Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
NA
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
Src family kinases are required for integrin but not PDGFR signal transduction . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
EGFR , PDGFR ) or cytoplasmic ( Src , Abl ) tyrosine kinases are found mutated in a variety of human tumors . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
The work of Chen and colleagues shows that dasatinib is a particularly potent inhibitor of PDGFR and that the compound also targets Src kinase . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
Using PDGFR mutants , we have shown that the phosphorylation is exerted via a PDGFR src pathway . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
Transcripts coding for transcription factors ( RB , P 53 , FOS , MYC , MYB , ERBA , REL ) , growth factors ( FGF 1 , FGF 2 , INT 2 , TGFA , TGFB , PDGF , IGF 1 , IGF 2 ) , interleukins , ( IL 1 , IL 2 , IL 3 , IL 4 , IL 6 , TNF ) , growth factor receptors or cytosolic protein kinases ( RAF , PIM , FES , MET , SRC , ROS , TRK , KIT , CSFR , IGFR , PDGFR , EGFR , NEU ) were quantified in cultured human mammary fibroblasts from normal tissues , benign tumours , carcinomas and post radiation fibrosis lesions by slot blot autoradiography and image analysis . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
A PDGFR mutant ( F 5 ) that lacks high affinity binding sites for the Src homology 2 domain containing proteins phosphatidylinositol 3 kinase ( PI 3 kinase ) , Ras guanosine triphosphatase activating protein , phospholipase C gamma , and a phosphotyrosine phosphatase ( Syp ) remained at the cell periphery . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
Predominant expression of the src homology 2 containing tyrosine phosphatase protein SHP 2 in vascular smooth muscle cells . src homology 2 ( SH 2 ) containing protein tyrosine phosphatase SHP 2 is known to transduce positive signals from activated receptor protein tyrosine kinases such as platelet derived growth factor receptor ( PDGFR ) beta and insulin receptor . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
Compound 4b inhibited the PDGFr , FGFr , EGFr , and c src tyrosine kinases with IC 50 values of 1 . 11 , 0 . 13 , 0 . 45 , and 0 . 22 microM , respectively . ^^^ Compound 4e inhibited the FGFr tyrosine kinase with an IC 50 of 0 . 060 microM , whereas IC50s for the inhibition of the PDGFr , FGFr , EGFr , c src , and InsR tyrosine kinases for this compound ( 4e ) were all greater than 50 microM . . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
This review covers the literature on significant studies of small molecule inhibitors of the epidermal growth factor receptor ( EGFR ) , platelet derived growth factor receptor ( PDGFR ) , fibroblast growth factor receptor ( FGFR ) , Flk 1 , and src family tyrosine kinases from 1996 through mid 1997 . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
With a chimeric alpha beta PDGF receptor ( PDGFR ) expressed in fibroblasts , we have investigated the importance of the PDGF mediated increase in Src activity at the G0 / G1 transition for subsequent cell cycle events . ^^^ A mutant PDGFR chimera that was not able to detectably associate with or activate Src was compromised in its ability to mediate tyrosine phosphorylation of receptor associated signaling molecules and initiated a submaximal activation of Erk . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
To understand the structural basis for the potency and specificity , a model for the binding mode of this class of inhibitors to the tyrosine kinase domains of c Src , PDGFr , FGFr , and EGFr tyrosine kinases was developed from structural information ( principally utilizing the catalytic domain of c AMP dependent protein kinase as template ) and structure activity relationship ( SAR ) information . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
