| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.64779689 |
| We show that mammalian eIF4A binds tightly to yeast eIF4G1 and , furthermore , that mutant yeast eIF4G ( 542 883 ) proteins , which do not bind yeast eIF4A , do not interact with mammalian eIF4A . 0.64779689^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.71166804 |
| The association of eIF4A with Saccharomyces cerevisiae eIF4F has not yet been demonstrated , and therefore the degree to which eIF4A ' s conserved function relies upon this association has remained unclear . 0.71166804^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.59314764 |
| In eukaryotes protein synthesis initiates with the binding of the multimeric translation initiation complex eIF4F eIF4E , eIF4A and eIF4G to the monomethylated cap present on the 5 ' end of mRNAs . eIF4E interacts directly with the cap nucleotide , while eIF4A is a highly conserved RNA helicase and eIF4G acts as a scaffold for the complex with binding sites for both eIF4E and eIF4A . eIF4F binding to the mRNA recruits the small ribosomal subunit to its 5 ' end . 0.59314764^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.96842143 |
| Mammalian translation initiation factor 4F ( eIF4F ) consists of three subunits , eIF4A , eIF4E , and eIF4G . eIF4G interacts directly with both eIF4A and eIF4E . 0.96842143^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.92266672 |
| The work presented here demonstrates that yeast eIF4G interacts with eIF4A both in vivo and in vitro . 0.92266672^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.81273172 |
| We show that in human embryonic kidney cells eIF4G is associated with eIF4A ( 1 ) or eIF4A ( 2 ) but not with both simultaneously , suggesting a stoichiometry of 1 : 1 rather than 1 : 2 . 0.81273172^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.8590894 |
| Interactions of eIF4G with eIF4E , eIF4A , eIF 3 , poly ( A ) binding protein , and Mnk1 / 2 have been mapped to discrete domains on eIF4G , and conversely , the eIF4G binding sites on all but one of these ligands have been determined . 0.8590894^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Mutually cooperative binding of eukaryotic translation initiation factor ( eIF ) 3 and eIF4A to human eIF4G 1 . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| The active complex therefore differs from eIF4F , the complex purified by cap analog affinity chromatography , in that it lacks the Mr 50 , 000 subunit which is antigenically identical to eIF4A . ^^^ The activities of eIF4F , CBP 1 and the eIF4A free complex purified here were compared in a fractionated system translating capped globin mRNA . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Most initiation factor polypeptides are moderately abundant proteins with concentrations approaching those of ribosomes . eIF4A and eIF5A are more abundant than ribosomes , whereas eIF4F alpha and eIF2B are considerably less abundant than the other factors . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| The binding of mRNA to the ribosome is mediated by eukaryotic initiation factors eukaryotic initiation factor 4F ( eIF4F ) , eIF4B , eIF4A , and eIF 3 , eIF4F binds to the mRNA cap structure and , in combination with eIF4B , is believed to unwind the secondary structure in the 5 ' untranslated region to facilitate ribosome binding . eIF 3 associates with the 40S ribosomal subunit prior to mRNA binding . eIF4B copurifies with eIF 3 and eIF4F through several purification steps , suggesting the involvement of a multisubunit complex during translation initiation . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| These processes are both mediated by eukaryotic initiation factor 4F ( eIF4F ) , which consists of eIF4A ( helicase ) , eIF4E ( cap binding protein ) , and eIF4G subunits . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| It has homology to the carboxy terminal portion of the eukaryotic translation initiation factor ( eIF ) 4G that binds eIF4A and eIF4E to form eIF4F . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Eukaryotic translation initiation factor 4F ( eIF4F ) is a cap binding protein complex that consists of three subunits : eIF4A , eIF4E and eIF4G . eIF4G interacts directly with eIF4E and eIF4A . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| After a brief introduction to the function of the mRNA specific translation factors eIF4A , eIF4B , and EIF4F , this article presents appropriate methodology for the study of the translation factors associated with the activation of mRNA for translation in eukaryotic systems . ^^^ The purification of eIF4A , eIF4B , and eIF4F from rabbit reticulocyte lysates is given along with a procedure for the purification of hemoglobin mRNA . ^^^ It is hoped that this information will facilitate the study of either the regulation of factor activity ( for eIF4A , eIF4B , or eIF4F ) or the translation efficiency ( sometimes regulated ) of various mRNAs . . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| To be active , it must bind eIF4G and form the eIF4F complex , which also contains eIF4A . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Mammalian eukaryotic translation initiation factor 4F ( eIF4F ) is a cap binding protein complex consisting of three subunits : eIF4E , eIF4A , and eIF4G . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Ribosomal binding and positioning on these mRNAs did not require the initiation factors eIF 3 , eIF4A , eIF4B , and eIF4F and translation of these mRNAs was not inhibited by a trans dominant eIF4A mutant . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| This protein has been purified to greater than 80 % homogeneity from rabbit reticulocyte lysate and has been given the name eIF4H . eIF4H was shown to stimulate the in vitro activities of eIF4B and eIF4F in globin synthesis , as well as the in vitro RNA dependent ATPase activities of eIF4A , eIF4B , and eIF4F . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| In the initiation of translation in eukaryotes , binding of the small ribosomal subunit to the messenger RNA results from recognition of the 5 ' cap structure ( m7GpppX ) of the mRNA by the cap binding complex eIF4F . eIF4F is itself a three subunit complex comprising the cap binding protein eIF4E , eIF4A , an ATP dependent RNA helicase , and eIF4G , which interacts with both eIF4A and eIF4E and enhances cap binding by eIF4E . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| In their absence , 43S ribosomal preinitiation complexes incubated with ATP , eIF4A , eIF4B and eIF4F bind exclusively to the cap proximal region but are unable to reach the initiation codon . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| In addition , we show that the amount of poly ( A ) binding protein ( PABP ) present in eIF4F complexes decreases during rotavirus infection , even though eIF4A and eIF4E remain unaffected . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Unexpectedly , we find that the cap binding complex eIF4F ( comprising eIF4E , eIF4G , and eIF4A ) assembles even when IRP 1 is bound to the cap proximal IRE . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Human eukaryotic translation initiation factor 4E ( eIF4E ) binds to the mRNA cap structure and interacts with eIF4G , which serves as a scaffold protein for the assembly of eIF4E and eIF4A to form the eIF4F complex . eIF4E is an important modulator of cell growth and proliferation . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Ribosomal binding and positioning on this mRNA to form a 48S complex did not require the initiation factors eIF4A , eIF4B , or eIF4F , and translation of this mRNA was resistant to inhibition by a trans dominant eIF4A mutant that inhibited cap mediated initiation of translation . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Eukaryotic initiation factor 4A ( eIF4A ) is an RNA dependent ATPase and ATP dependent RNA helicase that is thought to melt the 5 ' proximal secondary structure of eukaryotic mRNAs to facilitate attachment of the 40S ribosomal subunit . eIF4A functions in a complex termed eIF4F with two other initiation factors ( eIF4E and eIF4G ) . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Furthermore , eIF4A ( 46 kDa ) , a second component of eIF4F , is also cleaved in these later stages of the infection cycle . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| In contrast to mammalian eIF4B and eIF4A , the combination of wheat eIF4B and eIF4A does not stimulate RNA dependent ATP hydrolysis activity ; however , wheat eIF4B does stimulate eIF4F and eIF4A RNA dependent ATP hydrolysis activity . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| The resulting complex requires eIF 1 , eIF1A , eIF4A , eIF4B and eIF4F to bind to a messenger RNA and to scan to the initiation codon . eIF 5 stimulates hydrolysis of eIF 2 bound GTP and eIF 2 is released from the 48S complex formed at the initiation codon before it is joined by a 60S subunit to form an active 80S ribosome . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| These results suggest that , in terms of the scanning model of translation initiation , PABP may enhance the mRNA scanning rate of the complex formed by eIF4A , eIF4B , and eIF4F or eIF ( iso ) 4F and increase the rate of translation . . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| The RNA duplex unwinding activity of wheat germ eIF4A is similar to other mammalian systems ; however , eIF4F or eIFiso4F is required , probably because of the low binding affinity of wheat germ eIF4A for mRNA . ^^^ The data presented in this paper suggest that eIF4F or eIFiso4F acts to position the eIF4A and stabilize the interaction with mRNA . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Translation of most mRNAs requires formation of a cap binding initiation complex known as eIF4F , consisting of factors eIF4E , eIF4A , eIF4E kinase Mnk 1 , poly ( A ) binding protein , and adaptor protein eIF4G . ^^^ Hsp 27 specifically bound eIF4G during heat shock , preventing assembly of the cap initiation / eIF4F complex and trapping eIF4G in insoluble heat shock granules . eIF4G is a specific target of Hsp 27 , as eIF4E , eIF4A , Mnk 1 , poly ( A ) binding protein , eIF4B , and eIF 3 were not bound by Hsp 27 and were not recruited into insoluble complexes . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Functions of the constituent proteins of eIF4F include recognition of the mRNA 5 ' cap structure ( eIF4E ) , delivery of an RNA helicase to the 5 ' region ( eIF4A ) , bridging of the mRNA and the ribosome ( eIF4G ) , and circularization of the mRNA via interaction with poly ( A ) binding protein ( eIF4G ) . eIF 4 activity is regulated by transcription , phosphorylation , inhibitory proteins , and proteolytic cleavage . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Translation of cellular mRNAs involves formation of a cap binding translation initiation complex known as eIF4F , containing phosphorylated cap binding protein eIF4E , eIF4E kinase Mnk 1 , eIF4A , poly ( A ) binding protein and eIF4G . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Reconstitution of initiation using fully fractionated translation components indicated that 48S complex formation on both IRESs requires eIF 2 , eIF 3 , eIF4A , eIF4B , eIF4F , and the pyrimidine tract binding protein ( PTB ) but that the FMDV IRES additionally requires ITAF ( 45 ) , also known as murine proliferation associated protein ( Mpp 1 ) , a proliferation dependent protein that is not expressed in murine brain cells . ^^^ Specific binding sites for ITAF ( 45 ) , PTB , and a complex of the eIF4G and eIF4A subunits of eIF4F were mapped onto the FMDV IRES , and the cooperative function of PTB and ITAF ( 45 ) in promoting stable binding of eIF4G / 4A to the IRES was characterized by chemical and enzymatic footprinting . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| In spite of its interaction with endogenous eIF4G , lambda4A does not display this property . eIF4A thus appears to supply an essential auxiliary function to eIF4F that may require its ability to cycle into and out of this complex . . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| The cap binding complex eIF4F and the factors eIF4A and eIF4B are required for binding of 43S complexes ( comprising a 40S subunit , eIF2 / GTP / Met tRNAi and eIF 3 ) to the 5 ' end of capped mRNA but are not sufficient to promote ribosomal scanning to the initiation codon . eIF1A enhances the ability of eIF 1 to dissociate aberrantly assembled complexes from mRNA , and these factors synergistically mediate 48S complex assembly at the initiation codon . ^^^ The eIF4A and eIF4G subunits of eIF4F bind immediately upstream of the EMCV initiation codon and promote binding of 43S complexes . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Modulation of the helicase activity of eIF4A by eIF4B , eIF4H , and eIF4F . ^^^ This study demonstrates how the helicase activity of eIF4A is modulated by eIF4B , eIF4H , or as a subunit of eIF4F . ^^^ Results indicate that a linear relationship exists between the initial rate or amplitude of unwinding and duplex stability for all factor combinations tested . eIF4F , like eIF4A , behaves as a non processive helicase . ^^^ Furthermore , eIF4A ( or eIF4F ) becomes a slightly processive helicase in the presence of eIF4B or eIF4H . ^^^ The combinations of eIF4A , eIF4A + eIF4B , eIF4A + eIF4H , and eIF4F showed differences in their ability to unwind chemically modified duplexes . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Cap dependent translation is mediated by eIF4F , a protein complex composed of three subunits as follows : eIF4E , which recognizes the mRNA 5 ' cap structure ; eIF4A , an RNA helicase ; and eIF4G , a scaffolding protein that binds eIF4E , eIF4A , and the eIF4E kinase Mnk 1 simultaneously . eIF4E is hypophosphorylated and cap dependent translation is reduced at mitosis . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| The translational advantage conferred by the TEV IRES under these conditions was lost when the lysate reduced in eIF4F and eIFiso4F was supplemented with eIF4F ( or , to a lesser extent , eIFiso4F ) but not when supplemented with eIF4E , eIFiso4E , eIF4A , or eIF4B . eIF4G , the large subunit of eIF4F , was responsible for the competitive advantage conferred by the TEV IRES . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| We found that a ribosomal 40S subunit , eukaryotic initiation factor ( eIF ) 3 , and the eIF 2 ternary complex form a 43S complex that can bind to the 5 ' end of an unstructured 5 ' untranslated region ( 5 ' UTR ) and in the presence of eIF 1 scan along it and locate the initiation codon without a requirement for adenosine triphosphate ( ATP ) or factors ( eIF4A , eIF4B , eIF4F ) associated with ATP hydrolysis . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Recombinant Pdcd 4 specifically inhibited the helicase activity of eIF4A and eIF4F . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| The extreme sensitivity to secondary structure around the initiation codon is likely to be due to the fact that the eIF4F complex ( which has eIF4A as one of its subunits ) is not required for and does not participate in initiation on these IRESs . . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Translation initiating ribosome assembly at cap or IRES elements is mediated by a multiprotein complex of which the initiation factor 4F ( eIF4F ) consisting of eIF4A ( helicase ) , eIF4E ( cap binding protein ) , and eIF4G is a major constituent . eIF4G is a key target of picornaviral protease 2A , which cleaves this initiation factor into eIF4G ( Delta ) and ( Delta ) eIF4G to redirect the cellular translation machinery exclusively to its own IRES containing transcripts . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Together with eIF4E and eIF4A , eIF4G constitutes the eIF4F complex which is a key component in promoting ribosome binding to the mRNA . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| A critical test was provided by an mRNA with an unstructured 5 ' UTR , which is translated by scanning but does not absolutely need eIF4G and eIF4A : There was efficient reinitiation in a standard reticulocyte lysate , when initiation would be largely driven by eIF4F , but no reinitiation in an eIF4G depleted lysate . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| We have identified the initiation factor 4A ( eIF4A ) in a two dimensional protein database of Drosophila wing imaginal discs . eIF4A , a member of the DEAD box family of RNA helicases , forms the active eIF4F complex that in the presence of eIF4B and eIF4H unwinds the secondary structure of the 5 ' UTR of mRNAs during translational initiation . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| PH promoted the assembly of eukaryotic initiation factor ( eIF ) 4F complexes consisting of eIF4E , eIF4G , eIF4A1 , and poly A binding protein . eIF4F complex formation after PH occurred without detectable changes in eIF4E binding protein 1 ( 4E BP 1 ) phosphorylation or its binding eIF4E . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| The eukaryotic translation initiation factor 4F ( eIF4F ) consists of three polypeptides ( eIF4A , eIF4G , and eIF4E ) and is responsible for recruiting ribosomes to mRNA . eIF4E recognizes the mRNA 5 ' cap structure ( m7GpppN ) and plays a pivotal role in control of translation initiation , which is the rate limiting step in translation . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| In addition , a complex containing bacterially expressed Vhs and a glutathione S transferase ( GST ) eIF4H fusion protein has RNase activity . eIF4H shares a region of sequence homology with eIF4B , and it appears to be functionally similar in that both stimulate the RNA helicase activity of eIF4A , a component of the mRNA cap binding complex eIF4F . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| The translation initiation factor eIF4A is the prototypical DEAD box RNA helicase that works in conjunction with eIF4B and eIF4H and as a subunit of eIF4F to prepare the mRNA template for ribosome binding , possibly by unwinding the secondary structure proximal to the 5 ' m7GpppN cap structure . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| In addition , eIF1A , eIF4F ( or the C terminal fragment of eIF4G ) , and eIF4A strongly stimulated the assembly of this complex , whereas eIF4B had no effect . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| This model can explain the cooperativity between all binding partners of eIF4A ( eIF4G , RNA , ATP ) and stimulation of eIF4A activity in the eIF4F complex . . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Translation of m7G capped cellular mRNAs is initiated by recruitment of ribosomes to the 5 ' end of mRNAs via eukaryotic translation initiation factor 4F ( eIF4F ) , a heterotrimeric complex comprised of a cap binding subunit ( eIF4E ) and an RNA helicase ( eIF4A ) bridged by a scaffolding molecule ( eIF4G ) . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Recruitment of the 40S ribosome to the 5 ' end of a eukaryotic mRNA requires assembly of translation initiation factors eIF4E , the cap binding protein , together with eIF4A and eIF4G into a complex termed eIF4F . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Here we have investigated the role of two Trypanosoma brucei homologues of the translation initiation factor eIF4A ( in the light of subsequent experiments these were named as TbEIF4AI and TbEIF4AIII ) . eIF4A , a DEAD box RNA helicase , is a subunit of the translation initiation complex eIF4F which binds to the cap structure of eukaryotic mRNA and recruits the small ribosomal subunit . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| The eukaryotic translation initiation factor ( eIF ) 4B promotes the RNA dependent ATP hydrolysis activity and ATP dependent RNA helicase activity of eIF4A and eIF4F during translation initiation . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| We also demonstrate that both FCV and MNV RNA translation require the RNA helicase component of the eIF4F complex , namely eIF4A , because translation was sensitive ( albeit to different degrees ) to a dominant negative form and to a small molecule inhibitor of eIF4A ( hippuristanol ) . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| When the S 30 system was supplemented with high amounts of purified eIF 3 , eIF 4A , eIF 4F , and eIF 4G , B alpha A and B alpha A AMV 4 mRNAs were translated as efficiently as AMV RNA 4 and AMV 4 B alpha A mRNA . ^^^ These findings indicated that the mRNAs containing the B alpha A leader sequence required higher amounts of one or more of the initiation factors ( eIF 3 , eIF 4A , eIF 4F , and eIF 4G ) for efficient translation . ^^^ Determination of the amounts of the initiation factors required for translation in the fractionated system showed that AMV RNA 4 required 2 4 fold lower amounts of eIF 3 , eIF 4A , eIF 4F , and eIF 4G than did B alpha A mRNA . ^^^ Replacement of the B alpha A leader sequence with that of AMV RNA 4 decreased the amounts of eIF 4A , eIF 4G , and eIF 3 required , but did not affect the amount of eIF 4F required . ^^^ Replacement of the AMV RNA 4 leader sequence with that of B alpha A mRNA increased the amounts of eIF 4F , eIF 4G , and eIF 3 required , but did not affect the amount of eIF 4A required . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| RNAs were transcribed from these plasmids ( pSTNV 1239 and pSTNV 54 ) and tested for their ability to bind to wheat germ 40 S ribosomal subunits in the presence of wheat germ initiation factors eIF 4A , eIF 4F , eIF 4G , eIF 3 , eIF 2 , Met tRNA , ATP , and guanosine 5 ' ( beta , gamma imino ) triphosphate ( GMP PNP ) . ^^^ In contrast , close to maximal binding of STNV RNA transcribed from pSTNV 54 is obtained in the absence of eIF 4A , eIF 4F , eIF 4G , and ATP . ^^^ STNV RNAs containing more than 134 nucleotides from the 5 ' end require eIF 4A , eIF 4F , eIF 4G , and ATP for maximal binding to 40 S ribosomal subunits , whereas STNV RNAs containing 86 nucleotides or less no longer require ATP and these factors . ^^^ These findings indicate that a region 3 ' to the initiation codon affects the requirements for eIF 4A , eIF 4F , eIF 4G , and ATP . . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Further purification of the factor yields a preparation that contains one major polypeptide with a molecular weight of approximately 59 , 000 , This factor enhances the binding of globin mRNA to 40 S ribosomal subunits in the presence of eIF 2 , eIF 3 , eIF 4A , and either eIF 4B or eIF 4F and has been designated eIF 4G . . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Cap dependent binding of mRNA to the 40 S ribosomal subunit during translational initiation requires the association of eukaryotic initiation factor 4G ( eIF4G ; formerly eIF 4 gamma and p 220 ) with other initiation factors , notably eIF4E , eIF4A , and eIF 3 . ^^^ Rhinovirus 2A protease and foot and mouth disease virus L protease were used to analyze the association of eIF4G with eIF4A , eIF4E , and eIF 3 . ^^^ Both proteases bisect eIF4G into N and C terminal fragments termed cpN and cpC . cpN was shown to contain the eIF4E binding site , as judged by retention on m7GTP Sepharose , whereas cpC was bound to eIF 3 and eIF4A , based on ultracentrifugal co sedimentation . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| The N terminal cleavage product of eIF4G ( cpN ) , which binds eIF4E , was completely degraded within 6 12 h , while the C terminal cleavage product ( cpC ) , which binds to eIF 3 and eIF4A , was more stable over the same period . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| The foot and mouth disease virus encodes two forms of a cysteine proteinase ( L protease ) which bisects the eIF4G polypeptide into an N terminal fragment containing the eIF4E binding site , and a C terminal fragment which contains binding sites for eIF4A and eIF 3 and which associates with the 40S ribosomal subunit . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| With treatment of Saccharomyces cerevisiae with rapamycin or with entry of cells into the diauxic phase , eIF4G is rapidly degraded , whereas initiation factors eIF4E and eIF4A remain stable . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Addition of wild type or trans dominant mutant forms of eIF4A to binary IRES . eIF4G complexes did not further alter the pattern of chemical / enzymatic modification of the IRES . . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| The presence of other initiation factors such as eIF 3 , eIF 4A or eIF 4B mimics in part the stimulatory effect of magnesium ions and probably stabilizes the cleavage products of eIF 4G generated by 2Apro . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Deletion analysis defined the conserved central domain ( amino acids 642 1091 ) of eIF4G as an autonomous ' ribosome recruitment core ' and implicated eIF4A as a critical binding partner . ^^^ |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Physical association of eukaryotic initiation factor 4G ( eIF4G ) with eIF4A strongly enhances binding of eIF4G to the internal ribosomal entry site of encephalomyocarditis virus and is required for internal initiation of translation . ^^^ These data indicate that the eIF4G eIF4A complex , rather than eIF4G alone , is required for specific high affinity binding to the EMCV IRES and for internal ribosomal entry on this RNA . . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Characterization of the two eIF4A binding sites on human eIF4G 1 . ^^^ Eukaryotic translation initiation factor 4G 1 ( eIF4G ) plays a critical role in the recruitment of mRNA to the 43 S preinitiation complex . eIF4G has two binding sites for the RNA helicase eIF4A , one in the central domain and one in the COOH terminal domain . ^^^ Recombinant eIF4G fragments that contained each of these sites separately bound eIF4A with a 1 : 1 stoichiometry , but fragments containing both sites bound eIF4A with a 1 : 2 stoichiometry . eIF 3 did not interfere with eIF4A binding to the central site . ^^^ Interestingly , at the same concentration of free eIF4A , more eIF4A was bound to an eIF4G fragment containing both eIF4A sites than the sum of binding to fragments containing the single sites , indicating cooperative binding . ^^^ Binding of eIF4A to an immobilized fragment of eIF4G containing the COOH terminal site was competed by a soluble eIF4G fragment containing the central site , indicating that a single eIF4A molecule can not bind simultaneously to both sites . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Translation initiation factors eIF4G , eIF4A , and eIF4B bound to the 3 ' domain of the FMDV IRES . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Assembly of 48S ribosomal complexes on the IRES requires eukaryotic initiation factor 2 ( eIF 2 ) , eIF 3 , eIF4A , and the central domain of eIF4G to which eIF4A binds . ^^^ Directed hydroxyl radical probing , done by using Fe ( 2 ) tethered to surface residues in eIF4G ' s central domain , indicated that it is oriented with its N terminus towards the base of domain J and its C terminus towards the apex . eIF4G recruits eIF4A to a defined location on the IRES , and the eIF4G / eIF4A complex caused localized ATP independent conformational changes in the eIF4G binding region of the IRES . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| BACKGROUND : The recruitment of mRNA for translation involves the assembly at the 5 ' cap of a complex of three initiation factors : the cap binding protein eIF4E , the ATP dependent RNA helicase eIF4A and the scaffold protein eIF4G . eIF4G mediates the binding of this mRNA protein complex to the 43S ribosomal preinitiation complex . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Eukaryotic initiation factor 4G ( eIF4G ) promotes mRNA recruitment to the ribosome by binding to the mRNA cap and poly ( A ) tail binding proteins eIF4E and Pap1p . eIF4G also binds eIF4A at a distinct HEAT domain composed of five stacks of antiparallel alpha helices . ^^^ In vivo , co overexpression of eIF 1 or eIF 5 reverses the genetic suppression of an eIF4G HEAT domain Ts ( ) mutation by eIF4A overexpression . ^^^ In addition , excess eIF 1 inhibits growth of a second eIF4G mutant defective in eIF4E binding , which was also reversed by co overexpression of eIF4A . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Eukaryotic initiation factor 4A ( eIF4A ) 3 is a nuclear protein that interacts physically or functionally with translation initiation factors eIF4G and eIF4B , respectively , and shares strikingly high identity with the initiation factors eIF4AI / II . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| C terminal eIF4G ( eIG4Gc ) contains an MA 3 domain that is located within the eIF4A binding region , suggesting a role for eIF4A binding . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| The data revealed significant down regulation of eukaryotic initiation and elongation factors , initiation factor 2 ( IF 2 ) , eukaryotic initiation factor 4AI ( eIF4AI ) , eIF4G , eIF 5 , eIF 6 , eukaryotic elongation factor 1A 1 ( eEF1A 1 ) , EF 1 delta , eEF1gamma , 14 3 3epsilon , and 14 3 3zeta / delta ( P < . 05 ) . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Interaction between the NH 2 terminal domain of eIF4A and the central domain of eIF4G modulates RNA stimulated ATPase activity . ^^^ The eukaryotic translation factor 4A ( eIF4A ) is a member of DEA ( D / H ) box RNA helicase family , a diverse group of proteins that couples ATP hydrolysis to RNA binding and duplex separation . eIF4A participates in the initiation of translation by unwinding secondary structure in the 5 ' untranslated region of mRNAs and facilitating scanning by the 40 S ribosomal subunit for the initiation codon . eIF4A alone has only weak ATPase and helicase activities , but these are stimulated by eIF4G , eIF4B , and eIF4H . eIF4G has two eIF4A binding sites , one in the central domain ( cp ( C 3 ) ) and one in the COOH terminal domain ( cp ( C 2 ) ) . ^^^ In the current work , we demonstrate that these two eIF4G domains have different effects on the RNA stimulated ATPase activity of eIF4A . cp ( C 3 ) stimulates ATP hydrolytic efficiency by about 40 fold through two mechanisms : lowering K ( m ) ( RNA ) by 10 fold and raising k ( cat ) by 4 fold . cp ( C 3 ) also stimulates RNA cross linking to eIF4A in an ATP independent manner . ^^^ Studies with eIF4G and eIF4A variants suggest a model by which cp ( C 3 ) alters the conformation of the catalytic site to favor RNA binding . cp ( C 2 ) does not stimulate ATPase activity and furthermore increases both K ( m ) ( ATP ) ( at saturating RNA concentrations ) and K ( m ) ( RNA ) ( at subsaturating ATP concentrations ) . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| With the exception of the Q motif mutant eIF4AP56L , the eIF4A mutants inactivated for Pdcd 4 binding were inactivated for binding to eIF4G ( GM , GC , or both ) and for enhancing translation . ^^^ Several eIF4A mutants showing wild type level binding to Pdcd 4 were also inactivated for binding to eIF4G and for enhancing translation . ^^^ Thus , significant dissociation of eIF4A ' s Pdcd 4 and eIF4G binding regions appears to occur . ^^^ A structural homology model of eIF4A shows regions important for binding to Pdcd 4 and / or eIF4G lying on the perimeters of the hinge area of eIF4A . ^^^ A competition experiment revealed that Pdcd 4 competes with C terminal eIF4G for binding to eIF4A . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| To date , the role of each of the four eIF 4 , i . e . eIF4E , eIF4G , eIF4A and eIF4B , is well established . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Partial secondary structure predictions were derived and functional assays demonstrated that these IRES elements continued to be active when eIF4G was cleaved and when the activity of eIF4A was blocked . . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Two structurally atypical HEAT domains in the C terminal portion of human eIF4G support binding to eIF4A and Mnk 1 . ^^^ In higher eukaryotes , the C terminus of eIF4G ( 4G / C ) supports translational regulation by recruiting eIF4A , an RNA helicase , and Mnk 1 , the kinase responsible for phosphorylating eIF4E . ^^^ Structure guided surface mutagenesis and protein protein interaction assays were used to identify binding sites for eIF4A and Mnk 1 within the HEAT repeats of 4G / C . p97 / DAP5 , a translational modulator homologous to eIF4G , lacks an eIF4A binding site in the corresponding region . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| This interaction is mediated by a ribonucleoprotein network that contains , at a minimum , the poly ( A ) binding protein ( PABP ) , the capbinding protein eIF4E and a scaffolding protein , eIF4G . eIF4G , in turn , contains binding sites for eIF4A and eIF 3 , a 40S ribosome associated initiation factor . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Corresponding to the difference in the binding sites in eIF4G , apt 4 , but not apt 5 , hindered eIF4G from binding to eIF4A and eIF 3 , in a purified protein solution system as well as in a crude lysate system . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| The mammalian eukaryotic initiation factor 4GI ( eIF4GI ) may be divided into three roughly equal regions ; an amino terminal one third ( amino acids [ aa ] 1 to 634 ) , which contains the poly ( A ) binding protein ( PABP ) and eIF4E binding sites ; a middle third ( aa 635 to 1039 ) , which binds eIF4A and eIF 3 ; and a carboxy terminal third ( aa 1040 to 1560 ) , which harbors a second eIF4A binding site and a docking sequence for the Ser / Thr kinase Mnk 1 . ^^^ In agreement with this , a point mutation in eIF4GI which abolished eIF4A binding in the middle region completely inhibited ribosomal binding . ^^^ When the eIF4A binding site in the C terminal region of eIF4GI was mutated , ribosome binding was decreased three to fourfold . ^^^ These data indicate that the interaction of eIF4A with the middle region of eIF4GI is necessary for translation , whereas the interaction of eIF4A with the C terminal region plays a modulatory role . . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| Affinity chromatography on m7GTP Sepharose shows that M FAG retains the ability of eIF4GI to associate with both the mRNA cap binding protein eIF4E and initiation factor eIF4A and that the ribosome bound form of M FAG is also present as a complex with eIF4E and eIF4A . ^^^ These data suggest that the binding sites for eIF4E , eIF4A and eIF 3 on eIF4GI are retained in the caspase generated fragment . ^^^ |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q04637 and P60842 |
Pubmed |
SVM Score :0.0 |
| NA |
|