👤 Yuanzhi 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 L 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, 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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
Wen Zhao, Danlei Yu, Zhen Chen +4 more · 2021 · Cancer letters · Elsevier · added 2026-04-24
The promising therapeutic efficacy of the third generation EGFR inhibitor, osimertinib (AZD9291), for the treatment of patients with EGFR-mutant non-small cell lung cancer (NSCLC) has been demonstrate Show more
The promising therapeutic efficacy of the third generation EGFR inhibitor, osimertinib (AZD9291), for the treatment of patients with EGFR-mutant non-small cell lung cancer (NSCLC) has been demonstrated in the clinic both as first-line and second line therapy. However, inevitable acquired resistance limits its long-term benefit to patients and is thus a significant clinical challenge. The current study focuses on studying the potential role of targeting MEK5-ERK5 signaling in overcoming acquired resistance to osimertinib. Osimertinib and other third generation EGFR inhibitors exerted a rapid and sustained suppressive effect on ERK5 phosphorylation primarily in EGFR-mutant NSCLC cell lines and lost this activity in some osimertinib-resistant cell lines. Osimertinib combined with either ERK5 or MEK5 inhibitors synergistically decreased the survival of osimertinib-resistant cell lines with enhanced induction of apoptosis primarily via augmenting Bim expression. Moreover, the combination effectively inhibited the growth of osimertinib-resistant xenografts in vivo. Together, these findings suggest the potential role of MEK5-ERK5 signaling in modulating development of acquired resistance to osimertinib and value of targeting this signaling as a potential strategy in overcoming acquired resistance to osimertinib and possibly other third generation EGFR inhibitors. Show less
no PDF DOI: 10.1016/j.canlet.2021.07.007
MAP2K5
Wenqian Zhang, Jun Hong, Wencheng Zheng +2 more · 2021 · Aging · Impact Journals · added 2026-04-24
Traumatic brain injury (TBI) is a highly lethal event with a poor prognosis. Recovering residual neuronal function in the intermediate stage of TBI is important for treatment; however, neuroinflammati Show more
Traumatic brain injury (TBI) is a highly lethal event with a poor prognosis. Recovering residual neuronal function in the intermediate stage of TBI is important for treatment; however, neuroinflammation and neuronal apoptosis impede residual neuronal repair processes. Considering that hyperglycemia influences inflammatory processes and neuronal survival, we examined the effects of high glucose on neuroinflammation and neuronal death during the intermediate phase of TBI. Rat models of type 2 diabetes mellitus and/or TBI were developed and behaviorally assessed. Neurological function and cognitive abilities were impaired in TBI rats and worsened by type 2 diabetes mellitus. Histopathological staining and analyses of serum and hippocampal mRNA and protein levels indicated that neuroinflammation and apoptosis were induced in TBI rats and exacerbated by hyperglycemia. Hyperglycemia inhibited hippocampal mitogen-activated protein kinase kinase 5 (MEK5) phosphorylation in TBI rats. Show less
📄 PDF DOI: 10.18632/aging.203136
MAP2K5
Yan-Hui Yin, Xin-Hui Zhang, Xiao-Ai Wang +12 more · 2021 · Zoological research · added 2026-04-24
The Dianchi golden-line barbel,
📄 PDF DOI: 10.24272/j.issn.2095-8137.2020.321
MAP2K5
Nan Chen, Shan Song, Zhifen Yang +4 more · 2021 · Journal of diabetes and its complications · Elsevier · added 2026-04-24
In the present study, we investigated the effect of carbohydrate responsive element binding protein (ChREBP) on the TXNIP/oxidative stress and apoptosis in diabetic nephropathy. ChREBP Renal expressio Show more
In the present study, we investigated the effect of carbohydrate responsive element binding protein (ChREBP) on the TXNIP/oxidative stress and apoptosis in diabetic nephropathy. ChREBP Renal expression of ChREBP and thioredoxin-interacting protein (TXNIP) was increased in patients with type 2 diabetes mellitus (T2DM) and diabetic mice. ChREBP deficiency improved renal function, apoptosis as well as endoplasmic reticulum (ER) stress in diabetic mice. In addition, ChREBP deficiency prevented expression levels of TXNIP and NADPH oxidase 4 (Nox4), 8-hydroxydeoxyguanosine (8-OHdG) and heme oxygenase-1 (HO-1) in diabetic kidneys. The increased urinary 8-OHdG level induced by diabetes was also attenuated in ChREBP deficiency mice. Similarly, HG was shown to induce ChREBP expression and nuclear translocation in HK-2 cells. HG-induced apoptosis was inhibited by transfection of ChREBP shRNA plasmid. Moreover, we found that knockdown of ChREBP suppressed HG-induced TXNIP and Nox4 expression, reactive oxygen species (ROS) generation and ER stress in HK-2 cells. Furthermore, TXNIP knockdown effectively abrogated HG-induced apoptosis in HK-2 cells. These results suggest that ChREBP deficiency prevents diabetes-induced apoptosis via inhibiting oxidative stress and ER stress, highlighting ChREBP as a potential therapy target for diabetic nephropathy. Show less
no PDF DOI: 10.1016/j.jdiacomp.2021.108050
MLXIPL
Dou Yeon Youn, Alus M Xiaoli, Haihong Zong +5 more · 2021 · Molecular metabolism · Elsevier · added 2026-04-24
