PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
2753158-3	1989	Phosphorylation results in complete inactivation of EF-2 in the poly(U)-directed cell-free translation system.	Poly U	64-71	eukaryotic translation elongation factor 2	Homo sapiens	52-56
2510715-0	1989	The tumour promoter okadaic acid inhibits reticulocyte-lysate protein synthesis by increasing the net phosphorylation of elongation factor 2.	Okadaic Acid	20-32	eukaryotic translation elongation factor 2	Homo sapiens	121-140
2510715-6	1989	EF-2 is a specific substrate for a Ca2+/calmodulin-dependent protein kinase, which phosphorylates EF-2 on threonine residues.	Threonine	106-115	eukaryotic translation elongation factor 2	Homo sapiens	0-4
2510715-6	1989	EF-2 is a specific substrate for a Ca2+/calmodulin-dependent protein kinase, which phosphorylates EF-2 on threonine residues.	Threonine	106-115	eukaryotic translation elongation factor 2	Homo sapiens	98-102
2510715-8	1989	These agents attenuated the effects of okadaic acid on EF-2 phosphorylation and translation.	Okadaic Acid	39-51	eukaryotic translation elongation factor 2	Homo sapiens	55-59
2510715-9	1989	When ranges of concentrations of each agent were tested, their effects on EF-2 labelling correlated well with their ability to reverse the okadaic acid-induced inhibition of translation.	Okadaic Acid	139-151	eukaryotic translation elongation factor 2	Homo sapiens	74-78
2663845-13	1989	Finally, we found that insulin induction of EF-2 occurred normally in the presence of the RNA-transcription inhibitor, actinomycin D.	Dactinomycin	119-132	eukaryotic translation elongation factor 2	Homo sapiens	44-48
2693515-2	1989	A 20 min in vitro assay, in which a radioactive ADP-ribosyl residue is transferred specifically and 1:1 stoichiometrically to EF-2, is sufficient to estimate the total amounts of ADP-ribosylatable active EF-2.	Adenosine Diphosphate	48-51	eukaryotic translation elongation factor 2	Homo sapiens	126-130
2693515-2	1989	A 20 min in vitro assay, in which a radioactive ADP-ribosyl residue is transferred specifically and 1:1 stoichiometrically to EF-2, is sufficient to estimate the total amounts of ADP-ribosylatable active EF-2.	Adenosine Diphosphate	179-182	eukaryotic translation elongation factor 2	Homo sapiens	126-130
2693515-2	1989	A 20 min in vitro assay, in which a radioactive ADP-ribosyl residue is transferred specifically and 1:1 stoichiometrically to EF-2, is sufficient to estimate the total amounts of ADP-ribosylatable active EF-2.	Adenosine Diphosphate	179-182	eukaryotic translation elongation factor 2	Homo sapiens	204-208
2753158-6	1989	Thus, phosphorylation of EF-2 seems to block its ability to promote a shift of the aminoacyl(peptidyl)-tRNA from the A site to the P site, i.e. translocation itself.	aminoacyl(peptidyl)	83-102	eukaryotic translation elongation factor 2	Homo sapiens	25-29
2537725-1	1989	The binding stability of the different nucleotide-dependent and -independent interactions between elongation factor 2 (EF-2) and 80S ribosomes, as well as 60S subunits, was studied and correlated to the kinetics of the EF-2- and ribosome-dependent hydrolysis of GTP.	Guanosine Triphosphate	262-265	eukaryotic translation elongation factor 2	Homo sapiens	98-117
2930555-1	1989	The amount of protein elongation factor EF-2 that can be inactivated by diphtheria toxin-mediated ADP-ribosylation, a measure of its active content, decreases by 45% and 66% in G1-arrested normal human fibroblasts and in HeLa cells respectively.	Adenosine Diphosphate	98-101	eukaryotic translation elongation factor 2	Homo sapiens	40-44
2930555-3	1989	The apparent long half-lives of EF-2 mRNA and protein indicate possibilities of posttranslational ADP-ribosylation and de-ADP-ribosylation as the regulators of the amounts of active EF-2 during human cell cycle.	Adenosine Diphosphate	98-101	eukaryotic translation elongation factor 2	Homo sapiens	32-36
2537725-1	1989	The binding stability of the different nucleotide-dependent and -independent interactions between elongation factor 2 (EF-2) and 80S ribosomes, as well as 60S subunits, was studied and correlated to the kinetics of the EF-2- and ribosome-dependent hydrolysis of GTP.	Guanosine Triphosphate	262-265	eukaryotic translation elongation factor 2	Homo sapiens	119-123
2537725-2	1989	Empty reconstituted 80S ribosomes were found to contain two subpopulations of ribosomes, with approximately 80% capable of binding EF-2.GuoPP[CH2]P with high affinity (Kd less than 10(-9) M) and the rest only capable of binding the factor-nucleotide complex with low affinity (Kd = 3.7 x 10(-7) M).	guopp[	136-142	eukaryotic translation elongation factor 2	Homo sapiens	131-135
2537725-4	1989	At low EF-2/ribosome ratios the number of GTP molecules hydrolyzed/factor molecule was considerably lower than at higher ratios.	Guanosine Triphosphate	42-45	eukaryotic translation elongation factor 2	Homo sapiens	7-11
2536373-0	1989	Thrombin and histamine stimulate the phosphorylation of elongation factor 2 in human umbilical vein endothelial cells.	Histamine	13-22	eukaryotic translation elongation factor 2	Homo sapiens	56-75
2536373-7	1989	Phosphoamino acid analysis of the EF-2 immunoprecipitated from HUVEC revealed that all of the thrombin-stimulated phosphorylation occurred on threonine.	Phosphoamino Acids	0-17	eukaryotic translation elongation factor 2	Homo sapiens	34-38
2536373-8	1989	EF-2 was also phosphorylated when HUVEC were treated with the calcium ionophore, ionomycin.	Ionomycin	81-90	eukaryotic translation elongation factor 2	Homo sapiens	0-4
2536373-10	1989	The transient nature of the phosphorylation of EF-2 is consistent with it having a role in mediating some of the transient effects of thrombin and histamine on endothelial cell protein synthesis and functional capabilities.	Histamine	147-156	eukaryotic translation elongation factor 2	Homo sapiens	47-51
2536373-7	1989	Phosphoamino acid analysis of the EF-2 immunoprecipitated from HUVEC revealed that all of the thrombin-stimulated phosphorylation occurred on threonine.	Threonine	142-151	eukaryotic translation elongation factor 2	Homo sapiens	34-38
2536373-8	1989	EF-2 was also phosphorylated when HUVEC were treated with the calcium ionophore, ionomycin.	Calcium	62-69	eukaryotic translation elongation factor 2	Homo sapiens	0-4
2458772-5	1988	Unlike the substrate, the EF-2 kinase had no affinity for RNA and therefore could be separated from EF-2 by chromatography on RNA-Sepharose.	Sepharose	130-139	eukaryotic translation elongation factor 2	Homo sapiens	26-30
2844804-3	1988	In the pituitary cell line GH3, sphingosine inhibits the phosphorylation of microtubule-associated protein 2 by the multifunctional Ca2+/calmodulin-dependent protein kinase and the phosphorylation of elongation factor 2 by Ca2+/calmodulin-dependent kinase III.	Sphingosine	32-43	eukaryotic translation elongation factor 2	Homo sapiens	200-219
2514587-2	1989	2"-deoxyNAD is a substrate for the diphtheria toxin-catalyzed mono(ADP-ribosyl)ation of elongation factor-2, inactivating its function to enhance protein synthesis.	2'-deoxynicotinamide adenine dinucleotide	0-11	eukaryotic translation elongation factor 2	Homo sapiens	88-107
2514587-2	1989	2"-deoxyNAD is a substrate for the diphtheria toxin-catalyzed mono(ADP-ribosyl)ation of elongation factor-2, inactivating its function to enhance protein synthesis.	mono(adp-ribosyl)	62-79	eukaryotic translation elongation factor 2	Homo sapiens	88-107
3386756-3	1988	The in vivo activity of the EF-2 kinase depends upon growth factors and other agents affecting the level of Ca2+ and cAMP.	Cyclic AMP	117-121	eukaryotic translation elongation factor 2	Homo sapiens	28-32
3386756-5	1988	This work shows that the phosphorylation of EF-2 by the EF-2 kinase results in a drastic inhibition of polyphenylalanine synthesis in poly(U)-directed translation.	polyphenylalanine	103-120	eukaryotic translation elongation factor 2	Homo sapiens	44-48
3386756-5	1988	This work shows that the phosphorylation of EF-2 by the EF-2 kinase results in a drastic inhibition of polyphenylalanine synthesis in poly(U)-directed translation.	polyphenylalanine	103-120	eukaryotic translation elongation factor 2	Homo sapiens	56-60
3386756-5	1988	This work shows that the phosphorylation of EF-2 by the EF-2 kinase results in a drastic inhibition of polyphenylalanine synthesis in poly(U)-directed translation.	Poly U	134-141	eukaryotic translation elongation factor 2	Homo sapiens	44-48
3386756-5	1988	This work shows that the phosphorylation of EF-2 by the EF-2 kinase results in a drastic inhibition of polyphenylalanine synthesis in poly(U)-directed translation.	Poly U	134-141	eukaryotic translation elongation factor 2	Homo sapiens	56-60
2458772-5	1988	Unlike the substrate, the EF-2 kinase had no affinity for RNA and therefore could be separated from EF-2 by chromatography on RNA-Sepharose.	Sepharose	130-139	eukaryotic translation elongation factor 2	Homo sapiens	100-104
3338467-0	1988	Structural and functional studies of the interaction of the eukaryotic elongation factor EF-2 with GTP and ribosomes.	Guanosine Triphosphate	99-102	eukaryotic translation elongation factor 2	Homo sapiens	89-93
2840927-3	1988	The 15 amino-acid-residue sequence comprising the histidine-715, supposed to be of importance for the biological function of EF-2, is preserved in human EF-2.	Histidine	50-59	eukaryotic translation elongation factor 2	Homo sapiens	125-129
2840927-3	1988	The 15 amino-acid-residue sequence comprising the histidine-715, supposed to be of importance for the biological function of EF-2, is preserved in human EF-2.	Histidine	50-59	eukaryotic translation elongation factor 2	Homo sapiens	153-157
3338467-1	1988	The structure of the guanosine nucleotide binding site of EF-2 was studied by affinity labelling with the GTP analogue, oxidized GTP (oGTP), and by amino acid sequencing of polypeptides generated after partial degradation with trypsin and N-chlorosuccinimide.	guanosine nucleotide	21-41	eukaryotic translation elongation factor 2	Homo sapiens	58-62
3338467-1	1988	The structure of the guanosine nucleotide binding site of EF-2 was studied by affinity labelling with the GTP analogue, oxidized GTP (oGTP), and by amino acid sequencing of polypeptides generated after partial degradation with trypsin and N-chlorosuccinimide.	Guanosine Triphosphate	106-109	eukaryotic translation elongation factor 2	Homo sapiens	58-62
3338467-1	1988	The structure of the guanosine nucleotide binding site of EF-2 was studied by affinity labelling with the GTP analogue, oxidized GTP (oGTP), and by amino acid sequencing of polypeptides generated after partial degradation with trypsin and N-chlorosuccinimide.	Guanosine Triphosphate	129-132	eukaryotic translation elongation factor 2	Homo sapiens	58-62
3338467-1	1988	The structure of the guanosine nucleotide binding site of EF-2 was studied by affinity labelling with the GTP analogue, oxidized GTP (oGTP), and by amino acid sequencing of polypeptides generated after partial degradation with trypsin and N-chlorosuccinimide.	ogtp	134-138	eukaryotic translation elongation factor 2	Homo sapiens	58-62
3338467-1	1988	The structure of the guanosine nucleotide binding site of EF-2 was studied by affinity labelling with the GTP analogue, oxidized GTP (oGTP), and by amino acid sequencing of polypeptides generated after partial degradation with trypsin and N-chlorosuccinimide.	N-chlorosuccinimide	239-258	eukaryotic translation elongation factor 2	Homo sapiens	58-62
3338467-7	1988	EF-2 complex was capable of forming a high-affinity complex with ribosomes, indicating that oGTP, in this respect, induced a conformation in EF-2 indistinguishable from that produced by GTP.	Guanosine Triphosphate	93-96	eukaryotic translation elongation factor 2	Homo sapiens	0-4
3338467-7	1988	EF-2 complex was capable of forming a high-affinity complex with ribosomes, indicating that oGTP, in this respect, induced a conformation in EF-2 indistinguishable from that produced by GTP.	Guanosine Triphosphate	93-96	eukaryotic translation elongation factor 2	Homo sapiens	141-145
3338467-10	1988	EF-2 cleaved at Arg66 were unable to form the high-affinity complex with ribosomes while retaining the ability to form the low-affinity complex and to hydrolyse GTP.	Guanosine Triphosphate	161-164	eukaryotic translation elongation factor 2	Homo sapiens	0-4
3693353-9	1987	CaM-dependent protein kinase III phosphorylated EF-2 in vitro with a stoichiometry of approximately 1 mol/mol on a threonine residue.	Threonine	115-124	eukaryotic translation elongation factor 2	Homo sapiens	48-52
3693353-10	1987	Amino acid sequencing of the purified tryptic phosphopeptide revealed that this threonine residue lies within the sequence: Ala-Gly-Glu-Thr-Arg-Phe-Thr-Asp-Thr-Arg (residues 51-60 of EF-2).	Threonine	80-89	eukaryotic translation elongation factor 2	Homo sapiens	183-187
3693353-10	1987	Amino acid sequencing of the purified tryptic phosphopeptide revealed that this threonine residue lies within the sequence: Ala-Gly-Glu-Thr-Arg-Phe-Thr-Asp-Thr-Arg (residues 51-60 of EF-2).	Alanine	124-127	eukaryotic translation elongation factor 2	Homo sapiens	183-187
3693353-10	1987	Amino acid sequencing of the purified tryptic phosphopeptide revealed that this threonine residue lies within the sequence: Ala-Gly-Glu-Thr-Arg-Phe-Thr-Asp-Thr-Arg (residues 51-60 of EF-2).	Threonine	136-139	eukaryotic translation elongation factor 2	Homo sapiens	183-187
3693353-10	1987	Amino acid sequencing of the purified tryptic phosphopeptide revealed that this threonine residue lies within the sequence: Ala-Gly-Glu-Thr-Arg-Phe-Thr-Asp-Thr-Arg (residues 51-60 of EF-2).	Aspartic Acid	152-155	eukaryotic translation elongation factor 2	Homo sapiens	183-187
3693353-10	1987	Amino acid sequencing of the purified tryptic phosphopeptide revealed that this threonine residue lies within the sequence: Ala-Gly-Glu-Thr-Arg-Phe-Thr-Asp-Thr-Arg (residues 51-60 of EF-2).	Threonine	148-151	eukaryotic translation elongation factor 2	Homo sapiens	183-187
3693353-10	1987	Amino acid sequencing of the purified tryptic phosphopeptide revealed that this threonine residue lies within the sequence: Ala-Gly-Glu-Thr-Arg-Phe-Thr-Asp-Thr-Arg (residues 51-60 of EF-2).	Arginine	160-163	eukaryotic translation elongation factor 2	Homo sapiens	183-187
3693353-14	1987	Dephospho-EF-2 could support poly(U)-directed polyphenylalanine synthesis in a reconstituted elongation system when combined with EF-1.	Poly U	29-36	eukaryotic translation elongation factor 2	Homo sapiens	10-14
3693353-14	1987	Dephospho-EF-2 could support poly(U)-directed polyphenylalanine synthesis in a reconstituted elongation system when combined with EF-1.	polyphenylalanine	46-63	eukaryotic translation elongation factor 2	Homo sapiens	10-14
3663126-2	1987	All these proteins, like EF-2, were selectively retained by a heparin-Sepharose column, which we used as an affinity-chromatography step.	Heparin	62-69	eukaryotic translation elongation factor 2	Homo sapiens	25-29
