about
Relief of profound feedback inhibition of mitogenic signaling by RAF inhibitors attenuates their activity in BRAFV600E melanomasSelected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptorGrap is a novel SH3-SH2-SH3 adaptor protein that couples tyrosine kinases to the Ras pathwayLck-dependent tyrosyl phosphorylation of the phosphotyrosine phosphatase SH-PTP1 in murine T cellsp40phox, a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domainsExpression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell densityMeaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactionsBinding of Vav to Grb2 through dimerization of Src homology 3 domainsBinding of Bruton's tyrosine kinase to Fyn, Lyn, or Hck through a Src homology 3 domain-mediated interactionActivation of ternary complex factor Elk-1 by MAP kinasesA human oncogene of the RAS superfamily unmasked by expression cDNA cloningProtein kinase A antagonizes platelet-derived growth factor-induced signaling by mitogen-activated protein kinase in human arterial smooth muscle cellsA novel cytokine-inducible gene CIS encodes an SH2-containing protein that binds to tyrosine-phosphorylated interleukin 3 and erythropoietin receptorsRAS and RAF-1 form a signalling complex with MEK-1 but not MEK-2.Retroviral oncogenes: a historical primerMutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinaseAutophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src3pK, a new mitogen-activated protein kinase-activated protein kinase located in the small cell lung cancer tumor suppressor gene regionThe adaptor protein Grb2 is not essential for the establishment of the glomerular filtration barrierEndocytosis and Physiology: Insights from Disabled-2 Deficient MiceAssociation of p130CAS with phosphatidylinositol-3-OH kinase mediates adenovirus cell entryDifferential actions of p60c-Src and Lck kinases on the Ras regulators p120-GAP and GDP/GTP exchange factor CDC25MmRecent progress on the role of Axl, a receptor tyrosine kinase, in malignant transformation of myeloid leukemiasIQGAP1 binds ERK2 and modulates its activityMMTV mouse models and the diagnostic values of MMTV-like sequences in human breast cancerShcA tyrosine phosphorylation sites can replace ShcA binding in signalling by middle T-antigenOncogene proteins and proliferation antigens in thymomas: increased expression of epidermal growth factor receptor and Ki67 antigenThe role of the PH domain in the signal-dependent membrane targeting of Sos.Neuronal leucine-rich repeat protein-3 amplifies MAPK activation by epidermal growth factor through a carboxyl-terminal region containing endocytosis motifsImmunolocalization of the mitogen-activated protein kinases p42MAPK and JNK1, and their regulatory kinases MEK1 and MEK4, in adult rat central nervous systemThe N-terminal pleckstrin, coiled-coil, and IQ domains of the exchange factor Ras-GRF act cooperatively to facilitate activation by calciumShc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytesMASL1 induces erythroid differentiation in human erythropoietin-dependent CD34+ cells through the Raf/MEK/ERK pathwayThe Caenorhabditis elegans EGL-15 signaling pathway implicates a DOS-like multisubstrate adaptor protein in fibroblast growth factor signal transduction.The isoform-specific stretch of hSos1 defines a new Grb2-binding domain.Binding of the Grb2 SH2 domain to phosphotyrosine motifs does not change the affinity of its SH3 domains for Sos proline-rich motifs.Physical and functional interactions between SH2 and SH3 domains of the Src family protein tyrosine kinase p59fynRole of IRS-1-GRB-2 complexes in insulin signaling.Rapid T-cell receptor-mediated tyrosine phosphorylation of p120, an Fyn/Lck Src homology 3 domain-binding protein.Direct interaction of v-Src with the focal adhesion kinase mediated by the Src SH2 domain.
P2860
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P2860
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh-hant
name
Signal transduction. How receptors turn Ras on.
@en
Signal transduction. How receptors turn Ras on.
@nl
type
label
Signal transduction. How receptors turn Ras on.
@en
Signal transduction. How receptors turn Ras on.
@nl
prefLabel
Signal transduction. How receptors turn Ras on.
@en
Signal transduction. How receptors turn Ras on.
@nl
P356
P1433
P1476
Signal transduction. How receptors turn Ras on.
@en
P2093
McCormick F
P2888
P356
10.1038/363015A0
P407
P577
1993-05-01T00:00:00Z
P6179
1023945033