A mutation at the ATP-binding site of pp60v-src abolishes kinase activity, transformation, and tumorigenicity.
about
The leukocyte common antigen (CD45): a putative receptor-linked protein tyrosine phosphataseMolecular cloning and chromosome mapping of the human gene encoding protein phosphotyrosyl phosphatase 1BStructural basis for chromosome X-linked agammaglobulinemia: a tyrosine kinase diseaseMolecular features of the viral and cellular Src kinases involved in interactions with the GTPase-activating protein.KSR1 is a functional protein kinase capable of serine autophosphorylation and direct phosphorylation of MEK1Nuclear DBF-2-related kinases are essential regulators of cytokinesis in bloodstream stage Trypanosoma bruceiThe Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and diseaseRole of tyrosine kinase and membrane-spanning domains in signal transduction by the platelet-derived growth factor receptorSH3 domain of c-Src governs its dynamics at focal adhesions and the cell membrane.Mutations in v-Src SH3 and catalytic domains that jointly confer temperature-sensitive transformation with minimal temperature-dependent changes in cellular tyrosine phosphorylationDeletions in the SH2 domain of p60v-src prevent association with the detergent-insoluble cellular matrixSite-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src.Adenovirus E4 open reading frame 4-induced apoptosis involves dysregulation of Src family kinases.Deletions and insertions within an amino-terminal domain of pp60v-src inactivate transformation and modulate membrane stabilityInhibition of the tyrosine kinase activity of v-src, v-fgr, and v-yes gene products by a monoclonal antibody which binds both amino and carboxy peptide fragments of pp60v-src.Intracellular calcium mobilization induces immediate early gene pip92 via Src and mitogen-activated protein kinase in immortalized hippocampal cells.A lysine in the ATP-binding site of P130gag-fps is essential for protein-tyrosine kinase activity.Tissue-specific transformation by epidermal growth factor receptor: a single point mutation within the ATP-binding pocket of the erbB product increases its intrinsic kinase activity and activates its sarcomagenic potential.Tissue-specific expression of three distinct types of rabbit protein kinase C.Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- and antibody-stimulated glucose uptake and receptor kinase activity.Cell lines and peripheral blood leukocytes derived from individuals with chronic myelogenous leukemia display virtually identical proteins phosphorylated on tyrosine residuesTyrosine 416 is phosphorylated in the closed, repressed conformation of c-Src.Conformational processing of oncogenic v-Src kinase by the molecular chaperone Hsp90.Replacement of lys 622 in the ATP binding domain of P100gag-mil abolishes the in vitro autophosphorylation of the protein and the biological properties of the v-mil oncogene of MH2 virusThe conserved lysine of the catalytic domain of protein kinases is actively involved in the phosphotransfer reaction and not required for anchoring ATPA CDK-related kinase regulates the length and assembly of flagella in Chlamydomonas.Heat-shock protein hsp90 governs the activity of pp60v-src kinaseThe epidermal growth factor receptor phosphorylates GTPase-activating protein (GAP) at Tyr-460, adjacent to the GAP SH2 domainsUbiquitin-mediated degradation of active Src tyrosine kinaseSchizosaccharomyces pombe ras1 and byr1 are functionally related genes of the ste family that affect starvation-induced transcription of mating-type genes.An alternative non-tyrosine protein kinase product of the c-src gene in chicken skeletal muscleFunctional expression and RNA binding analysis of the interferon-induced, double-stranded RNA-activated, 68,000-Mr protein kinase in a cell-free systemPhosphatidylinositol kinase activity associates with viral p60src protein.Resistance to oncogenic transformation in revertant R1 of human ras-transformed NIH 3T3 cellsRegulation of pp60c-src and its interaction with polyomavirus middle T antigen in insect cellsp37mos-associated serine/threonine protein kinase activity correlates with the cellular transformation function of v-mos.Neither arginine nor histidine can carry out the function of lysine-295 in the ATP-binding site of p60src.A mutant epidermal growth factor receptor with defective protein tyrosine kinase is unable to stimulate proto-oncogene expression and DNA synthesis.Protein tyrosine phosphorylation in synaptic vesicles.Lysine residue 121 in the proposed ATP-binding site of the v-mos protein is required for transformation.
P2860
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P2860
A mutation at the ATP-binding site of pp60v-src abolishes kinase activity, transformation, and tumorigenicity.
description
1985 nî lūn-bûn
@nan
1985年の論文
@ja
1985年論文
@yue
1985年論文
@zh-hant
1985年論文
@zh-hk
1985年論文
@zh-mo
1985年論文
@zh-tw
1985年论文
@wuu
1985年论文
@zh
1985年论文
@zh-cn
name
A mutation at the ATP-binding ...... formation, and tumorigenicity.
@en
type
label
A mutation at the ATP-binding ...... formation, and tumorigenicity.
@en
prefLabel
A mutation at the ATP-binding ...... formation, and tumorigenicity.
@en
P2093
P2860
P356
P1476
A mutation at the ATP-binding ...... formation, and tumorigenicity.
@en
P2093
A D Levinson
J P McGrath
M A Snyder
P2860
P304
P356
10.1128/MCB.5.7.1772
P407
P577
1985-07-01T00:00:00Z