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Xiuwen Zhu
Researcher at Sanford-Burnham Institute for Medical Research
Publications - 10
Citations - 577
Xiuwen Zhu is an academic researcher from Sanford-Burnham Institute for Medical Research. The author has contributed to research in topics: TRAF3 & Peptide. The author has an hindex of 6, co-authored 9 publications receiving 538 citations. Previous affiliations of Xiuwen Zhu include Discovery Institute.
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Journal ArticleDOI
A Short Nur77-Derived Peptide Converts Bcl-2 from a Protector to a Killer
Siva Kumar Kolluri,Xiuwen Zhu,Xin Zhou,Bingzhen Lin,Ya Chen,Kai Sun,Xuefei Tian,James Town,Xihua Cao,Feng Lin,Dayong Zhai,Shinichi Kitada,Frederick Luciano,Edmond F. O’Donnell,Yu Cao,Feng He,Jialing Lin,John C. Reed,Arnold C. Satterthwait,Xiao-kun Zhang +19 more
TL;DR: The identification of a Nur77-derived Bcl-2-converting peptide with 9 amino acids (NuBCP-9) and its enantiomer, which induce apoptosis of cancer cells in vitro and in animals.
Journal ArticleDOI
Humanin binds and nullifies Bid activity by blocking its activation of Bax and Bak.
TL;DR: Bid represents an additional cellular target of HN, and it is proposed that HN-mediated suppression of Bid contributes to the antiapoptotic activity of this endogenous peptide.
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Cytoprotective peptide humanin binds and inhibits proapoptotic Bcl-2/Bax family protein BimEL.
Frederic Luciano,Dayong Zhai,Xiuwen Zhu,Béatrice Bailly-Maitre,Jean-Ehrland Ricci,Arnold C. Satterthwait,John C. Reed +6 more
TL;DR: The results indicate that the inhibition of BimEL may contribute to the antiapoptotic properties of the HN peptide.
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Key Molecular Contacts Promote Recognition of the BAFF Receptor by TNF Receptor-Associated Factor 3: Implications for Intracellular Signaling Regulation
Chao-Zhou Ni,Gagik Oganesyan,Kate Welsh,Xiuwen Zhu,John C. Reed,Arnold C. Satterthwait,Genhong Cheng,Kathryn R. Ely +7 more
TL;DR: The structure of the complex provides a molecular explanation for binding affinities and selective protein interactions in TNFR-TRAF interactions.
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LMP1 Protein from the Epstein-Barr Virus Is a Structural CD40 Decoy in B Lymphocytes for Binding to TRAF3 *
ShuangDing Wu,Ping Xie,Kate Welsh,Chenglong Li,Chao-Zhou Ni,Xiuwen Zhu,John C. Reed,Arnold C. Satterthwait,Gail A. Bishop,Kathryn R. Ely +9 more
TL;DR: The crystal structure of this portion of L MP1 C-terminal activation region-1 (204PQQATDD210) bound in complex with TRAF3 is reported, providing a molecular mechanism for LMP1 to act as a CD40 decoy for TRAF 3, influencing downstream signaling to B lymphocytes and contributing to dysregulated signaling by LMP 1.