA samples from the Korea Association Resource project with 352,228 single nucleotide polymorphisms (SNPs) genotyped for each sample, we identified 8 SNPs significantly associated with smoking initiation (SI) and 4 with nicotine dependence (ND). Because of the current unavailability of an independent Asian smoking sample, we replicated the discoveries in independent samples of European-American and African-American origin. Of the 12 SNPs examined in the replicated samples, we identified two SNPs, in the regulator of G-protein signaling 17 gene (rs7747583, p value(meta) = 6.40 × 10(-6); rs2349433, p value(meta) = 5.57 × 10(-6)), associated with SI. Also, we found two SNPs significantly associated with ND; one in the FERM domain containing 4A (rs4424567, p value(meta) = 2.30 × 10(-6)) and the other at 7q31.1 (rs848353, p value(meta) = 9.16 × 10(-8)). These SNPs represent novel targets for examination of smoking behavior and warrant further investigation using independent samples. Show less
no PDF DOI: 10.1007/s00439-011-1102-x
RGS17
Suk-Yee Li, Frederic K C Fung, Zhong Jie Fu +3 more · 2012 · Investigative ophthalmology & visual science · added 2026-04-24
Lutein protects retinal neurons by its anti-oxidative and anti-apoptotic properties in ischemia/reperfusion (I/R) injury while its anti-inflammatory effects remain unknown. As Müller cells play a crit Show more
Lutein protects retinal neurons by its anti-oxidative and anti-apoptotic properties in ischemia/reperfusion (I/R) injury while its anti-inflammatory effects remain unknown. As Müller cells play a critical role in retinal inflammation, the effect of lutein on Müller cells was investigated in a murine model of I/R injury and a culture model of hypoxic damage. Unilateral retinal I/R was induced by a blockade of internal carotid artery using the intraluminal method in mice. Ischemia was maintained for 2 hours followed by 22 hours of reperfusion, during which either lutein (0.2 mg/kg) or vehicle was administered. Flash electroretinogram (flash ERG) and glial fibrillary acidic protein (GFAP) activation were assessed. Lutein's effect on Müller cells was further evaluated in immortalized rat Müller cells (rMC-1) challenged with cobalt chloride-induced hypoxia. Levels of IL-1β, cyclooxygenase-2 (Cox-2), TNFα, and nuclear factor-NF-kappa-B (NF-κB) were examined by Western blot analysis. Lutein treatment minimized deterioration of b-wave/a-wave ratio and oscillatory potentials as well as inhibited up-regulation of GFAP in retinal I/R injury. In cultured Müller cells, lutein treatment increased cell viability and reduced level of nuclear NF-κB, IL-1β, and Cox-2, but not TNFα after hypoxic injury. Reduced gliosis in I/R retina was observed with lutein treatment, which may contribute to preserved retinal function. Less production of pro-inflammatory factors from Müller cells suggested an anti-inflammatory role of lutein in retinal ischemic/hypoxic injury. Together with our previous studies, our results suggest that lutein protected the retina from ischemic/hypoxic damage by its anti-oxidative, anti-apoptotic, and anti-inflammatory properties. Show less
no PDF DOI: 10.1167/iovs.12-10007
RMC1
Bei Cui, Jin-Hua Sun, Fen-Fen Xiang +2 more · 2012 · Experimental eye research · Elsevier · added 2026-04-24
Diabetic retinopathy is a leading cause of reduced visual acuity and acquired blindness. Diabetes is known to alter the amount of retinal expression of the water-selective channels aquaporin 4 (AQP4). Show more
Diabetic retinopathy is a leading cause of reduced visual acuity and acquired blindness. Diabetes is known to alter the amount of retinal expression of the water-selective channels aquaporin 4 (AQP4). However, the function and impact of AQP4 in diabetic retinopathy is not well understood. In the present work, diabetes was induced by intraperitoneal injection of streptozotocin in Sprague-Dawley rats. Two weeks later, AQP4 shRNA (r) lentiviral particles or negative lentiviral particles were delivered by intravitreal injection to the eyes. Gene delivery was confirmed by quantitative reverse-transcriptase polymerase chain reaction (qRT-PCR) and Western blotting analysis. Eight weeks later, BRB breakdown was measured using Evans blue dye. Images of retinal sections were obtained and the thicknesses of the retinas were determined. Retinal leukostasis measurement was performed using acridine orange leukocyte fluorography. The mRNA levels of IL-1β, IL-6, intercellular adhesion molecule 1 (ICAM-1), glial fibrillary acidic protein (GFAP) and vascular endothelial growth factor (VEGF) were determined using qRT-PCR method. AQP4 shRNA (r) lentiviral particles or negative lentiviral particles were transfected into rMC-1 cells to investigate its effect on inflammation induced by high glucose. Incubation with IL-1β or IL-6 was performed to test their effect on AQP4 expression in rMC-1 cells. In the current work, it was found that AQP4 expression was enhanced in the retina of diabetic rats. AQP4 knockdown led to exacerbation of retinopathy including enhancing retinal vascular permeability, retinal thickness, pro-inflammatory factors expression, and VEGF and GFAP expression in retinas of diabetic rats. AQP4 knockdown enhanced the expression of pro-inflammatory cytokines induced by high glucose in rMC-1 cells. In addition, AQP4 knockdown enhanced the release of IL-6 and VEGF from rMC-1 cells into the medium. Moreover, it was found that incubation with IL-1β or IL-6 suppressed AQP4 expression in rMC-1 cells. These results suggested that streptozotocin injection induced diabetes resulted in compensatory increases of AQP4 expression, and downregulation of AQP4 exacerbated diabetic retinopathy through aggravating inflammatory response, at last in part. Therefore, regulation of retinal function by AQP4 may attenuate diabetic retinopathy, offering a promising therapeutic strategy for diabetic retinopathy. Show less
no PDF DOI: 10.1016/j.exer.2012.02.013
RMC1
You-Wen Qian, Yao Chen, Wen Yang +13 more · 2012 · Gastroenterology · added 2026-04-24
Hepatocellular carcinoma (HCC) is believed to arise from tumor-initiating cells (T-ICs), although little is known about their stem cell-like properties. We quantified levels of p28(GANK) (Gankyrin), O Show more
Hepatocellular carcinoma (HCC) is believed to arise from tumor-initiating cells (T-ICs), although little is known about their stem cell-like properties. We quantified levels of p28(GANK) (Gankyrin), OV6, and Oct4 in 130 human HCC samples using immunohistochemistry. Magnetic-activated cell sorting was used to isolate OV6+ HCC cells. T-IC properties were evaluated by quantitative reverse-transcription polymerase chain reaction, flow cytometry, and spheroid formation. We used a coimmunoprecipitation assay to study interactions among p28(GANK), Oct4, and WWP2. Tumorigenicity and pulmonary metastasis were examined in nonobese diabetic and severe combined immunodeficient mice. In HCC samples, high levels of p28(GANK) correlated with expansion of OV6+ tumor cells; the combination of high levels of p28(GANK) and OV6 was associated with progression of HCC. p28(GANK) was predominantly expressed in liver T-ICs, isolated by magnetic sorting, and undifferentiated primary HCC spheroids. Increased levels of p28(GANK) in T-ICs increased their percentages in HCC samples, expression of stem cell genes, self-renewal potential, chemoresistance in vitro, and tumorigenicity and ability to develop into pulmonary metastases in mice. Conversely, knockdown of p28(GANK) reduced their T-IC properties. p28(GANK) likely activates liver T-ICs by impeding ubiquitination and degradation of the transcription factor Oct4 by WWP2. In support of this concept, levels of p28(GANK) correlated with those of Oct4 in HCC samples. p28(GANK) activates and maintains liver T-ICs in HCCs by preventing degradation of Oct4. Inhibitors of p28(GANK) might therefore be developed to inactivate T-ICs and slow tumor progression. Show less
no PDF DOI: 10.1053/j.gastro.2012.02.042
WWP2
Jonathan W Day, Pengyun Li, James T Patterson +4 more · 2011 · Journal of peptide science : an official publication of the European Peptide Society · Wiley · added 2026-04-24
Glucagon and glucagon-like peptide-1 (GLP-1)are two structurally related hormones that acutely regulate glucose control in opposite directions through homologous receptors. The molecular basis for sel Show more
