PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
187579-9	1976	They also indicate that there is a substantial difference in conformation between free EF-G, EF-G-GDP, and EF-G-GTP near the active site essential for interaction with ribosomes.	Guanosine Diphosphate	98-101	G elongation factor mitochondrial 1	Homo sapiens	93-97	
187579-3	1976	It was found that the ESR spectra of EF-G labeled with nitroxide maleimide reagents were modified by the addition of various guanine nucleotides such as GDP, GTP and, to a lesser extent, by Gpp(NH)p and Gpp(CH2)p, indicating that conformational changes accompany the binding of nucleotide ligand.	Guanosine Diphosphate	153-156	G elongation factor mitochondrial 1	Homo sapiens	37-41	
187579-9	1976	They also indicate that there is a substantial difference in conformation between free EF-G, EF-G-GDP, and EF-G-GTP near the active site essential for interaction with ribosomes.	Guanosine Diphosphate	98-101	G elongation factor mitochondrial 1	Homo sapiens	93-97	
4519646-2	1973	The translocated N-acetyl-Phe-tRNA, bound to the ribosomal donor site, prevents further interaction of EF-G with the ribosome, for it inhibits the GTP hydrolysis that takes place in the presence of EF-G and ribosomes and it decreases the formation of either the GDP.EF-G.fusidic acid.ribosome complex or the 5"-guanylylmethylenediphosphonate.EF-G.ribosome complex.	Guanosine Diphosphate	262-265	G elongation factor mitochondrial 1	Homo sapiens	103-107	
1103967-11	1975	Guanylyl methylene diphosphonate was displaced more readily than GDP from the EF-G-ribosome complex by GTP analogues insensitive to fusidic acid.	Guanosine Diphosphate	65-68	G elongation factor mitochondrial 1	Homo sapiens	78-82	
4519646-2	1973	The translocated N-acetyl-Phe-tRNA, bound to the ribosomal donor site, prevents further interaction of EF-G with the ribosome, for it inhibits the GTP hydrolysis that takes place in the presence of EF-G and ribosomes and it decreases the formation of either the GDP.EF-G.fusidic acid.ribosome complex or the 5"-guanylylmethylenediphosphonate.EF-G.ribosome complex.	Guanosine Diphosphate	262-265	G elongation factor mitochondrial 1	Homo sapiens	198-202	
4519646-2	1973	The translocated N-acetyl-Phe-tRNA, bound to the ribosomal donor site, prevents further interaction of EF-G with the ribosome, for it inhibits the GTP hydrolysis that takes place in the presence of EF-G and ribosomes and it decreases the formation of either the GDP.EF-G.fusidic acid.ribosome complex or the 5"-guanylylmethylenediphosphonate.EF-G.ribosome complex.	Guanosine Diphosphate	262-265	G elongation factor mitochondrial 1	Homo sapiens	198-202	
4519646-2	1973	The translocated N-acetyl-Phe-tRNA, bound to the ribosomal donor site, prevents further interaction of EF-G with the ribosome, for it inhibits the GTP hydrolysis that takes place in the presence of EF-G and ribosomes and it decreases the formation of either the GDP.EF-G.fusidic acid.ribosome complex or the 5"-guanylylmethylenediphosphonate.EF-G.ribosome complex.	Guanosine Diphosphate	262-265	G elongation factor mitochondrial 1	Homo sapiens	198-202	
26729758-3	2016	Fusidic acid inhibits protein synthesis by binding EF-G-GDP, which results in the inhibition of both peptide translocation and ribosome disassembly.	Guanosine Diphosphate	56-59	G elongation factor mitochondrial 1	Homo sapiens	51-55	
29408956-5	2018	The structure reveals a natural conformation of EF-G GDP in the ribosome, with a previously unseen conformation of its third domain.	Guanosine Diphosphate	53-56	G elongation factor mitochondrial 1	Homo sapiens	48-52	
