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Xiu Jun Wang
Researcher at Zhejiang University
Publications - 41
Citations - 3634
Xiu Jun Wang is an academic researcher from Zhejiang University. The author has contributed to research in topics: Cancer & Transcription factor. The author has an hindex of 22, co-authored 41 publications receiving 2797 citations. Previous affiliations of Xiu Jun Wang include Ninewells Hospital & University of Dundee.
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Nrf2 signaling pathway: Pivotal roles in inflammation.
TL;DR: The members of the Keap1/Nrf2/ARE signal pathway and its downstream genes, the effects of this pathway on animal models of inflammatory diseases, and crosstalk with the NF-κB pathway are discussed.
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Generation of a Stable Antioxidant Response Element–Driven Reporter Gene Cell Line and Its Use to Show Redox-Dependent Activation of Nrf2 by Cancer Chemotherapeutic Agents
TL;DR: The findings show that Nrf2 can be activated by certain anticancer agents, and this will influence the effectiveness of chemotherapy.
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Luteolin inhibits Nrf2 leading to negative regulation of the Nrf2/ARE pathway and sensitization of human lung carcinoma A549 cells to therapeutic drugs.
TL;DR: It is demonstrated that an Nrf2 inhibitor can enhance the responsiveness of cancer cells to chemotherapeutic drugs and indicates the potential application of luteolin as a natural sensitizer in chemotherapy.
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Identification of retinoic acid as an inhibitor of transcription factor Nrf2 through activation of retinoic acid receptor alpha
TL;DR: Cross-talk between Nrf2 and RARα could markedly influence the sensitivity of cells to electrophiles and oxidative stressors and, as a consequence, to carcinogenesis.
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RXRα Inhibits the NRF2-ARE Signaling Pathway through a Direct Interaction with the Neh7 Domain of NRF2
Hongyan Wang,Kaihua Liu,Miao Geng,Peng Gao,Xiaoyuan Wu,Yan Hai,Yangxia Li,Yulong Li,Lin Luo,John D. Hayes,Xiu Jun Wang,Xiuwen Tang +11 more
TL;DR: It is reported that retinoic X receptor alpha (RXRα) is a hitherto unrecognized repressor of NRF2, and its findings show that RXRα diminishes cytoprotection byNRF2 by binding directly to the newly defined Neh7 domain in NRF 2.