Glucagon and glucagon-like peptide-1 (GLP-1)are two structurally related hormones that acutely regulate glucose control in opposite directions through homologous receptors. The molecular basis for selectivity between these two hormones and their receptors is of physiological and medicinal importance. The application of co-agonists to enhance body weight reduction and correct multiple abnormalities associated with the metabolic syndrome has recently been reported. Substitution of amino acids 16, 18, and 20 in glucagon with those found in GLP-1 and exendin-4 were identified as partial contributors to balanced, high potency receptor action. The amidation of the C-terminus was an additional glucagon-based structural change observed to be of seminal importance to discriminate recognition by both receptors. In this work, the molecular basis for receptor selectivity associated with differences in C-terminal peptide sequence has been determined. A single charge inversion in glucagon and GLP-1 receptor sequence at position 68* was determined to significantly alter hormone action. Changing E68* in GLP-1R to the corresponding Lys of GCGR reduced receptor activity for natural GLP-1 hormones by eightfold. The enhanced C-terminal positive charges in GLP-1 peptides favor the native receptor's negative charge at position 68*, while the unfavorable interaction with the C-terminal acid of native glucagon is minimized by amidation. The extension of these observations to other glucagon-related hormones such as oxyntomodulin and exendin, as well as other related receptors such as GIPR, should assist in the assembly of additional hormones with broadened pharmacology. Show less
no PDF DOI: 10.1002/psc.1317
GIPR
Anniwaer Abulizi, Shan Yuan, Yi-tong Ma +7 more · 2011 · Zhonghua yi xue za zhi · added 2026-04-24
To explore the distribution characteristics of apolipoprotein A5 (ApoA5) gene c.553G > T polymorphism and the relationship of serum lipid in Chinese Han and Uighur populations in Xinjiang, China. The Show more
To explore the distribution characteristics of apolipoprotein A5 (ApoA5) gene c.553G > T polymorphism and the relationship of serum lipid in Chinese Han and Uighur populations in Xinjiang, China. The genotypes of ApoA5 gene c.553G > T polymorphism were detected in 406 Uighur and 527 Han people by polymerase chain reaction and restriction fragment length polymorphism (PCR-RFLP). The frequencies of GG, GT and TT genotypes of ApoA5 gene c.553G > T were 378 (93.1%), 27 (6.7%) and 1 (0.25%) patients in Uighurs versus 478 (90.7%) patients, 49 (9.3%) patients and 0% in Hans. There was no significant difference in the distribution of genotypes between two groups (P > 0.05). In both groups, individuals with T allele (TT + GT genotype) had a higher level of serum triglyceride than those with GG genotype. After adjusting for gender, age, smoking, alcoholism, body mass index, blood pressure and blood lipid, non-conditional logistic regression analyses revealed that individuals with T allele (TT + GT genotype) in both groups had an elevated risk of HTG versus the GG genotype (OR = 3.31, 95%CI: 1.31 - 8.36 in Uighurs vs OR = 3.98, 95%CI: 1.81 - 8.74 in Hans). The mutation of c.553G > T polymorphism of ApoA5 gene is associated with the level of serum triglyceride in Uighur and Han populations of Xinjiang. And T allele may be a risk factor of hypertriglyceridemia. Show less
no PDF
APOA5
Z Zhang, B Peng, R R Gong +6 more · 2011 · Bioscience trends · added 2026-04-24
The relation has not been reported consistently between the polymorphisms in the gene of apolipoprotein A5 (APO A5) and coronary artery disease (CAD). To clarify the discrepancy, we conducted a compre Show more
The relation has not been reported consistently between the polymorphisms in the gene of apolipoprotein A5 (APO A5) and coronary artery disease (CAD). To clarify the discrepancy, we conducted a comprehensive search of PubMed and EMBASE for all available casecontrol studies to explore the association between two APO A5 polymorphisms and CAD. Two reviewers independently selected studies. Statistical analyses were carried out using the STATA software package v 10.0. Thirteen studies investigated the association between the APO A5 -1131T>C polymorphism and risk of CAD were selected in this meta-analysis with 5,050 cases and 7,272 controls. For the S19W APO A5 gene polymorphism, 5 studies were included with 2,196 cases and 3,933 controls. We observed a significant statistical association between Apo A5 -1131T>C polymorphism and CAD (recessive genetic model: OR = 1.73, 95% CI = 1.37-2.19; dominant genetic model: OR = 1.42, 95% CI = 1.25-1.61; allelic contrast: OR = 1.31, 95% CI = 1.22-1.39, respectively). After restricting our analysis to Chinese individuals, we found that the association was stronger. We also observed strong association between the APO A5 S19>W polymorphism and risk of CAD under a recessive genetic model. This meta-analysis reveals that the minor allele of the -1131T>C polymorphism in the promoter of APO A5 gene significantly increases the susceptibility to CAD. This effect is more pronounced in Chinese subjects. Show less
no PDF DOI: 10.5582/bst.2011.v5.4.165
APOA5