PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16940356-2	2006	Recently, it was reported that, in contrast to previous observations, the affinity of EF-G was much weaker for GTP than for GDP and that ribosome-catalyzed GDP-GTP exchange would be required for translocation [Zavialov AV, Hauryliuk VV, Ehrenberg M (2005) J Biol 4:9].	Guanosine Diphosphate	124-127	G elongation factor mitochondrial 1	Homo sapiens	86-90	
16940356-3	2006	We have reinvestigated GTP/GDP binding and show that EF-G binds GTP and GDP with affinities in the 20 to 40 microM range (37 degrees C), in accordance with earlier reports.	Guanosine Diphosphate	27-30	G elongation factor mitochondrial 1	Homo sapiens	53-57	
16940356-3	2006	We have reinvestigated GTP/GDP binding and show that EF-G binds GTP and GDP with affinities in the 20 to 40 microM range (37 degrees C), in accordance with earlier reports.	Guanosine Diphosphate	72-75	G elongation factor mitochondrial 1	Homo sapiens	53-57	
16940356-4	2006	Furthermore, GDP exchange, which is extremely rapid on unbound EF-G, is retarded, rather than accelerated, on the ribosome, which, therefore, is not a nucleotide-exchange factor for EF-G.	Guanosine Diphosphate	13-16	G elongation factor mitochondrial 1	Homo sapiens	63-67