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BCR — SRC

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Bind_translation Interaction: SRC — BCR (affinity chromatography technology) Muller et al., Mol Cell Biol 1992
• IRef Hprd Interaction: SRC — BCR (in vitro) Muller et al., Mol Cell Biol 1992
• IRef Ophid Interaction: SRC — BCR (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Gazumyan et al., J Exp Med 2006 : BCR cross linking resulted in decreased Src and Syk activation but paradoxically enhanced and prolonged BCR signaling, as measured by cellular tyrosine phosphorylation, Ca ( ++ ) flux, AKT, and ERK activation
Fiskus et al., Clin Cancer Res 2006 (Leukemia, Myelogenous, Chronic, BCR-ABL Positive) : Treatment with dasatinib attenuated the levels of autophosphorylated Bcr-Abl , p-CrkL, phospho-signal transducer and activator of transcription 5 ( p-STAT5 ), p-c-Src, and p-Lyn ; inhibited the activity of Lyn and c-Src ; and induced apoptosis of the cultured CML cells
Li et al., Int J Biochem Cell Biol 2007 (Precursor Cell Lymphoblastic Leukemia-Lymphoma) : Retained activation of Src kinases by the BCR-ABL oncoprotein in leukaemic cells following inhibition of BCR-ABL kinase activity by imatinib indicates that Src activation by BCR-ABL is independent of BCR-ABL kinase activity and provides an explanation for reduced effectiveness of the BCR-ABL kinase activity inhibitors in Philadelphia chromosome positive acute lymphoblastic leukaemia
Konig et al., Blood 2008 (Leukemia, Myelogenous, Chronic, BCR-ABL Positive) : SKI-606 effectively inhibited Bcr-Abl kinase activity in CML CD34 ( + ) cells and inhibited Src phosphorylation more potently than imatinib
Konig et al., Cancer Res 2008 (Leukemia, Myelogenous, Chronic, BCR-ABL Positive) : In contrast, Imatinib inhibited only Bcr-Abl dependent Src activity
Mahon et al., Cancer Res 2008 (Leukemia, Myelogenous, Chronic, BCR-ABL Positive) : Two Src kinase inhibitors ( PP1 and PP2 ) partially removed resistance but did not significantly inhibit Bcr-Abl tyrosine kinase activity ... In contrast, dasatinib, a dual Bcr-Abl and Src kinase inhibitor, inhibited the phosphorylation of both BCR-ABL and Lyn, and induced apoptosis of the Bcr-Abl cell line overexpressing p53/56 Lyn
Ramadani et al., Science signaling 2010 : Whereas the activation of the tyrosine kinases Src and Syk is essential for BCR signaling, the pathways that act downstream of these kinases are incompletely defined
Takata et al., FEBS Lett 1995 : These results demonstrate that the BCR induced phosphorylation of Src-PTK is independent of Syk and that the kinase activity of Src-PTK is critical for BCR signaling ... These results demonstrate that the BCR induced phosphorylation of Src-PTK is independent of Syk and that the kinase activity of Src-PTK is critical for BCR signaling