3676324-1	1987	Ribosomal complexes containing elongation factor 2 (EF-2) were formed by incubation of 80 S ribosomes in the presence of EF-2 and the non-hydrolysable GTP analogue GuoPP[CH2]P. The factor was covalently coupled to the ribosomal proteins located at the factor binding site, by treatment with bifunctional reagents.	Guanosine Triphosphate	151-154	eukaryotic translation elongation factor 2	Homo sapiens	31-50
3676324-1	1987	Ribosomal complexes containing elongation factor 2 (EF-2) were formed by incubation of 80 S ribosomes in the presence of EF-2 and the non-hydrolysable GTP analogue GuoPP[CH2]P. The factor was covalently coupled to the ribosomal proteins located at the factor binding site, by treatment with bifunctional reagents.	Guanosine Triphosphate	151-154	eukaryotic translation elongation factor 2	Homo sapiens	52-56
3676324-4	1987	After cross-linking with bis(hydroxysuccinimidyl) tartrate (4 A between the reactive groups), protein S3/S3a, S7 and S11 were found as the major ribosomal proteins covalently linked to EF-2.	bis(hydroxysuccinimidyl) tartrate	25-58	eukaryotic translation elongation factor 2	Homo sapiens	185-189
3676324-5	1987	The longer reagent, dimethyl 3,8-diaza-4,7-dioxo-5,6-dihydroxydecanbisimidate (11 A between the reactive groups), covalently coupled proteins S7, S11, L5, L13, L21, L23, L26, L27a and L32 to EF-2.	dimethyl-3,8-diaza-4,7-dioxo-5,6-dihydroxydecanbis(imidate)	20-77	eukaryotic translation elongation factor 2	Homo sapiens	191-195
3427221-0	1987	Interaction of diphtheria toxin fragment A and of elongation factor 2 with cibacron blue.	Cibacron Blue	75-88	eukaryotic translation elongation factor 2	Homo sapiens	50-69
3427221-4	1987	The dye inhibits in a non-competitive way the fragment A-catalysed transfer of ADP-ribose from NAD to elongation factor 2 (EF2).	Adenosine Diphosphate Ribose	79-89	eukaryotic translation elongation factor 2	Homo sapiens	102-121
3427221-4	1987	The dye inhibits in a non-competitive way the fragment A-catalysed transfer of ADP-ribose from NAD to elongation factor 2 (EF2).	Adenosine Diphosphate Ribose	79-89	eukaryotic translation elongation factor 2	Homo sapiens	123-126
3427221-4	1987	The dye inhibits in a non-competitive way the fragment A-catalysed transfer of ADP-ribose from NAD to elongation factor 2 (EF2).	NAD	95-98	eukaryotic translation elongation factor 2	Homo sapiens	102-121
3427221-4	1987	The dye inhibits in a non-competitive way the fragment A-catalysed transfer of ADP-ribose from NAD to elongation factor 2 (EF2).	NAD	95-98	eukaryotic translation elongation factor 2	Homo sapiens	123-126
3427221-5	1987	By affinity chromatography on blue Sepharose a binding of EF2 and of ADP-ribosyl-EF2 with the dye is also demonstrated.	Sepharose	35-44	eukaryotic translation elongation factor 2	Homo sapiens	58-61
3427221-5	1987	By affinity chromatography on blue Sepharose a binding of EF2 and of ADP-ribosyl-EF2 with the dye is also demonstrated.	Sepharose	35-44	eukaryotic translation elongation factor 2	Homo sapiens	81-84
3427221-6	1987	GDP, GTP and GDP(CH2)P are able to displace EF2 from blue Sepharose.	Guanosine Diphosphate	0-3	eukaryotic translation elongation factor 2	Homo sapiens	44-47
3427221-6	1987	GDP, GTP and GDP(CH2)P are able to displace EF2 from blue Sepharose.	Guanosine Triphosphate	5-8	eukaryotic translation elongation factor 2	Homo sapiens	44-47
3427221-6	1987	GDP, GTP and GDP(CH2)P are able to displace EF2 from blue Sepharose.	gdp(ch2)p	13-22	eukaryotic translation elongation factor 2	Homo sapiens	44-47
3427221-6	1987	GDP, GTP and GDP(CH2)P are able to displace EF2 from blue Sepharose.	Sepharose	58-67	eukaryotic translation elongation factor 2	Homo sapiens	44-47
3663126-2	1987	All these proteins, like EF-2, were selectively retained by a heparin-Sepharose column, which we used as an affinity-chromatography step.	Sepharose	70-79	eukaryotic translation elongation factor 2	Homo sapiens	25-29
3801485-2	1987	Stable EF-2 X ribosome complexes formed in the presence of the non-hydrolysable GTP analogue GuoPP[CH2]P were cross-linked with the short (4 A between the reactive groups) bifunctional reagent, diepoxybutane.	Guanosine Triphosphate	80-83	eukaryotic translation elongation factor 2	Homo sapiens	7-11
3801485-2	1987	Stable EF-2 X ribosome complexes formed in the presence of the non-hydrolysable GTP analogue GuoPP[CH2]P were cross-linked with the short (4 A between the reactive groups) bifunctional reagent, diepoxybutane.	guanosine 5'-(beta,gamma-methylene)triphosphate	93-104	eukaryotic translation elongation factor 2	Homo sapiens	7-11
3801485-2	1987	Stable EF-2 X ribosome complexes formed in the presence of the non-hydrolysable GTP analogue GuoPP[CH2]P were cross-linked with the short (4 A between the reactive groups) bifunctional reagent, diepoxybutane.	diepoxybutane	194-207	eukaryotic translation elongation factor 2	Homo sapiens	7-11
3801485-6	1987	Treatment of the covalent ribosome-factor complexes with EDTA released approx 50% of the cross-linked EF-2 from the ribosome together with the 5 S rRNA X protein L5 complex.	Edetic Acid	57-61	eukaryotic translation elongation factor 2	Homo sapiens	102-106
3801485-8	1987	Polyacrylamide gel electrophoresis showed that EF-2 was directly linked to 5 S rRNA in the 5 S rRNA X L5 complex, as well as in the complexes isolated by density gradient centrifugation.	polyacrylamide	0-14	eukaryotic translation elongation factor 2	Homo sapiens	47-51
2427294-0	1986	[The ADP-ribosylation site and RNA-binding center are located in different regions of the elongation factor EF-2].	Adenosine Diphosphate	5-8	eukaryotic translation elongation factor 2	Homo sapiens	108-112
3780730-7	1986	Ricin-treated ribosomes showed an altered ability to stimulate the GTP hydrolysis catalysed by either EF-1 or EF-2.	Guanosine Triphosphate	67-70	eukaryotic translation elongation factor 2	Homo sapiens	110-114
3780730-11	1986	The results indicate that the EF-1- and EF-2-dependent hydrolysis of GTP was activated by a common center on the ribosome that was specifically adapted for promoting the GTP hydrolysis of either EF-1 or EF-2.	Guanosine Triphosphate	69-72	eukaryotic translation elongation factor 2	Homo sapiens	40-44
3780730-11	1986	The results indicate that the EF-1- and EF-2-dependent hydrolysis of GTP was activated by a common center on the ribosome that was specifically adapted for promoting the GTP hydrolysis of either EF-1 or EF-2.	Guanosine Triphosphate	69-72	eukaryotic translation elongation factor 2	Homo sapiens	203-207
3780730-11	1986	The results indicate that the EF-1- and EF-2-dependent hydrolysis of GTP was activated by a common center on the ribosome that was specifically adapted for promoting the GTP hydrolysis of either EF-1 or EF-2.	Guanosine Triphosphate	170-173	eukaryotic translation elongation factor 2	Homo sapiens	40-44
3780730-11	1986	The results indicate that the EF-1- and EF-2-dependent hydrolysis of GTP was activated by a common center on the ribosome that was specifically adapted for promoting the GTP hydrolysis of either EF-1 or EF-2.	Guanosine Triphosphate	170-173	eukaryotic translation elongation factor 2	Homo sapiens	203-207
3780730-12	1986	Furthermore, the results suggest that the GTP hydrolysis catalysed by EF-2 occurred in the low-affinity post-translocation complex.	Guanosine Triphosphate	42-45	eukaryotic translation elongation factor 2	Homo sapiens	70-74
3014523-0	1986	Amino acid sequence of mammalian elongation factor 2 deduced from the cDNA sequence: homology with GTP-binding proteins.	Guanosine Triphosphate	99-102	eukaryotic translation elongation factor 2	Homo sapiens	33-52
3014523-3	1986	Comparative studies of sequence homology among EF-2 and several GTP-binding proteins show that five regions in the amino-terminal position of EF-2, corresponding to about 160 amino acids, show homology with GTP-binding proteins, including protein synthesis elongation and initiation factors, mammalian ras proteins, and transducin.	Guanosine Triphosphate	64-67	eukaryotic translation elongation factor 2	Homo sapiens	142-146
3014523-3	1986	Comparative studies of sequence homology among EF-2 and several GTP-binding proteins show that five regions in the amino-terminal position of EF-2, corresponding to about 160 amino acids, show homology with GTP-binding proteins, including protein synthesis elongation and initiation factors, mammalian ras proteins, and transducin.	Guanosine Triphosphate	207-210	eukaryotic translation elongation factor 2	Homo sapiens	47-51
3014523-3	1986	Comparative studies of sequence homology among EF-2 and several GTP-binding proteins show that five regions in the amino-terminal position of EF-2, corresponding to about 160 amino acids, show homology with GTP-binding proteins, including protein synthesis elongation and initiation factors, mammalian ras proteins, and transducin.	Guanosine Triphosphate	207-210	eukaryotic translation elongation factor 2	Homo sapiens	142-146
3014523-4	1986	The carboxyl-terminal half of EF-2 contains several regions that have 34-75% homology with bacterial elongation factor G. These results suggest that the amino-terminal region of EF-2 participates in the GTP-binding and GTPase activity whereas the carboxyl-terminal region interacts with ribosomes.	Guanosine Triphosphate	203-206	eukaryotic translation elongation factor 2	Homo sapiens	30-34
3014523-4	1986	The carboxyl-terminal half of EF-2 contains several regions that have 34-75% homology with bacterial elongation factor G. These results suggest that the amino-terminal region of EF-2 participates in the GTP-binding and GTPase activity whereas the carboxyl-terminal region interacts with ribosomes.	Guanosine Triphosphate	203-206	eukaryotic translation elongation factor 2	Homo sapiens	178-182
3987690-0	1985	Localization of the sites of ADP-ribosylation and GTP binding in the eukaryotic elongation factor EF-2.	Adenosine Diphosphate	29-32	eukaryotic translation elongation factor 2	Homo sapiens	98-102
2409925-11	1985	Patients who achieved an Ef2-1 effect due to the administration of CDDP as part of the multitherapy made satisfactory progress.	Cisplatin	67-71	eukaryotic translation elongation factor 2	Homo sapiens	25-28
2996930-0	1985	1-N6-Etheno-ADP-ribosylation of elongation factor-2 by diphtheria toxin.	1,N(6)-ethenoadenosine diphosphate	0-15	eukaryotic translation elongation factor 2	Homo sapiens	32-51
2996930-1	1985	Diphtheria toxin fragment A is able to inhibit protein synthesis in the eukaryotic cell by ADP-ribosylating the diphthamide residue of elongation factor-2 (EF-2) [(1980) J. Biol.	diphthamide	112-123	eukaryotic translation elongation factor 2	Homo sapiens	135-154
2996930-1	1985	Diphtheria toxin fragment A is able to inhibit protein synthesis in the eukaryotic cell by ADP-ribosylating the diphthamide residue of elongation factor-2 (EF-2) [(1980) J. Biol.	diphthamide	112-123	eukaryotic translation elongation factor 2	Homo sapiens	156-160
2996930-5	1985	This work reports on the capacity of an NAD analog, the nicotinamide 1-N6-ethenoadenine dinucleotide (epsilon NAD), to be a substrate of diphtheria toxin fragment A in the transferring reaction of the fluorescent moiety, the epsilon ADP-ribose, to the EF-2.	NAD	40-43	eukaryotic translation elongation factor 2	Homo sapiens	252-256
2996930-5	1985	This work reports on the capacity of an NAD analog, the nicotinamide 1-N6-ethenoadenine dinucleotide (epsilon NAD), to be a substrate of diphtheria toxin fragment A in the transferring reaction of the fluorescent moiety, the epsilon ADP-ribose, to the EF-2.	nicotinamide 1,N(6)-ethenoadenine dinucleotide	56-100	eukaryotic translation elongation factor 2	Homo sapiens	252-256
2996930-5	1985	This work reports on the capacity of an NAD analog, the nicotinamide 1-N6-ethenoadenine dinucleotide (epsilon NAD), to be a substrate of diphtheria toxin fragment A in the transferring reaction of the fluorescent moiety, the epsilon ADP-ribose, to the EF-2.	NAD	110-113	eukaryotic translation elongation factor 2	Homo sapiens	252-256
2996930-5	1985	This work reports on the capacity of an NAD analog, the nicotinamide 1-N6-ethenoadenine dinucleotide (epsilon NAD), to be a substrate of diphtheria toxin fragment A in the transferring reaction of the fluorescent moiety, the epsilon ADP-ribose, to the EF-2.	Adenosine Diphosphate Ribose	233-243	eukaryotic translation elongation factor 2	Homo sapiens	252-256
2996930-7	1985	The epsilon ADP-ribosylated EF-2, like ADP-ribosylated EF-2, retains the capacity to bind GTP and ribosome.	Guanosine Triphosphate	90-93	eukaryotic translation elongation factor 2	Homo sapiens	28-32
2996930-7	1985	The epsilon ADP-ribosylated EF-2, like ADP-ribosylated EF-2, retains the capacity to bind GTP and ribosome.	Guanosine Triphosphate	90-93	eukaryotic translation elongation factor 2	Homo sapiens	55-59
3987690-0	1985	Localization of the sites of ADP-ribosylation and GTP binding in the eukaryotic elongation factor EF-2.	Guanosine Triphosphate	50-53	eukaryotic translation elongation factor 2	Homo sapiens	98-102
3987690-5	1985	The degradation of the 82-kDa polypeptide with either trypsin or chymotrypsin was facilitated by the presence of guanosine nucleotides, indicating a conformational shift in native EF-2 upon nucleotide binding.	guanosine nucleotides	113-134	eukaryotic translation elongation factor 2	Homo sapiens	180-184
3987690-7	1985	After affinity labelling of native EF-2 with oxidized [3H]GTP and subsequent trypsin treatment the radioactivity was recovered in the 48-kDa polypeptide showing that the GTP-binding site was located within this part of the factor.	[3h]gtp	54-61	eukaryotic translation elongation factor 2	Homo sapiens	35-39
3987690-7	1985	After affinity labelling of native EF-2 with oxidized [3H]GTP and subsequent trypsin treatment the radioactivity was recovered in the 48-kDa polypeptide showing that the GTP-binding site was located within this part of the factor.	Guanosine Triphosphate	58-61	eukaryotic translation elongation factor 2	Homo sapiens	35-39
3987690-8	1985	Correspondingly, tryptic degradation of EF-2 labelled with [14C]NAD+ in the presence of diphtheria toxin showed that the site of ADP-ribosylation was within the 34-kDa polypeptide.	[14c]nad+	59-68	eukaryotic translation elongation factor 2	Homo sapiens	40-44
3987690-8	1985	Correspondingly, tryptic degradation of EF-2 labelled with [14C]NAD+ in the presence of diphtheria toxin showed that the site of ADP-ribosylation was within the 34-kDa polypeptide.	Adenosine Diphosphate	129-132	eukaryotic translation elongation factor 2	Homo sapiens	40-44
6527187-9	1984	The inhibition of diphtheria toxin was NAD+ dependent, suggesting that ADP-ribosylation of EF-2 could be the cause of the inhibition as it is in mammalian cell lines.	NAD	39-43	eukaryotic translation elongation factor 2	Homo sapiens	91-95
6712255-1	1984	Diphtheria toxin inactivates protein synthesis elongation factor 2 by attaching ADP-ribose to an unusual post-translational amino acid derivative, diphthamide, in the factor.	Adenosine Diphosphate Ribose	80-90	eukaryotic translation elongation factor 2	Homo sapiens	47-66
6722159-0	1984	Affinity labelling of the eukaryotic elongation factor EF-2 with the guanosine nucleotide analogue 5"-p-fluorosulfonylbenzoylguanosine.	guanosine nucleotide	69-89	eukaryotic translation elongation factor 2	Homo sapiens	55-59