Liver glycogen levels are dynamic and highly regulated by nutrient availability as the levels decrease during fasting and are restored during the feeding cycle. However, feeding in the presence of fru Show more
Liver glycogen levels are dynamic and highly regulated by nutrient availability as the levels decrease during fasting and are restored during the feeding cycle. However, feeding in the presence of fructose in water suppresses glycogen accumulation in the liver by upregulating the expression of the glucose-6-phosphatase catalytic subunit (G6pc) gene, although the exact mechanism is unknown. We generated liver-specific knockout MED13 mice that lacked the transcriptional Mediator complex kinase module to examine its effect on the transcriptional activation of inducible target gene expression, such as the ChREBP- and FOXO1-dependent control of the G6pc gene promoter. The relative changes in liver expression of lipogenic and gluconeogenic genes as well as glycogen levels were examined in response to feeding standard low-fat laboratory chow supplemented with water or water containing sucrose or fructose in control (Med13 Although MED13 deficiency had no significant effect on constitutive gene expression, all the dietary inducible gene transcripts were significantly reduced despite the unchanged insulin sensitivity in the MED13-LKO mice compared to that in the control mice. G6pc gene transcription displayed the most significant difference between the Med13 Taken together, our data suggest that the kinase module of the Mediator complex is necessary for the transcriptional activation of metabolic genes such as G6pc and has an important role in regulating glycogen levels in the liver through altering transcription factor binding and activity at the G6pc promoter. Show less
📄 PDF DOI: 10.1016/j.molmet.2021.101227
MLXIPL
Li Zhong, Qing Liu, Qiaofeng Liu +4 more · 2021 · Chemical biology & drug design · Blackwell Publishing · added 2026-04-24
Thioredoxin-interacting protein (TXNIP) overexpression is implicated in the pathogenesis of type 2 diabetes. Previous studies have shown that a small molecule compound (W2476) was able to improve β-ce Show more
Thioredoxin-interacting protein (TXNIP) overexpression is implicated in the pathogenesis of type 2 diabetes. Previous studies have shown that a small molecule compound (W2476) was able to improve β-cell dysfunction and exert therapeutic effects in diabetic mice via repression of TXNIP signaling pathway. The impact of W2476 on TXNIP transcription was thus investigated using the chromatin immunoprecipitation method. It was found that W2476 promotes competitive binding of forkhead box O1 transcription factor (FOXO1) to the carbohydrate response element (ChoRE) sequence associated with ChoRE-binding protein (ChREBP)/Mlx interacting protein-like(Mlx) complexes. This interaction hinders the attachment of histone acetyltransferase p300 and reduces histone H4 acetylation on the TXNIP promoter, leading to decreasing TXNIP transcription. Show less
no PDF DOI: 10.1111/cbdd.13828
MLXIPL
Xiao Dong, Fan Wang, Chuan Liu +7 more · 2021 · Cell death discovery · Nature · added 2026-04-24
Hepatocellular carcinoma (HCC) is a globally prevailing cancer with a low 5-year survival rate. Little is known about its intricate gene expression profile. Single-cell RNA sequencing is an indispensa Show more
Hepatocellular carcinoma (HCC) is a globally prevailing cancer with a low 5-year survival rate. Little is known about its intricate gene expression profile. Single-cell RNA sequencing is an indispensable tool to explore the genetic characteristics of HCC at a more detailed level. In this study, we profiled the gene expression of single cells from human HCC tumor and para-tumor tissues using the Smart-seq 2 sequencing method. Based on differentially expressed genes, we identified heterogeneous subclones in HCC tissues, including five HCC and two hepatocyte subclones. We then carried out hub-gene co-network and functional annotations analysis followed pseudo-time analysis with regulated transcriptional factor co-networks to determine HCC cellular trajectory. We found that MLX interacting protein like (MLXIPL) was commonly upregulated in the single cells and tissues and associated with a poor survival rate in HCC. Mechanistically, MLXIPL activation is crucial for promoting cell proliferation and inhibits cell apoptosis by accelerating cell glycolysis. Taken together, our work identifies the heterogeneity of HCC subclones, and suggests MLXIPL might be a promising therapeutic target for HCC. Show less
📄 PDF DOI: 10.1038/s41420-021-00403-5
MLXIPL
Nan Chen, Lin Mu, Zhifen Yang +5 more · 2021 · Journal of cellular physiology · Wiley · added 2026-04-24
Lipid deposition caused by the disorder of renal lipid metabolism is involved in diabetic nephropathy (DN). Carbohydrate response element-binding protein (ChREBP) is a key transcription factor in high Show more
