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Jun Sun

Researcher at University of Miami

Publications -  16
Citations -  1145

Jun Sun is an academic researcher from University of Miami. The author has contributed to research in topics: Proto-oncogene tyrosine-protein kinase Src & Estrogen receptor alpha. The author has an hindex of 10, co-authored 16 publications receiving 985 citations.

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p27 Phosphorylation by Src Regulates Inhibition of Cyclin E-Cdk2

TL;DR: The data indicate that phosphorylation by Src impairs the Cdk2 inhibitory action of p27 and reduces its steady-state binding to cyclin E-Cdk2-dependent p27 proteolysis, and this provides a new rationale for Src inhibitors in cancer therapy.
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VEGF Drives Cancer-Initiating Stem Cells Through VEGFR-2/Stat3 Signaling to Upregulate Myc and Sox2

TL;DR: High-VEGF tumors may be most likely to escape anti-angiogenics by upregulating VEGF, driving CSC self-renewal to re-populate post-treatment, and highlights the need to better define V EGF-driven cancer subsets and supports further investigation of combined therapeutic blockade of VEGFR-2 and JAK2/STAT3.
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Cytoplasmic p27 promotes epithelial–mesenchymal transition and tumor metastasis via STAT3-mediated Twist1 upregulation

TL;DR: An oncogenic feedforward loop in which p27pT157pT198 binds Janus kinase 2 (JAK2) promoting STAT3 (signal transducer and activator of transcription 3) recruitment and activation is described.
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WW domain binding protein-2, an E6-associated protein interacting protein, acts as a coactivator of estrogen and progesterone receptors.

TL;DR: It is demonstrated that WBP-2 and E6-associated protein each enhance PR function, and their effect on PR action are additive when coexpressed, suggesting a common signaling pathway.
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Src promotes estrogen-dependent estrogen receptor α proteolysis in human breast cancer

TL;DR: The results indicate that Src cooperates with estrogen to activate ERα proteolysis, and support a model whereby crosstalk between liganded ERα and Src drives ERα transcriptional activity and targets ERα for ubiquitin-dependent proteolytic activity.