👤 Y L Yang

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Also published as: A Yang, A-Li Yang, Acong Yang, Ai-Lun Yang, Aige Yang, Airong Yang, Aiting Yang, Aizhen Yang, Albert C Yang, Alex J T Yang, An-Qi Yang, Andrew Yang, Angang Yang, Angela Wei Hong Yang, Anni Yang, Aram Yang, B Yang, Baigao Yang, Baixia Yang, Bangjia Yang, Bao Yang, Baofeng Yang, Baoli Yang, Baoxin Yang, Baoxue Yang, Bei Yang, Beibei Yang, Biao Yang, Bin Q Yang, Bin Yang, Bing Xiang Yang, Bing Yang, Bingyu Yang, Bo Yang, Bohui Yang, Boo-Keun Yang, Bowen Yang, Boya Yang, Burton B Yang, Byoung Chul Yang, Caimei Yang, Caixia Yang, Caixian Yang, Caixin Yang, Can Yang, Canchai Yang, Ce Yang, Celi Yang, Chan Mo Yang, Chan-Mo Yang, Chang Yang, Chang-Hao Yang, Changheng Yang, Changqing Yang, Changsheng Yang, Changwei Yang, Changyun Yang, Chanjuan Yang, Chao Yang, Chao-Yuh Yang, Chaobo Yang, Chaofei Yang, Chaogang Yang, Chaojie Yang, Chaolong Yang, Chaoping Yang, Chaoqin Yang, Chaoqun Yang, Chaowu Yang, Chaoyun Yang, Chaozhe Yang, Chen Die Yang, Chen Yang, Cheng Yang, Cheng-Gang Yang, Chengfang Yang, Chenghao Yang, Chengkai Yang, Chengkun Yang, Chengran Yang, Chenguang Yang, Chengyingjie Yang, Chengzhang Yang, Chensi Yang, Chensu Yang, Chenxi Yang, Chenyu Yang, Chenzi Yang, Chi Yang, Chia-Wei Yang, Chieh-Hsin Yang, Chien-Wen Yang, Chih-Hao Yang, Chih-Min Yang, Chih-Yu Yang, Chihyu Yang, Ching-Fen Yang, Ching-Wen Yang, Chongmeng Yang, Chuan He Yang, Chuan Yang, Chuanbin Yang, Chuang Yang, Chuanli Yang, Chuhu Yang, Chun Yang, Chun-Chun Yang, Chun-Mao Yang, Chun-Seok Yang, Chunbaixue Yang, Chung-Hsiang Yang, Chung-Shi Yang, Chung-Yi Yang, Chunhua Yang, Chunhui Yang, Chunjie Yang, Chunjun Yang, Chunlei Yang, Chunli Yang, Chunmao Yang, Chunping Yang, Chunqing Yang, Chunru Yang, Chunxiao Yang, Chunyan Yang, Chunyu Yang, Congyi Yang, Cui Yang, Cuiwei Yang, Cunming Yang, Dai-Qin Yang, Dan Yang, Dan-Dan Yang, Dan-Hui Yang, Dandan Yang, Danlu Yang, Danrong Yang, Danzhou Yang, Dapeng Yang, De-Hua Yang, De-Zhai Yang, Decao Yang, Defu Yang, Deguang Yang, Dehao Yang, Dehua Yang, Dejun Yang, Deli Yang, Dengfa Yang, Deok Chun Yang, Deshuang Yang, Di Yang, Dianqiang Yang, Ding Yang, Ding-I Yang, Diya Yang, Diyuan Yang, Dong Yang, Dong-Hua Yang, Dongfeng Yang, Dongjie Yang, Dongliang Yang, Dongmei Yang, Dongren Yang, Dongshan Yang, Dongwei Yang, Dongwen Yang, DuJiang Yang, Eddy S Yang, Edwin Yang, Ei-Wen Yang, Emily Yang, Enlu Yang, Enzhi Yang, Eric Yang, Eryan Yang, Ethan Yang, Eunho Yang, Fajun Yang, Fan Yang, Fang Yang, Fang-Ji Yang, Fang-Kun Yang, Fei Yang, Feilong Yang, Feiran Yang, Feixiang Yang, Fen Yang, Feng Yang, Feng-Ming Yang, Feng-Yun Yang, Fengjie Yang, Fengjiu Yang, Fengjuan Yang, Fenglian Yang, Fengling Yang, Fengping Yang, Fengying Yang, Fengyong Yang, Fu Yang, Fude Yang, Fuhe Yang, Fuhuang Yang, Fumin Yang, Fuquan Yang, Furong Yang, Fuxia Yang, Fuyao Yang, G Y Yang, G Yang, Gan Yang, Gang Yang, Gangyi Yang, Gao Yang, Gaohong Yang, Gaoxiang Yang, Ge Yang, Gong Yang, Gong-Li Yang, Grace H Y Yang, Guan Yang, Guang Yang, Guangdong Yang, Guangli Yang, Guangwei Yang, Guangyan Yang, Guanlin Yang, Gui-Zhi Yang, Guigang Yang, Guitao Yang, Guo Yang, Guo-Can Yang, Guobin Yang, Guofen Yang, Guojun Yang, Guokun Yang, Guoli Yang, Guomei Yang, Guoping Yang, Guoqi Yang, Guosheng Yang, Guotao Yang, Guowang Yang, Guowei Yang, H X Yang, H Yang, Hai Yang, Hai-Chun Yang, Haibo Yang, Haihong Yang, Haikun Yang, Hailei Yang, Hailing Yang, Haiming Yang, Haiping Yang, Haiqiang Yang, Haitao Yang, Haixia Yang, Haiyan Yang, Haiying Yang, Han Yang, Hanchen Yang, Handong Yang, Hang Yang, Hannah Yang, Hanseul Yang, Hanteng Yang, Hao Yang, Hao-Jan Yang, HaoXiang Yang, Haojie Yang, Haolan Yang, Haoqing Yang, Haoran Yang, Haoyu Yang, Harrison Hao Yang, Hee Joo Yang, Heng Yang, Hengwen Yang, Henry Yang, Heqi Yang, Heyi Yang, Heyun Yang, Hoe-Saeng Yang, Hong Yang, Hong-Fa Yang, Hong-Li Yang, HongMei Yang, Hongbing Yang, Hongbo Yang, Hongfa Yang, Honghong Yang, Hongjie Yang, Hongjun Yang, Hongli Yang, Hongling Yang, Hongqun Yang, Hongxia Yang, Hongxin Yang, Hongyan Yang, Hongyu Yang, Hongyuan Yang, Hongyue Yang, Howard H Yang, Howard Yang, Hsin-Chou Yang, Hsin-Jung Yang, Hsin-Sheng Yang, Hua Yang, Hua-Yuan Yang, Huabing Yang, Huafang Yang, Huaijie Yang, Huan Yang, Huanhuan Yang, Huanjie Yang, Huanming Yang, Huansheng Yang, Huanyi Yang, Huarong Yang, Huaxiao Yang, Huazhao Yang, Hui Yang, Hui-Ju Yang, Hui-Li Yang, Hui-Ting Yang, Hui-Yu Yang, Hui-Yun Yang, Huifang Yang, Huihui Yang, Huijia Yang, Huijie Yang, Huiping Yang, Huiran Yang, Huixia Yang, Huiyu Yang, Hung-Chih Yang, Hwai-I Yang, Hye Jeong Yang, Hyerim Yang, Hyun Suk Yang, Hyun-Sik Yang, Ill Yang, Ivana V Yang, J S Yang, J Yang, James Y Yang, Jaw-Ji Yang, Jee Sun Yang, Jenny J Yang, Jerry Yang, Ji Hye Yang, Ji Yang, Ji Yeong Yang, Ji-chun Yang, Jia Yang, Jia-Ling Yang, Jia-Ying Yang, Jiahong Yang, Jiahui Yang, Jiajia Yang, Jiakai Yang, Jiali Yang, Jialiang Yang, Jian Yang, Jian-Bo Yang, Jian-Jun Yang, Jian-Ming Yang, Jian-Ye Yang, JianHua Yang, JianJun Yang, Jianbo Yang, Jiang-Min Yang, Jiang-Yan Yang, Jianing Yang, Jianke Yang, Jianli Yang, Jianlou Yang, Jianmin Yang, Jianming Yang, Jianqi Yang, Jianwei Yang, Jianyu Yang, Jiao Yang, Jiarui Yang, Jiawei Yang, Jiaxin Yang, Jiayan Yang, Jiayi Yang, Jiaying Yang, Jiayue Yang, Jichun Yang, Jie Yang, Jie-Cheng Yang, Jie-Hong Yang, Jie-Kai Yang, Jiefeng Yang, Jiehong Yang, Jieping Yang, Jiexiang Yang, Jihong Yang, Jimin Yang, Jin Yang, Jin-Jian Yang, Jin-Kui Yang, Jin-gang Yang, Jin-ju Yang, Jinan Yang, Jinfeng Yang, Jing Yang, Jing-Quan Yang, Jing-Yu Yang, Jingang Yang, Jingfeng Yang, Jinggang Yang, Jinghua Yang, Jinghui Yang, Jingjing Yang, Jingmin Yang, Jingping Yang, Jingran Yang, Jingshi Yang, Jingwen Yang, Jingya Yang, Jingyan Yang, Jingyao Yang, Jingye Yang, Jingyu Yang, Jingyun Yang, Jingze Yang, Jinhua Yang, Jinhui Yang, Jinjian Yang, Jinpeng Yang, Jinru Yang, Jinshan Yang, Jinsong Yang, Jinsung Yang, Jinwen Yang, Jinzhao Yang, Jiong Yang, Ju Dong Yang, Ju Young Yang, Juan Yang, Juesheng Yang, Jumei Yang, Jun J Yang, Jun Yang, Jun-Hua Yang, Jun-Xia Yang, Jun-Xing Yang, Junbo Yang, Jung Dug Yang, Jung Wook Yang, Jung-Ho Yang, Junhan Yang, Junjie Yang, Junlin Yang, Junlu Yang, Junping Yang, Juntao Yang, Junyao Yang, Junyi Yang, Kai Yang, Kai-Chien Yang, Kai-Chun Yang, Kaidi Yang, Kaifeng Yang, Kaijie Yang, Kaili Yang, Kailin Yang, Kaiwen Yang, Kang Yang, Kang Yi Yang, Kangning Yang, Karen Yang, Ke Yang, Keming Yang, Keping Yang, Kexin Yang, Kuang-Yao