Lipid deposition caused by the disorder of renal lipid metabolism is involved in diabetic nephropathy (DN). Carbohydrate response element-binding protein (ChREBP) is a key transcription factor in high glucose-induced cellular fat synthesis. At present, the regulation and mechanism of ChREBP on fat metabolism in diabetic kidneys are still unclear. In this study, we showed that lack of ChREBP significantly improved renal injury, inhibited oxidative stress, lipid deposition, fatty acid synthase (FASN), acetyl-CoA carboxylase (ACC) and thioredoxin-interacting protein (TXNIP) expression, as well as the activity of mammalian target of rapamycin complex 1 (mTORC1) in diabetic kidneys. Meanwhile, ChREBP deficiency upregulated the expression of peroxisome proliferator-activated receptor-α (PPARα), carnitine palmitoyltransferaser 1A (CPT1A) and acyl-coenzyme A oxidase 1 (ACOX1) in diabetic kidneys. In vitro, knockdown of ChREBP attenuated lipid deposition, mTORC1 activation, and expression of FASN and ACC, increased PPARα, CPT1A, and ACOX1 expression in HK-2 cells and podocytes under high glucose (HG) conditions. Moreover, HG-induced lipid deposition, increased expression of FASN and ACC and decreased expression of PPARα, CPT1A, and ACOX1 were reversed by rapamycin, a specific inhibitor of mTORC1, in HK-2 cells. These results indicate that ChREBP deficiency alleviates diabetes-associated renal lipid accumulation by inhibiting mTORC1 activity and suggest that reduction of ChREBP is a potential therapeutic strategy to treat DN. Show less
no PDF DOI: 10.1002/jcp.29890
MLXIPL
Hong Yang, Hong Wang, Zongzhe Li +6 more · 2021 · Frontiers in cardiovascular medicine · Frontiers · added 2026-04-24
Coarctation of the aorta (CoA) is a common congenital cardiovascular malformation with aortic narrowing in the region of the ligamentum arteriosum. Hypertrophic cardiomyopathy (HCM) is a primary cardi Show more
Coarctation of the aorta (CoA) is a common congenital cardiovascular malformation with aortic narrowing in the region of the ligamentum arteriosum. Hypertrophic cardiomyopathy (HCM) is a primary cardiomyopathy that is characterized by left ventricular wall thickening and likely left ventricular outflow tract (LVOT) obstruction. They are two irrelevant diseases, and their coexistence has not been reported before. Here, we described a young female patient who concurrently has CoA and HCM. The patient has had hypertension since 18-years old and complained of chest discomfort on effort and fatigue thereafter. Initially, she was diagnosed as having hypertrophic cardiomyopathy and primary hypertension. The presence of CoA was not found until she was 35 years old when she had an onset of paroxysmal supraventricular tachycardia (PSVT) and presented with syncope. Failure of the ablation procedure Here, we reported the diagnostic challenges, management, and 8-yeasr follow-up findings in a rare case of CoA combined with HCM. The case highlighted the importance for physicians to exclude CoA in young hypertensive patients, and proved the efficacy of stent repair in treating CoA in older patients. Show less
no PDF DOI: 10.3389/fcvm.2021.818884
MYBPC3
Wen Liu, Zongkai Wei, Yanfen Zhang +5 more · 2021 · Clinica chimica acta; international journal of clinical chemistry · Elsevier · added 2026-04-24
Familial hypertrophic cardiomyopathy (HCM) is a leading cause of sudden cardiac death, but exhibits heterogeneous clinical features. A major research focus is to identify specific ultrasonic phenotype Show more
Familial hypertrophic cardiomyopathy (HCM) is a leading cause of sudden cardiac death, but exhibits heterogeneous clinical features. A major research focus is to identify specific ultrasonic phenotypes, and causal gene mutations, as well as to elucidate the possible metabolic pathogenic effects in familial HCM through multi-omics study. Nine members of two familial HCM pedigrees were enrolled in this study. Their clinical data were collected, and the data of multiparameter ultrasound, whole-exome sequencing, and untargeted metabolomics were analyzed. We identified three novel pathogenic sarcomere gene mutations, TNNT2-rs397516484, MYH6-rs372446459 and MYBPC3-rs786204339 in two familial HCM pedigrees. The proband of Family 1 and his father carried TNNT2-rs397516484 and MYH6-rs372446459 missense mutations, while the proband of Family 2 and her brother carried MYBPC3-rs786204339 frameshift mutation. They presented with heart failure and abnormal electrocardiogram, accompanied by diastolic and systolic dysfunction and impaired myocardial work. They also showed disturbances of carbohydrate metabolism, including the citrate cycle (TCA cycle), glycolysis/gluconeogenesis, fructose and mannose metabolism, pentose and glucuronate interconversions and amino sugar and nucleotide sugar metabolism. Novel TNNT2-rs397516484, MYH6-rs372446459, and MYBPC3-rs786204339 are pathogenic sarcomere gene mutations in familial HCM, leading to decreased cardiac function and metabolic disturbances of carbohydrate metabolism, which have important implications for biologically defined diagnoses and precision medicine. Show less
no PDF DOI: 10.1016/j.cca.2021.05.034
MYBPC3
Xiao-Qun Liu, Man Luo, Qi Liu +1 more · 2021 · Reproductive sciences (Thousand Oaks, Calif.) · Springer · added 2026-04-24
Prader-Willi syndrome (PWS) is a neurogenetic disorder caused by deficiency expression of paternally imprinted genes of the chromosomal region 15. In this study, we report a novel mutation in the myos Show more