6722159-0	1984	Affinity labelling of the eukaryotic elongation factor EF-2 with the guanosine nucleotide analogue 5"-p-fluorosulfonylbenzoylguanosine.	5'-(4-fluorosulfonylbenzoyl)guanosine	99-134	eukaryotic translation elongation factor 2	Homo sapiens	55-59
6722159-1	1984	During the translocation of the nascent peptide chain from the ribosomal aminoacyl-site to the peptidyl-site, GTP is hydrolyzed by a mechanism dependent on both ribosomes and the elongation factor EF-2.	Guanosine Triphosphate	110-113	eukaryotic translation elongation factor 2	Homo sapiens	197-201
6722159-3	1984	Pre-incubation of EF-2 with FSO2BzGuo at increasing concentrations progressively inactivated the EF-2 and ribosome-dependent GTPase activity.	fso2bzguo	28-37	eukaryotic translation elongation factor 2	Homo sapiens	18-22
6722159-3	1984	Pre-incubation of EF-2 with FSO2BzGuo at increasing concentrations progressively inactivated the EF-2 and ribosome-dependent GTPase activity.	fso2bzguo	28-37	eukaryotic translation elongation factor 2	Homo sapiens	97-101
6722159-5	1984	Thus, one molecule of covalently bound FSO2BzGuo completely inactivated the GTPase activity of EF-2.	fso2bzguo	39-48	eukaryotic translation elongation factor 2	Homo sapiens	95-99
6722159-6	1984	Ribosomes or 60-S ribosomal subunits pre-incubated with FSO2BzGuo were not inactivated, consistent with the idea that the GTP hydrolysis involved in the ribosomal translocation takes place on EF-2.	Guanosine Triphosphate	122-125	eukaryotic translation elongation factor 2	Homo sapiens	192-196
6427766-8	1984	It was confirmed by using two-dimensional gel electrophoresis that PA toxin resistance in hybrid cells was caused by the presence of EF-2 resistant to ADP-ribosylation by fragment A of diphtheria toxin.	Protactinium	67-69	eukaryotic translation elongation factor 2	Homo sapiens	133-137
6427766-8	1984	It was confirmed by using two-dimensional gel electrophoresis that PA toxin resistance in hybrid cells was caused by the presence of EF-2 resistant to ADP-ribosylation by fragment A of diphtheria toxin.	Adenosine Diphosphate	151-154	eukaryotic translation elongation factor 2	Homo sapiens	133-137
6712255-1	1984	Diphtheria toxin inactivates protein synthesis elongation factor 2 by attaching ADP-ribose to an unusual post-translational amino acid derivative, diphthamide, in the factor.	diphthamide	147-158	eukaryotic translation elongation factor 2	Homo sapiens	47-66
6629822-0	1983	Hemoglobin Quin-Hai, beta 78 (EF2) Leu replaced by Arg, a new abnormal hemoglobin found in Guangdong, China.	Leucine	35-38	eukaryotic translation elongation factor 2	Homo sapiens	30-33
6629822-3	1983	Structural studies indicated a new variant beta 78 (EF2) Leu replaced by Arg.	Leucine	57-60	eukaryotic translation elongation factor 2	Homo sapiens	52-55
6629822-3	1983	Structural studies indicated a new variant beta 78 (EF2) Leu replaced by Arg.	Arginine	73-76	eukaryotic translation elongation factor 2	Homo sapiens	52-55
6927363-5	1982	The inhibitory action of bouvardin seems to be result of the selective blocking of peptidyl-tRNA translocation dependent on elongation factor EF-2 and GTP.	bouvardin	25-34	eukaryotic translation elongation factor 2	Homo sapiens	142-154
6267047-1	1981	Site and configuration of ADP-ribosylation of diphthamide in elongation factor 2.	Adenosine Diphosphate	26-29	eukaryotic translation elongation factor 2	Homo sapiens	61-80
6267047-1	1981	Site and configuration of ADP-ribosylation of diphthamide in elongation factor 2.	diphthamide	46-57	eukaryotic translation elongation factor 2	Homo sapiens	61-80
6267047-2	1981	Diphtheria toxin inactivates protein synthesis elongation factor 2 by catalyzing the ADP-ribosylation of a novel derivative of histidine, diphthamide, in the protein (Van Ness, B. G., Howard, J.	Adenosine Diphosphate	85-88	eukaryotic translation elongation factor 2	Homo sapiens	47-66
6267047-2	1981	Diphtheria toxin inactivates protein synthesis elongation factor 2 by catalyzing the ADP-ribosylation of a novel derivative of histidine, diphthamide, in the protein (Van Ness, B. G., Howard, J.	Histidine	127-136	eukaryotic translation elongation factor 2	Homo sapiens	47-66
6267047-2	1981	Diphtheria toxin inactivates protein synthesis elongation factor 2 by catalyzing the ADP-ribosylation of a novel derivative of histidine, diphthamide, in the protein (Van Ness, B. G., Howard, J.	diphthamide	138-149	eukaryotic translation elongation factor 2	Homo sapiens	47-66
7430147-2	1980	NMR spectral analysis of the novel amino acid, diphthamide, in elongation factor 2 which is ADP-ribosylated by diphtheria toxin suggests that it is 2-[3-carboxyamido-3-(trimethylammonio)propyl]histidine.	diphthamide	47-58	eukaryotic translation elongation factor 2	Homo sapiens	63-82
7439387-0	1980	Recognition of elongation factor 2 by diphtheria toxin is not solely defined by the presence of diphthamide.	diphthamide	96-107	eukaryotic translation elongation factor 2	Homo sapiens	15-34
7430147-2	1980	NMR spectral analysis of the novel amino acid, diphthamide, in elongation factor 2 which is ADP-ribosylated by diphtheria toxin suggests that it is 2-[3-carboxyamido-3-(trimethylammonio)propyl]histidine.	diphthamide	148-202	eukaryotic translation elongation factor 2	Homo sapiens	63-82
7430147-3	1980	Ribosyl-diphthamide was prepared by enzymatic hydrolysis of ADP-ribosyl-elongation factor 2 and three compounds were produced by its chemical hydrolysis (Van Ness, B. G., Howard, J.	ribosyl-diphthamide	0-19	eukaryotic translation elongation factor 2	Homo sapiens	72-91
6776409-6	1980	One clear-cut difference between prokaryotes and eukaryotes is the diphtheria toxin reaction, which catalyses the covalent binding of adenosine diphosphate-ribose (ADPR) to the eukaryotic peptide elongation factor EF2 in contrast to the homologous prokaryotic factor EF-G.	Adenosine Diphosphate	134-155	eukaryotic translation elongation factor 2	Homo sapiens	214-217
6776409-8	1980	In this respect, these factors have to be assigned to the EF2 type; we suppose that the ADP-ribosylatable structure arising so early in evolution is of fundamental importance for the elongation process.	Adenosine Diphosphate	88-91	eukaryotic translation elongation factor 2	Homo sapiens	58-61
188760-0	1977	Mechanism of action of Pseudomonas aeruginosa exotoxin Aiadenosine diphosphate-ribosylation of mammalian elongation factor 2 in vitro and in vivo.	aiadenosine diphosphate	55-78	eukaryotic translation elongation factor 2	Homo sapiens	105-124
221484-5	1979	All three species of Fragment A are active in catalyzing ADP ribosylation of elongation factor 2, an essential component of protein synthesis.	Adenosine Diphosphate	57-60	eukaryotic translation elongation factor 2	Homo sapiens	77-96
689031-1	1978	Conditions are described whereby the ADP-ribosylation (from NAD+) of reticulocyte elongation factor EF-2, catalyzed by diphtheria toxin, is essentially complete and whereby the reverse of this process may be carried out with recovery of 60--70% of the original EF-2 activity.	NAD	60-64	eukaryotic translation elongation factor 2	Homo sapiens	100-104
196649-0	1977	The mechanism of ADP-ribosylation of elongation factor 2 catalyzed by fragment A from diphtheria toxin.	Adenosine Diphosphate	17-20	eukaryotic translation elongation factor 2	Homo sapiens	37-56
196649-2	1977	The Michaelis constants for EF-2 and NAD are 0.15 and 1.4 muM, respectively.	NAD	37-40	eukaryotic translation elongation factor 2	Homo sapiens	28-32
196649-4	1977	Based on these and earlier results, we propose an ordered sequential mechanism for the reaction; the sequence of binding of substrates is NAD, followed by EF-2.	NAD	138-141	eukaryotic translation elongation factor 2	Homo sapiens	155-159
197953-0	1977	Structure and phosphorylation of an acidic protein from 60S ribosomes and its involvement in elongation factor-2 dependent GTP hydrolysis.	Guanosine Triphosphate	123-126	eukaryotic translation elongation factor 2	Homo sapiens	93-112
849463-2	1977	Fragment A loses its ability to inactivate ADP-ribosylation of the elongation factor 2, as a function of the number of residues modified.	Adenosine Diphosphate	43-46	eukaryotic translation elongation factor 2	Homo sapiens	67-86
849463-6	1977	Finally, results of nicotinamide-adenine dinucleotide-binding measurements suggest that tryptophan 153 would be concerned with the elongation factor 2 binding site or with the catalytic site itself.	NAD	20-53	eukaryotic translation elongation factor 2	Homo sapiens	131-150
849463-6	1977	Finally, results of nicotinamide-adenine dinucleotide-binding measurements suggest that tryptophan 153 would be concerned with the elongation factor 2 binding site or with the catalytic site itself.	Tryptophan	88-98	eukaryotic translation elongation factor 2	Homo sapiens	131-150
403520-6	1977	Preliminary results also indicate that the isolated A chain is about an order of magnitude more active in incorporating adenosine diphosphoribose into translocase (elongation factor 2) than whole or nicked toxin is under identical conditions.	Adenosine Diphosphate Ribose	120-145	eukaryotic translation elongation factor 2	Homo sapiens	164-183
188760-1	1977	Previous studies showed that Pseudomonas aeruginosa exotoxin A (PA toxin) catalyzes nicotinamide adenine dinucleotide (NAD)-dependent inhibition of protein synthesis in a rabbit reticulocyte lysate and transfer of radioactivity from [14C]adenine-labeled NAD to a protein having the same molecular weight as elongation factor 2 (EF-2) (B.H.	NAD	84-117	eukaryotic translation elongation factor 2	Homo sapiens	307-326
188760-1	1977	Previous studies showed that Pseudomonas aeruginosa exotoxin A (PA toxin) catalyzes nicotinamide adenine dinucleotide (NAD)-dependent inhibition of protein synthesis in a rabbit reticulocyte lysate and transfer of radioactivity from [14C]adenine-labeled NAD to a protein having the same molecular weight as elongation factor 2 (EF-2) (B.H.	NAD	119-122	eukaryotic translation elongation factor 2	Homo sapiens	307-326
1112784-0	1975	Interaction of guanosine nucleotides with elongation factor 2.	guanosine nucleotides	15-36	eukaryotic translation elongation factor 2	Homo sapiens	42-61
1009951-4	1976	On the other hand it was clearly shown that EF-2 attached at each translocation event and was then released before a new Phe-tRNA could be bound.	Phenylalanine	121-124	eukaryotic translation elongation factor 2	Homo sapiens	44-48
789367-1	1976	The binding of adenosine diphosphate-ribosylated elongation factor 2 (ADPRib-EF-2) to ribosomes was inhibited both in the presence and absence of GTP in proportion to the amounts of unmodified EF-2 added.	Guanosine Triphosphate	146-149	eukaryotic translation elongation factor 2	Homo sapiens	77-81
789367-2	1976	Concomitant with this inhibition, an increase in the activity of ribosome-bound EF-2 in polyphenylalanine synthesis was observed.	polyphenylalanine	88-105	eukaryotic translation elongation factor 2	Homo sapiens	80-84
789367-3	1976	On the other hand, the addition of ADPRib-EF-2 reduced the rate of poly(Phe) synthesis observed in the presence of a saturating amount of EF-2 and increased the amount of EF-2 required for the half-maximal rate of poly(Phe) synthesis.	poly(phe)	67-76	eukaryotic translation elongation factor 2	Homo sapiens	42-46
789367-3	1976	On the other hand, the addition of ADPRib-EF-2 reduced the rate of poly(Phe) synthesis observed in the presence of a saturating amount of EF-2 and increased the amount of EF-2 required for the half-maximal rate of poly(Phe) synthesis.	poly(phe)	67-76	eukaryotic translation elongation factor 2	Homo sapiens	138-142
789367-3	1976	On the other hand, the addition of ADPRib-EF-2 reduced the rate of poly(Phe) synthesis observed in the presence of a saturating amount of EF-2 and increased the amount of EF-2 required for the half-maximal rate of poly(Phe) synthesis.	poly(phe)	67-76	eukaryotic translation elongation factor 2	Homo sapiens	138-142
789367-3	1976	On the other hand, the addition of ADPRib-EF-2 reduced the rate of poly(Phe) synthesis observed in the presence of a saturating amount of EF-2 and increased the amount of EF-2 required for the half-maximal rate of poly(Phe) synthesis.	poly	67-71	eukaryotic translation elongation factor 2	Homo sapiens	42-46
789367-3	1976	On the other hand, the addition of ADPRib-EF-2 reduced the rate of poly(Phe) synthesis observed in the presence of a saturating amount of EF-2 and increased the amount of EF-2 required for the half-maximal rate of poly(Phe) synthesis.	poly	67-71	eukaryotic translation elongation factor 2	Homo sapiens	138-142
789367-3	1976	On the other hand, the addition of ADPRib-EF-2 reduced the rate of poly(Phe) synthesis observed in the presence of a saturating amount of EF-2 and increased the amount of EF-2 required for the half-maximal rate of poly(Phe) synthesis.	poly	67-71	eukaryotic translation elongation factor 2	Homo sapiens	138-142
789367-3	1976	On the other hand, the addition of ADPRib-EF-2 reduced the rate of poly(Phe) synthesis observed in the presence of a saturating amount of EF-2 and increased the amount of EF-2 required for the half-maximal rate of poly(Phe) synthesis.	Phenylalanine	72-76	eukaryotic translation elongation factor 2	Homo sapiens	42-46
789367-3	1976	On the other hand, the addition of ADPRib-EF-2 reduced the rate of poly(Phe) synthesis observed in the presence of a saturating amount of EF-2 and increased the amount of EF-2 required for the half-maximal rate of poly(Phe) synthesis.	Phenylalanine	72-76	eukaryotic translation elongation factor 2	Homo sapiens	138-142
789367-3	1976	On the other hand, the addition of ADPRib-EF-2 reduced the rate of poly(Phe) synthesis observed in the presence of a saturating amount of EF-2 and increased the amount of EF-2 required for the half-maximal rate of poly(Phe) synthesis.	Phenylalanine	72-76	eukaryotic translation elongation factor 2	Homo sapiens	138-142
789367-4	1976	Phe-tRNA, nonenzymatically bound to the ribosome in the presence of poly(U), inhibited the subsequent binding of ADPHRib-EF-2.	Phenylalanine	0-3	eukaryotic translation elongation factor 2	Homo sapiens	121-125
789367-4	1976	Phe-tRNA, nonenzymatically bound to the ribosome in the presence of poly(U), inhibited the subsequent binding of ADPHRib-EF-2.	Poly U	68-75	eukaryotic translation elongation factor 2	Homo sapiens	121-125
789367-6	1976	The Scatchard plot of the binding of ADPRib-EF-2 to the ribosome in the presence of GTP revealed the presence of two ribosomal binding sites (or ribosomal populations) with apparent different affinities for the modified factor (K371 degrees d,1 = 6.6 nM and K37 degrees d,2 = 126 nM).	Guanosine Triphosphate	84-87	eukaryotic translation elongation factor 2	Homo sapiens	44-48
789367-8	1976	The binding of ADPRib-EF-2 to the ribosome was stimulated by GTP.	Guanosine Triphosphate	61-64	eukaryotic translation elongation factor 2	Homo sapiens	22-26
789367-9	1976	The binding of radioactive GTP to the ribosome was observed concomitantly with the binding of ADPRib-EF-2.	Guanosine Triphosphate	27-30	eukaryotic translation elongation factor 2	Homo sapiens	101-105
789367-10	1976	One mole of GTP was bound per mole of ADPRib-EF-2.	Guanosine Triphosphate	12-15	eukaryotic translation elongation factor 2	Homo sapiens	45-49
