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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Characterization of a normal avian cell protein related to the avian sarcoma virus transforming gene product.
TL;DR: A protein from normal uninfected avian cells that is antigenically related to the pp60 src viral protein responsible for transformation by ASV is identified and characterized.
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Phage display selection of ligand residues important for Src homology 3 domain binding specificity
TL;DR: Additional ligand residue preferences were identified that can increase the affinity of SH3 peptide ligands at least 20-fold compared with core peptides and indicate that residues that flank the core binding sequences shared by many SH3 domains are important determinants of SH 3 binding affinity and selectivity.
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Adhesive ligand binding to integrin alpha IIb beta 3 stimulates tyrosine phosphorylation of novel protein substrates before phosphorylation of pp125FAK.
Min-Mei Huang,Lorraine Lipfert,Michael Cunningham,Joan S. Brugge,Mark H. Ginsberg,Sanford J. Shattil +5 more
TL;DR: It is demonstrated that fibrinogen binding to alpha IIb beta 3 initiates a process of tyrosine phosphorylation that precedes platelet aggregation and theosphorylation of pp125FAK, which may depend on the oligomerization of integrin receptors and on the state of actin polymerization.
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Identification of a novel integrin signaling pathway involving the kinase Syk and the guanine nucleotide exchange factor Vav1.
TL;DR: Syk and Vav1 regulate a unique integrin signaling pathway that differs from the FAK pathway in its proximity to the integrin itself, its localization to lamellipodia, and its activation, which is independent of actin polymerization.
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Requirements for Vav Guanine Nucleotide Exchange Factors and Rho GTPases in FcγR- and Complement-Mediated Phagocytosis
Amy B. Hall,M. Angelica Martinez Gakidis,Michael Glogauer,Julie L. Wilsbacher,Sizhen Gao,Wojciech Swat,Joan S. Brugge +6 more
TL;DR: Analysis of primary murine macrophages shows that constitutively active Rac is able to rescue actin polymerization and complement-mediated phagocytosis in Vav-deficient macrophage, suggesting that Rac is regulated by GEFs other than Vav downstream of the FcgammaR.