27313204-4	2016	Free EF-G, not bound to the ribosome, adopts quite different structures in its GTP and GDP forms.	Guanosine Diphosphate	87-90	G elongation factor mitochondrial 1	Homo sapiens	5-9	
27063503-4	2016	Here, we show that while EF-G GDP does not stably bind to the ribosome and induce translocation, EF-G GDP in complex with phosphate group analogs BeF3(-) and AlF4(-) promotes the translocation of tRNA and mRNA.	Guanosine Diphosphate	30-33	G elongation factor mitochondrial 1	Homo sapiens	25-29	
27063503-4	2016	Here, we show that while EF-G GDP does not stably bind to the ribosome and induce translocation, EF-G GDP in complex with phosphate group analogs BeF3(-) and AlF4(-) promotes the translocation of tRNA and mRNA.	Guanosine Diphosphate	102-105	G elongation factor mitochondrial 1	Homo sapiens	25-29	
27063503-4	2016	Here, we show that while EF-G GDP does not stably bind to the ribosome and induce translocation, EF-G GDP in complex with phosphate group analogs BeF3(-) and AlF4(-) promotes the translocation of tRNA and mRNA.	Guanosine Diphosphate	102-105	G elongation factor mitochondrial 1	Homo sapiens	97-101	
23150791-0	2012	GTPases IF2 and EF-G bind GDP and the SRL RNA in a mutually exclusive manner.	Guanosine Diphosphate	26-29	G elongation factor mitochondrial 1	Homo sapiens	16-20	
22308410-5	2012	By binding to EF-G on the ribosome, FusB-type proteins promote the dissociation of stalled ribosome EF-G GDP complexes that form in the presence of FA, thereby allowing the ribosomes to resume translation.	Guanosine Diphosphate	105-108	G elongation factor mitochondrial 1	Homo sapiens	14-18	
22308410-5	2012	By binding to EF-G on the ribosome, FusB-type proteins promote the dissociation of stalled ribosome EF-G GDP complexes that form in the presence of FA, thereby allowing the ribosomes to resume translation.	Guanosine Diphosphate	105-108	G elongation factor mitochondrial 1	Homo sapiens	100-104	
23150791-5	2012	We show that binding of IF2 and EF-G to a 27 nucleotide RNA fragment mimicking the sarcin-ricin loop is mutually exclusive with that of GDP, but not of GTP, providing a mechanism for destabilization of the ribosome-bound GDP forms of translational GTPases.	Guanosine Diphosphate	136-139	G elongation factor mitochondrial 1	Homo sapiens	32-36	
23150791-5	2012	We show that binding of IF2 and EF-G to a 27 nucleotide RNA fragment mimicking the sarcin-ricin loop is mutually exclusive with that of GDP, but not of GTP, providing a mechanism for destabilization of the ribosome-bound GDP forms of translational GTPases.	Guanosine Diphosphate	221-224	G elongation factor mitochondrial 1	Homo sapiens	32-36	
17630323-2	2007	Here, we have used a combination of chemical footprinting, peptidyl transferase activity assays, and mRNA toeprinting to monitor the effects of EF-G on the positions of tRNA and mRNA relative to the A, P, and E sites of the ribosome in the presence of GTP, GDP, GDPNP, and fusidic acid.	Guanosine Diphosphate	257-260	G elongation factor mitochondrial 1	Homo sapiens	144-148	
18836081-2	2008	We have used isothermal titration calorimetry to characterize the binding of GDP and GTP to free EF-G at 4 degrees C, 20 degrees C, and 37 degrees C. The binding affinity of EF-G is higher to GDP than to GTP at 4 degrees C, but lower at 37 degrees C. The binding enthalpy and entropy change little with temperature in the case of GDP binding but change greatly in the case of GTP binding.	Guanosine Diphosphate	77-80	G elongation factor mitochondrial 1	Homo sapiens	97-101	