789367-12	1976	The binding of ADPRib-EF-2 to the ribosome required the presence of Mg2+ and reached a maximum at 5 mM.	magnesium ion	68-72	eukaryotic translation elongation factor 2	Homo sapiens	22-26
974064-1	1976	The extent of the inhibitory effect of ricin in polyphenylalanine synthesis by eukaryotic ribosomes is strongly dependent upon the concentration of ribosomes and the elongation factors EF 1 and EF2.	polyphenylalanine	48-65	eukaryotic translation elongation factor 2	Homo sapiens	194-197
1112784-5	1975	However, by analyzing the incubation mixtures by thin layer chromatography the fraction of the total nucleotide binding to EF-2 which was due to GDP could be determined and corrected for.	Guanosine Diphosphate	145-148	eukaryotic translation elongation factor 2	Homo sapiens	123-127
1112784-6	1975	A GTP binding curve, corrected for GDP binding, and GTP hydrolysis extrapolated to one binding site with a dissociation constant of approximately 2 times 10--6 M. The nonhydrolyzable GTP analogue, theta, gamma-methylene-guanosine-5-triphosphate, also bound to EF-2 in a 1:1 ratio.	gamma-methylene-guanosine-5-triphosphate	204-244	eukaryotic translation elongation factor 2	Homo sapiens	260-264
1112784-7	1975	During the studies of GTP binding to EF-2 it was observed that the enzyme preparation contained a GTP-GDP transphosphorylase activity.	Guanosine Triphosphate	22-25	eukaryotic translation elongation factor 2	Homo sapiens	37-41
1112785-0	1975	Interaction of guanosine nucleotides with elongation factor 2.	guanosine nucleotides	15-36	eukaryotic translation elongation factor 2	Homo sapiens	42-61
1112785-3	1975	The effects of ribosomes and Mg-2plus on the binding of GDP and GTP to elongation factor 2 (EF-2) have been studied by an improved filter-binding assay.	Guanosine Diphosphate	56-59	eukaryotic translation elongation factor 2	Homo sapiens	71-90
1112785-3	1975	The effects of ribosomes and Mg-2plus on the binding of GDP and GTP to elongation factor 2 (EF-2) have been studied by an improved filter-binding assay.	Guanosine Diphosphate	56-59	eukaryotic translation elongation factor 2	Homo sapiens	92-96
1112785-3	1975	The effects of ribosomes and Mg-2plus on the binding of GDP and GTP to elongation factor 2 (EF-2) have been studied by an improved filter-binding assay.	Guanosine Triphosphate	64-67	eukaryotic translation elongation factor 2	Homo sapiens	71-90
1112785-3	1975	The effects of ribosomes and Mg-2plus on the binding of GDP and GTP to elongation factor 2 (EF-2) have been studied by an improved filter-binding assay.	Guanosine Triphosphate	64-67	eukaryotic translation elongation factor 2	Homo sapiens	92-96
1112785-5	1975	An apparent stimulation by ribosomes of GTP binding to EF-2 is time-dependent and parallels a concomitant increase of the GDP concentration in the incubation mixture.	Guanosine Triphosphate	40-43	eukaryotic translation elongation factor 2	Homo sapiens	55-59
1112785-5	1975	An apparent stimulation by ribosomes of GTP binding to EF-2 is time-dependent and parallels a concomitant increase of the GDP concentration in the incubation mixture.	Guanosine Diphosphate	122-125	eukaryotic translation elongation factor 2	Homo sapiens	55-59
1112785-7	1975	Further evidence of the role GDP may play as a modulator of protein synthesis might possibly be provided by studies of the GTP-GDP transphosphorylase activity which is present as an impurity in highly purified preparations of EF-2 as well as in ribosome preparations.	Guanosine Diphosphate	29-32	eukaryotic translation elongation factor 2	Homo sapiens	226-230
1112785-8	1975	It is demonstrated that relatively high concentrations of GDP in the presence of GTP completely block the ribosome-dependent GTPase activity of EF-2.	Guanosine Diphosphate	58-61	eukaryotic translation elongation factor 2	Homo sapiens	144-148
1112785-8	1975	It is demonstrated that relatively high concentrations of GDP in the presence of GTP completely block the ribosome-dependent GTPase activity of EF-2.	Guanosine Triphosphate	81-84	eukaryotic translation elongation factor 2	Homo sapiens	144-148
1112785-9	1975	Instead, the transphosphorylase enzyme(s) catalyzes an exchange reaction between GTP and GDP during which GDP remains bound to EF-2 and the relative concentrations of the two nucleotides do not change.	Guanosine Triphosphate	81-84	eukaryotic translation elongation factor 2	Homo sapiens	127-131
1112785-9	1975	Instead, the transphosphorylase enzyme(s) catalyzes an exchange reaction between GTP and GDP during which GDP remains bound to EF-2 and the relative concentrations of the two nucleotides do not change.	Guanosine Diphosphate	89-92	eukaryotic translation elongation factor 2	Homo sapiens	127-131
1112785-9	1975	Instead, the transphosphorylase enzyme(s) catalyzes an exchange reaction between GTP and GDP during which GDP remains bound to EF-2 and the relative concentrations of the two nucleotides do not change.	Guanosine Diphosphate	106-109	eukaryotic translation elongation factor 2	Homo sapiens	127-131
32430400-3	2020	Here, we show that exposure of three different human cancer cell lines to FLZ increases the phosphorylation of key translation factors, particularly of initiation factor 2 (eIF2) and elongation factor 2 (eEF2), modifications that inhibit their activities.	flz	74-77	eukaryotic translation elongation factor 2	Homo sapiens	183-202
1137991-0	1975	Proceedings: Elongation factor 2: amino acid sequence at the site of ADP-ribosylation.	Adenosine Diphosphate	69-72	eukaryotic translation elongation factor 2	Homo sapiens	13-32
4718780-0	1973	A novel reaction of reticulocyte peptide-chain elongation factor, EF2, with guanosine nucleotides.	guanosine nucleotides	76-97	eukaryotic translation elongation factor 2	Homo sapiens	66-69
4693484-0	1973	Competitive binding of EF1 and EF2 by mammalian ribosomes: role of GTP hydrolysis in overcoming inhibition by EF2 of aminoacyl-tRNA binding.	Guanosine Triphosphate	67-70	eukaryotic translation elongation factor 2	Homo sapiens	110-113
33057331-1	2020	Diphthamide is a unique post-translationally modified histidine residue (His715 in all mammals) found only in eukaryotic elongation factor-2 (eEF-2).	diphthamide	0-11	eukaryotic translation elongation factor 2	Homo sapiens	110-140
33057331-1	2020	Diphthamide is a unique post-translationally modified histidine residue (His715 in all mammals) found only in eukaryotic elongation factor-2 (eEF-2).	diphthamide	0-11	eukaryotic translation elongation factor 2	Homo sapiens	142-147
33057331-1	2020	Diphthamide is a unique post-translationally modified histidine residue (His715 in all mammals) found only in eukaryotic elongation factor-2 (eEF-2).	Histidine	54-63	eukaryotic translation elongation factor 2	Homo sapiens	110-140
33057331-1	2020	Diphthamide is a unique post-translationally modified histidine residue (His715 in all mammals) found only in eukaryotic elongation factor-2 (eEF-2).	Histidine	54-63	eukaryotic translation elongation factor 2	Homo sapiens	142-147
33057331-10	2020	Therefore, this work demonstrates that Dph1-7, along with the newly identified Miz1 transcription factor, are likely to represent the essential protein factors required for diphthamide modification on eEF2.	diphthamide	173-184	eukaryotic translation elongation factor 2	Homo sapiens	201-205
4341048-0	1972	The ribosomal subunit requirements for GTP hydrolysis by reticulocyte polypeptide elongation factors EF-1 and EF-2.	Guanosine Triphosphate	39-42	eukaryotic translation elongation factor 2	Homo sapiens	101-114
33909501-9	2021	MPS and the phosphorylation of Akt, p70S6K and eEF2 were increased in myotubes treated with young serum in response to leucine treatment, with a blunted response identified in cells treated with old serum (P < 0.05).	Leucine	119-126	eukaryotic translation elongation factor 2	Homo sapiens	47-51
33860211-0	2021	Target-Driven Design of a Coumarinyl Chalcone Scaffold Based Novel EF2 Kinase Inhibitor Suppresses Breast Cancer Growth In Vivo.	coumarinyl chalcone	26-45	eukaryotic translation elongation factor 2	Homo sapiens	67-70
33288716-2	2020	The ribosomal stalk is a multimeric ribosomal protein complex which plays an essential role in the recruitment of EF1A and EF2 to the ribosome and their GTP hydrolysis for efficient and accurate translation elongation.	Guanosine Triphosphate	153-156	eukaryotic translation elongation factor 2	Homo sapiens	123-126
32576952-6	2020	The gene products DPH1 and DPH2 are components of a heterodimeric enzyme complex that mediates the first step of the posttranslational diphthamide modification on the nonredundant eukaryotic translation elongation factor 2 (eEF2).	diphthamide	135-146	eukaryotic translation elongation factor 2	Homo sapiens	180-222
32576952-6	2020	The gene products DPH1 and DPH2 are components of a heterodimeric enzyme complex that mediates the first step of the posttranslational diphthamide modification on the nonredundant eukaryotic translation elongation factor 2 (eEF2).	diphthamide	135-146	eukaryotic translation elongation factor 2	Homo sapiens	224-228
32430400-9	2020	We show that FLZ induces cancer cell death and that this effect involves contributions from the phosphorylation of both eEF2 and eIF2.	flz	13-16	eukaryotic translation elongation factor 2	Homo sapiens	120-124
32430400-3	2020	Here, we show that exposure of three different human cancer cell lines to FLZ increases the phosphorylation of key translation factors, particularly of initiation factor 2 (eIF2) and elongation factor 2 (eEF2), modifications that inhibit their activities.	flz	74-77	eukaryotic translation elongation factor 2	Homo sapiens	204-208
32430400-7	2020	We also demonstrate that FLZ induces a swift and marked rise in intracellular Ca2+ levels, likely explaining the effects on eEF2.	flz	25-28	eukaryotic translation elongation factor 2	Homo sapiens	124-128
31827434-7	2019	Our data also suggest that STAT3 might play a role in ketamine"s antidepressant effects, mediated, at least in part, through eukaryotic elongation factor 2 (EEF2), resulting in the augmentation of brain-derived neurotropic factor (BDNF) expression and promoting the synthesis of synaptic proteins postsynaptic density protein 95 (PSD95) and synapsin I (SYN1).	Ketamine	54-62	eukaryotic translation elongation factor 2	Homo sapiens	125-155
32499677-0	2020	D1 Dopamine Receptor Activation Induces Neuronal eEF2 Pathway-Dependent Protein Synthesis.	Dopamine	3-11	eukaryotic translation elongation factor 2	Homo sapiens	49-53
32499677-3	2020	In order to examine the molecular pathways downstream of dopamine receptors, we used genetic, pharmacologic, biochemical, and imaging methods, and found that activation of dopamine receptor D1 but not D2 leads to rapid dephosphorylation of eEF2 at Thr56 but not eIF2alpha in cortical primary neuronal culture in a time-dependent manner.	Dopamine	57-65	eukaryotic translation elongation factor 2	Homo sapiens	240-244
32298235-5	2020	Decoding speeds depend on the relative abundance of each tRNA, the cognate:near-cognate tRNA ratios and the degree of tRNA modification, whereas eEF2-dependent ribosome translocation is negatively regulated by phosphorylation on threonine-56 by eEF2 kinase.	Threonine	229-238	eukaryotic translation elongation factor 2	Homo sapiens	145-149
32616215-0	2020	The role of eEF2 kinase in the rapid antidepressant actions of ketamine.	Ketamine	63-71	eukaryotic translation elongation factor 2	Homo sapiens	12-16
32616215-6	2020	Our studies show ketamine blocks synaptic NMDA receptors involved in spontaneous synaptic transmission, which deactivates calcium/calmodulin-dependent kinase eukaryotic elongation factor 2 kinase (eEF2K), resulting in dephosphorylation of eukaryotic elongation factor 2 (eEF2), and the subsequent desuppression of brain-derived neurotrophic factor (BDNF) protein synthesis in the hippocampus.	Ketamine	17-25	eukaryotic translation elongation factor 2	Homo sapiens	158-188
32616215-6	2020	Our studies show ketamine blocks synaptic NMDA receptors involved in spontaneous synaptic transmission, which deactivates calcium/calmodulin-dependent kinase eukaryotic elongation factor 2 kinase (eEF2K), resulting in dephosphorylation of eukaryotic elongation factor 2 (eEF2), and the subsequent desuppression of brain-derived neurotrophic factor (BDNF) protein synthesis in the hippocampus.	Ketamine	17-25	eukaryotic translation elongation factor 2	Homo sapiens	197-201
32616215-6	2020	Our studies show ketamine blocks synaptic NMDA receptors involved in spontaneous synaptic transmission, which deactivates calcium/calmodulin-dependent kinase eukaryotic elongation factor 2 kinase (eEF2K), resulting in dephosphorylation of eukaryotic elongation factor 2 (eEF2), and the subsequent desuppression of brain-derived neurotrophic factor (BDNF) protein synthesis in the hippocampus.	Calcium	122-129	eukaryotic translation elongation factor 2	Homo sapiens	158-188
32616215-6	2020	Our studies show ketamine blocks synaptic NMDA receptors involved in spontaneous synaptic transmission, which deactivates calcium/calmodulin-dependent kinase eukaryotic elongation factor 2 kinase (eEF2K), resulting in dephosphorylation of eukaryotic elongation factor 2 (eEF2), and the subsequent desuppression of brain-derived neurotrophic factor (BDNF) protein synthesis in the hippocampus.	Calcium	122-129	eukaryotic translation elongation factor 2	Homo sapiens	197-201
32042799-0	2019	eEF2 kinase mediated autophagy as a potential therapeutic target for paclitaxel-resistant triple-negative breast cancer.	Paclitaxel	69-79	eukaryotic translation elongation factor 2	Homo sapiens	0-4
31827434-7	2019	Our data also suggest that STAT3 might play a role in ketamine"s antidepressant effects, mediated, at least in part, through eukaryotic elongation factor 2 (EEF2), resulting in the augmentation of brain-derived neurotropic factor (BDNF) expression and promoting the synthesis of synaptic proteins postsynaptic density protein 95 (PSD95) and synapsin I (SYN1).	Ketamine	54-62	eukaryotic translation elongation factor 2	Homo sapiens	157-161
31488789-6	2019	Magnesium and ketamine have a common mechanism of action in the treatment of depression: an increase in GluN2B (NMDAR subunit) expression is related to the administration of both of the agents, as well as inhibition of phosphorylation of eEF2 (eukaryotic elongation factor 2) in cell culture and increase of the expression of BDNF in the hippocampus.	Magnesium	0-9	eukaryotic translation elongation factor 2	Homo sapiens	238-242
31463593-1	2019	Diphthamide, the target of diphtheria toxin, is a post-translationally modified histidine residue found in archaeal and eukaryotic translation elongation factor 2 (EF2).	diphthamide	0-11	eukaryotic translation elongation factor 2	Homo sapiens	120-162
31463593-1	2019	Diphthamide, the target of diphtheria toxin, is a post-translationally modified histidine residue found in archaeal and eukaryotic translation elongation factor 2 (EF2).	diphthamide	0-11	eukaryotic translation elongation factor 2	Homo sapiens	164-167
31463593-1	2019	Diphthamide, the target of diphtheria toxin, is a post-translationally modified histidine residue found in archaeal and eukaryotic translation elongation factor 2 (EF2).	Histidine	80-89	eukaryotic translation elongation factor 2	Homo sapiens	120-162
