PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10349744-7	1999	Influence of the structural features of the cap-analogues, especially the type of the second nucleoside in the dinucleotide caps, on their association with eIF4E and biological activities in in vitro protein translation systems has been discussed in light of the known structures of the eIF4E-7-methyl-GDP complexes in crystal and solution.	Guanosine Diphosphate	302-305	eukaryotic translation initiation factor 4E	Homo sapiens	156-161	
22985415-7	2012	Our data have important implications for the regulatory role of m(7)GDP in mRNA metabolic pathways due to its possible interactions with different cap-binding proteins, such as DcpS or eIF4E.	Guanosine Diphosphate	68-71	eukaryotic translation initiation factor 4E	Homo sapiens	185-190	
14675529-1	2003	The structure of the eukaryotic initiation factor eIF4E bound to a cognate domain of eIF4G and m(7)GDP in this issue of Cell shows that these factors undergo coupled folding to form a stable complex with high cap binding activity that promotes efficient ribosomal attachment to mRNA during translation initiation.	Guanosine Diphosphate	99-102	eukaryotic translation initiation factor 4E	Homo sapiens	50-55	
11076512-5	2000	To further understand the structural requirements for the specific recognition of an m(7)G mRNA cap, we determined the effects of amino acid substitutions in eIF4E and VP39 cap-binding sites on their affinity for m(7)GDP.	Guanosine Diphosphate	217-220	eukaryotic translation initiation factor 4E	Homo sapiens	158-163	
11076512-7	2000	The results suggest that both eIF4E and VP39 require a complicated pattern of both orientation and identity of the stacking aromatic residues to permit the selective binding of m(7)GDP.	Guanosine Diphosphate	181-184	eukaryotic translation initiation factor 4E	Homo sapiens	30-35