Compounds of this series were competitive with ATP and displayed submicromolar to low nanomolar potency against a panel of TKs , including receptor ( platelet derived growth factor , PDGFr ; fibroblast growth factor , FGFr ; epidermal growth factor , EGFr ) and nonreceptor ( c Src ) classes . ^^^ One of the more thoroughly evaluated members was 63 with IC 50 values of 0 . 079 microM ( PDGFr ) , 0 . 043 microM ( bFGFr ) , 0 . 044 microM ( EGFr ) , and 0 . 009 microM ( c Src ) . ^^^ In in vivo studies against a panel of seven xenograft tumor models with known and / or inferred dependence on the EGFr , PDGFr , and c Src TKs , compound 63 produced a tumor growth delay of 10 . 6 days against the relatively refractory SK OV 3 ovarian xenograft and also displayed activity against the HT 29 tumor . ^^^ Because of the excellent potency of 63 against selected TKs , in vitro and in vivo studies are underway for this compound in additional tumor models dependent upon PDGFr , FGFr , and c Src to assess its potential for advancement to clinical trials . . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
Screening of a compound library led to the identification of 2 amino 6 ( 2 , 6 dichlorophenyl ) 8 methylpyrido [ 2 , 3 d ] pyrimidine ( 1 ) as a inhibitor of the platelet derived growth factor receptor ( PDGFr ) , fibroblast growth factor receptor ( FGFr ) , and c src tyrosine kinases ( TKs ) . ^^^ Compound 54 , which had IC 50 values of 31 , 88 , and 31 nM against PDGFr , FGFr , and c src TK activity , respectively , was active in a variety of PDGF dependent cellular assays and blocked the in vivo growth of three PDGF dependent tumor lines . . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
An essential role for c Src was confirmed using the c Src inhibitor , PP 1 , which abolished p42 / p44 MAPK activation ( PP 1 and PTX were without effect on PDGFR tyrosine phosphorylation ) . ^^^ These findings suggest that the PDGFR can utilize the PTX sensitive G protein , Gi , to regulate c Src and subsequent p42 / p44 MAPK activation . ^^^ In conclusion , our results demonstrate that Gi enables the PDGFR to signal more efficiently to p42 / p44 MAPK , and this appears to be achieved through the regulation of c Src and Grb 2 / PI3K , which are intermediates in the p42 / p44 MAPK cascade . . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
Tyrosine kinase activity was modulated by inhibitors of beta PDGFR autophosphorylation in cells , but not by specific inhibitors of EGFR or c Src tyrosine kinase . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
Moreover , by using the specific platelet derived growth factor receptor ( PDGFR ) inhibitor AG 1296 or by overexpressing a kinase mutant PDGFR , we show that PDGFR kinase activity is essential for 5 HT2B triggered MAPK / cyclin D 1 , but not cyclin E , signaling pathways . 5 HT2B receptor activation also increases activity of the Src family kinase , c Src , Fyn , and c Yes . ^^^ Inhibition of c Src activity by 4 amino 5 ( 4 methylphenyl ) 7 ( t butyl ) pyrazolo [ 3 , 4 d ] pyrimidine ( PP 1 ) or depletion of c Src is sufficient to abolish the 5 HT induced ( 1 ) PDGFR tyrosine kinase phosphorylation and MAPK activation , ( 2 ) cyclin D 1 and cyclin E expression levels , and ( 3 ) thymidine incorporation . ^^^ This paper elucidates a model of 5 HT2B receptor mitogenesis in which c Src acts alone to control cyclin E induction and in concert with the receptor tyrosine kinase PDGFR to induce cyclin D 1 expression via the MAPK / ERK pathway . . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
Overall , there was a high degree of correlation of the activities against the different kinases , with c Src being generally the most sensitive to structural changes . 1 , 6 Naphthyridin 2 ( 1H ) one analogues bearing basic aliphatic side chains [ 7 NH ( CH ( 2 ) ) ( n ) ( ) NRR , 7 NHPhO ( CH ( 2 ) ) ( n ) ( ) NRR , or 7 NHPhN ( CH ( 2 ) ) ( 4 ) NMe ] were the most potent against c Src ( IC ( 50 ) s of 10 80 nM ) , showing good selectivity with respect to PDGFR ( 10 300 fold ) but less with respect to FGFR . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
The compounds were ATP competitive inhibitors of c Src kinase with IC ( 50 ) values < 10 nM and from 6 to > 100 fold selectivity for c Src tyrosine kinase relative to basic fibroblast growth factor receptor ( bFGFr ) tyrosine kinase , platelet derived growth factor receptor ( PDGFr ) tyrosine kinase , and epidermal growth factor receptor ( EGFr ) tyrosine kinase . ^^^ Autophosphorylation of EGFr tyrosine kinase or PDGFr tyrosine kinase was not inhibited by c Src inhibitors , thus showing the selective nature of the compounds in cells . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