31463593-1	2019	Diphthamide, the target of diphtheria toxin, is a post-translationally modified histidine residue found in archaeal and eukaryotic translation elongation factor 2 (EF2).	Histidine	80-89	eukaryotic translation elongation factor 2	Homo sapiens	164-167
31463593-2	2019	In the first step of diphthamide biosynthesis, a [4Fe-4S] cluster-containing radical SAM enzyme, Dph1-Dph2 heterodimer in eukaryotes or Dph2 homodimer in archaea, cleaves S-adenosylmethionine and transfers the 3-amino-3-carboxypropyl group to EF2.	diphthamide	21-32	eukaryotic translation elongation factor 2	Homo sapiens	243-246
31463593-2	2019	In the first step of diphthamide biosynthesis, a [4Fe-4S] cluster-containing radical SAM enzyme, Dph1-Dph2 heterodimer in eukaryotes or Dph2 homodimer in archaea, cleaves S-adenosylmethionine and transfers the 3-amino-3-carboxypropyl group to EF2.	S-Adenosylmethionine	171-191	eukaryotic translation elongation factor 2	Homo sapiens	243-246
31558304-0	2019	miR-183-5p acts as a potential prognostic biomarker in gastric cancer and regulates cell functions by modulating EEF2.	mir-183-5p	0-10	eukaryotic translation elongation factor 2	Homo sapiens	113-117
31558304-14	2019	EEF2 may be a potential target gene regulated by miR-183-5p in GC.	mir-183-5p	49-59	eukaryotic translation elongation factor 2	Homo sapiens	0-4
31558304-15	2019	CONCLUSION: miR-183-5p acts as a potential prognostic biomarker in gastric cancer and regulates cell functions by modulating EEF2.	mir-183-5p	12-22	eukaryotic translation elongation factor 2	Homo sapiens	125-129
31488789-6	2019	Magnesium and ketamine have a common mechanism of action in the treatment of depression: an increase in GluN2B (NMDAR subunit) expression is related to the administration of both of the agents, as well as inhibition of phosphorylation of eEF2 (eukaryotic elongation factor 2) in cell culture and increase of the expression of BDNF in the hippocampus.	Magnesium	0-9	eukaryotic translation elongation factor 2	Homo sapiens	244-274
31488789-6	2019	Magnesium and ketamine have a common mechanism of action in the treatment of depression: an increase in GluN2B (NMDAR subunit) expression is related to the administration of both of the agents, as well as inhibition of phosphorylation of eEF2 (eukaryotic elongation factor 2) in cell culture and increase of the expression of BDNF in the hippocampus.	Ketamine	14-22	eukaryotic translation elongation factor 2	Homo sapiens	238-242
31488789-6	2019	Magnesium and ketamine have a common mechanism of action in the treatment of depression: an increase in GluN2B (NMDAR subunit) expression is related to the administration of both of the agents, as well as inhibition of phosphorylation of eEF2 (eukaryotic elongation factor 2) in cell culture and increase of the expression of BDNF in the hippocampus.	Ketamine	14-22	eukaryotic translation elongation factor 2	Homo sapiens	244-274
31222087-6	2019	DTA exerts its toxic activity through inhibition of eukaryotic translation elongation factor 2 (eEF2) via adenosine diphosphate (ADP)-ribosylation of a modified histidine residue, diphthamide, at His715, which blocks protein translation and leads to cell death.	diphtheria toxin fragment A	0-3	eukaryotic translation elongation factor 2	Homo sapiens	52-94
31227218-0	2019	Muscarinic acetylcholine receptors regulate the dephosphorylation of eukaryotic translation elongation factor 2 in SNU-407 colon cancer cells.	Acetylcholine	11-24	eukaryotic translation elongation factor 2	Homo sapiens	69-111
31227218-4	2019	When SNU-407 cells were treated with the cholinergic agonist carbachol, eEF2 phosphorylation at T56 was decreased in a dose- and time-dependent manner.	4-(1H-Pyrrol-1-yl)aniline	5-8	eukaryotic translation elongation factor 2	Homo sapiens	72-76
31227218-4	2019	When SNU-407 cells were treated with the cholinergic agonist carbachol, eEF2 phosphorylation at T56 was decreased in a dose- and time-dependent manner.	Carbachol	61-70	eukaryotic translation elongation factor 2	Homo sapiens	72-76
31227218-5	2019	The muscarinic antagonist atropine almost completely blocked this effect of carbachol, demonstrating that mAChRs specifically regulate eEF2 dephosphorylation.	Atropine	26-34	eukaryotic translation elongation factor 2	Homo sapiens	135-139
31227218-5	2019	The muscarinic antagonist atropine almost completely blocked this effect of carbachol, demonstrating that mAChRs specifically regulate eEF2 dephosphorylation.	Carbachol	76-85	eukaryotic translation elongation factor 2	Homo sapiens	135-139
31227218-7	2019	Treating cells with U0126, a potent MEK1/2 inhibitor, decreased carbachol-stimulated eEF2 dephosphorylation.	U 0126	20-25	eukaryotic translation elongation factor 2	Homo sapiens	85-89
31227218-7	2019	Treating cells with U0126, a potent MEK1/2 inhibitor, decreased carbachol-stimulated eEF2 dephosphorylation.	Carbachol	64-73	eukaryotic translation elongation factor 2	Homo sapiens	85-89
31227218-9	2019	We also found that the protein kinase C (PKC) inhibitor GF109203X substantially reduced eEF2 dephosphorylation.	bisindolylmaleimide I	56-65	eukaryotic translation elongation factor 2	Homo sapiens	88-92
31417118-7	2019	The study indicated that the sequential regulation of AMPK-mammalian target of rapamycin complex 1-eEF2 signaling was altered and protein synthesis ability was reduced in the cerebral cortex of hibernating chipmunks.	Sirolimus	79-88	eukaryotic translation elongation factor 2	Homo sapiens	99-103
31222087-6	2019	DTA exerts its toxic activity through inhibition of eukaryotic translation elongation factor 2 (eEF2) via adenosine diphosphate (ADP)-ribosylation of a modified histidine residue, diphthamide, at His715, which blocks protein translation and leads to cell death.	diphtheria toxin fragment A	0-3	eukaryotic translation elongation factor 2	Homo sapiens	96-100
31222087-6	2019	DTA exerts its toxic activity through inhibition of eukaryotic translation elongation factor 2 (eEF2) via adenosine diphosphate (ADP)-ribosylation of a modified histidine residue, diphthamide, at His715, which blocks protein translation and leads to cell death.	Adenosine	106-115	eukaryotic translation elongation factor 2	Homo sapiens	52-94
31222087-6	2019	DTA exerts its toxic activity through inhibition of eukaryotic translation elongation factor 2 (eEF2) via adenosine diphosphate (ADP)-ribosylation of a modified histidine residue, diphthamide, at His715, which blocks protein translation and leads to cell death.	Adenosine	106-115	eukaryotic translation elongation factor 2	Homo sapiens	96-100
31222087-6	2019	DTA exerts its toxic activity through inhibition of eukaryotic translation elongation factor 2 (eEF2) via adenosine diphosphate (ADP)-ribosylation of a modified histidine residue, diphthamide, at His715, which blocks protein translation and leads to cell death.	Adenosine Diphosphate	129-132	eukaryotic translation elongation factor 2	Homo sapiens	52-94
31222087-6	2019	DTA exerts its toxic activity through inhibition of eukaryotic translation elongation factor 2 (eEF2) via adenosine diphosphate (ADP)-ribosylation of a modified histidine residue, diphthamide, at His715, which blocks protein translation and leads to cell death.	Adenosine Diphosphate	129-132	eukaryotic translation elongation factor 2	Homo sapiens	96-100
31222087-6	2019	DTA exerts its toxic activity through inhibition of eukaryotic translation elongation factor 2 (eEF2) via adenosine diphosphate (ADP)-ribosylation of a modified histidine residue, diphthamide, at His715, which blocks protein translation and leads to cell death.	Histidine	161-170	eukaryotic translation elongation factor 2	Homo sapiens	52-94
31222087-6	2019	DTA exerts its toxic activity through inhibition of eukaryotic translation elongation factor 2 (eEF2) via adenosine diphosphate (ADP)-ribosylation of a modified histidine residue, diphthamide, at His715, which blocks protein translation and leads to cell death.	Histidine	161-170	eukaryotic translation elongation factor 2	Homo sapiens	96-100
31222087-6	2019	DTA exerts its toxic activity through inhibition of eukaryotic translation elongation factor 2 (eEF2) via adenosine diphosphate (ADP)-ribosylation of a modified histidine residue, diphthamide, at His715, which blocks protein translation and leads to cell death.	diphthamide	180-191	eukaryotic translation elongation factor 2	Homo sapiens	52-94
30312900-5	2019	Diphthamide-eEF2 occupies the aminoacyl-tRNA translocation site at which UGA either stalls translation or decodes selenocysteine.	diphthamide	0-11	eukaryotic translation elongation factor 2	Homo sapiens	12-16
30218597-0	2019	Interplay between reversible phosphorylation and irreversible ADP-ribosylation of eukaryotic translation elongation factor 2.	Adenosine Diphosphate	62-65	eukaryotic translation elongation factor 2	Homo sapiens	82-124
30312900-5	2019	Diphthamide-eEF2 occupies the aminoacyl-tRNA translocation site at which UGA either stalls translation or decodes selenocysteine.	Selenocysteine	114-128	eukaryotic translation elongation factor 2	Homo sapiens	12-16
30357593-5	2018	Once internalised, PE38 catalyses the ADP ribosylation of the diphthamide residue in elongation factor-2 (EF-2), resulting in the rapid fall in levels of the anti-apoptotic protein myeloid cell leukaemia 1 (Mcl-1), leading to apoptotic cell death.	Adenosine Diphosphate	38-41	eukaryotic translation elongation factor 2	Homo sapiens	106-110
30517857-3	2018	Here, we present three high-resolution structures of intermediates of translocation on the mammalian ribosome where, in contrast to bacteria, ribosomal complexes containing the translocase eEF2 and the complete tRNA2 mRNA module are trapped by the non-hydrolyzable GTP analog GMPPNP.	Guanosine Triphosphate	265-268	eukaryotic translation elongation factor 2	Homo sapiens	189-193
30517857-3	2018	Here, we present three high-resolution structures of intermediates of translocation on the mammalian ribosome where, in contrast to bacteria, ribosomal complexes containing the translocase eEF2 and the complete tRNA2 mRNA module are trapped by the non-hydrolyzable GTP analog GMPPNP.	Guanylyl Imidodiphosphate	276-282	eukaryotic translation elongation factor 2	Homo sapiens	189-193
30357593-5	2018	Once internalised, PE38 catalyses the ADP ribosylation of the diphthamide residue in elongation factor-2 (EF-2), resulting in the rapid fall in levels of the anti-apoptotic protein myeloid cell leukaemia 1 (Mcl-1), leading to apoptotic cell death.	Adenosine Diphosphate	38-41	eukaryotic translation elongation factor 2	Homo sapiens	85-104
30357593-5	2018	Once internalised, PE38 catalyses the ADP ribosylation of the diphthamide residue in elongation factor-2 (EF-2), resulting in the rapid fall in levels of the anti-apoptotic protein myeloid cell leukaemia 1 (Mcl-1), leading to apoptotic cell death.	diphthamide	62-73	eukaryotic translation elongation factor 2	Homo sapiens	85-104
30357593-5	2018	Once internalised, PE38 catalyses the ADP ribosylation of the diphthamide residue in elongation factor-2 (EF-2), resulting in the rapid fall in levels of the anti-apoptotic protein myeloid cell leukaemia 1 (Mcl-1), leading to apoptotic cell death.	diphthamide	62-73	eukaryotic translation elongation factor 2	Homo sapiens	106-110
28913610-3	2018	Immunohistochemical staining was used to verify eEF2 protein in a set of 97 formalin-fixed, paraffin-embedded primary PCa tissues.	Paraffin	92-100	eukaryotic translation elongation factor 2	Homo sapiens	48-52
30060827-1	2018	Eukaryotic elongation factors 2 (eEF2) plays an essential role in the GTP-dependent translocation of the ribosome along mRNA.	Guanosine Triphosphate	70-73	eukaryotic translation elongation factor 2	Homo sapiens	0-31
28913610-3	2018	Immunohistochemical staining was used to verify eEF2 protein in a set of 97 formalin-fixed, paraffin-embedded primary PCa tissues.	Formaldehyde	76-84	eukaryotic translation elongation factor 2	Homo sapiens	48-52
29800565-1	2018	Eukaryotic elongation factor 2 kinase (eEF-2K), the only known calmodulin (CaM)-activated alpha-kinase, phosphorylates eukaryotic elongation factor 2 (eEF-2) on a specific threonine (Thr-56) diminishing its affinity for the ribosome and reducing the rate of nascent chain elongation during translation.	Threonine	172-181	eukaryotic translation elongation factor 2	Homo sapiens	11-30
29800565-1	2018	Eukaryotic elongation factor 2 kinase (eEF-2K), the only known calmodulin (CaM)-activated alpha-kinase, phosphorylates eukaryotic elongation factor 2 (eEF-2) on a specific threonine (Thr-56) diminishing its affinity for the ribosome and reducing the rate of nascent chain elongation during translation.	Threonine	172-181	eukaryotic translation elongation factor 2	Homo sapiens	39-44
29800565-1	2018	Eukaryotic elongation factor 2 kinase (eEF-2K), the only known calmodulin (CaM)-activated alpha-kinase, phosphorylates eukaryotic elongation factor 2 (eEF-2) on a specific threonine (Thr-56) diminishing its affinity for the ribosome and reducing the rate of nascent chain elongation during translation.	Threonine	183-186	eukaryotic translation elongation factor 2	Homo sapiens	11-30
29800565-1	2018	Eukaryotic elongation factor 2 kinase (eEF-2K), the only known calmodulin (CaM)-activated alpha-kinase, phosphorylates eukaryotic elongation factor 2 (eEF-2) on a specific threonine (Thr-56) diminishing its affinity for the ribosome and reducing the rate of nascent chain elongation during translation.	Threonine	183-186	eukaryotic translation elongation factor 2	Homo sapiens	39-44
30060827-1	2018	Eukaryotic elongation factors 2 (eEF2) plays an essential role in the GTP-dependent translocation of the ribosome along mRNA.	Guanosine Triphosphate	70-73	eukaryotic translation elongation factor 2	Homo sapiens	33-37
29362492-1	2018	The diphthamide biosynthesis 1 (DPH1) gene encodes one of the essential components of the enzyme catalyzing the first step of diphthamide formation on eukaryotic elongation factor 2 (EEF2).	diphthamide	4-15	eukaryotic translation elongation factor 2	Homo sapiens	151-181
29453282-8	2018	The efficiency of this reaction depended on the concentrations of eEF2 and cognate tRNAs and increased in the presence of nonhydrolyzable GTP analogues.	Guanosine Triphosphate	138-141	eukaryotic translation elongation factor 2	Homo sapiens	66-70
29453282-9	2018	Of note, ADP-ribosylation of eEF2 domain IV blocked reverse translocation, suggesting a crucial role of interactions of this domain with the ribosome for the catalysis of the reaction.	Adenosine Diphosphate	9-12	eukaryotic translation elongation factor 2	Homo sapiens	29-33
29537287-4	2018	A second calcium ion then binds to the EF2 loop and, consequently, the structure of the protein changes from the semiopen to the open state.	Calcium	9-16	eukaryotic translation elongation factor 2	Homo sapiens	39-42
29362492-1	2018	The diphthamide biosynthesis 1 (DPH1) gene encodes one of the essential components of the enzyme catalyzing the first step of diphthamide formation on eukaryotic elongation factor 2 (EEF2).	diphthamide	4-15	eukaryotic translation elongation factor 2	Homo sapiens	183-187