Prader-Willi syndrome (PWS) is a neurogenetic disorder caused by deficiency expression of paternally imprinted genes of the chromosomal region 15. In this study, we report a novel mutation in the myosin binding protein C (MYBPC3) gene in a Prader-Willi syndrome pedigree. Next-generation sequencing (NGS) and Sanger sequencing were performed to define and confirm the MYBPC3 gene mutation. Bioinformatics analysis was also performed for the mutated MYBPC3 protein using available software tools. The proband was diagnosed as PWS with about 4.727Mb copy number missed in the long arm of chromosome 15 and treated with growth hormone on 0.3 IU/day. Sanger sequencing identified a novel heterozygous mutation in the MYBPC3 gene, c.2002C>G (p.R668G). Bioinformatics analysis suggested the variant disease-causing; the Pro residue at 668 in the MYBPC3 protein was highly conserved. Moreover, interactions among MYBPC3 and other proteins suggested the potential effects on the development of cardiomyopathies. This is the first report of PWS with MYBPC3 gene mutation. Besides general examinations, it is vital for physicians to amply molecular genetics to get an accurate diagnosis in the clinic especially for rare diseases. Show less
no PDF DOI: 10.1007/s43032-021-00620-4
MYBPC3
Qian-Li Yang, Lei Zuo, Zhi-Ling Ma +9 more · 2021 · Heart and vessels · Springer · added 2026-04-24
The mutation MYBPC3-E334K is a culprit mutation of hypertrophic cardiomyopathy (HCM). The pathogenicity of MYBPC3-E334K is conflicting in ClinVar because of the limited segregation data and the relati Show more
The mutation MYBPC3-E334K is a culprit mutation of hypertrophic cardiomyopathy (HCM). The pathogenicity of MYBPC3-E334K is conflicting in ClinVar because of the limited segregation data and the relatively high frequency in gnomAD (0.03% overall, with 0.3% in East Asians and 0.8% in Japanese). The main aim is to clarify the clinical importance and phenotype-genotype correlations in subjects with or without MYBPC3-E334K alone. The prevalence of MYBPC3-E334K was sequenced in 1017 HCM unrelated probands. The clinical features, morphology phenotypes, and electrical phenotypes were further analyzed according to the phenotype and genotype status in families with single-mutation MYBPC3-E334K. Nine of 1017 (0.88%) unrelated HCM probands were detected harboring MYBPC3-E334K, and three of them harbored a second variant in sarcomere protein gene. Family study and co-segregation analyses indicated that patients with single-mutation MYBPC3-E334K showed autosomal dominant mode of inheritance with incomplete penetrance. The overall disease penetrance was 52.6%, and the disease penetrance was higher in males than in females (100% in men vs 25% in women, p = 0.003). The mean age at diagnosis of males was approximately 25 years younger than females (36.57 ± 18.65 vs 62.33 ± 12.10, p = 0.062). The variant MYBPC3-E334K was classified as a likely pathogenic variant, and a second sarcomere variant did not reveal obvious cumulative effects. The patients harboring single-mutation MYBPC3-E334K had incomplete penetrance, and males demonstrated higher penetrance and early onset HCM than females. A second sarcomere variant did not reveal obvious cumulative effects. Show less
no PDF DOI: 10.1007/s00380-021-01834-x
MYBPC3
R Guo, B Yang · 2021 · Folia biologica · added 2026-04-24
Gastric cancer is characterized by the presence of high invasion ability, hypoxia and chemoresistance. Previous studies reported that liver X receptor α (LXRα) was involved in epithelial-mesenchymal t Show more
Gastric cancer is characterized by the presence of high invasion ability, hypoxia and chemoresistance. Previous studies reported that liver X receptor α (LXRα) was involved in epithelial-mesenchymal transition (EMT) of gastric cancer cells. However, hypoxia-mediated EMT and the role of LXRα in gastric cancer remained elusive. In this study, we demonstrated that LXRa mRNA and protein levels were up-regulated by hypoxia treatment and LXRα played an important role in HIF-1 dimer induced-EMT. The putative HIF-1α binding site was identified in the LXRa promoter. Expression of LXRα and HIF-1α was significantly up-regulated in gastric cancer tissues compared to that in normal tissues. More importantly, we noticed that the expression of LXRα and HIF-1α was significantly correlated. Taken together, these data suggested that LXRα is regulated by the activity and accumulation of HIF-1α and contributes to EMT of gastric cancer cells. This suggests that targeting LXRα might be a potential approach for improving survival of gastric cancer patients. Show less
no PDF DOI: 10.14712/fb2021067030091
NR1H3
Yao Li, Yanhu Shi, Yaoli He +2 more · 2021 · Bioengineered · Taylor & Francis · added 2026-04-24
Myocardial hypertrophy is a pathological thickening of the myocardium, leading to various ailments, such as myocardial infarction and heart failure. RBM38 is critical in modulating mRNA translation fo Show more
Myocardial hypertrophy is a pathological thickening of the myocardium, leading to various ailments, such as myocardial infarction and heart failure. RBM38 is critical in modulating mRNA translation for multiple protective activities such as p53 tumor repressor and p21 kinase cell cycle inhibitors. Liver X receptors (LXR-α) agonists reduce cellular hypertrophy initiated by various hypertrophic stimuli as lipopolysaccharides and Ang II. This research investigates the possible cooperation between RBM38 and LXR-α and mechanisms in modulating myocardial hypertrophy. H9C2 cells were treated with PE, TNF-α, and AngII to induce myocardial hypertrophy. RBM38 and LXR- α were overexpressed or silenced in H9C2 cells, and hypertrophy markers (ANF and Myh7) were determined with Western blot and RT-qPCR. Binding assays were done through RNA immunoprecipitation. H&E and Rhodamine-labeled phalloidin staining assays were used to assess the relative cell surface change. The results demonstrated RBM38 downregulation in in vitro models of myocardial hypertrophy. Modulation of RBM38 expression also exerted inverse effects on myocardial hypertrophy markers. Further observations also showed that LXR-α expression regulates the myocardial hypertrophy markers in H9C2 cells and RBM38 binds with LXR-α mRNA, consequently inhibiting LXR-α expression. Finally, overexpression of RBM38 rescues Angiotensin II-induced myocardial hypertrophy by regulating LXR-α dependent lipogenesis pathway. In conclusion, RBM38 Overexpression rescues Angiotensin II-induced myocardial hypertrophy by regulating LXR-α dependent lipogenesis pathway. Show less
