Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src.
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Regulation of FynT function by dual domain docking on PAG/CbpCsk inhibition of c-Src activity requires both the SH2 and SH3 domains of SrcIntroduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinasesIdentification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeletonInhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.Eps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signalsThe SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth factor and epidermal growth factor treatmentThe 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 Fyn-ADAP Axis: Cytotoxicity Versus Cytokine Production in Killer CellsDirect binding of C-terminal region of p130Cas to SH2 and SH3 domains of Src kinaseProline-rich sequences that bind to Src homology 3 domains with individual specificitiesMutational analysis of the regulatory function of the c-Abl Src homology 3 domain.Molecular rulers: an assessment of distance and spatial relationships of Src tyrosine kinase Sh2 and active site regions.Intramolecular regulatory interactions in the Src family kinase Hck probed by mutagenesis of a conserved tryptophan residue.The role of the Src homology domains in morphological transformation by v-srcRequirement for c-Src catalytic activity and the SH3 domain in platelet-derived growth factor BB and epidermal growth factor mitogenic signaling.Deletion of the ABL SH3 domain reactivates de-oligomerized BCR-ABL for growth factor independence.Regulation of the Src protein tyrosine kinase.LckBP1, a proline-rich protein expressed in haematopoietic lineage cells, directly associates with the SH3 domain of protein tyrosine kinase p56lck.3BP-1, an SH3 domain binding protein, has GAP activity for Rac and inhibits growth factor-induced membrane ruffling in fibroblasts.SH3 domains specifically regulate kinase activity of expressed Src family proteins.Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527.Physical and functional interactions between SH2 and SH3 domains of the Src family protein tyrosine kinase p59fynMutations in v-Src SH3 and catalytic domains that jointly confer temperature-sensitive transformation with minimal temperature-dependent changes in cellular tyrosine phosphorylationAberrant protein phosphorylation at tyrosine is responsible for the growth-inhibitory action of pp60v-src expressed in the yeast Saccharomyces cerevisiae.Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides.The Src homology 2 domain of the protein-tyrosine kinase p56lck mediates both intermolecular and intramolecular interactions.Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae.En bloc substitution of the Src homology region 2 domain activates the transforming potential of the c-Abl protein tyrosine kinase.Activated lck tyrosine protein kinase stimulates antigen-independent interleukin-2 production in T cells.Host range mutants of v-src: alterations in kinase activity and substrate interactionsEffects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src.Mutations in the SH3 domain of the src oncogene which decrease association of phosphatidylinositol 3'-kinase activity with pp60v-src and alter cellular morphology.Selective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-srcIdentification and characterization of a novel cytoskeleton-associated pp60src substrate.The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110.BCR first exon sequences specifically activate the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias.Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins.Deletions in the SH2 domain of p60v-src prevent association with the detergent-insoluble cellular matrixMutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells.
P2860
Q24302122-B5961FF8-CE0D-452A-8671-BD0F31AE4687Q24310206-4F0CF411-7BF6-44F2-A6EC-0933C9DFEF40Q24316242-31F13CEF-BAF3-41B2-8EDC-641882749A7BQ24317739-96BC53B0-E188-4F4D-B720-C0CC29528444Q24564127-EE13BBDA-DAE3-427B-B846-24FD79DD8A38Q24564389-A37574C7-7A86-4F0A-B477-165D8249A265Q24600605-FF4063A7-0A44-4EE1-8D1C-BEE024FE6CB5Q24606662-6D5B8084-DE93-4D04-8117-7F7C03E339E9Q26781282-98713A24-2F4E-4B23-A216-367CF6494CB5Q28277700-93F9BC16-EA0F-4C2D-93D8-94B68107BE85Q28287774-3F6DFC09-F608-46E9-9E2F-35040153642AQ30167708-A7577656-B5C4-4F07-9F61-B1E71E1E8410Q30168550-2474960E-CD60-4257-A6E3-4DE2B1A073BDQ30175972-B33FFBD9-D70F-489B-ACA2-D1B682C8595CQ30176487-34EDDB57-EDF3-43AB-AD5D-63EDF4F86A0BQ30176895-A4878238-36C6-4E27-9FF8-2B49DE5DDC5CQ30192639-2A25AE7A-E124-47D3-B920-382278D45A99Q30193218-E8905EB3-CF2E-4086-AD52-C1DE826135CBQ30193253-0D4C9E98-D9D8-4C69-8EA7-05F77AD463D5Q30193301-29C70429-00BB-4AB5-87CD-A2C5C48813B2Q30193738-FD56477B-1FCE-4FE1-9C2D-73F1EAA97523Q30194001-FC13EF50-4C03-4B52-928B-34E293F38C57Q30194111-6BE8F98F-A5C5-42BB-BC04-4E720B68BF6EQ30194212-68422895-E522-4D53-A10C-200DF749CB52Q30194494-FD091C10-CC79-44E6-AF92-C803535D4E2CQ30194700-6CB9F128-F223-415E-A903-6C7D3A9C6DC0Q30194739-037987D9-10AF-411C-882F-368957C05897Q30194837-12200CDF-B390-4367-9163-2D95037A0816Q30195067-25CA7760-2E43-4C7C-BFE5-22EB4BECC8F8Q30195263-10B661FB-E7AF-469C-B6E9-79DC158CC495Q30195331-3063E1E1-7B01-473A-BE76-8394742427D2Q30195430-B7E31F27-0B84-43BD-B63D-46E129C3B636Q30195440-ECF6CA63-A7FF-4C8E-9B60-E4F805D48C94Q30195559-F7ED9A46-572F-4ECF-A2F1-0A34BD21018AQ30195583-A2BE29E3-AECF-4700-A54D-27EB29FDBD81Q30195658-EE6E426E-33DB-4405-B422-F0A9CF5ABD7DQ30195698-B0BEC555-F3C0-401E-B8C5-71498D3E25D5Q30195712-C439D144-0972-4FB9-A60B-0DE125F15831Q30195717-A415C7D4-4EF0-41A9-90B6-96D2D3328110Q30195788-4C3F013E-3FA9-4C38-9F01-D432408B80B8
P2860
Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src.
description
1990 nî lūn-bûn
@nan
1990 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Site-directed mutagenesis of t ...... ogenic activation of p60c-src.
@ast
Site-directed mutagenesis of t ...... ogenic activation of p60c-src.
@en
type
label
Site-directed mutagenesis of t ...... ogenic activation of p60c-src.
@ast
Site-directed mutagenesis of t ...... ogenic activation of p60c-src.
@en
prefLabel
Site-directed mutagenesis of t ...... ogenic activation of p60c-src.
@ast
Site-directed mutagenesis of t ...... ogenic activation of p60c-src.
@en
P2860
P356
P1476
Site-directed mutagenesis of t ...... ogenic activation of p60c-src.
@en
P2093
P2860
P304
P356
10.1128/MCB.10.4.1307
P407
P577
1990-04-01T00:00:00Z