18836081-2	2008	We have used isothermal titration calorimetry to characterize the binding of GDP and GTP to free EF-G at 4 degrees C, 20 degrees C, and 37 degrees C. The binding affinity of EF-G is higher to GDP than to GTP at 4 degrees C, but lower at 37 degrees C. The binding enthalpy and entropy change little with temperature in the case of GDP binding but change greatly in the case of GTP binding.	Guanosine Diphosphate	77-80	G elongation factor mitochondrial 1	Homo sapiens	174-178	
18836081-2	2008	We have used isothermal titration calorimetry to characterize the binding of GDP and GTP to free EF-G at 4 degrees C, 20 degrees C, and 37 degrees C. The binding affinity of EF-G is higher to GDP than to GTP at 4 degrees C, but lower at 37 degrees C. The binding enthalpy and entropy change little with temperature in the case of GDP binding but change greatly in the case of GTP binding.	Guanosine Diphosphate	192-195	G elongation factor mitochondrial 1	Homo sapiens	97-101	
18836081-2	2008	We have used isothermal titration calorimetry to characterize the binding of GDP and GTP to free EF-G at 4 degrees C, 20 degrees C, and 37 degrees C. The binding affinity of EF-G is higher to GDP than to GTP at 4 degrees C, but lower at 37 degrees C. The binding enthalpy and entropy change little with temperature in the case of GDP binding but change greatly in the case of GTP binding.	Guanosine Diphosphate	192-195	G elongation factor mitochondrial 1	Homo sapiens	174-178	
18836081-2	2008	We have used isothermal titration calorimetry to characterize the binding of GDP and GTP to free EF-G at 4 degrees C, 20 degrees C, and 37 degrees C. The binding affinity of EF-G is higher to GDP than to GTP at 4 degrees C, but lower at 37 degrees C. The binding enthalpy and entropy change little with temperature in the case of GDP binding but change greatly in the case of GTP binding.	Guanosine Diphosphate	192-195	G elongation factor mitochondrial 1	Homo sapiens	97-101	
18836081-2	2008	We have used isothermal titration calorimetry to characterize the binding of GDP and GTP to free EF-G at 4 degrees C, 20 degrees C, and 37 degrees C. The binding affinity of EF-G is higher to GDP than to GTP at 4 degrees C, but lower at 37 degrees C. The binding enthalpy and entropy change little with temperature in the case of GDP binding but change greatly in the case of GTP binding.	Guanosine Diphosphate	192-195	G elongation factor mitochondrial 1	Homo sapiens	174-178	
18836081-3	2008	These observations are compatible with a large decrease in the solvent-accessible hydrophobic surface area of EF-G on GTP, but not GDP, binding.	Guanosine Diphosphate	131-134	G elongation factor mitochondrial 1	Homo sapiens	110-114	
18836081-5	2008	From these data, in conjunction with previously reported structural data on guanine nucleotide-bound EF-G, we suggest that EF-G enters the pretranslocation ribosome as an "activity chimera," with the G domain activated by the presence of GTP but the overall factor conformation in the inactive form typical of a GDP-bound multidomain guanosine triphosphatase.	Guanosine Diphosphate	312-315	G elongation factor mitochondrial 1	Homo sapiens	123-127	
20713063-1	2010	In addition to their natural substrates GDP and GTP, the bacterial translational GTPases initiation factor (IF) 2 and elongation factor G (EF-G) interact with the alarmone molecule guanosine tetraphosphate (ppGpp), which leads to GTPase inhibition.	Guanosine Diphosphate	40-43	G elongation factor mitochondrial 1	Homo sapiens	118-137	
20713063-1	2010	In addition to their natural substrates GDP and GTP, the bacterial translational GTPases initiation factor (IF) 2 and elongation factor G (EF-G) interact with the alarmone molecule guanosine tetraphosphate (ppGpp), which leads to GTPase inhibition.	Guanosine Diphosphate	40-43	G elongation factor mitochondrial 1	Homo sapiens	139-143	