29362492-1	2018	The diphthamide biosynthesis 1 (DPH1) gene encodes one of the essential components of the enzyme catalyzing the first step of diphthamide formation on eukaryotic elongation factor 2 (EEF2).	diphthamide	126-137	eukaryotic translation elongation factor 2	Homo sapiens	151-181
29362492-1	2018	The diphthamide biosynthesis 1 (DPH1) gene encodes one of the essential components of the enzyme catalyzing the first step of diphthamide formation on eukaryotic elongation factor 2 (EEF2).	diphthamide	126-137	eukaryotic translation elongation factor 2	Homo sapiens	183-187
29362492-2	2018	Diphthamide is the posttranslationally modified histidine residue on EEF2 that promotes protein chain elongation in the ribosome.	diphthamide	0-11	eukaryotic translation elongation factor 2	Homo sapiens	69-73
29362492-2	2018	Diphthamide is the posttranslationally modified histidine residue on EEF2 that promotes protein chain elongation in the ribosome.	Histidine	48-57	eukaryotic translation elongation factor 2	Homo sapiens	69-73
27689327-6	2016	We showed that a low CHO diet resulted in AMPK activation and mTOR inhibition leading to eukaryotic elongation factor 2 (eEF2) inhibition, blocking protein translation elongation.	CAV protocol	21-24	eukaryotic translation elongation factor 2	Homo sapiens	89-119
29590073-3	2018	In the presence of the substrate protein, elongation factor 2, this intermediate converts to an organic radical, formed by addition of the ACP radical to a histidine side chain.	acp radical	139-150	eukaryotic translation elongation factor 2	Homo sapiens	42-61
29590073-3	2018	In the presence of the substrate protein, elongation factor 2, this intermediate converts to an organic radical, formed by addition of the ACP radical to a histidine side chain.	Histidine	156-165	eukaryotic translation elongation factor 2	Homo sapiens	42-61
28245596-1	2017	The diphthamide on eukaryotic translation elongation factor 2 (eEF2) is the target of ADPribosylating toxins and -derivatives that serve as payloads in targeted tumor therapy.	diphthamide	4-15	eukaryotic translation elongation factor 2	Homo sapiens	19-61
28245596-1	2017	The diphthamide on eukaryotic translation elongation factor 2 (eEF2) is the target of ADPribosylating toxins and -derivatives that serve as payloads in targeted tumor therapy.	diphthamide	4-15	eukaryotic translation elongation factor 2	Homo sapiens	63-67
27510652-2	2016	Adenosine diphosphate (ADP)-ribosylation is a post-translational modification reaction that catalyzes the transfer of ADP-ribose group to eEF2 and this causes the inhibition of protein synthesis.	Adenosine Diphosphate	0-21	eukaryotic translation elongation factor 2	Homo sapiens	138-142
27510652-2	2016	Adenosine diphosphate (ADP)-ribosylation is a post-translational modification reaction that catalyzes the transfer of ADP-ribose group to eEF2 and this causes the inhibition of protein synthesis.	Adenosine Diphosphate	23-26	eukaryotic translation elongation factor 2	Homo sapiens	138-142
27510652-2	2016	Adenosine diphosphate (ADP)-ribosylation is a post-translational modification reaction that catalyzes the transfer of ADP-ribose group to eEF2 and this causes the inhibition of protein synthesis.	Adenosine Diphosphate	118-121	eukaryotic translation elongation factor 2	Homo sapiens	138-142
27510652-2	2016	Adenosine diphosphate (ADP)-ribosylation is a post-translational modification reaction that catalyzes the transfer of ADP-ribose group to eEF2 and this causes the inhibition of protein synthesis.	Ribose	122-128	eukaryotic translation elongation factor 2	Homo sapiens	138-142
30097101-1	2018	Diphthamide is a unique posttranslational modification on translation elongation factor 2 (EF2) in archaea and eukaryotes.	diphthamide	0-11	eukaryotic translation elongation factor 2	Homo sapiens	91-94
30097101-5	2018	Radical SAM enzymes in diphthamide biosynthesis cleave a different CS bond in SAM to generate a 3-amino-3-carboxypropyl radical and modify a histidine residue of substrate protein EF2.	diphthamide	23-34	eukaryotic translation elongation factor 2	Homo sapiens	180-183
30097101-5	2018	Radical SAM enzymes in diphthamide biosynthesis cleave a different CS bond in SAM to generate a 3-amino-3-carboxypropyl radical and modify a histidine residue of substrate protein EF2.	Cesium	67-69	eukaryotic translation elongation factor 2	Homo sapiens	180-183
30097101-5	2018	Radical SAM enzymes in diphthamide biosynthesis cleave a different CS bond in SAM to generate a 3-amino-3-carboxypropyl radical and modify a histidine residue of substrate protein EF2.	3-Amino-3-carboxypropyl radical	96-127	eukaryotic translation elongation factor 2	Homo sapiens	180-183
30097101-5	2018	Radical SAM enzymes in diphthamide biosynthesis cleave a different CS bond in SAM to generate a 3-amino-3-carboxypropyl radical and modify a histidine residue of substrate protein EF2.	Histidine	141-150	eukaryotic translation elongation factor 2	Homo sapiens	180-183
28938523-5	2017	Importantly, isoflurane and propofol anesthesia reduced fibroblast growth factor (FGF2) and activity-regulated cytoskeleton-associated protein (Arc) expressions, enhanced glial fibrillary acidic protein (GFAP), Iba1 and phosphorylated-Eukaryotic elongation factor 2 (eEF2) levels as well as down-regulated mitogen-activated protein kinases (MAPKs) family members, including p38, ERK1/2 and JNK, in the hippocampus of animals.	Isoflurane	13-23	eukaryotic translation elongation factor 2	Homo sapiens	220-265
28938523-5	2017	Importantly, isoflurane and propofol anesthesia reduced fibroblast growth factor (FGF2) and activity-regulated cytoskeleton-associated protein (Arc) expressions, enhanced glial fibrillary acidic protein (GFAP), Iba1 and phosphorylated-Eukaryotic elongation factor 2 (eEF2) levels as well as down-regulated mitogen-activated protein kinases (MAPKs) family members, including p38, ERK1/2 and JNK, in the hippocampus of animals.	Isoflurane	13-23	eukaryotic translation elongation factor 2	Homo sapiens	267-271
28938523-5	2017	Importantly, isoflurane and propofol anesthesia reduced fibroblast growth factor (FGF2) and activity-regulated cytoskeleton-associated protein (Arc) expressions, enhanced glial fibrillary acidic protein (GFAP), Iba1 and phosphorylated-Eukaryotic elongation factor 2 (eEF2) levels as well as down-regulated mitogen-activated protein kinases (MAPKs) family members, including p38, ERK1/2 and JNK, in the hippocampus of animals.	Propofol	28-36	eukaryotic translation elongation factor 2	Homo sapiens	220-265
28938523-5	2017	Importantly, isoflurane and propofol anesthesia reduced fibroblast growth factor (FGF2) and activity-regulated cytoskeleton-associated protein (Arc) expressions, enhanced glial fibrillary acidic protein (GFAP), Iba1 and phosphorylated-Eukaryotic elongation factor 2 (eEF2) levels as well as down-regulated mitogen-activated protein kinases (MAPKs) family members, including p38, ERK1/2 and JNK, in the hippocampus of animals.	Propofol	28-36	eukaryotic translation elongation factor 2	Homo sapiens	267-271
28502587-8	2017	RESULTS &amp; CONCLUSIONS: AMPK activation leads to increased eEF2 phosphorylation in MEFs mainly by direct activation of eEF2K and partly by inhibition of mammalian target of rapamycin complex 1 (mTORC1) signaling.	Adenosine Monophosphate	9-12	eukaryotic translation elongation factor 2	Homo sapiens	62-66
28060762-8	2017	Validation showed that total eEF2 and phosphorylated eEF2 at threonine 56 are prognostic markers for overall survival of HCC-patients.	Threonine	61-70	eukaryotic translation elongation factor 2	Homo sapiens	53-57
27689327-6	2016	We showed that a low CHO diet resulted in AMPK activation and mTOR inhibition leading to eukaryotic elongation factor 2 (eEF2) inhibition, blocking protein translation elongation.	CAV protocol	21-24	eukaryotic translation elongation factor 2	Homo sapiens	121-125
27571275-8	2016	Indeed, mutation of two conserved C-terminal tyrosines (Y712A/Y713A) in eEF-2K previously shown to abolish eEF-2 phosphorylation leads to the unfolding of eEF-2K627-725.	Tyrosine	45-54	eukaryotic translation elongation factor 2	Homo sapiens	72-77
27572820-3	2016	Here we show that inhibitors of the HIV aspartyl protease (HIV-PIs), nelfinavir in particular, trigger a robust activation of eEF2K leading to the phosphorylation of eEF2.	Nelfinavir	69-79	eukaryotic translation elongation factor 2	Homo sapiens	126-130
27572820-5	2016	We show that nelfinavir-resistant cells specifically evade eEF2 inhibition.	Nelfinavir	13-23	eukaryotic translation elongation factor 2	Homo sapiens	59-63
27428999-3	2016	Here, DTA ADP-ribosylates elongation factor 2 inhibits protein synthesis and leads to cell death.	deoxythymidylyl-3'-5'-deoxyadenylate	6-9	eukaryotic translation elongation factor 2	Homo sapiens	26-45
27159451-8	2016	The structure explains how diphthamide, a eukaryotic and archaeal specific post-translational modification of a histidine residue of eEF2, is involved in translocation.	Histidine	112-121	eukaryotic translation elongation factor 2	Homo sapiens	133-137
27159452-2	2016	Using electron cryo-microscopy of a single specimen, we present five ribosome structures formed with the Taura syndrome virus IRES and translocase eEF2 GTP bound with sordarin.	Guanosine Triphosphate	152-155	eukaryotic translation elongation factor 2	Homo sapiens	147-151
27159451-6	2016	Elongation factor eEF2 with a GTP analog stabilizes the ribosome-IRES complex in a rotated state with an extra ~3 degrees of rotation.	Guanosine Triphosphate	30-33	eukaryotic translation elongation factor 2	Homo sapiens	18-22
27159452-2	2016	Using electron cryo-microscopy of a single specimen, we present five ribosome structures formed with the Taura syndrome virus IRES and translocase eEF2 GTP bound with sordarin.	sordarin	167-175	eukaryotic translation elongation factor 2	Homo sapiens	147-151
27159451-8	2016	The structure explains how diphthamide, a eukaryotic and archaeal specific post-translational modification of a histidine residue of eEF2, is involved in translocation.	diphthamide	27-38	eukaryotic translation elongation factor 2	Homo sapiens	133-137
26939705-6	2016	In summary, H89 increased RIT activity by enhancing the two key events: ADP-ribosylation of eEF2 and reduction of MCL1 levels.	Adenosine Diphosphate	72-75	eukaryotic translation elongation factor 2	Homo sapiens	92-96
27060894-2	2016	Sordarin, a promising fungicidal agent, inhibits fungal protein synthesis by impairing elongation factor-2 (eEF2) function.	sordarin	0-8	eukaryotic translation elongation factor 2	Homo sapiens	87-106
27060894-2	2016	Sordarin, a promising fungicidal agent, inhibits fungal protein synthesis by impairing elongation factor-2 (eEF2) function.	sordarin	0-8	eukaryotic translation elongation factor 2	Homo sapiens	108-112
27060894-4	2016	The sordarin binding site on eEF2 as well as its mechanism of action is known.	sordarin	4-12	eukaryotic translation elongation factor 2	Homo sapiens	29-33
27060894-5	2016	In a previous study, we have detailed the interactions between sordarin and eEF2 cavities from different fungal species at the molecular level and predicted the probable cause of sordarin sensitivity.	sordarin	63-71	eukaryotic translation elongation factor 2	Homo sapiens	76-80
27060894-5	2016	In a previous study, we have detailed the interactions between sordarin and eEF2 cavities from different fungal species at the molecular level and predicted the probable cause of sordarin sensitivity.	sordarin	179-187	eukaryotic translation elongation factor 2	Homo sapiens	76-80
27060894-6	2016	Guided by our previous analysis, we aimed for computer-aided designing of sordarin derivatives as potential fungicidal agents that still remain ineffective against human eEF2.	sordarin	74-82	eukaryotic translation elongation factor 2	Homo sapiens	170-174
27060894-7	2016	We have performed structural knowledge-based designing of several sordarin derivatives and evaluated predicted interactions of those derivatives with the sordarin-binding cavities of different eEF2s, against which sordarin shows no inhibitory action.	sordarin	154-162	eukaryotic translation elongation factor 2	Homo sapiens	193-197
27060894-7	2016	We have performed structural knowledge-based designing of several sordarin derivatives and evaluated predicted interactions of those derivatives with the sordarin-binding cavities of different eEF2s, against which sordarin shows no inhibitory action.	sordarin	154-162	eukaryotic translation elongation factor 2	Homo sapiens	193-197
26584024-3	2015	We suspected that this was due to an intermolecular crystal contact between T80 and a surface glutamate (E153) that precluded coordination of a Ca(2+) ion in EF2.	Glutamic Acid	94-103	eukaryotic translation elongation factor 2	Homo sapiens	158-161
26703466-4	2016	An NMR-derived model of GCAP1(V77E) contains Mg(2+) bound at EF2 and looks similar to Ca(2+) saturated GCAP1 (root mean square deviations = 2.0 A).	magnesium ion	45-51	eukaryotic translation elongation factor 2	Homo sapiens	61-64
26889829-9	2016	The structural variation of EF2 is related to these differences in the structural fluctuation and the number of the hydrogen bonds (H-bonds).	Hydrogen	116-124	eukaryotic translation elongation factor 2	Homo sapiens	28-31
27073354-5	2016	Ketamine not only blocks the glutamate receptor, it activates eukaroyotic elongation factor 2 (eEF2).	Ketamine	0-8	eukaryotic translation elongation factor 2	Homo sapiens	62-93
27073354-5	2016	Ketamine not only blocks the glutamate receptor, it activates eukaroyotic elongation factor 2 (eEF2).	Ketamine	0-8	eukaryotic translation elongation factor 2	Homo sapiens	95-99
26861281-0	2016	Isolation of Flavonoids from Deguelia duckeana and Their Effect on Cellular Viability, AMPK, eEF2, eIF2 and eIF4E.	Flavonoids	13-23	eukaryotic translation elongation factor 2	Homo sapiens	93-97
26861281-7	2016	Furthermore, the flavonoids 2, 3, 4, 7, and 10 induced phosphorylation of the AMP-activated protein kinase (AMPK) and the eukaryotic elongation factor 2 (eEF2).	Flavonoids	17-27	eukaryotic translation elongation factor 2	Homo sapiens	122-152
26861281-7	2016	Furthermore, the flavonoids 2, 3, 4, 7, and 10 induced phosphorylation of the AMP-activated protein kinase (AMPK) and the eukaryotic elongation factor 2 (eEF2).	Flavonoids	17-27	eukaryotic translation elongation factor 2	Homo sapiens	154-158
26584024-3	2015	We suspected that this was due to an intermolecular crystal contact between T80 and a surface glutamate (E153) that precluded coordination of a Ca(2+) ion in EF2.	e153	105-109	eukaryotic translation elongation factor 2	Homo sapiens	158-161
26577048-5	2015	The X-ray structures of Sorcin in the apo (apoSor) and in calcium bound form (CaSor) reveal the structural basis of Sorcin action: calcium binding to the EF1-3 hands promotes a large conformational change, involving a movement of the long D-helix joining the EF1-EF2 sub-domain to EF3 and the opening of EF1.	Calcium	58-65	eukaryotic translation elongation factor 2	Homo sapiens	154-159