Yang, Kui Yang, Kun Yang, Kunao Yang, Kunqi Yang, Kunyu Yang, Kuo Tai Yang, L Yang, Lamei Yang, Lan Yang, Le Yang, Lei Yang, Lexin Yang, Leyi Yang, Li Chun Yang, Li Yang, Li-Kun Yang, Li-Qin Yang, Li-li Yang, LiMan Yang, Lian-he Yang, Liang Yang, Liang-Yo Yang, Liangbin Yang, Liangle Yang, Liangliang Yang, Lichao Yang, Lichuan Yang, Licong Yang, Liehao Yang, Lihong Yang, Lihua Yang, Lihuizi Yang, Lijia Yang, Lijie Yang, Lijuan Yang, Lijun Yang, Lili Yang, Lin Sheng Yang, Lin Yang, Lina Yang, Ling Ling Yang, Ling Yang, Lingfeng Yang, Lingling Yang, Lingzhi Yang, Linlin Yang, Linnan Yang, Linqing Yang, Linquan Yang, Lipeng Yang, Liping Yang, Liting Yang, Liu Yang, Liu-Kun Yang, LiuMing Yang, Liuliu Yang, Liwei Yang, Lixian Yang, Lixue Yang, Long In Yang, Long Yang, Long-Yan Yang, Longbao Yang, Longjun Yang, Longyan Yang, Lu M Yang, Lu Yang, Lu-Hui Yang, Lu-Kun Yang, Lu-Qin Yang, Luda Yang, Man Yang, Manqing Yang, Maojie Yang, Maoquan Yang, Mei Yang, Meichan Yang, Meihua Yang, Meili Yang, Meiting Yang, Meixiang Yang, Meiying Yang, Meng Yang, Menghan Yang, Menghua Yang, Mengjie Yang, Mengli Yang, Mengliu Yang, Mengmeng Yang, Mengsu Yang, Mengwei Yang, Mengying Yang, Miaomiao Yang, Mickey Yang, Min Hee Yang, Min Yang, Mina Yang, Ming Yang, Ming-Hui Yang, Ming-Yan Yang, Minghui Yang, Mingjia Yang, Mingjie Yang, Mingjun Yang, Mingli Yang, Mingqian Yang, Mingshi Yang, Mingyan Yang, Mingyu Yang, Minyi Yang, Misun Yang, Mu Yang, Muh-Hwa Yang, Na Yang, Nan Yang, Nana Yang, Nanfei Yang, Neil V Yang, Ni Yang, Ning Yang, Ningjie Yang, Ningli Yang, Pan Yang, Pan-Chyr Yang, Paul Yang, Peichang Yang, Peiran Yang, Peiyan Yang, Peiying Yang, Peiyuan Yang, Peizeng Yang, Peng Yang, Peng-Fei Yang, PengXiang Yang, Pengfei Yang, Penghui Yang, Pengwei Yang, Pengyu Yang, Phillip C Yang, Pin Yang, Ping Yang, Ping-Fen Yang, Pinghong Yang, Pu Yang, Q H Yang, Q Yang, Qi Yang, Qi-En Yang, Qian Yang, Qian-Jiao Yang, Qian-Li Yang, QianKun Yang, Qiang Yang, Qianhong Yang, Qianqian Yang, Qianru Yang, Qiaoli Yang, Qiaorong Yang, Qiaoyuan Yang, Qifan Yang, Qifeng Yang, Qiman Yang, Qimeng Yang, Qiming Yang, Qin Yang, Qinbo Yang, Qing Yang, Qing-Cheng Yang, Qingcheng Yang, Qinghu Yang, Qingkai Yang, Qinglin Yang, Qingling Yang, Qingmo Yang, Qingqing Yang, Qingtao Yang, Qingwu Yang, Qingya Yang, Qingyan Yang, Qingyi Yang, Qingyu Yang, Qingyuan Yang, Qiong Yang, Qiu Yang, Qiu-Yan Yang, Qiuhua Yang, Qiuhui Yang, Qiulan Yang, Qiuli Yang, Qiuxia Yang, Qiwei Yang, Qiwen Yang, Quan Yang, Quanjun Yang, Quanli Yang, Qun-Fang Yang, R Yang, Ran Yang, Ren-Zhi Yang, Renchi Yang, Renhua Yang, Renjun Yang, Renqiang Yang, Renzhi Yang, Ri-Yao Yang, Richard K Yang, Robert Yang, Rong Yang, Rongrong Yang, Rongxi Yang, Rongyuan Yang, Rongze Yang, Rui Xu Yang, Rui Yang, Rui-Xu Yang, Rui-Yi Yang, Ruicheng Yang, Ruifang Yang, Ruihua Yang, Ruilan Yang, Ruili Yang, Ruiqin Yang, Ruirui Yang, Ruiwei Yang, Rulai Yang, Ruming Yang, Run Yang, Runjun Yang, Runxu Yang, Runyu Yang, Runzhou Yang, Ruocong Yang, Ruoyun Yang, Ruyu Yang, S J Yang, Se-Ran Yang, Sen Yang, Senwen Yang, Seung Yun Yang, Seung-Jo Yang, Seung-Ok Yang, Shan Yang, Shangchen Yang, Shanghua Yang, Shangwen Yang, Shanzheng Yang, Shao-Hua Yang, Shaobin Yang, Shaohua Yang, Shaoling Yang, Shaoqi Yang, Shaoqing Yang, Sheng Sheng Yang, Sheng Yang, Sheng-Huei Yang, Sheng-Qian Yang, Sheng-Wu Yang, ShengHui Yang, Shenglin Yang, Shengnan Yang, Shengqian Yang, Shengyong Yang, Shengzhuang Yang, Shenhui Yang, Shi-Ming Yang, Shiaw-Der Yang, Shifeng Yang, Shigao Yang, Shijie Yang, Shiming Yang, Shipeng Yang, Shiping Yang, Shiu-Ju Yang, Shiyi Yang, Shizhong Yang, Shizhuo Yang, Shu Yang, ShuSheng Yang, Shuai Yang, Shuaibing Yang, Shuaini Yang, Shuang Yang, Shuangshuang Yang, Shucai Yang, Shufang Yang, Shuhua Yang, Shujuan Yang, Shujun Yang, Shulan Yang, Shulin Yang, Shuming Yang, Shun-Fa Yang, Shuo Yang, Shuofei Yang, Shuping Yang, Shuqi Yang, Shuquan Yang, Shurong Yang, Shushen Yang, Shuye Yang, Shuyu Yang, Si Yang, Si-Fu Yang, Sibao Yang, Sibo Yang, Sichong Yang, Sihui Yang, Sijia Yang, Siqi Yang, Sirui Yang, Sisi Yang, Sitao Yang, Siwen Yang, Siyi Yang, Siyu Yang, Sizhen Yang, Sizhu Yang, Song Yang, Song-na Yang, Songpeng Yang, Songye Yang, Soo Hyun Yang, Su Yang, Su-Geun Yang, Suhong Yang, Sujae Yang, Sujuan Yang, Suk-Kyun Yang, Sun Kyung Yang, Suwol Yang, Suxia Yang, Suyi Yang, Suyu Yang, Tai-Hui Yang, Tailai Yang, Tao Yang, Tengyun Yang, Thomas P Yang, Ti Yang, Tian Yang, Tianbao Yang, Tianfeng Yang, Tianjie Yang, Tianmin Yang, Tianpeng Yang, Tianqiong Yang, Tiantian Yang, Tianxin Yang, Tianyou Yang, Tianyu Yang, Tianze Yang, Tianzhong Yang, Ting Yang, Ting-Xian Yang, Tingting Yang, Tingyu Yang, Tong Yang, Tong Yi Yang, Tong-Xin Yang, Tonglin Yang, Tongren Yang, Tuanmin Yang, Ueng-Cheng Yang, W Yang, Wan-Chen Yang, Wan-Jung Yang, Wang Yang, Wannian Yang, Wei Qiang Yang, Wei Yang, Wei-Fa Yang, Wei-Xin Yang, Weidong Yang, Weiguang Yang, Weihan Yang, Weijian Yang, Weili Yang, Weimin Yang, Weiran Yang, Weiwei Yang, Weixian Yang, Weizhong Yang, Wen Yang, Wen Z Yang, Wen-Bin Yang, Wen-Chin Yang, Wen-He Yang, Wen-Hsuan Yang, Wen-Ming Yang, Wen-Wen Yang, Wen-Xiao Yang, WenKai Yang, Wenbo Yang, Wenchao Yang, Wending Yang, Wenfei Yang, Wenhong Yang, Wenhua Yang, Wenhui Yang, Wenjian Yang, Wenjie Yang, Wenjing Yang, Wenjuan Yang, Wenjun Yang, Wenli Yang, Wenlin Yang, Wenming Yang, Wenqin Yang, Wenshan Yang, Wentao Yang, Wenwen Yang, Wenwu Yang, Wenxin Yang, Wenxing Yang, Wenying Yang, Wenzhi Yang, Wenzhu Yang, William Yang, Woong-Suk Yang, Wu Yang, Wu-de Yang, X Yang, X-J Yang, Xi Yang, Xi-You Yang, Xia Yang, Xian Yang, Xiang Yang, Xiang-Hong Yang, Xiang-Jun Yang, Xianggui Yang, Xianghong Yang, Xiangliang Yang, Xiangling Yang, Xiangqiong Yang, Xiangxiang Yang, Xiangyu Yang, Xiao Yang, Xiao-Dong Yang, Xiao-Fang Yang, Xiao-Hong Yang, Xiao-Jie Yang, Xiao-Juan Yang, Xiao-Meng Yang, Xiao-Ming Yang, Xiao-Qian Yang, Xiao-Yan Yang, Xiao-Ying Yang, Xiao-Yu Yang, Xiao-guang Yang, XiaoYan Yang, Xiaoao Yang, Xiaobin Yang, Xiaobo Yang, Xiaochen Yang, Xiaodan Yang, Xiaodi Yang, Xiaodong Yang, Xiaofei Yang, Xiaofeng Yang, Xiaohao Yang, Xiaohe Yang, Xiaohong R Yang, Xiaohong Yang, Xiaohuang Yang, Xiaohui Yang, Xiaojian Yang, Xiaojie Yang, Xiaojing Yang, Xiaojuan Yang, Xiaojun Yang, Xiaoli Yang, Xiaolu Yang, Xiaomeng Yang, Xiaoming Yang, Xiaonan Yang, Xiaoping Yang, Xiaoqian Yang, Xiaoqin Yang, Xiaoqun Yang, Xiaorong Yang, Xiaoshan Yang, Xiaoshi Yang, Xiaosong Yang, Xiaotian Yang, Xiaotong Yang, Xiaowei Yang, Xiaowen