Evidence that the Abelson virus protein functions in vivo as a protein kinase that phosphorylates tyrosine
about
ABL tyrosine kinases: evolution of function, regulation, and specificityThe PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activityThe Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and diseaseMultiple signaling interactions of Abl and Arg kinases with the EphB2 receptorBiology-driven cancer drug development: back to the futureIdentification and biochemical characterization of p70TRK, product of the human TRK oncogene.Phosphoproteomics in cancerTransformation-defective mutants of Snyder-Theilen feline sarcoma virus lack tyrosine-specific protein kinase activity.Phosphorylation of the Abelson murine leukemia virus transforming protein.Similarities and differences between the effects of epidermal growth factor and Rous sarcoma virus.The 46,000-dalton tyrosine protein kinase substrate is widespread, whereas the 36,000-dalton substrate is only expressed at high levels in certain rodent tissuesPhosphorylation of synthetic peptides by a tyrosine protein kinase from the particulate fraction of a lymphoma cell lineAnalysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation.Altered epidermal growth factor (EGF)-stimulated protein kinase activity in variant A431 cells with altered growth responses to EGF.Insertional mutagenesis of the Abelson murine leukemia virus genome: identification of mutants with altered kinase activity and defective transformation ability.Oncogene expression in autoimmune and normal peripheral blood mononuclear cellsTemperature-sensitive mutants of Abelson murine leukemia virus deficient in protein tyrosine kinase activity.Conservation of function of Drosophila melanogaster abl and murine v-abl proteins in transformation of mammalian cells.Multiple steps are required for the induction of tumors by Abelson murine leukemia virus.Activation of the c-abl oncogene by viral transduction or chromosomal translocation generates altered c-abl proteins with similar in vitro kinase propertiesOnly site-directed antibodies reactive with the highly conserved src-homologous region of the v-abl protein neutralize kinase activity.Detection of the v-abl gene product at cell-substratum contact sites in Abelson murine leukemia virus-transformed fibroblasts.Phosphotyrosine antibodies identify the p210c-abl tyrosine kinase and proteins phosphorylated on tyrosine in human chronic myelogenous leukemia cellsMonoclonal antibodies to the transforming protein of Fujinami avian sarcoma virus discriminate between different fps-encoded proteinsPhosphorylation of the ribosomal protein S6 is elevated in cells transformed by a variety of tumor viruses.Normal cellular and transformation-associated abl proteins share common sites for protein kinase C phosphorylation.Abelson murine leukemia virus P120: identification and characterization of tyrosine phosphorylation sites.Detection of an 85,000-dalton phosphoprotein in ts110 murine sarcoma virus-infected cells with antiserum against a v-mos peptide.Phosphorylation patterns of tumour antigens in cells lytically infected or transformed by simian virus 40.Gene products of McDonough feline sarcoma virus have an in vitro-associated protein kinase that phosphorylates tyrosine residues: lack of detection of this enzymatic activity in vivo.Some lymphoid cell lines transformed by Abelson murine leukemia virus lack a major 36,000-dalton tyrosine protein kinase substrateTransformation by avian sarcoma viruses leads to phosphorylation of multiple cellular proteins on tyrosine residues.Detection of c-abl tyrosine kinase activity in vitro permits direct comparison of normal and altered abl gene productsCharacterization of the protein apparently responsible for the elevated tyrosine protein kinase activity in LSTRA cells.Four different classes of retroviruses induce phosphorylation of tyrosines present in similar cellular proteins.Two structurally and functionally different forms of the transforming protein of PRC II avian sarcoma virusCharacterization and use of monoclonal antibodies for isolation of phosphotyrosyl proteins from retrovirus-transformed cells and growth factor-stimulated cellsTargeted gene disruption of the endogenous c-abl locus by homologous recombination with DNA encoding a selectable fusion protein.Ras complements the carboxyl terminus of v-Abl protein in lymphoid transformation.Fighting Cancer with Mathematics and Viruses.