no PDF DOI: 10.1080/21655979.2021.1977552
NR1H3
Xiaoling Zhou, Qiongxian Yan, Hong Yang +3 more · 2021 · Animal nutrition (Zhongguo xu mu shou yi xue hui) · Elsevier · added 2026-04-24
The biological mechanism by which maternal undernutrition increases the metabolic disorder risk of skeletal muscles in offspring is not fully understood. We hypothesize that maternal intake restrictio Show more
The biological mechanism by which maternal undernutrition increases the metabolic disorder risk of skeletal muscles in offspring is not fully understood. We hypothesize that maternal intake restriction influences metabolic signals in the skeletal muscles of offspring via a glucagon-mediated pathway. Twenty-four pregnant goats were assigned to the control group (100% of the nutrients requirement, Show less
no PDF DOI: 10.1016/j.aninu.2021.09.006
NR1H3
Bao Long Zhang, Xiu Hong Yang, Hui Min Jin +1 more · 2021 · FEBS open bio · Wiley · added 2026-04-24
Diabetic kidney disease (DKD) is the leading cause of end-stage renal disease. However, because of shared complications between DKD and chronic kidney disease (CKD), the description and characterizati Show more
Diabetic kidney disease (DKD) is the leading cause of end-stage renal disease. However, because of shared complications between DKD and chronic kidney disease (CKD), the description and characterization of DKD remain ambiguous in the clinic, hindering the diagnosis and treatment of early-stage DKD patients. Although estimated glomerular filtration rate and albuminuria are well-established biomarkers of DKD, early-stage DKD is rarely accompanied by a high estimated glomerular filtration rate, and thus there is a need for new sensitive biomarkers. Transcriptome profiling of kidney tissue has been reported previously, although RNA sequencing (RNA-Seq) analysis of the venous blood platelets in DKD patients has not yet been described. In the present study, we performed RNA-Seq analysis of venous blood platelets from three patients with CKD, five patients with DKD and 10 healthy controls, and compared the results with a CKD-related microarray dataset. In total, 2097 genes with differential transcript levels were identified in platelets of DKD patients and healthy controls, and 462 genes with differential transcript levels were identified in platelets of DKD patients and CKD patients. Through Kyoto Encyclopedia of Genes and Genomes pathway enrichment analysis, we selected 11 pathways, from which nine potential biomarkers (IL-1B, CD-38, CSF1R, PPARG, NR1H3, DDO, HDC, DPYS and CAD) were identified. Furthermore, by comparing the RNA-Seq results with the GSE30566 dataset, we found that the biomarker KCND3 was the only up-regulated gene in DKD patients. These biomarkers may have potential application for the therapy and diagnosis of DKD, as well aid in determining the mechanisms underlying DKD. Show less
no PDF DOI: 10.1002/2211-5463.13199
NR1H3
Yanhua Pu, Qian Zhao, Xuelin Men +2 more · 2021 · Life sciences · Elsevier · added 2026-04-24
MicroRNA-325 (miR-325) was significantly upregulated in diabetic atherosclerosis, while its specific role in atherosclerosis has not been established. The present study was set to probe the effects of Show more
MicroRNA-325 (miR-325) was significantly upregulated in diabetic atherosclerosis, while its specific role in atherosclerosis has not been established. The present study was set to probe the effects of miR-325 on the atherosclerosis progression and to explore the mechanisms. The ApoE miR-325 was elevated in arterial tissues of atherosclerotic mice, and miR-325 inhibition in mice reduced the contents of total cholesterol, triglyceride, low-density lipoprotein, and CRP, IL-6, IL-1β and TNF-ɑ levels in mouse serum. miR-325 inhibitor facilitated the cholesterol efflux and decreased the lipid content in RAW264.7 cells, and also diminished HA-VSMC viability. miR-325 targeted KDM1A to reduce SREBF1 expression, and further KDM1A suppression inhibited cholesterol efflux in RAW264.7 cells and the activation of PPARγ-LXR-ABCA1 pathway. miR-325 lowers SREBF1 expression by decreasing KDM1A expression, thereby inhibiting the activation of the PPARγ-LXR-ABCA1 pathway and thus promoting atherosclerosis. Show less
no PDF DOI: 10.1016/j.lfs.2021.119464
NR1H3
Haixia Du, Chang Li, Zhixiong Wang +5 more · 2021 · Journal of ethnopharmacology · Elsevier · added 2026-04-24
Danhong injection (DHI) is a Chinese medical injection applied to the clinical treatment of cardiovascular diseases that has anti-inflammatory, antiplatelet aggregation and antithrombotic effects. Thi Show more