Yang, Xiaoxiao Yang, Xiaoxin Yang, Xiaoxu Yang, Xiaoyao Yang, Xiaoyi Yang, Xiaoyong Yang, Xiaoyu Yang, Xiaoyun Yang, Xiaozhen Yang, Xifei Yang, Xiling Yang, Ximan Yang, Xin Yang, Xin-He Yang, Xin-Yu Yang, Xin-Zhuang Yang, Xing Yang, Xinghai Yang, Xinglong Yang, Xingmao Yang, Xingming Yang, Xingsheng Yang, Xingyu Yang, Xingyue Yang, Xingzhi Yang, Xinjing Yang, Xinming Yang, Xinpu Yang, Xinwang Yang, Xinxin Yang, Xinyan Yang, Xinyi Yang, Xinyu Yang, Xinyue Yang, Xiong Ling Yang, Xiru Yang, Xitong Yang, Xiu Hong Yang, Xiuhua Yang, Xiulin Yang, Xiuna Yang, Xiuqin Yang, Xiurong Yang, Xiuwei Yang, Xiwen Yang, Xiyue Yang, Xu Yang, Xuan Yang, Xue Yang, Xue-Feng Yang, Xue-Ping Yang, Xuecheng Yang, Xuehan Yang, Xuejing Yang, Xuejun Yang, Xueli Yang, Xuena Yang, Xueping Yang, Xuesong Yang, Xuhan Yang, Xuhui Yang, Xuping Yang, Xuyang Yang, Y C Yang, Y F Yang, Y P Yang, Y Q Yang, Y Yang, Y-T Yang, Ya Yang, Ya-Chen Yang, Yadong Yang, Yafang Yang, Yajie Yang, Yalan Yang, Yali Yang, Yaming Yang, Yan Yang, Yan-Bei Yang, Yan-Ling Yang, Yanan Yang, Yanfang Yang, Yang Yang, Yangfan Yang, Yangyang Yang, Yanhui Yang, Yanjianxiong Yang, Yanling Yang, Yanmei Yang, Yanmin Yang, Yanping Yang, Yanru Yang, Yanting Yang, Yanyan Yang, Yanzhen Yang, Yaorui Yang, Yaping Yang, Yaqi Yang, Yaxi Yang, Ye Yang, Yefa Yang, Yefeng Yang, Yeqing Yang, Yexin Yang, Yi Yang, Yi-Chieh Yang, Yi-Fang Yang, Yi-Feng Yang, Yi-Liang Yang, Yi-Ping Yang, Yi-ning Yang, Yibing Yang, Yichen Yang, Yidong Yang, Yifan Yang, Yifang Yang, Yifei Yang, Yifeng Yang, Yihe Yang, Yijie Yang, Yilian Yang, Yimei Yang, Yimin Yang, Yiming Yang, Yimu Yang, Yin-Rong Yang, Yinfeng Yang, Ying Yang, Ying-Hua Yang, Ying-Ying Yang, Yingdi Yang, Yingjun Yang, Yingqing Yang, Yingrui Yang, Yingxia Yang, Yingyu Yang, Yinhua Yang, Yining Yang, Yinxi Yang, Yiping Yang, Yiting Yang, Yiyi Yang, Yiying Yang, Yong Yang, Yong-Yu Yang, Yongfeng Yang, Yongguang Yang, Yonghong Yang, Yonghui Yang, Yongjia Yang, Yongjie Yang, Yongkang Yang, Yongqiang Yang, Yongsan Yang, Yongxin Yang, Yongxing Yang, Yongzhong Yang, Yoon La Yang, Yoon Mee Yang, Youhua Yang, YoungSoon Yang, Yu Yang, Yu-Fan Yang, Yu-Feng Yang, Yu-Jie Yang, Yu-Shi Yang, Yu-Tao Yang, Yu-Ting Yang, Yuan Yang, Yuan-Han Yang, Yuan-Jian Yang, Yuanhao Yang, Yuanjin Yang, Yuanquan Yang, Yuanrong Yang, Yuanying Yang, Yuanzhang Yang, Yuanzhi Yang, Yuchen Yang, Yucheng Yang, Yue Yang, Yueh-Ning Yang, Yuejin Yang, Yuexiang Yang, Yueze Yang, Yufan Yang, Yuhan Yang, Yuhang Yang, Yuhua Yang, Yujie Yang, Yujing Yang, Yulin Yang, Yuling Yang, Yulong Yang, Yun Yang, YunKai Yang, Yunfan Yang, Yung-Li Yang, Yunhai Yang, Yunlong Yang, Yunmei Yang, Yunwen Yang, Yunyun Yang, Yunzhao Yang, Yupeng Yang, Yuqi Yang, Yuta Yang, Yutao Yang, Yuting Yang, Yutong Yang, Yuwei Yang, Yuxi Yang, Yuxing Yang, Yuxiu Yang, Yuyan Yang, Yuyao Yang, Yuying Yang, Z Yang, Zaibin Yang, Zaiming Yang, Zaiqing Yang, Zanhao Yang, Ze Yang, Zemin Yang, Zeng-Ming Yang, Zengqiang Yang, Zengqiao Yang, Zeyu Yang, Zhang Yang, Zhangping Yang, Zhanyi Yang, Zhao Yang, 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Yang, Ziheng Yang, Zijiang Yang, Zishan Yang, Zixia Yang, Zixuan Yang, Ziying Yang, Ziyou Yang, Ziyu Yang, Zong-de Yang, Zongfang Yang, Zongyu Yang, Zunxian Yang, Zuozhen Yang
articles
Srinivas B Narayan, Dinesh Rakheja, Johanne V Pastor +5 more · 2006 · Molecular genetics and metabolism · Elsevier · added 2026-04-24
Juvenile neuronal ceroid-lipofuscinosis (JNCL) or Batten/Spielmeyer-Vogt-Sjogren disease (OMIM #204200) is one of a group of nine clinically related inherited neurodegenerative disorders (CLN1-9). JNC Show more
Juvenile neuronal ceroid-lipofuscinosis (JNCL) or Batten/Spielmeyer-Vogt-Sjogren disease (OMIM #204200) is one of a group of nine clinically related inherited neurodegenerative disorders (CLN1-9). JNCL results from mutations in CLN3 on chromosome 16p12.1. The neuronal loss in Batten disease has been shown to be due to a combination of apoptosis and autophagy suggesting that CLN3P, the defective protein, may have an anti-neuronal death function. PANDER (PANcreatic-DERived factor) is a novel cytokine that was recently cloned from pancreatic islet cells. PANDER is specifically expressed in the pancreatic islets, small intestine, testis, prostate, and neurons of the central nervous system, and has been demonstrated to induce apoptosis. In this study, we over-expressed CLN3P in SH-SY5Y neuroblastoma cells and monitored the effects on PANDER-induced apoptosis. CLN3P significantly increased the survival rate of the SH-SY5Y cells in this system. This study provides additional evidence that the function of CLN3P is related to preventing neuronal apoptosis. Show less
no PDF DOI: 10.1016/j.ymgme.2006.01.011
CLN3
Chia-Houng Tsai, Sheng-Huei Yang, Ching-Ming Chien +5 more · 2006 · Clinical and experimental pharmacology & physiology · Blackwell Publishing · added 2026-04-24
Cardiotoxin III (CTX III) is a basic polypeptide with 60 amino acid residues isolated from Naja naja atra venom. This is the first report on the mechanism of the anticancer effect of CTX III in human Show more
Cardiotoxin III (CTX III) is a basic polypeptide with 60 amino acid residues isolated from Naja naja atra venom. This is the first report on the mechanism of the anticancer effect of CTX III in human colorectal cancer Colo205 cells. 2. Cardiotoxin III-induced Colo205 cell apoptosis was confirmed by DNA fragmentation (DNA ladder and sub-G1 formation) with an IC(50) of 4 mg/mL at 48 h. 3. Further mechanistic analysis demonstrate that CTX III induced the loss of mitochondrial membrane potential (Dym), cytochrome c release from mitochondria into the cytosol and activation of capase-9, caspase 3, as well as markedly enhancing the expression of Bax, but not Bcl-2, protein in the cells. Moreover, the CTX III-induced apoptosis was significantly blocked by the broad-spectrum caspase inhibitor benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone. 4. However, CTX III did not generate the formation of reactive oxygen species and anti-oxidants, including N-acetylcysteine, and catalase could not block CTX III-induced apoptosis in the Colo205 cells. 5. Taken together, these results suggest that CTX III may induce apoptosis through a mitochondrial- and caspase-dependent mechanism and alteration of Bax/Bcl-2 ratio in human colorectal Colo205 cancer cells. Show less
no PDF DOI: 10.1111/j.1440-1681.2006.04334.x
DYM
