9 Papers
61 Citations
Jun Wu is an academic researcher from Shanghai Jiao Tong University. The author has contributed to research in topics: T cell & Proto-oncogene tyrosine-protein kinase Src. The author has an hindex of 7, co-authored 9 publications. Previous affiliations of Jun Wu include Chinese National Human Genome Center.
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Papers
Functional characterization of human PFTK1 as a cyclin-dependent kinase
Fang Shu,Shun Lv,Yan Qin,Xinlu Ma,Xin Wang,Xiaozhong Peng,Ying Luo,Bing-e Xu,Xiaoqing Sun,Jun Wu +9 more
TL;DR: It is suggested that PFTK1 acts as a CDK that regulates cell cycle progression and cell proliferation and the tumor suppressor Rb is identified as a potential downstream substrate for the P FTK1/CCND3 complex.
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TRB3 interacts with CtIP and is overexpressed in certain cancers.
TL;DR: TRB3 interacted with an important cell cycle regulator CtIP (CtBP-interacting protein) and the interaction involved the C-terminus of both proteins and Interestingly, TRB3 and CtIP co-localized to the nucleus in HeLa cells and exhibited a unique dot-like pattern.
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Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells.
Fengwei Tan,Lifang Lu,Yun Cai,Jinglan Wang,Yunfei Xie,Lin Wang,Yanhua Gong,Bing-e Xu,Jun Wu,Ying Luo,Boqin Qiang,Jiangang Yuan,Xiaoqing Sun,Xiaozhong Peng +13 more
TL;DR: This study used immobilized GST‐S5a fusion protein to affinity‐purify ubiquitinated proteins from Chang liver cells to identify potential ubiquitination substrates, which are mainly related to important cellular functions including metabolism, translation and transcription.
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iASPP mediates p53 selectivity through a modular mechanism fine-tuning DNA recognition.
Sheng-hong Chen,Jun Wu,Shan Zhong,Yin Li,P Zhang,Jianhui Ma,Jingshan Ren,Yun Tan,Yunhao Wang,Kin Fai Au,Christian Siebold,Gareth L. Bond,Zuojia Chen,Min Lu,E Y Jones,Xin Lu +15 more
TL;DR: This study addresses the mechanism by which iASPP, a p53 partner, influences p53 target gene selection and identifies sequence signatures enriched in genomic p53-binding sites modulated by the transcription cofactor i ASPP.
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Adapter protein NRBP associates with Jab1 and negatively regulates AP-1 activity.
TL;DR: It is shown here that Jab1 interacts in vivo with nuclear receptor binding protein (NRBP), an evolutionarily conserved adapter protein with a kinase‐like domain that may be an important negative regulator of Jab1‐mediated functions such as gene transcription and tumor progression.
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