Danhong injection (DHI) is a Chinese medical injection applied to the clinical treatment of cardiovascular diseases that has anti-inflammatory, antiplatelet aggregation and antithrombotic effects. This study aimed to explore the effects of DHI on dyslipidemia and cholesterol metabolism in high-fat diet-fed rats. Sprague Dawley (SD) rats were randomly divided into six groups: normal group (Normal); hyperlipidemia model group (Model); DHI-treated groups at doses of 1.0 mL/kg, 2.0 mL/kg, 4.0 mL/kg; and simvastatin positive control group (2.0 mg/kg). The hypolipidemic effects of DHI were evaluated by measuring serum lipid levels, hepatic function and oxidative stress, respectively. And pathological changes in liver tissues were determined using hematoxylin-eosin (H&E) and oil red O staining. Moreover, the mRNA and protein expression levels of cholesterol metabolism related genes were detected by real-time PCR (RT-PCR) and Western blot. Compared with the Model group, DHI treatment markedly decreased the liver index and improved the pathological morphology of liver tissues. DHI treatment dose-dependently decreased the levels of total cholesterol (TC), triglycerides (TG), low-density lipoprotein cholesterol (LDL-C), malondialdehyde (MDA), and free fatty acids (FFA) in serum or liver tissues (P < 0.01 or P < 0.05), and increased the high-density lipoprotein cholesterol (HDL-C) and tripeptide glutathione (GSH) (P < 0.01 or P < 0.05). The activities of superoxide dismutase (SOD) and glutathione peroxidase (GSH-PX) were increased in the DHI-treated groups (P < 0.01 or P < 0.05), while the alanine transaminase (ALT) and aspartate transaminase (AST) were decreased (P < 0.01 or P < 0.05). Furthermore, the expression levels of LDL receptor (LDLR), cholesterol 7-α-hydroxylase (CYP7A1), liver X receptor α (LXRα), and peroxisome proliferator-activated receptor α (PPARα) were dose-dependently upregulated in the DHI-treated groups, whereas the expression of sterol regulatory element-binding protein-2 (SREBP-2) was downregulated. Our study demonstrated that DHI markedly ameliorated hyperlipidemia rats by regulating serum lipid levels, inhibiting hepatic lipid accumulation and steatosis, improving hepatic dysfunction, and reducing oxidative stress. The potential mechanism was also tentatively investigated and may be related to the promotion of bile acid synthesis via activation of the PPARα-LXRα-CYP7A1 pathway. Therefore, DHI could be regarded as a potential hypolipidemic drug for the treatment of hyperlipidemia. Show less
no PDF DOI: 10.1016/j.jep.2021.114058
NR1H3
Lin Zhao, Wangrui Lei, Chao Deng +8 more · 2021 · Journal of cellular physiology · Wiley · added 2026-04-24
Liver X receptor α (LXRα; also known as NR1H3), an isoform of LXRs, is a member of the nuclear receptor family of transcription factors and plays essential roles in the transcriptional control of chol Show more
Liver X receptor α (LXRα; also known as NR1H3), an isoform of LXRs, is a member of the nuclear receptor family of transcription factors and plays essential roles in the transcriptional control of cholesterol homeostasis. Previous in-depth phenotypic analyses of mouse models with deficient LXRα have also demonstrated various physiological functions of this receptor within inflammatory responses. LXRα activation exerts a combination of metabolic and anti-inflammatory actions resulting in the modulation and the amelioration of inflammatory disorders. The tight "repercussions" between LXRα and inflammation, as well as cholesterol homeostasis, have suggested that LXRα could be pharmacologically targeted in pathologies such as atherosclerosis, acute lung injury, and Alzheimer's disease. This review gives an overview of the recent advances in understanding the roles of LXRα in inflammation and inflammation-associated diseases, which will help in the design of future experimental researches on the potential of LXRα and advance the investigation of LXRα as pharmacological inflammatory targets. Show less
no PDF DOI: 10.1002/jcp.30204
NR1H3
Liang Liu, Peng Zhang, Xuchen Dong +7 more · 2021 · Cell death & disease · Nature · added 2026-04-24
Many studies have reported that circular RNAs play a vital role in the malignant progression of human cancers. However, the role and underlying mechanism of circRNAs in the development of gliomas have Show more
Many studies have reported that circular RNAs play a vital role in the malignant progression of human cancers. However, the role and underlying mechanism of circRNAs in the development of gliomas have not been fully clarified. In this study, we found that circ₀₀₀₁₃₆₇ was downregulated in glioma tissues and showed a close correlation with glioma patient survival. Functional assays demonstrated that upregulation of circ₀₀₀₁₃₆₇ could suppress the proliferation, migration and invasion of glioma cells in vitro and inhibit glioma growth in vivo. Furthermore, bioinformatics analysis, luciferase reporter assay and RNA immunoprecipitation assay indicated that circ₀₀₀₁₃₆₇ can serve as a sponge for miR-431 and that miR-431 acts as an oncogene by regulating neurexin 3 (NRXN3). In addition, rescue experiments verified that circ₀₀₀₁₃₆₇ could regulate both the expression and function of NRXN3 in a miR-431-dependent manner. In conclusion, circ₀₀₀₁₃₆₇ functions as an suppressor in glioma by targeting the miR-431/NRXN3 axis and may be a promising therapeutic target against gliomas. Show less
no PDF DOI: 10.1038/s41419-021-03834-1
NRXN3
Chuanyin Li, Tianting Han, Qingrun Li +15 more · 2021 · Nucleic acids research · Oxford University Press · added 2026-04-24
