Gene interactions and pathways from curated databases and text-mining

◀ Back to BCR

BCR — PTK7

Text-mined interactions from Literome

Bentley et al., Br J Haematol 2001 (Leukemia, Myelogenous, Chronic, BCR-ABL Positive) : In this study, we found that activation of Bcr -- Abl protein tyrosine kinase was associated with the stimulation of glucose transport in the multipotent haemopoietic cell line FDCP-mix, a cell model for chronic-phase chronic myeloid leukaemia ( CML )
Kawauchi et al., Int J Hematol 2002 (Leukemia, Lymphocytic, Chronic, B-Cell...) : However, in contrast to normal B-cells, in B-CLL cells several important signaling pathways, such as the activation of protein tyrosine kinase via BCR , are defective
Chen et al., Blood 2006 (Lymphoma) : BCR dependent activation of the SYK PTK initiates downstream signaling events and amplifies the original BCR signal
Barua et al., J Immunol 2012 (Calcium Signaling) : To study the effects of the positive and negative feedback loops on the dynamical stability of BCR signaling and the relative contributions of Lyn and Fyn to BCR signaling, we consider in this study a rule based model for early events in BCR signaling that encompasses membrane-proximal interactions of six proteins, as follows : BCR, Lyn, Fyn, Csk, PAG1, and Syk, a cytosolic protein tyrosine kinase that is activated as a result of SFK mediated phosphorylation of BCR
Kong et al., Immunity 1995 : Loss of the Syk PTK results in a nonfunctional BCR
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
Kawauchi et al., Mol Immunol 1996 : Ligation of the B cell Ag receptor (BCR) activates a protein-tyrosine kinase ( PTK ) and CD45 protein-tyrosine phosphatase ( PTPase ) -dependent signaling cascade that results in the activation of Ras
Li et al., J Biol Chem 1996 : These data show that tyrosine phosphorylation by FES affects the interaction of BCR with multiple signaling partners and suggest a general role for BCR in non-receptor protein-tyrosine kinase regulation and signal transduction