Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.82269704
The alpha subunit of eukaryotic protein synthesis initiation factor ( eIF 2 alpha ) is phosphorylated at a single serine residue ( Ser 51 ) by two distinct and well characterized protein kinase , the haem controlled repressor ( HCR ) and the double stranded RNA activated inhibitor ( dsI ) . 0.82269704^^^
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.5898971
Eukaryotic protein synthesis initiation factor 2 ( eIF 2 ) can be phosphorylated on its alpha subunit by two well characterised protein kinases , termed the haem controlled repressor ( HCR ) and the double stranded RNA activated inhibitor ( dsI ) . 0.5898971^^^
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
The interferon inducible 68 kDa dsRNA dependent eIF 2 alpha kinase ( dsI ) is a potent cellular antiviral enzyme which is activated by autophosphorylation in response to double stranded RNA ( dsRNA ) . ^^^
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
The interferon induced double stranded RNA dependent eIF 2 alpha kinase ( dsI ) has an established role in mediating part of interferon ' s antiviral effects . ^^^
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
It was phosphorylated by both of the well characterised eIF 2 alpha kinases viz . ; the heme controlled repressor ( HCR ) and the double stranded RNA dependent inhibitor ( dsI ) . ^^^ Only the residue corresponding to serine 51 in eIF 2 alpha was phosphorylated by HCR , dsI or PKC . ^^^ The phosphorylation of the peptide by dsI and the phosphorylation of eIF 2 alpha by dsI or HCR showed sigmoidal kinetics with respect to substrate concentration . . ^^^
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
The data presented here show that serine 51 of the alpha subunit of eukaryotic initiation factor eIF 2 is the only residue phosphorylated by the eIF 2 alpha specific kinases HCR ( haem controlled repressor ) and dsI ( double stranded RNA activated inhibitor ) in vitro . ^^^
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
We have previously reported that cultured mouse 3T3 F442A cells exhibit a transient , double stranded RNA ( dsRNA ) dependent phosphorylation of the dsRNA dependent eIF 2 alpha kinase ( eIF 2 alpha , alpha subunit of the eukaryotic initiation factor 2 ) ( dsI ) . ^^^
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
This phosphoprotein is similar but not identical to the dsRNA dependent eukaryotic initiation factor 2 ( eIF 2 ) alpha protein kinase ( dsI ) , which regulates protein synthesis in rabbit reticulocytes . ^^^ The phosphorylation of dsI and the phosphorylation of a 38K protein identified as the alpha subunit ( 38K ) of 3T3 eIF 2 ( eIF 2 alpha ) occurred concomitantly ; the levels of these phosphorylations confluent and thereafter decreased markedly . ^^^
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
The inhibitory component was characterized as dsRNA by several criteria including ( 1 ) the ability to activate the lysate dsRNA dependent eIF 2 alpha kinase ( dsI ) ; ( 2 ) the prevention of both dsI activation and inhibition of protein synthesis by high levels of dsRNA or cAMP ; ( 3 ) the reversal of inhibition by eIF 2 ; and ( 4 ) the inability to inhibit protein synthesis in wheat germ extracts which lack latent dsI . ^^^
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
Reticulocyte lysates contain a latent form of eukaryotic peptide chain initiation factor 2 ( eIF 2 ) kinase ( dsI ) which becomes activated in the presence of double stranded RNA and ATP and inhibits protein synthesis . ^^^ Purified dsI phosphorylates the 38 , 000 dalton subunit of eIF 2 and , under conditions of eIF 2 phosphorylation , dsI strongly inhibits AUG dependent Met tRNAf binding to 40 S ribosomes . ^^^ Also , in partial reactions , eIF 2 alpha ( P ) formed by phosphorylation of eIF 2 using dsI and ATP , is not recognized by two eIF 2 ancillary factors , Co eIF 2B and Co eIF 2C . ^^^ A . 76 , 5076 5079 ) and suggest that dsI , like the heme regulated eIF 2 kinase phosphorylates eIF 2 and eIF 2 alpha ( P ) thus formed , in both cases , is not recognized by Co eIF 2B and Co eIF 2C , and is inactive in some step ( s ) of Met tRNAf . 40 S initiation complex formation . . ^^^
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
Two mammalian enzymes , the haem controlled repressor ( HCR ) and the double stranded RNA activated inhibitor ( dsI ) , phosphorylate Ser 51 of the alpha subunit , thereby inhibiting the exchange of bound nucleotides on , and thus the recycling of , eIF 2 . ^^^ Mammalian HCR and dsI are shown to phosphorylate specifically Ser 51 of yeast eIF 2 alpha , whereas extracts from yeast cells do not . ^^^
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
The results are as follows : ( 1 ) Both hemin and p 67 inhibited HRI ( heme regulated protein synthesis inhibitor ) and dsI ( double stranded RNA activated protein synthesis inhibitor ) catalyzed phosphorylation of eIF 2 alpha subunit in vitro . ^^^
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
Mechanism of action of an eukaryotic initiation factor 2 ( eIF 2 ) associated 67 kDa glycoprotein ( p 67 ) and an eIF 2 kinase ( dsI ) . ^^^ Mechanism of regulation of eIF 2 alpha subunit phosphorylation by dsI and p 67 was studied . ^^^ The results are as follows : ( 1 ) At low dsI concentration , p 67 protected equimolar concentration of eIF 2 . ( 2 ) At high dsI concentration , dsI efficiently phosphorylated eIF 2 alpha subunit even when equimolar concentrations of both p 67 and eIF 2 were present . ^^^ Significantly increased p 67 concentration was necessary to protect eIF 2 alpha subunit at high dsI concentration . ( 3 ) dsI was also phosphorylated as it phosphorylated eIF 2 alpha subunit . p 67 inhibited both eIF 2 alpha subunit and dsI phosphorylation similarly . ( 4 ) Although the [ 32P ] labelled dsI formed during the reaction could be effectively chased upon subsequent addition of excess unlabelled eIF 2 and ATP , the [ 32P ] labelled eIF 2 formed under identical conditions , retained most of the radioactivity . ( 5 ) dsI coimmunoprecipitated with three subunit eIF 2 and p 67 inhibited this coimmunoprecipitation reaction . ^^^ It has been proposed : Three subunit eIF 2 and free p 67 are in equilibrium with eIF 2 bound to p 67 and , eIF 2 . p67 complex is resistant to dsI phosphorylation . ^^^
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
NA
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
NA
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
NA
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
NA
Interacting proteins: P07237 and P05198 Pubmed SVM Score :0.0
NA