C
Chuan-Jin Wu
Researcher at University of Pennsylvania
Publications - 6
Citations - 678
Chuan-Jin Wu is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Kinase & Cell surface receptor. The author has an hindex of 6, co-authored 6 publications receiving 647 citations. Previous affiliations of Chuan-Jin Wu include University of Science and Technology of China.
Papers
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Journal ArticleDOI
Rationally designed anti-HER2/neu peptide mimetic disables P185HER2/neu tyrosine kinases in vitro and in vivo.
Byeong Woo Park,Hongtao Zhang,Chuan-Jin Wu,Alan Berezov,Xin Zhang,Raj Dua,Qiang Wang,Gary D. Kao,Donald M. O'Rourke,Mark I. Greene,Ramachandran Murali +10 more
TL;DR: A structure-based derivation of the AHNP represents a novel strategy for the design of receptor-specific tumor therapies for p185HER2/neu-expressing human cancers.
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The tyrosine phosphatase SHP-2 is required for mediating phosphatidylinositol 3-kinase/Akt activation by growth factors.
TL;DR: It is concluded that SHP-2 is required for mediating PI3K/Akt activation, and the N-terminal SH2 domain is critically important for a ‘positive’ role of SHp-2 in regulatingPI3K pathway activation.
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Hypoxia-inducible factor-2 regulates vascular tumorigenesis in mice.
Erinn B. Rankin,Jennifer Rha,Travis L. Unger,Chuan-Jin Wu,H P Shutt,Randall S. Johnson,M. C. Simon,Brian Keith,Volker H. Haase +8 more
TL;DR: It is demonstrated genetically that conditional inactivation of Hif-2α suppressed the development of VHL-associated liver hemangiomas and that angiogenic gene expression in hepatocytes is predominantly regulated by HIF-2 and not by H IF-1.
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Inhibition of EGFR-mediated phosphoinositide-3-OH kinase (PI3-K) signaling and glioblastoma phenotype by Signal-Regulatory Proteins (SIRPs)
TL;DR: Results suggest that negative regulation of PI3-K pathway activation by the SIRP family of transmembrane receptors may diminish EGFR-mediated motility and survival phenotypes that contribute to transformation of glioblastoma cells.
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Inhibition of a naturally occurring EGFR oncoprotein by the p185neu ectodomain: implications for subdomain contributions to receptor assembly.
Donald M. O'Rourke,Eric Jl Nute,James G. Davis,Chuan-Jin Wu,Acha Lee,Ramachandran Murali,Hongtao Zhang,Xiaolan Qian,Chih-Ching Kao,Mark I. Greene +9 more
TL;DR: T691stop neu mutant receptors abrogate the dramatic growth advantage conferred by ΔEGFR in vivo, suggesting that physical associations primarily between subdomains III and IV of the p185neu and EGFR ectodomains are sufficient to modulate signaling from activated EGFR complexes.