19833919-3	2009	Fusidic acid traps EF-G in a conformation intermediate between the guanosine triphosphate and guanosine diphosphate forms.	Guanosine Diphosphate	94-115	G elongation factor mitochondrial 1	Homo sapiens	19-23	
17630323-3	2007	Chemical footprinting experiments show that binding of EF-G in the presence of the non-hydrolyzable GTP analog GDPNP or GDP.fusidic acid induces movement of a deacylated tRNA from the classical P/P state to the hybrid P/E state.	Guanosine Diphosphate	111-114	G elongation factor mitochondrial 1	Homo sapiens	55-59	
17630323-5	2007	A deacylated tRNA bound to the P site and a peptidyl-tRNA in the A site are completely translocated to the E and P sites, respectively, in the presence of EF-G with GTP or GDPNP but not with EF-G.GDP.	Guanosine Diphosphate	172-175	G elongation factor mitochondrial 1	Homo sapiens	191-195	
17630323-7	2007	Our results show that binding of EF-G in the presence of GDPNP or GDP.fusidic acid stabilizes the ribosomal intermediate hybrid state, but that complete translocation is supported only by EF-G.GTP or EF-G.GDPNP.	Guanosine Diphosphate	57-60	G elongation factor mitochondrial 1	Homo sapiens	33-37	
16292341-6	2005	In contrast, the release of inorganic phosphate (Pi) from ribosome-bound EF-G.GDP.Pi was strongly inhibited and became rate-limiting for the turnover of EF-G.	Guanosine Diphosphate	78-81	G elongation factor mitochondrial 1	Homo sapiens	73-77	
16337596-1	2005	During tRNA translocation on the ribosome, an arc-like connection (ALC) is formed between the G" domain of elongation factor G (EF-G) and the L7/L12-stalk base of the large ribosomal subunit in the GDP state.	Guanosine Diphosphate	198-201	G elongation factor mitochondrial 1	Homo sapiens	107-126	
16337596-1	2005	During tRNA translocation on the ribosome, an arc-like connection (ALC) is formed between the G" domain of elongation factor G (EF-G) and the L7/L12-stalk base of the large ribosomal subunit in the GDP state.	Guanosine Diphosphate	198-201	G elongation factor mitochondrial 1	Homo sapiens	128-132	
16337596-3	2005	Two distinct positions for the undecagold, observed in the GTP-state and GDP-state cryo-EM maps of the ribosome bound EF-G, allowed us to determine the movement of the labeled amino acid.	Guanosine Diphosphate	73-76	G elongation factor mitochondrial 1	Homo sapiens	118-122	
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	
16292341-6	2005	In contrast, the release of inorganic phosphate (Pi) from ribosome-bound EF-G.GDP.Pi was strongly inhibited and became rate-limiting for the turnover of EF-G.	Guanosine Diphosphate	78-81	G elongation factor mitochondrial 1	Homo sapiens	153-157	
15985151-2	2005	A new study reports that EF-G binds to ribosomes as an EF-G.GDP complex and that GTP is exchanged for GDP on the ribosome.	Guanosine Diphosphate	60-63	G elongation factor mitochondrial 1	Homo sapiens	25-29	
16083884-5	2005	Comparison of this structure with that of EF-G in complex with GDP suggests that the GTP and GDP conformations in solution are very similar and that the major contribution to the active GTPase conformation, which is quite different, therefore comes from its interaction with the ribosome.	Guanosine Diphosphate	63-66	G elongation factor mitochondrial 1	Homo sapiens	42-46	
16083884-5	2005	Comparison of this structure with that of EF-G in complex with GDP suggests that the GTP and GDP conformations in solution are very similar and that the major contribution to the active GTPase conformation, which is quite different, therefore comes from its interaction with the ribosome.	Guanosine Diphosphate	93-96	G elongation factor mitochondrial 1	Homo sapiens	42-46	
