PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3338993-3	1988	The kinetic data demonstrate that, in analogy to procaryotes, dissociation of GDP occurs via the formation of a transient ternary complex of EF-1 alpha.GDP.EF-1 beta gamma.	Guanosine Diphosphate	78-81	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	141-151	
3338993-3	1988	The kinetic data demonstrate that, in analogy to procaryotes, dissociation of GDP occurs via the formation of a transient ternary complex of EF-1 alpha.GDP.EF-1 beta gamma.	Guanosine Diphosphate	152-155	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	141-151	
3338993-4	1988	The rate constants for the dissociation of GDP from EF-1 alpha.GDP and from the ternary complex EF-1 alpha.GDP.EF-1 beta gamma were found to be 0.7 x 10(-3) and greater than or equal to 0.7 s-1, respectively.	Guanosine Diphosphate	43-46	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	52-62	
3338993-4	1988	The rate constants for the dissociation of GDP from EF-1 alpha.GDP and from the ternary complex EF-1 alpha.GDP.EF-1 beta gamma were found to be 0.7 x 10(-3) and greater than or equal to 0.7 s-1, respectively.	Guanosine Diphosphate	43-46	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	96-106	
3338993-4	1988	The rate constants for the dissociation of GDP from EF-1 alpha.GDP and from the ternary complex EF-1 alpha.GDP.EF-1 beta gamma were found to be 0.7 x 10(-3) and greater than or equal to 0.7 s-1, respectively.	Guanosine Diphosphate	63-66	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	52-62	
3338993-4	1988	The rate constants for the dissociation of GDP from EF-1 alpha.GDP and from the ternary complex EF-1 alpha.GDP.EF-1 beta gamma were found to be 0.7 x 10(-3) and greater than or equal to 0.7 s-1, respectively.	Guanosine Diphosphate	63-66	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	96-106	
3338993-4	1988	The rate constants for the dissociation of GDP from EF-1 alpha.GDP and from the ternary complex EF-1 alpha.GDP.EF-1 beta gamma were found to be 0.7 x 10(-3) and greater than or equal to 0.7 s-1, respectively.	Guanosine Diphosphate	63-66	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	52-62	
3338993-4	1988	The rate constants for the dissociation of GDP from EF-1 alpha.GDP and from the ternary complex EF-1 alpha.GDP.EF-1 beta gamma were found to be 0.7 x 10(-3) and greater than or equal to 0.7 s-1, respectively.	Guanosine Diphosphate	63-66	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	96-106	
3338993-5	1988	The equilibrium association constants of GDP to EF-1 alpha.EF-1 beta gamma and of EF-1 beta gamma to EF-1 alpha.GDP were found to be 2.3 x 10(5) and 4.2 x 10(5) M-1, respectively.	Guanosine Diphosphate	41-44	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	48-58	
3338993-5	1988	The equilibrium association constants of GDP to EF-1 alpha.EF-1 beta gamma and of EF-1 beta gamma to EF-1 alpha.GDP were found to be 2.3 x 10(5) and 4.2 x 10(5) M-1, respectively.	Guanosine Diphosphate	41-44	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	101-111	
3338993-5	1988	The equilibrium association constants of GDP to EF-1 alpha.EF-1 beta gamma and of EF-1 beta gamma to EF-1 alpha.GDP were found to be 2.3 x 10(5) and 4.2 x 10(5) M-1, respectively.	Guanosine Diphosphate	112-115	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	48-58	
3338993-5	1988	The equilibrium association constants of GDP to EF-1 alpha.EF-1 beta gamma and of EF-1 beta gamma to EF-1 alpha.GDP were found to be 2.3 x 10(5) and 4.2 x 10(5) M-1, respectively.	Guanosine Diphosphate	112-115	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	101-111	
3276514-5	1988	Both EF-1 beta gamma and EF-1 beta have been shown to stimulate the following three reactions to a comparable degree: (a) exchange of GDP bound to EF-1 alpha with exogenous GDP; (b) EF-1 alpha-dependent binding of Phe-tRNA to ribosomes; (c) poly(U)-dependent poly(phenylalanine) synthesis.	Guanosine Diphosphate	134-137	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	147-157	
28900796-5	2017	The experimental solution of the three-dimensional structure of mammalian eEF1A1 has proved elusive so far and the highly homologous eEF1A2 from rabbit muscle has been crystallized and solved only as a homodimer in a GDP-bound conformation.	Guanosine Diphosphate	217-220	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	133-139	
31611569-0	2019	Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations.	Guanosine Diphosphate	80-83	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	59-63	
31611569-1	2019	Translation elongation factor EF1A delivers aminoacyl-tRNA to the ribosome in a GTP-bound form, and is released from the ribosome in a GDP-bound form.	Guanosine Diphosphate	135-138	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	30-34	
8743958-3	1996	After release of aminoacyl-tRNA to the ribosome under concomitant hydrolysis of GTP, the inactive EF-1 alpha.GDP form is recycled to EF-1 alpha.GTP by EF-1 beta gamma delta.	Guanosine Diphosphate	109-112	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	98-108	
25326326-0	2014	Mammalian translation elongation factor eEF1A2: X-ray structure and new features of GDP/GTP exchange mechanism in higher eukaryotes.	Guanosine Diphosphate	84-87	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	40-46	
25326326-6	2014	Here, we report the first crystal structure of the mammalian eEF1A2*GDP complex which indicates major differences in the organization of the nucleotide-binding domain and intramolecular movements of eEF1A compared to EF-Tu.	Guanosine Diphosphate	68-71	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	61-67	
10368288-3	1999	EF-1beta regulates the activity of EF-1alpha by catalyzing the exchange of GDP for GTP and thereby regenerating the active form of EF-1alpha.	Guanosine Diphosphate	75-78	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	35-44	
8743958-3	1996	After release of aminoacyl-tRNA to the ribosome under concomitant hydrolysis of GTP, the inactive EF-1 alpha.GDP form is recycled to EF-1 alpha.GTP by EF-1 beta gamma delta.	Guanosine Diphosphate	109-112	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	133-143	
2026171-3	1991	In contrast to amino-terminal fragments, those derived from the carboxy-terminal part of EF-1 beta were still active in enhancing the guanine nucleotide exchange of GDP bound to EF-1 alpha.	Guanosine Diphosphate	165-168	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	178-188	
8743583-8	1996	We investigated the effects of GTP/GDP and Ca2+/calmodulin on F-actin bundling activity of EF-1alpha.	Guanosine Diphosphate	35-38	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	91-100	
8743583-9	1996	The presence of GTP, GDP, or guanylyl-imidodiphosphate (GMP-PNP) slightly decreased the amount of EF-1 alpha which bound to F-actin, but each had virtually no effect on the F-actin bundling activity.	Guanosine Diphosphate	21-24	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	98-108