26577048-5	2015	The X-ray structures of Sorcin in the apo (apoSor) and in calcium bound form (CaSor) reveal the structural basis of Sorcin action: calcium binding to the EF1-3 hands promotes a large conformational change, involving a movement of the long D-helix joining the EF1-EF2 sub-domain to EF3 and the opening of EF1.	Calcium	131-138	eukaryotic translation elongation factor 2	Homo sapiens	154-159
25700642-11	2015	The major components in HLJDD, geniposide, berberine and baicalin, additively act on eEF2, and contributed to the responsible activity.	geniposide	31-41	eukaryotic translation elongation factor 2	Homo sapiens	85-89
26414509-10	2015	Our data show that bouvardin treatment blocked translation elongation on human ribosomes and suggest that it did so by blocking the dissociation of elongation factor 2 from the ribosome.	bouvardin	19-28	eukaryotic translation elongation factor 2	Homo sapiens	148-167
26101849-5	2015	In addition, a CpG site located in the 3"-untranslated region on the north shore of EEF2 (cg12255298) was hypermethylated in those who drank more frequently (P &lt; 0.05).	cg12255298	90-100	eukaryotic translation elongation factor 2	Homo sapiens	84-88
26101849-6	2015	Importantly, the association between several genetic variants within the mGluR-eEF2-AMPAR pathway and alcohol use behavior (i.e., consumption and alcohol-related problems) replicated in the Grady Trauma Project (GTP), an independent sample of adults living in Atlanta, Georgia (n = 1034; 95% African American), including individual variants in GRM1, GRM5, EEF2, MTOR, GRIA1, GRIA4 and HOMER2 (P &lt; 0.05).	Alcohols	102-109	eukaryotic translation elongation factor 2	Homo sapiens	79-83
26101849-6	2015	Importantly, the association between several genetic variants within the mGluR-eEF2-AMPAR pathway and alcohol use behavior (i.e., consumption and alcohol-related problems) replicated in the Grady Trauma Project (GTP), an independent sample of adults living in Atlanta, Georgia (n = 1034; 95% African American), including individual variants in GRM1, GRM5, EEF2, MTOR, GRIA1, GRIA4 and HOMER2 (P &lt; 0.05).	Alcohols	102-109	eukaryotic translation elongation factor 2	Homo sapiens	356-360
25912040-3	2015	EF1 differed from EF2 by containing sucrose.	Sucrose	36-43	eukaryotic translation elongation factor 2	Homo sapiens	18-21
26261303-1	2015	The diphthamide on human eukaryotic translation elongation factor 2 (eEF2) is the target of ADP ribosylating diphtheria toxin (DT) and Pseudomonas exotoxin A (PE).	diphthamide	4-15	eukaryotic translation elongation factor 2	Homo sapiens	25-67
26261303-1	2015	The diphthamide on human eukaryotic translation elongation factor 2 (eEF2) is the target of ADP ribosylating diphtheria toxin (DT) and Pseudomonas exotoxin A (PE).	diphthamide	4-15	eukaryotic translation elongation factor 2	Homo sapiens	69-73
26261303-4	2015	Cells with heterozygous gene inactivation still contained predominantly diphthamide-modified eEF2 and were as sensitive to PE and DT as parent cells.	diphthamide	72-83	eukaryotic translation elongation factor 2	Homo sapiens	93-97
26261303-7	2015	DPH1ko, DPH2ko, and DPH4ko harbored unmodified eEF2 and DPH5ko ACP- (diphthine-precursor) modified eEF2.	acp	63-66	eukaryotic translation elongation factor 2	Homo sapiens	99-103
26261303-7	2015	DPH1ko, DPH2ko, and DPH4ko harbored unmodified eEF2 and DPH5ko ACP- (diphthine-precursor) modified eEF2.	diphthine	69-78	eukaryotic translation elongation factor 2	Homo sapiens	99-103
26261303-8	2015	Loss of diphthamide prevented ADP ribosylation of eEF2, rendered cells resistant to PE and DT, but does not affect sensitivity toward other protein synthesis inhibitors, such as saporin or cycloheximide.	diphthamide	8-19	eukaryotic translation elongation factor 2	Homo sapiens	50-54
26261303-8	2015	Loss of diphthamide prevented ADP ribosylation of eEF2, rendered cells resistant to PE and DT, but does not affect sensitivity toward other protein synthesis inhibitors, such as saporin or cycloheximide.	Adenosine Diphosphate	30-33	eukaryotic translation elongation factor 2	Homo sapiens	50-54
26101849-6	2015	Importantly, the association between several genetic variants within the mGluR-eEF2-AMPAR pathway and alcohol use behavior (i.e., consumption and alcohol-related problems) replicated in the Grady Trauma Project (GTP), an independent sample of adults living in Atlanta, Georgia (n = 1034; 95% African American), including individual variants in GRM1, GRM5, EEF2, MTOR, GRIA1, GRIA4 and HOMER2 (P &lt; 0.05).	Alcohols	146-153	eukaryotic translation elongation factor 2	Homo sapiens	79-83
26101849-6	2015	Importantly, the association between several genetic variants within the mGluR-eEF2-AMPAR pathway and alcohol use behavior (i.e., consumption and alcohol-related problems) replicated in the Grady Trauma Project (GTP), an independent sample of adults living in Atlanta, Georgia (n = 1034; 95% African American), including individual variants in GRM1, GRM5, EEF2, MTOR, GRIA1, GRIA4 and HOMER2 (P &lt; 0.05).	Guanosine Triphosphate	212-215	eukaryotic translation elongation factor 2	Homo sapiens	79-83
26101849-6	2015	Importantly, the association between several genetic variants within the mGluR-eEF2-AMPAR pathway and alcohol use behavior (i.e., consumption and alcohol-related problems) replicated in the Grady Trauma Project (GTP), an independent sample of adults living in Atlanta, Georgia (n = 1034; 95% African American), including individual variants in GRM1, GRM5, EEF2, MTOR, GRIA1, GRIA4 and HOMER2 (P &lt; 0.05).	Guanosine Triphosphate	212-215	eukaryotic translation elongation factor 2	Homo sapiens	356-360
26101849-7	2015	Gene-based analyses conducted in the GTP indicated that GRM1 (empirical P &lt; 0.05) and EEF2 (empirical P &lt; 0.01) withstood multiple test corrections and predicted increased alcohol consumption and related problems.	Guanosine Triphosphate	37-40	eukaryotic translation elongation factor 2	Homo sapiens	89-93
26101849-7	2015	Gene-based analyses conducted in the GTP indicated that GRM1 (empirical P &lt; 0.05) and EEF2 (empirical P &lt; 0.01) withstood multiple test corrections and predicted increased alcohol consumption and related problems.	Alcohols	178-185	eukaryotic translation elongation factor 2	Homo sapiens	89-93
26101849-8	2015	In conclusion, insights from rodent studies enabled the identification of novel human alcohol candidate genes within the mGluR-eEF2-AMPAR pathway.	Alcohols	86-93	eukaryotic translation elongation factor 2	Homo sapiens	127-131
26085270-4	2015	DDD107498 was developed from a screening programme against blood-stage malaria parasites; its molecular target has been identified as translation elongation factor 2 (eEF2), which is responsible for the GTP-dependent translocation of the ribosome along messenger RNA, and is essential for protein synthesis.	Guanosine Triphosphate	203-206	eukaryotic translation elongation factor 2	Homo sapiens	167-171
25700642-11	2015	The major components in HLJDD, geniposide, berberine and baicalin, additively act on eEF2, and contributed to the responsible activity.	Berberine	43-52	eukaryotic translation elongation factor 2	Homo sapiens	85-89
25700642-11	2015	The major components in HLJDD, geniposide, berberine and baicalin, additively act on eEF2, and contributed to the responsible activity.	baicalin	57-65	eukaryotic translation elongation factor 2	Homo sapiens	85-89
25762683-4	2015	In this study, we demonstrate that eukaryotic elongation factor 2 (eEF2), which catalyzes the GTP-dependent translocation of the ribosome during protein synthesis, acts as a biochemical sensor that is tuned to the pattern of neuronal stimulation.	Guanosine Triphosphate	94-97	eukaryotic translation elongation factor 2	Homo sapiens	35-65
25762683-4	2015	In this study, we demonstrate that eukaryotic elongation factor 2 (eEF2), which catalyzes the GTP-dependent translocation of the ribosome during protein synthesis, acts as a biochemical sensor that is tuned to the pattern of neuronal stimulation.	Guanosine Triphosphate	94-97	eukaryotic translation elongation factor 2	Homo sapiens	67-71
25888318-9	2015	With the exchanged EF1 and EF2, the resulting chimeras noted as CaM(1TnC) and CaM(2TnC), displayed a two sequential binding mode with a one-order weaker binding affinity and lower DeltaH than that of CaM, while CaM(3TnC) and CaM(4TnC) had similar binding thermodynamics as CaM.	deltah	180-186	eukaryotic translation elongation factor 2	Homo sapiens	27-30
25248493-1	2015	Eukaryotic elongation factor 2 (eEF2) is a member of the GTP-binding translation elongation factor family that is essential for protein synthesis.	Guanosine Triphosphate	57-60	eukaryotic translation elongation factor 2	Homo sapiens	0-30
25248493-1	2015	Eukaryotic elongation factor 2 (eEF2) is a member of the GTP-binding translation elongation factor family that is essential for protein synthesis.	Guanosine Triphosphate	57-60	eukaryotic translation elongation factor 2	Homo sapiens	32-36
25231979-4	2014	The human FAM86A (family with sequence similarity 86) protein belongs to a recently identified family of protein MTases, and we here show that FAM86A catalyzes the trimethylation of eukaryotic elongation factor 2 (eEF2) on Lys-525.	Lysine	223-226	eukaryotic translation elongation factor 2	Homo sapiens	182-212
25565102-2	2015	This study reveals how dimerization and Fe(2+) binding are required for modification of both tRNA and EF2, thus suggesting a mechanism for regulation of translation elongation via two different pathways.	ammonium ferrous sulfate	40-46	eukaryotic translation elongation factor 2	Homo sapiens	102-105
25383520-8	2015	Importantly, treatment of established APC-deficient adenomas with rapamycin (which can target eEF2 through the mTORC1-S6K-eEF2K axis) causes tumour cells to undergo growth arrest and differentiation.	Sirolimus	66-75	eukaryotic translation elongation factor 2	Homo sapiens	94-98
25258313-5	2014	The N-lobe consists of EF1 and EF2 in a closed conformation with either Mg(2+) or Ca(2+) bound at EF1.	magnesium ion	72-78	eukaryotic translation elongation factor 2	Homo sapiens	31-34
25231979-4	2014	The human FAM86A (family with sequence similarity 86) protein belongs to a recently identified family of protein MTases, and we here show that FAM86A catalyzes the trimethylation of eukaryotic elongation factor 2 (eEF2) on Lys-525.	Lysine	223-226	eukaryotic translation elongation factor 2	Homo sapiens	214-218
25231979-5	2014	Moreover, we demonstrate that the Saccharomyces cerevisiae MTase Yjr129c, which displays sequence homology to FAM86A, is a functional FAM86A orthologue, modifying the corresponding residue (Lys-509) in yeast eEF2, both in vitro and in vivo.	Lysine	190-193	eukaryotic translation elongation factor 2	Homo sapiens	208-212
25231979-7	2014	In summary, the present study establishes the function of the previously uncharacterized MTases FAM86A and Yjr129c, demonstrating that these enzymes introduce a functionally important lysine methylation in eEF2.	Lysine	184-190	eukaryotic translation elongation factor 2	Homo sapiens	206-210
24422557-3	2014	The first step is the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-l-methionine (SAM) to the histidine residue of EF2, forming a C-C bond.	S-Adenosylmethionine	98-101	eukaryotic translation elongation factor 2	Homo sapiens	131-134
24363282-0	2014	Suppression of vascular endothelial growth factor via inactivation of eukaryotic elongation factor 2 by alkaloids in Coptidis rhizome in hepatocellular carcinoma.	Alkaloids	104-113	eukaryotic translation elongation factor 2	Homo sapiens	70-100
25064856-7	2014	Inhibition of the dimerization process through targeting a conserved leucine inside of this motif abolishes the capacity of RBPMS2 to interact with the translational elongation eEF2 protein, to upregulate NOGGIN mRNA in vivo and to drive SMC dedifferentiation.	Leucine	69-76	eukaryotic translation elongation factor 2	Homo sapiens	177-181
25012662-9	2014	In cells, Thr-348 autophosphorylation appears to control the catalytic output of active eEF-2K, contributing more than 5-fold to its ability to promote eEF-2 phosphorylation.	Threonine	10-13	eukaryotic translation elongation factor 2	Homo sapiens	88-93
25086354-3	2014	Mass spectrometric analysis of EF2 tryptic peptides localised this loss of methylation to lysine 509, in peptide LVEGLKR.	Peptides	43-51	eukaryotic translation elongation factor 2	Homo sapiens	31-34
25086354-3	2014	Mass spectrometric analysis of EF2 tryptic peptides localised this loss of methylation to lysine 509, in peptide LVEGLKR.	Lysine	90-96	eukaryotic translation elongation factor 2	Homo sapiens	31-34
25086354-4	2014	In vitro methylation, using recombinant methyltransferases and purified EF2, validated YJR129Cp as responsible for methylation of lysine 509 and Efm2p as responsible for methylation at lysine 613.	Lysine	130-136	eukaryotic translation elongation factor 2	Homo sapiens	72-75
25086354-4	2014	In vitro methylation, using recombinant methyltransferases and purified EF2, validated YJR129Cp as responsible for methylation of lysine 509 and Efm2p as responsible for methylation at lysine 613.	Lysine	185-191	eukaryotic translation elongation factor 2	Homo sapiens	72-75
24958351-12	2014	The alteration in eEF2 phosphorylation, PP2A activity and sensitivity to okadaic acid were also observed in a second HER2 positive cell line model of acquired lapatinib resistance, HCC1954-L.	Okadaic Acid	73-85	eukaryotic translation elongation factor 2	Homo sapiens	18-22
24958351-12	2014	The alteration in eEF2 phosphorylation, PP2A activity and sensitivity to okadaic acid were also observed in a second HER2 positive cell line model of acquired lapatinib resistance, HCC1954-L.	Lapatinib	159-168	eukaryotic translation elongation factor 2	Homo sapiens	18-22
24739148-1	2014	Present on archaeal and eukaryotic translation elongation factor 2, diphthamide represents one of the most intriguing post-translational modifications on proteins.	diphthamide	68-79	eukaryotic translation elongation factor 2	Homo sapiens	24-66
24422557-1	2014	Diphthamide, the target of diphtheria toxin, is a unique posttranslational modification on translation elongation factor 2 (EF2) in archaea and eukaryotes.	diphthamide	0-11	eukaryotic translation elongation factor 2	Homo sapiens	124-127
24422557-3	2014	The first step is the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-l-methionine (SAM) to the histidine residue of EF2, forming a C-C bond.	S-Adenosylmethionine	73-96	eukaryotic translation elongation factor 2	Homo sapiens	131-134
24422557-3	2014	The first step is the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-l-methionine (SAM) to the histidine residue of EF2, forming a C-C bond.	Histidine	110-119	eukaryotic translation elongation factor 2	Homo sapiens	131-134
24140707-0	2014	Elongation factor 2 diphthamide is critical for translation of two IRES-dependent protein targets, XIAP and FGF2, under oxidative stress conditions.	diphthamide	20-31	eukaryotic translation elongation factor 2	Homo sapiens	0-19
24140707-2	2014	A single histidine residue in eEF2 (H715) is modified to form diphthamide.	Histidine	9-18	eukaryotic translation elongation factor 2	Homo sapiens	30-34
24140707-2	2014	A single histidine residue in eEF2 (H715) is modified to form diphthamide.	diphthamide	62-73	eukaryotic translation elongation factor 2	Homo sapiens	30-34