15985151-2	2005	A new study reports that EF-G binds to ribosomes as an EF-G.GDP complex and that GTP is exchanged for GDP on the ribosome.	Guanosine Diphosphate	60-63	G elongation factor mitochondrial 1	Homo sapiens	55-59	
15985151-2	2005	A new study reports that EF-G binds to ribosomes as an EF-G.GDP complex and that GTP is exchanged for GDP on the ribosome.	Guanosine Diphosphate	102-105	G elongation factor mitochondrial 1	Homo sapiens	25-29	
9678602-3	1998	Furthermore, the structure of EF-G:GDP is the form of EF-G that dissociates from the ribosome.	Guanosine Diphosphate	35-38	G elongation factor mitochondrial 1	Homo sapiens	30-34	
10891280-2	2000	In the crystal structure of GDP-bound EF-G, domain 1 (G domain) makes direct contacts with domains 2 and 5, whereas domain 4 protrudes from the body of the molecule.	Guanosine Diphosphate	28-31	G elongation factor mitochondrial 1	Homo sapiens	38-42	
10404220-1	1999	Cryo-electron microscopy has been used to visualize elongation factor G (EF-G) on the 70S ribosome in GDP and GTP states.	Guanosine Diphosphate	102-105	G elongation factor mitochondrial 1	Homo sapiens	52-71	
10404220-1	1999	Cryo-electron microscopy has been used to visualize elongation factor G (EF-G) on the 70S ribosome in GDP and GTP states.	Guanosine Diphosphate	102-105	G elongation factor mitochondrial 1	Homo sapiens	73-77	
15491605-5	2004	The functional cycle of EF-G, i.e. binding of EF-G.GTP to the ribosome, GTP hydrolysis, Pi release, and dissociation of EF-G.GDP from the ribosome, was not affected either, indicating that EF-G turnover is not coupled directly to tRNA-mRNA movement.	Guanosine Diphosphate	125-128	G elongation factor mitochondrial 1	Homo sapiens	24-28	
12471894-2	2000	Unlike other GTPases, but by analogy to the myosin motor, EF-G performs its function of powering translocation in the GDP-bound form; that is, in a kinetically stable ribosome-EF-G(GDP) complex formed by GTP hydrolysis on the ribosome.	Guanosine Diphosphate	118-121	G elongation factor mitochondrial 1	Homo sapiens	58-62	
12471894-2	2000	Unlike other GTPases, but by analogy to the myosin motor, EF-G performs its function of powering translocation in the GDP-bound form; that is, in a kinetically stable ribosome-EF-G(GDP) complex formed by GTP hydrolysis on the ribosome.	Guanosine Diphosphate	118-121	G elongation factor mitochondrial 1	Homo sapiens	176-180	
12471894-2	2000	Unlike other GTPases, but by analogy to the myosin motor, EF-G performs its function of powering translocation in the GDP-bound form; that is, in a kinetically stable ribosome-EF-G(GDP) complex formed by GTP hydrolysis on the ribosome.	Guanosine Diphosphate	181-184	G elongation factor mitochondrial 1	Homo sapiens	58-62	
12471894-2	2000	Unlike other GTPases, but by analogy to the myosin motor, EF-G performs its function of powering translocation in the GDP-bound form; that is, in a kinetically stable ribosome-EF-G(GDP) complex formed by GTP hydrolysis on the ribosome.	Guanosine Diphosphate	181-184	G elongation factor mitochondrial 1	Homo sapiens	176-180	
9678602-4	1998	Since it mimics the structure of the ternary complex of EF-Tu:GTP with aminoacyl-tRNA, which subsequently binds to the ribosome, EF-G:GDP leaves an imprint on the ribosome for the ternary complex.	Guanosine Diphosphate	134-137	G elongation factor mitochondrial 1	Homo sapiens	129-133	
9678602-3	1998	Furthermore, the structure of EF-G:GDP is the form of EF-G that dissociates from the ribosome.	Guanosine Diphosphate	35-38	G elongation factor mitochondrial 1	Homo sapiens	54-58	