P2860
Q24299738-A46DAD36-9488-49E0-ADDB-71CC93C6C181Q24606662-B673AEDD-3E4D-4163-920D-8157D21BCB61Q24677033-472852CF-4982-4D3C-A8C8-EDE4A91FDB80Q28211704-FDE3E1AB-1CAD-44B8-A2AD-C96AB5DFF2A1Q33552888-21A5A162-A10D-4C3E-8DD8-548441424A7DQ34348845-E4842DF6-FA24-4FD7-87B0-913C8DF4A69FQ34539788-AD170F80-539E-4536-89E6-98D0D29F39E3Q35239924-F8C010B6-B2C9-4B1E-9B89-4C0BA35DA36DQ35241008-29D63766-DBC9-4CA4-A4E3-B27CAC1933D1Q36208799-DD2C3338-AAD1-406B-AB3C-9F176FE3B472Q36210101-8CED2768-0BD9-41BF-A4C5-261944F49E5FQ36276081-C474F65E-BA69-4556-A6B7-38D03F8CF932Q36281307-8C6ADB81-8DD4-4FA5-AA4C-720F12CF9B9CQ36291922-A07F1723-8D6B-446D-A1ED-46C5AF5F507BQ36305808-0392B1DC-7444-413D-B743-F8D0413AD150Q36351827-4A0C7B52-70C0-468A-973F-3F0887D9476FQ36782791-A0D3C496-A28B-4650-BECF-D98EC4B1B120Q36805895-711CF604-E464-44E7-A29D-49656F91EA11Q36827267-887993BB-26B1-4895-86C9-ADB10C25B9E0Q36884997-F1EFFB01-CAE4-4CFA-923B-A9B7B87B2B1CQ36892674-0129D678-C134-4B1A-8CD7-F6C7D6FD5F77Q36894083-621E6474-41A9-472D-B690-A1FC69649492Q36914545-1BD5587D-446C-4A56-A804-5A0C6BC706C0Q36916263-6A0D0792-D70A-4C3D-BAE1-605167ABDCB3Q36918313-EB15E556-A5BD-459C-BCCD-13E25D6104BCQ36924977-E4025C13-9BBC-4FC4-955F-16C9E4721E7AQ36928307-B418B07E-E646-4EB1-BC02-246EE29F961DQ36931771-561ECD12-A715-4CF8-9064-107BA307EC9CQ36933037-1C51458A-F025-495C-9105-A6D9D0834183Q36935559-499A644E-8B2C-4E82-9343-FB926038E305Q36935761-DDEC2546-A6EC-47DE-A4B9-17F29729044FQ36940699-86E47F23-A1F7-4F07-A9A3-2DFBCC534B74Q36951425-7ADCCF0B-1D64-45D7-83D3-39E7F664488BQ36955441-C85A51BA-5FA2-4A09-9C9F-208A4B37BFCAQ36956528-2ACDCC72-04BF-4B25-B706-39E0A357E550Q36974222-A6EE77C9-EEFD-4A09-B60E-6579D1D5922DQ36977273-A09BA04D-390B-48AF-BD73-2AC1C9A841EFQ37745308-58C16D41-7A22-46D0-A410-16A74302622EQ38362429-961607A6-3619-4B37-90C0-07B73C9030AAQ38612646-E180B90E-7623-4185-8D80-815E7CCD23BD
P2860
Evidence that the Abelson virus protein functions in vivo as a protein kinase that phosphorylates tyrosine
description
1981 nî lūn-bûn
@nan
1981 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1981 թվականի մարտին հրատարակված գիտական հոդված
@hy
1981年の論文
@ja
1981年論文
@yue
1981年論文
@zh-hant
1981年論文
@zh-hk
1981年論文
@zh-mo
1981年論文
@zh-tw
1981年论文
@wuu
name
Evidence that the Abelson viru ...... e that phosphorylates tyrosine
@ast
Evidence that the Abelson viru ...... e that phosphorylates tyrosine
@en
type
label
Evidence that the Abelson viru ...... e that phosphorylates tyrosine
@ast
Evidence that the Abelson viru ...... e that phosphorylates tyrosine
@en
prefLabel
Evidence that the Abelson viru ...... e that phosphorylates tyrosine
@ast
Evidence that the Abelson viru ...... e that phosphorylates tyrosine
@en
P2093
P2860
P356
P1476
Evidence that the Abelson viru ...... e that phosphorylates tyrosine
@en
P2093
P2860
P304
P356
10.1073/PNAS.78.3.1552
P407
P577
1981-03-01T00:00:00Z