The family of Poly(A)-binding proteins (PABPs) regulates the stability and translation of messenger RNAs (mRNAs). Here we reported that the three members of PABPs, including PABPC1, PABPC3 and PABPC4, Show more
The family of Poly(A)-binding proteins (PABPs) regulates the stability and translation of messenger RNAs (mRNAs). Here we reported that the three members of PABPs, including PABPC1, PABPC3 and PABPC4, were identified as novel substrates for MKRN3, whose deletion or loss-of-function mutations were genetically associated with human central precocious puberty (CPP). MKRN3-mediated ubiquitination was found to attenuate the binding of PABPs to the poly(A) tails of mRNA, which led to shortened poly(A) tail-length of GNRH1 mRNA and compromised the formation of translation initiation complex (TIC). Recently, we have shown that MKRN3 epigenetically regulates the transcription of GNRH1 through conjugating poly-Ub chains onto methyl-DNA bind protein 3 (MBD3). Therefore, MKRN3-mediated ubiquitin signalling could control both transcriptional and post-transcriptional switches of mammalian puberty initiation. While identifying MKRN3 as a novel tissue-specific translational regulator, our work also provided new mechanistic insights into the etiology of MKRN3 dysfunction-associated human CPP. Show less
no PDF DOI: 10.1093/nar/gkab155
PABPC4
Guohua Chen, Xiaobing He, Huaijie Jia +6 more · 2021 · Virology journal · BioMed Central · added 2026-04-24
Orf virus (ORFV) is a member of the genus Parapoxvirus and family Poxviridae. The virus has a worldwide distribution and infects sheep, goats, humans, and wild animals. However, due to the complex str Show more
Orf virus (ORFV) is a member of the genus Parapoxvirus and family Poxviridae. The virus has a worldwide distribution and infects sheep, goats, humans, and wild animals. However, due to the complex structure of the poxvirus, the underlying mechanism of the entry and infection by ORFV remains largely unknown. ORFV ORF047 encodes a protein named L1R. Poxviral L1R serves as the receptor-binding protein and blocks virus binding and entry independently of glycosaminoglycans (GAGs). The study aimed to identify the host interaction partners of ORFV ORF047. Yeast two-hybrid cDNA library of sheep testicular cells was applied to screen the host targets with ORF047 as the bait. ORF047 was cloned into a pBT3-N vector and expressed in the NMY51 yeast strain. Then, the expression of bait proteins was validated by Western blot analysis. Sheep SERP1and PABPC4 were identified as host target proteins of ORFV ORF047, and a Co-IP assay further verified their interaction. New host cell proteins SERP1and PABPC4 were found to interact with ORFV ORF047 and might involve viral mRNA translation and replication. Show less
no PDF DOI: 10.1186/s12985-021-01499-y
PABPC4
Yiming Lei, Xuan Xu, Huiling Liu +5 more · 2021 · Autophagy · Taylor & Francis · added 2026-04-24
The hepatitis B virus X protein (HBx) is involved in the process of hepatocellular carcinoma via the activation of various oncogenes. Our previous study indicated that ARBB1 (arrestin beta 1) promotes Show more
The hepatitis B virus X protein (HBx) is involved in the process of hepatocellular carcinoma via the activation of various oncogenes. Our previous study indicated that ARBB1 (arrestin beta 1) promotes hepatocellular carcinogenesis (HCC). However, the role of ARRB1 in HBx-related HCC remains unclear. Herein, we identified that ARRB1 was upregulated by HBx Show less
no PDF DOI: 10.1080/15548627.2021.1917948
PIK3C3
Tzu-Yin Lee, Wan-Jung Lu, Chun A Changou +11 more · 2021 · Autophagy · Taylor & Francis · added 2026-04-24
Basal macroautophagy/autophagy has recently been found in anucleate platelets. Platelet autophagy is involved in platelet activation and thrombus formation. However, the mechanism underlying autophagy Show more
Basal macroautophagy/autophagy has recently been found in anucleate platelets. Platelet autophagy is involved in platelet activation and thrombus formation. However, the mechanism underlying autophagy in anucleate platelets require further clarification. Our data revealed that LC3-II formation and SQSTM1/p62 degradation were noted in H Show less
no PDF DOI: 10.1080/15548627.2021.1904495
PIK3C3
Guan Yang, Wenqiang Song, Jielin Xu +6 more · 2021 · Cellular & molecular immunology · Nature · added 2026-04-24
The PIK3C3/VPS34 subunit of the class III phosphatidylinositol 3-kinase (PtdIns3K) complex plays a role in both canonical and noncanonical autophagy, key processes that control immune-cell responsiven Show more
The PIK3C3/VPS34 subunit of the class III phosphatidylinositol 3-kinase (PtdIns3K) complex plays a role in both canonical and noncanonical autophagy, key processes that control immune-cell responsiveness to a variety of stimuli. Our previous studies found that PIK3C3 is a critical regulator that controls the development, homeostasis, and function of dendritic and T cells. In this study, we investigated the role of PIK3C3 in myeloid cell biology using myeloid cell-specific Pik3c3-deficient mice. We found that Pik3c3-deficient macrophages express increased surface levels of major histocompatibility complex (MHC) class I and class II molecules. In addition, myeloid cell-specific Pik3c3 ablation in mice caused a partial impairment in the homeostatic maintenance of macrophages expressing the apoptotic cell uptake receptor TIM-4. Pik3c3 deficiency caused phenotypic changes in myeloid cells that were dependent on the early machinery (initiation/nucleation) of the classical autophagy pathway. Consequently, myeloid cell-specific Pik3c3-deficient animals showed significantly reduced severity of experimental autoimmune encephalomyelitis (EAE), a primarily CD4 Show less