9254632-2	1997	Crystallographic investigations have revealed that EF-G.GDP resembles the EF-Tu.GTP.	Guanosine Diphosphate	56-59	G elongation factor mitochondrial 1	Homo sapiens	51-55	
9254632-5	1997	However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex.	Guanosine Diphosphate	68-71	G elongation factor mitochondrial 1	Homo sapiens	63-67	
9254632-5	1997	However, its significance is uncertain because the affinity of EF-G.GDP for the ribosome is much lower than that of the ternary complex it resembles and because EF-Tu.GDP, the form of EF-Tu that has low ribosome affinity, has a conformation radically different from that of EF-Tu.GTP or EF-Tu in the ternary complex.	Guanosine Diphosphate	167-170	G elongation factor mitochondrial 1	Homo sapiens	63-67	
9254632-6	1997	The small-angle X-ray scattering study described here was undertaken to ascertain if the form of EF-G that has high ribosome affinity, EF-G.GTP, the structure of which is unknown, could be a mimic of EF-Tu.GDP.	Guanosine Diphosphate	206-209	G elongation factor mitochondrial 1	Homo sapiens	97-101	
8736554-0	1996	The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange.	Guanosine Diphosphate	53-56	G elongation factor mitochondrial 1	Homo sapiens	17-36	
8736554-2	1996	During translocation EF-G passes through four main conformational states: the GDP complex, the nucleotide-free state, the GTP complex, and the GTPase conformation.	Guanosine Diphosphate	78-81	G elongation factor mitochondrial 1	Homo sapiens	21-25	
8736554-4	1996	RESULTS: The structure of EF-G-GDP has been refined at 2.4 A resolution.	Guanosine Diphosphate	31-34	G elongation factor mitochondrial 1	Homo sapiens	26-30	
8736554-7	1996	The magnesium ion is absent in EF-G-GDP.	Guanosine Diphosphate	36-39	G elongation factor mitochondrial 1	Homo sapiens	31-35	
8642600-7	1996	The revertant mutations probably restore the balance between the GDP and GTP conformations of EF-G off the ribosome, and most of them are located close to the interface between the G domain and domain II.	Guanosine Diphosphate	65-68	G elongation factor mitochondrial 1	Homo sapiens	94-98	
10397336-9	1998	The structural comparison of this ternary complex with the structure of EF-G:GDP displays an unexpected macromolecular mimicry, where three domains of EF-G mimick the shape of the tRNA in the ternary complex.	Guanosine Diphosphate	77-80	G elongation factor mitochondrial 1	Homo sapiens	72-76	
10397336-9	1998	The structural comparison of this ternary complex with the structure of EF-G:GDP displays an unexpected macromolecular mimicry, where three domains of EF-G mimick the shape of the tRNA in the ternary complex.	Guanosine Diphosphate	77-80	G elongation factor mitochondrial 1	Homo sapiens	151-155	
9254632-7	1997	The data show that nucleotide-free EF-G, EF-G.GDP, EF-G.	Guanosine Diphosphate	46-49	G elongation factor mitochondrial 1	Homo sapiens	41-45	
9254632-7	1997	The data show that nucleotide-free EF-G, EF-G.GDP, EF-G.	Guanosine Diphosphate	46-49	G elongation factor mitochondrial 1	Homo sapiens	41-45	
9254632-8	1997	GTP, and EF-G.GMPPCP cannot be distinguished by solution scattering and that it is likely they all resemble crystalline EF-G.GDP.	Guanosine Diphosphate	125-128	G elongation factor mitochondrial 1	Homo sapiens	120-124	
34635670-5	2021	EF-G in the active GDP-Pi form stabilizes the rotated conformation of ribosomal subunits and induces twisting of the sarcin-ricin loop of the 23 S rRNA.	Guanosine Diphosphate	19-22	G elongation factor mitochondrial 1	Homo sapiens	0-4