Xing-Hong Ma, Shi-Jun Hu, Hua Ni +8 more · 2006 · The Journal of biological chemistry · American Society for Biochemistry and Molecular Biology · added 2026-04-24
Although oligonucleotide chips, cDNA microarrays, differential display reverse transcription-PCR, and other approaches have been used to screen implantation-related molecules, the mechanism by which e Show more
Although oligonucleotide chips, cDNA microarrays, differential display reverse transcription-PCR, and other approaches have been used to screen implantation-related molecules, the mechanism by which embryo implantation occurs is still unknown. The aim of this study was to profile the differential gene expression between interimplantation site and implantation site in mouse uterus on day 5 of pregnancy by serial analysis of gene expression (SAGE). In our two SAGE libraries of 11-bp tags, the total numbers of tags sequenced were 48,121 for the interimplantation site and 50,227 for the implantation site. There were 1,039 tags specifically expressed at interimplantation site, and 1,252 tags specifically expressed at the implantation site. Based on the p value, there were 195 tags significantly up-regulated at the interimplantation site and 261 tags significantly up-regulated at the implantation site, of which 100 genes were single matched at the interimplantation site and 127 genes were single matched at the implantation site, respectively. By reverse transcription-PCR, the tag ratio between the implantation site and interimplantation site was verified on 14 significantly changed genes. Using in situ hybridization, 1810014L12Rik, Psmb5, Cd63, Npm1, Fads3, and Tagln2 were shown to be highly expressed at the implantation site compared with the interimplantation site. Compared with the interimplantation site, Ddx39 was strongly expressed in the subluminal stromal cells at the implantation site on day 5 of pregnancy. Ddx39 expression at the implantation site was specifically induced by active blastocysts. Additionally, Ddx39 expression was significantly up-regulated by estrogen in the ovariectomized mice. In our SAGE data, many implantation-related genes were identified in mouse uterus. Our data could be a valuable source for future study on embryo implantation. Show less
no PDF DOI: 10.1074/jbc.M511512200
FADS3
Shahrzad Abbasi, Jiing-Dwan Lee, Bing Su +5 more · 2006 · The Journal of biological chemistry · American Society for Biochemistry and Molecular Biology · added 2026-04-24
Calcineurin is a serine/threonine protein phosphatase that plays a critical role in many physiologic processes such as T-cell activation, skeletal myocyte differentiation, and cardiac hypertrophy. We Show more
Calcineurin is a serine/threonine protein phosphatase that plays a critical role in many physiologic processes such as T-cell activation, skeletal myocyte differentiation, and cardiac hypertrophy. We previously showed that active MEKK3 is capable of stimulating calcineurin/nuclear factor of activated T-cells (NFAT) signaling in cardiac myocytes through phosphorylation of modulatory calcineurin-interacting protein 1 (MCIP1). However, the protein kinases that function downstream of MEKK3 to mediate MCIP1 phosphorylation and the mechanism of MCIP1-mediated calcineurin regulation have not been defined. Here, we show that MEK5 and big MAP kinase 1 (BMK1) function downstream of MEKK3 in a signaling cascade that induces calcineurin activity through phosphorylation of MCIP1. Genetic studies showed that BMK1-deficient mouse lung fibroblasts failed to mediate MCIP1 phosphorylation and activate calcineurin/NFAT in response to angiotensin II, a potent NFAT activator. Conversely, restoring BMK1 to the deficient cells restored angiotensin II-mediated calcineurin/NFAT activation. Thus, using BMK1-deficient mouse lung fibroblast cells, we provided the genetic evidence that BMK1 is required for angiotensin II-mediated calcineurin/NFAT activation through MICP1 phosphorylation. Finally, we discovered that phosphorylated MCIP1 dissociates from calcineurin and binds with 14-3-3, thereby relieving its inhibitory effect on calcineurin activity. In summary, our findings reveal a previously unrecognized essential regulatory role of mitogen-activated protein kinase signaling in calcineurin activation through the reversible phosphorylation of a calcineurin-interacting protein, MCIP1. Show less
no PDF DOI: 10.1074/jbc.M510775200
MAP2K5
Wen-ling Liu, Wen-li Xie, Da-Yi Hu +11 more · 2006 · Zhonghua xin xue guan bing za zhi · added 2026-04-24
The aim of this study was to screen the disease-causing gene mutations and investigate the genotype-phenotype correlation in 10 Chinese pedigrees with familial hypertrophic cardiomyopathy (HCM). There Show more
The aim of this study was to screen the disease-causing gene mutations and investigate the genotype-phenotype correlation in 10 Chinese pedigrees with familial hypertrophic cardiomyopathy (HCM). There are 91 family members from these 10 pedigrees and 5 members were normal mutated carriers, 23 members were HCM patients (14 male) aged from 1.5 to 73 years old. The functional regions of myosin heavy chain gene (MYH7), cardiac myosin-binding protein C (MYBPC3) and cardiac troponin T gene (TNNT2) were screened with PCR and direct sequencing technique. Clinical information from all patients was also evaluated in regard to the genotype. Mutations were found in 5 out of 10 pedigrees. Mutations in MYH7 (Arg663His, Glu924Lys and Ile736Thr) were found in 3 pedigrees and 3 patients from these pedigrees suffered sudden death at age 20-48 years old during sport. Mutations in MYBPC3 were found in 2 pedigrees, 1 with complex mutation (Arg502Trp and splicing mutation IVS27 + 12C > T) and 1 with novel frame shift mutation (Gly347fs) and the latter pedigree has sudden death history. No mutation was identified in TNNT2. Although the Han Chinese is a relatively homogeneous ethnic group, different HCM gene mutations were responsible for familiar HCM suggesting the heterogeneity nature of the disease-causing genes and HCM MYH7 mutations are associated with a higher risk of sudden death in this cohort. Furthermore, identical mutation might result in different phenotypes suggesting that multiple factors might be involved in the pathogenesis of familiar HCM. Show less
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MYBPC3
Chao-Yu Hu, Chang-Hao Yang, Wei-Yu Chen +4 more · 2006 · Molecular vision · added 2026-04-24
To identify the changes in zebrafish embryonic ocular development after early growth response factor 1 (Egr1) gene knockdown by Egr1-specific translation inhibitor, morpholino oligonucleotides (MO). T Show more
