Ras GTPase-activating protein: a substrate and a potential binding protein of the protein-tyrosine kinase p56lck.
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Evidence that Llck-mediated phosphorylation of p56dok and p62dok may play a role in CD2 signalingTyrosine phosphorylation of CD45 phosphotyrosine phosphatase by p50csk kinase creates a binding site for p56lck tyrosine kinase and activates the phosphataseThe kinase, SH3, and SH2 domains of Lck play critical roles in T-cell activation after ZAP-70 membrane localizationLck-dependent tyrosyl phosphorylation of the phosphotyrosine phosphatase SH-PTP1 in murine T cellsThe human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activityAssociation of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1Differential actions of p60c-Src and Lck kinases on the Ras regulators p120-GAP and GDP/GTP exchange factor CDC25MmThe Ras GTPase-activating protein (GAP) is an SH3 domain-binding protein and substrate for the Src-related tyrosine kinase, HckKos1, a nonreceptor tyrosine kinase that suppresses Ras signalingPlatelet-derived growth factor receptor mediates activation of ras through different signaling pathways in different cell typesThe Lck SH3 domain negatively regulates localization to lipid rafts through an interaction with c-Cbl.Downregulation of Lck-mediated signal transduction by tip of herpesvirus saimiriIdentification of Lck-binding elements in tip of herpesvirus saimiri.Lck unique domain influences Lck specificity and biological function.The Src homology 2 domain of the protein-tyrosine kinase p56lck mediates both intermolecular and intramolecular interactions.Lck protein tyrosine kinase is a key regulator of T-cell activation and a target for signal intervention by Herpesvirus saimiri and other viral gene products.Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL.Overexpression, purification, and characterization of SHPTP1, a Src homology 2-containing protein-tyrosine-phosphatase.Kinetics of p56lck and p60src Src homology 2 domain binding to tyrosine-phosphorylated peptides determined by a competition assay or surface plasmon resonance.Dissociation of intracellular signaling pathways in response to partial agonist ligands of the T cell receptor.Binding of human immunodeficiency virus type 1 to CD4 induces association of Lck and Raf-1 and activates Raf-1 by a Ras-independent pathwayActivation of Ras in vitro and in intact fibroblasts by the Vav guanine nucleotide exchange protein.Direct stimulation of Vav guanine nucleotide exchange activity for Ras by phorbol esters and diglyceridesThe human immunodeficiency virus type 1 (HIV-1) CD4 receptor and its central role in promotion of HIV-1 infection.Enhancement of protein kinase C-dependent O2 production in Epstein-Barr virus-transformed B lymphocytes by p120Ras-GAP antisense oligonucleotide.The cytoplasmic domain of CD4 is sufficient for its down-regulation from the cell surface by human immunodeficiency virus type 1 Nef.Phosphorylation and cytoskeletal anchoring of the acetylcholine receptor by Src class protein-tyrosine kinases. Activation by rapsyn.p120 GAP requirement in normal and malignant human hematopoiesis.Mouse monoclonal antibodies that specifically recognize an amino-terminal epitope of p56lck protein tyrosine kinase.
P2860
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P2860
Ras GTPase-activating protein: a substrate and a potential binding protein of the protein-tyrosine kinase p56lck.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Ras GTPase-activating protein: ...... rotein-tyrosine kinase p56lck.
@en
type
label
Ras GTPase-activating protein: ...... rotein-tyrosine kinase p56lck.
@en
prefLabel
Ras GTPase-activating protein: ...... rotein-tyrosine kinase p56lck.
@en
P2093
P2860
P356
P1476
Ras GTPase-activating protein: ...... rotein-tyrosine kinase p56lck.
@en
P2093
P2860
P304
P356
10.1073/PNAS.89.8.3343
P407
P577
1992-04-01T00:00:00Z