J
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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Journal ArticleDOI
Tyrosine phosphorylation and cytoskeletal reorganization in platelets are triggered by interaction of integrin receptors with their immobilized ligands.
TL;DR: Results indicate that platelet adhesion to fibrinogen or collagen induces signal transduction that is initiated through integrins GP IIb-IIIa and alpha 2 beta 1, respectively, which is accompanied by cytoskeletal reorganization and changes in cell shape.
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Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is required for induction of autophagy during lumen formation in vitro
TL;DR: It is shown that the tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) mediates induction of autophagic processes associated with lumen formation during MCF-10A morphogenesis.
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Vav family GEFs link activated Ephs to endocytosis and axon guidance.
Christopher W. Cowan,Yu Raymond Shao,Mustafa Sahin,Mustafa Sahin,Steven M. Shamah,Michael Z. Lin,Paul L. Greer,Sizhen Gao,Eric C. Griffith,Joan S. Brugge,Michael E. Greenberg +10 more
TL;DR: It is found that, during axon guidance, ephrin binding to Ephs triggers Vav-dependent endocytosis of the ligand-receptor complex, thus converting an initially adhesive interaction into a repulsive event.
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Identification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domains.
Zhigang Weng,Sheila M. Thomas,R. J. Rickles,J. A. Taylor,A. W. Brauer,C. Seidel-Dugan,W. M. Michael,Gideon Dreyfuss,Joan S. Brugge +8 more
TL;DR: A role for the Src SH3 domain is strongly suggested in the recruitment of substrates to this protein tyrosine kinase, either through direct interaction with the SH3domain or indirectly through interactions with proteins that bind to theSH3 domain.
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Cooperation of the ErbB2 receptor and transforming growth factor β in induction of migration and invasion in mammary epithelial cells
Sarah E. Seton-Rogers,Yu Lu,Lisa M. Hines,Malvika Koundinya,Joshua LaBaer,Senthil K. Muthuswamy,Senthil K. Muthuswamy,Joan S. Brugge +7 more
TL;DR: The role of TGFbeta as a pro-invasion factor in the progression of breast cancers with activated ErbB2 is supported and activation of the Erk and epidermal growth factor receptor pathways are suggested to be key in mediating these events.