To identify the changes in zebrafish embryonic ocular development after early growth response factor 1 (Egr1) gene knockdown by Egr1-specific translation inhibitor, morpholino oligonucleotides (MO). Two kinds of Egr1-MO were microinjected separately with various dosages into one to four celled zebrafish embryos to find an optimal dose generating an acceptable mortality rate and high frequency of specific phenotype. Chordin-MO served as the positive control; a 5 mismatch MO of Egr1-MO1 and a nonspecific MO served as negative controls. We graded the Egr1 morphants according to their gross abnormalities, and measured their ocular dimensions accordingly. Western blot analysis and synthetic Egr1 mRNA rescue experiments confirmed whether the deformities were caused by Egr1 gene knockdown. Histological examination and three kinds of immunohistochemical staining were applied to identify glutamate receptor one expression in retinal ganglion cells and amacrine cells, to recognize acetylated alpha-tubulin expression which indicated axonogenesis, and to label photoreceptor cells with zpr-1 antibody. After microinjection of 8 ng Egr1-MO1 or 2 ng Egr1-MO2, 81.8% and 97.3% of larvae at 72 h postfertilization had specific defects, respectively. The gross phenotype included string-like heart, flat head, and deformed tail. The more severely deformed larvae had smaller eyes and pupils. Co-injection of 8 ng Egr1-MO1 and supplementary 12 pg synthetic Egr1 mRNA reduced the gross abnormality rate from 84.4% to 29.7%, and decreased the severity of deformities. Egr1 protein appeared in the wildtype and rescued morphants, but was lacking in the Egr1 morphants with specific deformities. Lenses of Egr1 morphants were smaller and had some residual nucleated lens fiber cells. Morphants' retinal cells arranged disorderly and compactly with thin plexiform layers. Immunohistochemical studies showed that morphants had a markedly decreased number of mature retinal ganglion cells, amacrine cells, and photoreceptor cells. Retinal axonogenesis was prominently reduced in morphants. The Egr1 gene plays an important role in zebrafish embryonic oculogenesis. Ocular structures including lens and retina were primitive and lacked appropriate differentiation. Such arrested retinal and lenticular development in Egr1 morphants resulted in microphthalmos. Show less
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ZPR1
Xiaofa Qin, Hui Shen, Min Liu +5 more · 2005 · American journal of physiology. Gastrointestinal and liver physiology · added 2026-04-24
Glucagon-like peptide 1 (GLP-1) is a gastrointestinal hormone secreted in response to meal ingestion by enteroendocrine L cells located predominantly in the lower small intestine and large intestine. Show more
Glucagon-like peptide 1 (GLP-1) is a gastrointestinal hormone secreted in response to meal ingestion by enteroendocrine L cells located predominantly in the lower small intestine and large intestine. GLP-1 inhibits the secretion and motility of the upper gut and has been suggested to play a role in the "ileal brake." In this study, we investigated the effect of recombinant GLP-1-(7-36) amide (rGLP-1) on lipid absorption in the small intestine in intestinal lymph duct-cannulated rats. In addition, the effects of rGLP-1 on intestinal production of apolipoprotein (apo) B and apo A-IV, two apolipoproteins closely related to lipid absorption, were evaluated. rGLP-1 was infused through the jugular vein, and lipids were infused simultaneously through a duodenal cannula. Our results showed that infusion of rGLP-1 at 20 pmol.kg(-1).min(-1) caused a dramatic and prompt decrease in lymph flow from 2.22 +/- 0.15 (SE) ml/h at baseline (n = 6) to 1.24 +/- 0.06 ml/h at 2 h (P < 0.001). In contrast, a significant increase in lymph flow was observed in the saline (control) group: 2.19 +/- 0.20 and 3.48 +/- 0.09 ml/h at baseline and at 6 h of lipid infusion, respectively (P < 0.001). rGLP-1 also inhibited intestinal triolein absorption (P < 0.05) and lymphatic apo B and apo A-IV output (P < 0.05) but did not affect cholesterol absorption. In conclusion, rGLP-1 dramatically decreases intestinal lymph flow and reduces triglyceride absorption and apo B and apo A-IV production. These findings suggest a novel role for GLP-1 in lipid absorption. Show less
no PDF DOI: 10.1152/ajpgi.00303.2004
APOA4
Edward A Ruiz-Narváez, Yadong Yang, Yukiko Nakanishi +2 more · 2005 · Journal of lipid research · added 2026-04-24
Genetic variation in the APOC3 and APOA5 genes has been associated with plasma triglyceride concentrations and may affect the risk of myocardial infarction (MI). To assess whether APOC3/A5 haplotypes Show more
Genetic variation in the APOC3 and APOA5 genes has been associated with plasma triglyceride concentrations and may affect the risk of myocardial infarction (MI). To assess whether APOC3/A5 haplotypes are associated with risk of MI, we examined three single-nucleotide polymorphisms (SNPs) in APOC3 (3238C>G, -455T>C, and -482C>T) and six SNPs in the APOA5 gene (-1131T>C, c.-3A>G, c.56C>G, IVS3+476G>A, c.553G>T, and c.1259T>C) in incident cases (n = 1,703) of a first nonfatal MI matched for gender, age, and area of residence with population-based controls (n = 1,703). Conditional logistic regression models, adjusted for potential environmental confounders, were used for analysis. The common APOC3*222 haplotype was more frequent in cases than in controls (17.4% and 13.7%, respectively, P < 0.001) and was associated with increased risk of MI [odds ratio (OR) = 1.27; 95% confidence interval (95% CI), 1.09, 1.48] compared with APOC3*111 wild-type haplotype. This association was independent of the APOA5 SNPs. Although the APOC3 3238G, APOA5 -1131C, APOA5 c.-3G, and APOA5 c.1259C alleles were associated with higher triglyceride plasma concentrations, these effects could not explain the associations with MI in this population. In summary, this study supports the hypothesis that haplotypes in the APOC3 gene but not in the APOA5 gene increase susceptibility to MI. Show less
no PDF DOI: 10.1194/jlr.M500040-JLR200
APOA5
Melissa A Fath, Robert F Mullins, Charles Searby +10 more · 2005 · Human molecular genetics · Oxford University Press · added 2026-04-24
McKusick-Kaufman syndrome (MKS) is an autosomal recessive disorder characterized by post-axial polydactyly, congenital heart defects and hydrometrocolpos, a congenital structural abnormality of female Show more
