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Joan S. Brugge

Researcher at Harvard University

Publications -  302
Citations -  51153

Joan S. Brugge is an academic researcher from Harvard University. The author has contributed to research in topics: Proto-oncogene tyrosine-protein kinase Src & Phosphorylation. The author has an hindex of 115, co-authored 286 publications receiving 47965 citations. Previous affiliations of Joan S. Brugge include Howard Hughes Medical Institute & Massachusetts Institute of Technology.

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Peptide analysis of the transformation-specific antigen from avian sarcoma virus-transformed cells.

TL;DR: Sera from rabbits bearing tumors induced by avian sarcoma virus were ussed to immunopecipitate virus-specific proteins from extracts of chicken, hamster, and field vole cells transformed by ASV, suggesting that the 60K protein is virus coded.
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Functional proteomics approach to investigate the biological activities of cDNAs implicated in breast cancer.

TL;DR: The functional activity of a subset of the BC1000 collection was evaluated in cell-based assays that monitor changes in cell proliferation, migration, and morphogenesis in MCF-10A mammary epithelial cells expressing a variant of ErbB2 that can be inducibly activated through dimerization.
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PTK6 regulates IGF-1-induced anchorage-independent survival.

TL;DR: The combined genomic and proteomic approaches in this report provide an effective strategy for identifying oncogenes and their mechanism of action and highlight PTK6 as a critical regulator of anchorage-independent survival of breast and ovarian tumor cells via modulation of IGF-1 receptor signaling.
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Thrombin receptor activation and integrin engagement stimulate tyrosine phosphorylation of the proto-oncogene product, p95vav, in platelets.

TL;DR: Results show that Vav phosphorylation by tyrosine kinases occurs during platelet activation by potent agonists, also occurs when platelets adhere to biologically relevant matrix proteins, requires neither platelet aggregation nor the release of secondary agonists such as ADP and TxA, and can be initiated by at least some members of two additional classes of receptors.