no PDF DOI: 10.1038/s41423-020-00589-1
PIK3C3
Wenxin Du, Aixiao Xu, Yunpeng Huang +6 more · 2021 · Autophagy · Taylor & Francis · added 2026-04-24
Although molecular targeted therapies have recently displayed therapeutic effects in acute myeloid leukemia (AML), limited response and acquired resistance remain common problems. Numerous studies hav Show more
Although molecular targeted therapies have recently displayed therapeutic effects in acute myeloid leukemia (AML), limited response and acquired resistance remain common problems. Numerous studies have associated autophagy, an essential degradation process involved in the cellular response to stress, with the development and therapeutic response of cancers including AML. Thus, we review studies on the role of autophagy in AML development and summarize the linkage between autophagy and several recurrent genetic abnormalities in AML, highlighting the potential of capitalizing on autophagy modulation in targeted therapy for AML. Show less
no PDF DOI: 10.1080/15548627.2020.1822628
PIK3C3
Boli Hu, Yina Zhang, Tingjuan Deng +9 more · 2021 · Autophagy · Taylor & Francis · added 2026-04-24
PDPK1 (3-phosphoinositide dependent protein kinase 1) is a phosphorylation-regulated kinase that plays a central role in activating multiple signaling pathways and cellular processes. Here, this study Show more
PDPK1 (3-phosphoinositide dependent protein kinase 1) is a phosphorylation-regulated kinase that plays a central role in activating multiple signaling pathways and cellular processes. Here, this study shows that PDPK1 turns on macroautophagy/autophagy as a SUMOylation-regulated kinase. Show less
no PDF DOI: 10.1080/15548627.2020.1817279
PIK3C3
Yuanyuan Chu, Yingjin Kang, Cong Yan +4 more · 2021 · Autophagy · Taylor & Francis · added 2026-04-24
Macroautophagy/autophagy is a membrane-mediated intracellular degradation pathway, through which bulky cytoplasmic content is digested in lysosomes. How the autophagy initiation and maturation steps a Show more
Macroautophagy/autophagy is a membrane-mediated intracellular degradation pathway, through which bulky cytoplasmic content is digested in lysosomes. How the autophagy initiation and maturation steps are regulated is not clear. In this study, we found an E3 ubiquitin ligase complex, linear ubiquitin chain assembly complex (LUBAC) and a deubiquitinating enzyme (DUB) OTULIN localize to the phagophore area to control autophagy initiation and maturation. LUBAC key component RNF31/HOIP translocates to the LC3 puncta area when autophagy is induced. Show less
no PDF DOI: 10.1080/15548627.2020.1781393
PIK3C3
Guan Yang, Wenqiang Song, J Luke Postoak +5 more · 2021 · Autophagy · Taylor & Francis · added 2026-04-24
The PIK3C3/VPS34 subunit of the class III phosphatidylinositol 3-kinase (PtdIns3K) complex is a key early player in macroautophagy/autophagy. In this study, we assessed the contribution of PIK3C3 to T Show more
The PIK3C3/VPS34 subunit of the class III phosphatidylinositol 3-kinase (PtdIns3K) complex is a key early player in macroautophagy/autophagy. In this study, we assessed the contribution of PIK3C3 to T cell metabolism and function. We found that Show less
no PDF DOI: 10.1080/15548627.2020.1752979
PIK3C3
Shuifang Lei, Lixi Li, Xiaoqin Yang +6 more · 2021 · Journal of human genetics · Nature · added 2026-04-24
DNA methylation in peripheral blood is associated with breast cancer (BC) but has mainly been studied in Caucasian populations. We investigated the association between blood-based methylation of recep Show more
DNA methylation in peripheral blood is associated with breast cancer (BC) but has mainly been studied in Caucasian populations. We investigated the association between blood-based methylation of receptor-associated protein of the synapse (RAPSN) and BC in Chinese population. The methylation levels of 12 RAPSN CpG sites were quantitatively evaluated by mass spectrometry in two case-control studies with 283 sporadic BC cases and 331 controls totally. The association was analyzed by logistic regression adjusted for covariants. The RAPSN methylation levels in patients with variant clinical characteristics were investigated by non-parametric tests. We found a significant association between BC and altered RAPSN methylation in blood in women at premenopausal and perimenopausal (age < 50 years old), but not in the elder women. This was approved by two independent case-control studies as well as by combining the subjects of the two studies (taken all subjects together, age < 50 years old, per 5% of methylation, odds ratio (OR) range from 1.17 to 1.30 for two CpG sites; OR = 0.75 for one CpG site; all p values < 0.02). This age-related RAPSN methylation was further modified by human epidermal growth factor receptor 2 (HER2) status (age < 50 years old, HER2 negative, per 5% of methylation, OR range from 1.27 to 1.48 for two CpG sites; OR = 0.76 for one CpG site; all p values < 0.02). We elucidated an association between BC and blood-based RAPSN methylation influenced by age and the status of HER2 in Chinese population. Show less
no PDF DOI: 10.1038/s10038-021-00933-x
RAPSN