McKusick-Kaufman syndrome (MKS) is an autosomal recessive disorder characterized by post-axial polydactyly, congenital heart defects and hydrometrocolpos, a congenital structural abnormality of female genitalia. Mutations in the MKKS gene have also been shown to cause some cases of Bardet-Biedl syndrome (BBS) which is characterized by obesity, pigmentary retinopathy, polydactyly, renal abnormalities and hypogenitalism with secondary features of hypertension and diabetes. Although there is overlap in clinical features between MKS and BBS, MKS patients are not obese and do not develop retinopathy or have learning disabilities. To further explore the pathophysiology of BBS and the related disorder MKS, we have developed an Mkks(-/-) mouse model. This model shows that the absence of Mkks leads to retinal degeneration through apoptosis, failure of spermatozoa flagella formation, elevated blood pressure and obesity. The obesity is associated with hyperphagia and decreased activity. In addition, neurological screening reveals deficits in olfaction and social dominance. The mice do not have polydactyly or vaginal abnormalities. The phenotype of the Mkks(-/-) mice closely resembles the phenotype of other mouse models of BBS (Bbs2(-/-) and Bbs4(-/-)). These observations suggest that the complete absence of MKKS leads to BBS while the MKS phenotype is likely to be due to specific mutations. Show less
no PDF DOI: 10.1093/hmg/ddi123
BBS4
Haiyan Xu, Qing Yang, Minhui Shen +6 more · 2005 · The Journal of biological chemistry · American Society for Biochemistry and Molecular Biology · added 2026-04-24
Insulin is a key hormone that controls glucose homeostasis. In liver, insulin suppresses gluconeogenesis by inhibiting the transcriptions of phosphoenolpyruvate carboxylase (PEPCK) and glucose-6-phosp Show more
Insulin is a key hormone that controls glucose homeostasis. In liver, insulin suppresses gluconeogenesis by inhibiting the transcriptions of phosphoenolpyruvate carboxylase (PEPCK) and glucose-6-phosphatase (G6Pase) genes. In insulin resistance and type II diabetes there is an elevation of hepatic gluconeogenesis, which contributes to hyperglycemia. To search for novel genes that negatively regulate insulin signaling in controlling metabolic pathways, we screened a cDNA library derived from the white adipose tissue of ob/ob mice using a reporter system comprised of the PEPCK promoter placed upstream of the alkaline phosphatase gene. The mitogen-activated dual specificity protein kinase phosphatase 3 (MKP-3) was identified as a candidate gene that antagonized insulin suppression on PEPCK gene transcription from this screen. In this study, we showed that MKP-3 was expressed in insulin-responsive tissues and that its expression was markedly elevated in the livers of insulin-resistant obese mice. In addition, MKP-3 can activate PEPCK promoter in synergy with dexamethasone in hepatoma cells. Furthermore, ectopic expression of MKP-3 in hepatoma cells by adenoviral infection increased the expression of PEPCK and G6Pase genes and led to elevated glucose production. Taken together, our data strongly suggests that MKP-3 plays a role in regulating gluconeogenic gene expression and hepatic gluconeogenesis. Therefore, dysregulation of MKP-3 expression and/or function in liver may contribute to the pathogenesis of insulin resistance and type II diabetes. Show less
no PDF DOI: 10.1074/jbc.M508027200
DUSP6
Nan Hu, Chaoyu Wang, Ying Hu +9 more · 2005 · Cancer research · added 2026-04-24
Whole genome association studies of complex human diseases represent a new paradigm in the postgenomic era. In this study, we report application of the Affymetrix, Inc. (Santa Clara, CA) high-density Show more
Whole genome association studies of complex human diseases represent a new paradigm in the postgenomic era. In this study, we report application of the Affymetrix, Inc. (Santa Clara, CA) high-density single nucleotide polymorphism (SNP) array containing 11,555 SNPs in a pilot case-control study of esophageal squamous cell carcinoma (ESCC) that included the analysis of germ line samples from 50 ESCC patients and 50 matched controls. The average genotyping call rate for the 100 samples analyzed was 96%. Using the generalized linear model (GLM) with adjustment for potential confounders and multiple comparisons, we identified 37 SNPs associated with disease, assuming a recessive mode of transmission; similarly, 48 SNPs were identified assuming a dominant mode and 53 SNPs in a continuous mode. When the 37 SNPs identified from the GLM recessive mode were used in a principal components analysis, the first principal component correctly predicted 46 of 50 cases and 47 of 50 controls. Among all the SNPs selected from GLMs for the three modes of transmission, 39 could be mapped to 1 of 33 genes. Many of these genes are involved in various cancers, including GASC1, shown previously to be amplified in ESCCs, and EPHB1 and PIK3C3. In conclusion, we have shown the feasibility of the Affymetrix 10K SNP array in genome-wide association studies of common cancers and identified new candidate loci to study in ESCC. Show less
no PDF DOI: 10.1158/0008-5472.CAN-04-3247
PIK3C3
Darryl Y Nishimura, Melissa Fath, Robert F Mullins +10 more · 2004 · Proceedings of the National Academy of Sciences of the United States of America · National Academy of Sciences · added 2026-04-24
Bardet-Biedl syndrome (BBS) is a heterogeneous, pleiotropic human disorder characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, hypogenitalism, a Show more
Bardet-Biedl syndrome (BBS) is a heterogeneous, pleiotropic human disorder characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, hypogenitalism, and an increased incidence of diabetes and hypertension. No information is available regarding the specific function of BBS2. We show that mice lacking Bbs2 gene expression have major components of the human phenotype, including obesity and retinopathy. In addition, these mice have phenotypes associated with cilia dysfunction, including retinopathy, renal cysts, male infertility, and a deficit in olfaction. With the exception of male infertility, these phenotypes are not caused by a complete absence of cilia. We demonstrate that BBS2 retinopathy involves normal retina development followed by apoptotic death of photoreceptors, the primary ciliated cells of the retina. Photoreceptor cell death is preceded by mislocalization of rhodopsin, indicating a defect in transport. We also demonstrate that Bbs2(-/-) mice and a second BBS mouse model, Bbs4(-/-), have a defect in social function. The evaluation of Bbs2(-/-) mice indicates additional phenotypes that should be evaluated in human patients, including deficits in social interaction and infertility. Show less