Direct alkylation of the anion of the ( unprotected ) 7 amino group with excess 4 ( 3 chloropropyl ) morpholine in DMF gave low ( 10 % ) yields of the desired product , but alkylation of the 7 acetamido anion , followed by mild alkaline hydrolysis , raised this to 64 % . 3 Phenyl analogues were nonspecific inhibitors of isolated c Src , FGFR , and PDGFR tyrosine kinases , whereas 3 ( 2 , 6 dichlorophenyl ) analogues were most effective against c Src and FGFR , and 3 ( 3 , 5 dimethoxyphenyl ) derivatives showed high selectivity for FGFR alone . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
Two other peptides based on the C terminal regulatory site of the Src protein and the platelet derived growth factor receptor ( PDGFR ) are also investigated . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
The c Abl tyrosine ( Tyr ) kinase is activated after platelet derived growth factor receptor ( PDGFR ) stimulation in a manner that is partially dependent on Src kinase activity . ^^^ However , the activity of Src kinases alone is not sufficient for activation of c Abl by PDGFR . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
In the present study , we examined the activation of Src tyrosine kinase , a crucially important signaling molecule for PDGFR , and assessed the role of Src in PDGF B dependent renal tubular regeneration afterischemia / reperfusion injury . ^^^ In vitro kinase assay confirmed increased Src activity that concurred with PDGFR beta activation as detected by the increment of receptor phosphorylated tyrosine . ^^^ This enhanced expression of active Src was co localized with the increased PDGFR expression in the tubular cells that were undergoing cell proliferation cycle . ^^^ Trapidil administration suppressed Src and PDGFR beta activation in the reperfused kidney and resulted in deteriorated renal function . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
We therefore explored the possibility that integrin alpha 5 beta 3 cooperates with PDGFr to promote cell migration in glioblastoma cells , and extended the study to identify the Src family members that are activated on PDGF stimulation . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
PDGFR , not FAK or EGFR , appears to be the upstream protein tyrosine kinase responsible for the detachment induced Src activation in the lung tumor cells . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
The 3 ( 3 , 5 dimethoxyphenyl ) derivatives were low nanomolar inhibitors of both FGFR and VEGFR and were highly selective ( > 100 fold ) over PDGFR and c Src . ^^^ The 3 ( 2 , 6 dichlorophenyl ) 2 urea derivatives were slightly less active against VEGFR and less selective , being more effective against PDGFR ( ca . 10 fold ) and c Src ( ca . 500 fold ) . ^^^ The 3 ( 3 , 5 dimethoxyphenyl ) 1 , 6 naphthyridines were generally more potent than the corresponding pyrido [ 2 , 3 d ] pyrimidines against both VEGFR and FGFR ( 2 to 20 fold ) , with only slightly increased PDGFR and c Src activity . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
This event is also essential for complete PDGF induced activation of c Src kinase by Tyr 416 phosphorylation , and the involvement of c Src kinase on H2O2 induced PDGFr tyrosine phosphorylation is demonstrated , suggesting a role of this kinase on the redox regulation of PDGFr activation . ^^^ Therefore , we suggest a redox circuit whereby , upon PDGF stimulation , PKC , PI3K and NADPH oxidase activity contribute to complete c Src kinase activation , thus promoting maximal phosphorylation and activation of PDGFr tyrosine phosphorylation . . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
The Src homology 2 ( SH 2 ) domains of the p 85 subunit of phosphatidylinositol 3 ' kinase have been shown to bind to the tyrosine phosphorylated platelet derived growth factor receptor ( PDGFR ) . ^^^
Interacting proteins: P09619 and P12931 Pubmed SVM Score :0.0
In vascular smooth muscle cells ( VSMCs ) , through its G protein coupled AngII Type 1 receptor ( AT ( 1 ) ) , AngII activates various intracellular protein kinases , such as receptor or non receptor tyrosine kinases , which includes epidermal growth factor receptor ( EGFR ) , platelet derived growth factor receptor ( PDGFR ) , c Src , PYK 2 , FAK , JAK 2 . ^^^