no PDF DOI: 10.1073/pnas.0405496101
BBS4
Kirk Mykytyn, Robert F Mullins, Michael Andrews +7 more · 2004 · Proceedings of the National Academy of Sciences of the United States of America · National Academy of Sciences · added 2026-04-24
The functions of the proteins encoded by the Bardet-Biedl syndrome (BBS) genes are unknown. Mutations in these genes lead to the pleiotropic human disorder BBS, which is characterized by obesity, reti Show more
The functions of the proteins encoded by the Bardet-Biedl syndrome (BBS) genes are unknown. Mutations in these genes lead to the pleiotropic human disorder BBS, which is characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, and hypogenitalism. Secondary features include diabetes mellitus and hypertension. Recently, it has been suggested that the BBS phenotypes are the result of a lack of cilia formation or function. In this study, we show that mice lacking the Bbs4 protein have major components of the human phenotype, including obesity and retinal degeneration. We show that Bbs4-null mice develop both motile and primary cilia, demonstrating that Bbs4 is not required for global cilia formation. Interestingly, male Bbs4-null mice do not form spermatozoa flagella, and BBS4 retinopathy involves apoptotic death of photoreceptors, the primary ciliated cells of the retina. These mutation data demonstrate a connection between the function of a BBS protein and cilia. To further evaluate an association between cilia and BBS, we performed homology comparisons of BBS proteins in model organisms and find that BBS proteins are specifically conserved in ciliated organisms. Show less
no PDF DOI: 10.1073/pnas.0402354101
BBS4
S M Bahri, W Chia, X Yang · 2001 · Mechanisms of development · Elsevier · added 2026-04-24
Sibling neurons in the embryonic central nervous system (CNS) of Drosophila can adopt distinct states as judged by gene expression and axon projection. In the NB4-2 lineage, two even-skipped (eve)-exp Show more
Sibling neurons in the embryonic central nervous system (CNS) of Drosophila can adopt distinct states as judged by gene expression and axon projection. In the NB4-2 lineage, two even-skipped (eve)-expressing sibling neuronal cells, RP2 and RP2sib, are formed in each hemineuromere. Throughout embryogenesis, only RP2, but not RP2sib, maintains eve expression. In this report, we describe a P-element induced mutation that alters the expression pattern of EVE in RP2 motoneurons in the Drosophila embryonic CNS. The mutation was mapped to a Drosophila homolog of human AF10/AF17 leukemia fusion genes (alf), and therefore named Dalf. Like its human counterparts, Dalf encodes a zinc finger/leucine zipper nuclear protein that is widely expressed in embryonic and larval tissues including neurons and glia. In Dalf mutant embryos, the RP2 motoneuron no longer maintains EVE expression. The effect of the Dalf mutation on EVE expression is RP2-specific and does not affect other characteristics of the RP2 motoneuron. In addition to the embryonic phenotype, Dalf mutant larvae are retarded in their growth and this defect can be rescued by the ectopic expression of a Dalf transgene under the control of a neuronal GAL4 driver. This indicates a requirement for Dalf function in the nervous system for maintaining gene expression and the facilitation of normal growth. Show less
no PDF DOI: 10.1016/s0925-4773(00)00539-6
MLLT10
I Karakesisoglou, Y Yang, E Fuchs · 2000 · The Journal of cell biology · added 2026-04-24
Plakins are cytoskeletal linker proteins initially thought to interact exclusively with intermediate filaments (IFs), but recently were found to associate additionally with actin and microtubule netwo Show more
Plakins are cytoskeletal linker proteins initially thought to interact exclusively with intermediate filaments (IFs), but recently were found to associate additionally with actin and microtubule networks. Here, we report on ACF7, a mammalian orthologue of the Drosophila kakapo plakin genetically involved in epidermal-muscle adhesion and neuromuscular junctions. While ACF7/kakapo is divergent from other plakins in its IF-binding domain, it has at least one actin (K(d) = 0.35 microM) and one microtubule (K(d) approximately 6 microM) binding domain. Similar to its fly counterpart, ACF7 is expressed in the epidermis. In well spread epidermal keratinocytes, ACF7 discontinuously decorates the cytoskeleton at the cell periphery, including microtubules (MTs) and actin filaments (AFs) that are aligned in parallel converging at focal contacts. Upon calcium induction of intercellular adhesion, ACF7 and the cytoskeleton reorganize at cell-cell borders but with different kinetics from adherens junctions and desmosomes. Treatments with cytoskeletal depolymerizing drugs reveal that ACF7's cytoskeletal association is dependent upon the microtubule network, but ACF7 also appears to stabilize actin at sites where microtubules and microfilaments meet. We posit that ACF7 may function in microtubule dynamics to facilitate actin-microtubule interactions at the cell periphery and to couple the microtubule network to cellular junctions. These attributes provide a clear explanation for the kakapo mutant phenotype in flies. Show less
📄 PDF DOI: 10.1083/jcb.149.1.195
MACF1
A D Simmons, M M Musy, C S Lopes +3 more · 1999 · Human molecular genetics · Oxford University Press · added 2026-04-24
Hereditary multiple exostoses (HME) is an autosomal dominant condition in which bony outgrowths occur from the juxtaepiphyseal regions of the long bones. In a few percent of cases these exostoses unde Show more
Hereditary multiple exostoses (HME) is an autosomal dominant condition in which bony outgrowths occur from the juxtaepiphyseal regions of the long bones. In a few percent of cases these exostoses undergo malignant transformation to chondrosarcomas. HME results from mutations in one of two homologous genes, EXT1 and EXT2. These are members of a new gene family that is conserved from Caenorhabditis elegans to higher vertebrates. In humans this family comprises five genes which are most conserved at their C-termini, but they do not contain any discernible functional motifs and their function(s) is unclear. Indirect evidence suggests that EXT proteins are involved in glycosaminoglycan synthesis, act as tumor suppressors and affect hedgehog signaling. One recent study has also reported that these proteins co-purify with glycosyltransferase (GlcA and GlcNAc transferase) activity and on that basis it has been postulated that they are themselves glycosyl-transferases. We performed two-hybrid screens with a fragment of EXT2 from the region that is most highly conserved in the gene family and identified two interacting proteins: the tumor necrosis factor type 1 associated protein and a novel UDP-GalNAc:poly-peptide N -acetylgalactosaminyltransferase. Significantly, both these interactions were abrogated by a disease-causing EXT mutation, indicating that they are important in the etiology of HME. The EXT2-GalNAc-T5 interaction provides the first direct physical link between EXT proteins and known components of glycosamino-glycan synthesis. Show less
no PDF DOI: 10.1093/hmg/8.12.2155
EXT1
K Hunter, J Greenwood, Y L Yang +3 more · 1999 · Genomics · added 2026-04-24
Rmc1, the cellular receptor for the polytropic class of murine retroviruses, determines the tissue tropism of the virus and therefore plays a critical role in the pathogenesis of polytropic virus-indu Show more
Rmc1, the cellular receptor for the polytropic class of murine retroviruses, determines the tissue tropism of the virus and therefore plays a critical role in the pathogenesis of polytropic virus-induced leukemia. Previously we reported the physical mapping of this gene to a 5-cM region of mouse chromosome 1 and the construction of a yeast artificial chromosome (YAC) contig across this region. In this report we describe the refinement of the Rmc1 candidate region to approximately 600 kb and the generation of an integrated somatic cell hybrid, YAC, and bacterial artificial chromosome contig spanning the region. A number of genes and loci were physically ordered along the chromosome, including a recently identified candidate for Rmc1. Show less
no PDF DOI: 10.1006/geno.1999.5841
RMC1
Y L Yang, L Guo, S Xu +4 more · 1999 · Nature genetics · Nature · added 2026-04-24
The onset of leukaemia caused by type C retroviruses (MLV) in mice is accelerated by the emergence of recombinant polytropic or mink cell focus-forming (MCF) viruses. Susceptibility to infection by po Show more
The onset of leukaemia caused by type C retroviruses (MLV) in mice is accelerated by the emergence of recombinant polytropic or mink cell focus-forming (MCF) viruses. Susceptibility to infection by polytropic/MCF and also by closely related xenotropic MLV has been mapped to Rmc1 on mouse chromosome 1 (refs 5-7). To identify this gene, we introduced an expression cDNA library prepared from mouse NIH3T3 fibroblasts into nonpermissive hamster cells and screened these cells for acquired susceptibility to MCF viruses encoding beta-galactosidase and G418 resistance. From hamster cell clones identified in the screen, we recovered a mouse cDNA that maps to Rmc1 and confers MCF MLV infection when expressed in nonpermissive cell lines. It encodes a membrane protein related to Syg1p (suppressor of yeast G alpha deletion; ref. 8). The receptor-binding domain of the MCF MLV envelope protein binds specifically to Xenopus laevis oocytes that express mouse Syg1, suggesting it functions as a receptor that mediates virus entry. We also obtained the cDNA encoding human SYG1. When expressed in hamster cells, it establishes infectivity by MCF MLV as well as xenotropic MLV, which do not infect laboratory mice. Show less
no PDF DOI: 10.1038/6005
RMC1
J Yang, J A Drazba, D G Ferguson +1 more · 1998 · The Journal of cell biology · added 2026-04-24
Stimulation of beta-adrenergic receptors activates type I and II cyclic AMP-dependent protein kinase A, resulting in phosphorylation of various proteins in the heart. It has been proposed that PKA II Show more
Stimulation of beta-adrenergic receptors activates type I and II cyclic AMP-dependent protein kinase A, resulting in phosphorylation of various proteins in the heart. It has been proposed that PKA II compartmentalization by A-kinase-anchoring proteins (AKAPs) regulates cyclic AMP-dependent signaling in the cell. We investigated the expression and localization of AKAP100 in adult hearts. By immunoblotting, we identified AKAP100 in adult rat and human hearts, and showed that type I and II regulatory (RI and II) subunits of PKA are present in the rat heart. By immunofluorescence and confocal microscopy of rat cardiac myocytes and cryostat sections of rat left ventricle papillary muscles, we localized AKAP100 to the nucleus, sarcolemma, intercalated disc, and at the level of the Z-line. After double immunostaining of transverse cross-sections of the papillary muscles with AKAP100 plus alpha-actinin-specific antibodies or AKAP100 plus ryanodine receptor-specific antibodies, confocal images showed AKAP100 localization at the region of the transverse tubule/junctional sarcoplasmic reticulum. RI is distributed differently from RII in the myocytes. RII, but not RI, was colocalized with AKAP100 in the rat heart. Our studies suggest that AKAP100 tethers PKA II to multiple subcellular compartments for phosphorylation of different pools of substrate proteins in the heart. Show less
📄 PDF DOI: 10.1083/jcb.142.2.511
AKAP6
B L Schneider, Q H Yang, A B Futcher · 1996 · Science (New York, N.Y.) · Science · added 2026-04-24
In Saccharomyces cerevisiae, three G1 cyclins (Clns) are important for Start, the event committing cells to division. Sic1, an inhibitor of C1b-Cdc28 kinases, became phosphorylated at Start, and this Show more
In Saccharomyces cerevisiae, three G1 cyclins (Clns) are important for Start, the event committing cells to division. Sic1, an inhibitor of C1b-Cdc28 kinases, became phosphorylated at Start, and this phosphorylation depended on the activity of Clns. Sic1 was subsequently lost, which depended on the activity of Clns and the ubiquitin-conjugating enzyme Cdc34. Inactivation of Sic1 was the only nonredundant essential function of Clns, because a sic1 deletion rescued the inviability of the cln1 cln2 cln3 triple mutant. In sic1 mutants, DNA replication became uncoupled from budding. Thus, Sic1 may be a substrate of Cln-Cdc28 complexes, and phosphorylation and proteolysis of Sic1 may regulate commitment to replication at Start. Show less
no PDF DOI: 10.1126/science.272.5261.560
CLN3