24140707-6	2014	These results suggest that diphthamide may play a role in protection against the degradation of eEF2.	diphthamide	27-38	eukaryotic translation elongation factor 2	Homo sapiens	96-100
24140707-9	2014	Our findings therefore suggest that eEF2 diphthamide controls the selective translation of IRES-dependent protein targets XIAP and FGF2, critical for cell survival under conditions of oxidative stress.	diphthamide	41-52	eukaryotic translation elongation factor 2	Homo sapiens	36-40
24359813-13	2014	In addition, eEF2 phosphorylation was linearly decreased by Ile and Leu.	Isoleucine	60-63	eukaryotic translation elongation factor 2	Homo sapiens	13-17
24359813-13	2014	In addition, eEF2 phosphorylation was linearly decreased by Ile and Leu.	Leucine	68-71	eukaryotic translation elongation factor 2	Homo sapiens	13-17
24359813-14	2014	Threonine curvilinearly decreased eEF2 phosphorylation, Ile and Leu negatively interacted on eEF2, and Thr tended to inhibit Leu effects on eEF2.	Threonine	0-9	eukaryotic translation elongation factor 2	Homo sapiens	34-38
24359813-14	2014	Threonine curvilinearly decreased eEF2 phosphorylation, Ile and Leu negatively interacted on eEF2, and Thr tended to inhibit Leu effects on eEF2.	Threonine	0-3	eukaryotic translation elongation factor 2	Homo sapiens	34-38
24117378-5	2014	Using a chemical genomics approach, we identified Elongation Factor 2 as the molecular target of girolline, which inhibits protein synthesis at the elongation step.	girolline	97-106	eukaryotic translation elongation factor 2	Homo sapiens	50-69
23971743-1	2013	Eukaryotic and archaeal elongation factor 2 contains a unique post-translationally modified histidine residue, named diphthamide.	Histidine	92-101	eukaryotic translation elongation factor 2	Homo sapiens	24-43
24392693-4	2014	These clinical findings have been reverse-translated into preclinical models in an effort to elucidate ketamine"s antidepressant mechanism of action, and three important targets have been identified: mammalian target of rapamycin (mTOR), eukaryotic elongation factor 2 (eEF2), and glycogen synthase kinase-3 (GSK-3).	Ketamine	103-111	eukaryotic translation elongation factor 2	Homo sapiens	238-268
24392693-4	2014	These clinical findings have been reverse-translated into preclinical models in an effort to elucidate ketamine"s antidepressant mechanism of action, and three important targets have been identified: mammalian target of rapamycin (mTOR), eukaryotic elongation factor 2 (eEF2), and glycogen synthase kinase-3 (GSK-3).	Ketamine	103-111	eukaryotic translation elongation factor 2	Homo sapiens	270-274
24049063-4	2013	Our results revealed that carbimazole induces an inhibitory phosphorylation of eukaryotic elongation factor 2 (eEF2) that was associated with a marked inhibition of global protein synthesis.	Carbimazole	26-37	eukaryotic translation elongation factor 2	Homo sapiens	79-109
24049063-4	2013	Our results revealed that carbimazole induces an inhibitory phosphorylation of eukaryotic elongation factor 2 (eEF2) that was associated with a marked inhibition of global protein synthesis.	Carbimazole	26-37	eukaryotic translation elongation factor 2	Homo sapiens	111-115
23971743-1	2013	Eukaryotic and archaeal elongation factor 2 contains a unique post-translationally modified histidine residue, named diphthamide.	diphthamide	117-128	eukaryotic translation elongation factor 2	Homo sapiens	24-43
23486472-6	2013	Analysis of EF2 in the mutant cells revealed a novel form of diphthamide with an additional methyl group that prevented ADP-ribosylation and inactivation of EF2.	diphthamide	61-72	eukaryotic translation elongation factor 2	Homo sapiens	12-15
23861744-3	2013	Modeling of experimental data indicates that ADPR EF2 fully blocks the late-phase translocation of tRNAs; but the impairment in the translocation upstream process, mainly the GTP-dependent factor binding with the pretranslocation ribosome and/or the guanine nucleotide exchange in EF2, is responsible for the overall inhibition kinetics.	Guanosine Triphosphate	175-178	eukaryotic translation elongation factor 2	Homo sapiens	281-284
23861744-5	2013	Minimum association with the ribosome also keeps ADPR EF2 in an accessible state for toxins to catalyze the reverse reaction when nicotinamide becomes available.	Niacinamide	130-142	eukaryotic translation elongation factor 2	Homo sapiens	54-57
23337256-8	2013	In preclinical studies, the mammalian target of rapamycin (mTOR) in the medial prefrontal cortex and the eukaryotic elongation factor (eEF2) in the hippocampus have been proposed as critical mediators of ketamine"s rapid antidepressant actions.	Ketamine	204-212	eukaryotic translation elongation factor 2	Homo sapiens	135-139
23062356-7	2013	These findings also uncover eukaryotic elongation factor 2 kinase (eEF2K), a Ca2+/calmodulin dependent serine/threonine kinase that phosphorylates eEF2 and regulates the elongation step of protein translation, as a major molecular substrate mediating the rapid antidepressant effect of ketamine.	Ketamine	286-294	eukaryotic translation elongation factor 2	Homo sapiens	67-71
23062356-8	2013	Our results show that ketamine-mediated suppression of resting NMDA receptor activity leads to inhibition of eEF2 kinase and subsequent dephosphorylation of eEF2 and augmentation of BDNF synthesis.	Ketamine	22-30	eukaryotic translation elongation factor 2	Homo sapiens	109-113
23486472-6	2013	Analysis of EF2 in the mutant cells revealed a novel form of diphthamide with an additional methyl group that prevented ADP-ribosylation and inactivation of EF2.	diphthamide	61-72	eukaryotic translation elongation factor 2	Homo sapiens	157-160
23486472-6	2013	Analysis of EF2 in the mutant cells revealed a novel form of diphthamide with an additional methyl group that prevented ADP-ribosylation and inactivation of EF2.	Adenosine Diphosphate	120-123	eukaryotic translation elongation factor 2	Homo sapiens	12-15
23303710-3	2013	Here we show that myriaporone 3/4 stalls protein synthesis in the elongation phase by inducing phosphorylation of eukaryotic elongation factor 2.	myriaporone	18-29	eukaryotic translation elongation factor 2	Homo sapiens	125-144
23041477-0	2013	Carbon monoxide releasing molecule-2 CORM-2 represses global protein synthesis by inhibition of eukaryotic elongation factor eEF2.	Carbon Monoxide	0-15	eukaryotic translation elongation factor 2	Homo sapiens	125-129
23271118-9	2013	Diphteria toxin is the part which has the FA enzymatic activity corresponding the N-terminal section of the toxin, which inhibits the protein synthesis by ADP-ribosylating the elongation factor 2 in the presence of NAD.	NAD	215-218	eukaryotic translation elongation factor 2	Homo sapiens	176-195
23397219-2	2013	One such antibiotic sordarin selectively inhibits fungal translation by impairing the function of elongation factor 2 (eEF2) while being ineffective to higher eukaryotes.	sordarin	20-28	eukaryotic translation elongation factor 2	Homo sapiens	98-117
23397219-2	2013	One such antibiotic sordarin selectively inhibits fungal translation by impairing the function of elongation factor 2 (eEF2) while being ineffective to higher eukaryotes.	sordarin	20-28	eukaryotic translation elongation factor 2	Homo sapiens	119-123
23397219-4	2013	The binding cavity of sordarin on eEF2 has been localized by X-ray crystallographic study and its unique specificity towards sordarin has been attributed to the species specific substitutions within a stretch of amino acids (sordarin specificity region, SSR) at the entrance of the cavity.	sordarin	22-30	eukaryotic translation elongation factor 2	Homo sapiens	34-38
23397219-5	2013	In this study, we have analyzed the sordarin-binding cavity of eEF2 from different species both in isolated and ribosome-bound forms in order to decipher the mechanism of sordarin binding selectivity.	sordarin	36-44	eukaryotic translation elongation factor 2	Homo sapiens	63-67
23397219-5	2013	In this study, we have analyzed the sordarin-binding cavity of eEF2 from different species both in isolated and ribosome-bound forms in order to decipher the mechanism of sordarin binding selectivity.	sordarin	171-179	eukaryotic translation elongation factor 2	Homo sapiens	63-67
23184662-2	2013	One mechanism that inhibits elongation is phosphorylation of eukaryotic elongation factor 2 (eEF2) on threonine 56 (T56) by eEF2 kinase (eEF2K).	Threonine	102-111	eukaryotic translation elongation factor 2	Homo sapiens	61-91
23184662-2	2013	One mechanism that inhibits elongation is phosphorylation of eukaryotic elongation factor 2 (eEF2) on threonine 56 (T56) by eEF2 kinase (eEF2K).	Threonine	102-111	eukaryotic translation elongation factor 2	Homo sapiens	93-97
23184662-5	2013	We describe a new mode of eEF2 regulation and show that its phosphorylation by cyclin A-cyclin-dependent kinase 2 (CDK2) on a novel site, serine 595 (S595), directly regulates T56 phosphorylation by eEF2K.	Serine	138-144	eukaryotic translation elongation factor 2	Homo sapiens	26-30
23013770-6	2012	This enzyme catalyzes the last ATP-dependent step in the synthesis of diphthamide, a complex modification of Elongation Factor 2 that can be ADP-ribosylated by bacterial toxins.	Adenosine Triphosphate	31-34	eukaryotic translation elongation factor 2	Homo sapiens	109-128
23534055-6	2012	They focus on their recent work demonstrating that ketamine-mediated blockade of NMDA receptors at rest deactivates eukaryotic elongation factor 2 (eEF2) kinase, resulting in reduced eEF2 phosphorylation and desuppression of rapid dendritic protein translation, including BDNF (brain-derived neurotrophic factor), which then contributes to synaptic plasticity mechanisms that mediate longterm effects of the drug.	Ketamine	51-59	eukaryotic translation elongation factor 2	Homo sapiens	127-146
23534055-6	2012	They focus on their recent work demonstrating that ketamine-mediated blockade of NMDA receptors at rest deactivates eukaryotic elongation factor 2 (eEF2) kinase, resulting in reduced eEF2 phosphorylation and desuppression of rapid dendritic protein translation, including BDNF (brain-derived neurotrophic factor), which then contributes to synaptic plasticity mechanisms that mediate longterm effects of the drug.	Ketamine	51-59	eukaryotic translation elongation factor 2	Homo sapiens	148-152
23534055-6	2012	They focus on their recent work demonstrating that ketamine-mediated blockade of NMDA receptors at rest deactivates eukaryotic elongation factor 2 (eEF2) kinase, resulting in reduced eEF2 phosphorylation and desuppression of rapid dendritic protein translation, including BDNF (brain-derived neurotrophic factor), which then contributes to synaptic plasticity mechanisms that mediate longterm effects of the drug.	Ketamine	51-59	eukaryotic translation elongation factor 2	Homo sapiens	183-187
23013770-6	2012	This enzyme catalyzes the last ATP-dependent step in the synthesis of diphthamide, a complex modification of Elongation Factor 2 that can be ADP-ribosylated by bacterial toxins.	diphthamide	70-81	eukaryotic translation elongation factor 2	Homo sapiens	109-128
22329831-9	2012	Mutagenesis studies suggest that phosphorylation of Thr-348 is required for substrate (eEF-2 or a peptide substrate) phosphorylation, but not self-phosphorylation.	Threonine	52-55	eukaryotic translation elongation factor 2	Homo sapiens	87-92
22580036-8	2012	Daidzein, coumestrol and enterolactone induced an up-regulation of EF2 and FKPB4 proteins, while tamoxifen and resveratrol induced a down-regulation.	daidzein	0-8	eukaryotic translation elongation factor 2	Homo sapiens	67-70
22580036-8	2012	Daidzein, coumestrol and enterolactone induced an up-regulation of EF2 and FKPB4 proteins, while tamoxifen and resveratrol induced a down-regulation.	Coumestrol	10-20	eukaryotic translation elongation factor 2	Homo sapiens	67-70
22580036-8	2012	Daidzein, coumestrol and enterolactone induced an up-regulation of EF2 and FKPB4 proteins, while tamoxifen and resveratrol induced a down-regulation.	2,3-bis(3'-hydroxybenzyl)butyrolactone	25-38	eukaryotic translation elongation factor 2	Homo sapiens	67-70
22421144-10	2012	In other studies, metformin decreased the phosphorylation of 4E-BP1 at Ser65, Thr37/46 and Thr70 sites, but drastically increased the phosphorylation of EF2 at Thr56 and AMPK at Thr172, which results in global translational inhibition.	Metformin	18-27	eukaryotic translation elongation factor 2	Homo sapiens	153-156
22308030-2	2012	We have studied the post-transcriptional changes in the proteome of mammalian cells elicited by acute hypoxia and found that phosphorylation of eukaryotic elongation factor 2 (eEF2), a ribosomal translocase whose phosphorylation inhibits protein synthesis, is under the precise and reversible control of O(2) tension.	o(2)	304-308	eukaryotic translation elongation factor 2	Homo sapiens	144-174
22308030-2	2012	We have studied the post-transcriptional changes in the proteome of mammalian cells elicited by acute hypoxia and found that phosphorylation of eukaryotic elongation factor 2 (eEF2), a ribosomal translocase whose phosphorylation inhibits protein synthesis, is under the precise and reversible control of O(2) tension.	o(2)	304-308	eukaryotic translation elongation factor 2	Homo sapiens	176-180
22308030-3	2012	Upon exposure to hypoxia, phosphorylation of eEF2 at Thr(56) occurred rapidly (&lt;15 min) and resulted in modest translational arrest, a fundamental homeostatic response to hypoxia that spares ATP and thus facilitates cell survival.	Threonine	53-56	eukaryotic translation elongation factor 2	Homo sapiens	45-49
22669845-2	2012	eEF2K-mediated phosphorylation of eEF2 on threonine 56 (Thr56) decreases its affinity for the ribosome, thereby inhibiting elongation.	Threonine	42-51	eukaryotic translation elongation factor 2	Homo sapiens	0-4
22442136-12	2012	EtOH enhanced AMPK activity, resulting in increased TSC2 (S1387) and eEF2 phosphorylation, whereas Leu had the opposite effect.	Ethanol	0-4	eukaryotic translation elongation factor 2	Homo sapiens	69-73
21822730-9	2012	Moreover, eEF2 suppression of the eIF5A(K56A) mutant is correlated with the improvement of total protein synthesis and with the increased resistance to the protein synthesis inhibitor hygromycin B.	Hygromycin B	184-196	eukaryotic translation elongation factor 2	Homo sapiens	10-14
22204954-8	2012	eEF2 Thr(56) phosphorylation increased 25% during ischemia and 43% during reperfusion (P &lt; 0.05).	Threonine	5-8	eukaryotic translation elongation factor 2	Homo sapiens	0-4
22352903-8	2012	To test the possibility that NH125 is a potent inhibitor of eEF2 phosphorylation, we assessed its ability to inhibit the phosphorylation of eEF2.	NH 125	29-34	eukaryotic translation elongation factor 2	Homo sapiens	60-64
22352903-8	2012	To test the possibility that NH125 is a potent inhibitor of eEF2 phosphorylation, we assessed its ability to inhibit the phosphorylation of eEF2.	NH 125	29-34	eukaryotic translation elongation factor 2	Homo sapiens	140-144
22139586-1	2012	Diphtheria toxin (DT) and its N-terminal fragment A (FA) catalyse the transfer of the ADP-ribose moiety of nicotinamide adenine dinucleotide (NAD) into a covalent linkage with eukaryotic elongation factor 2 (eEF2).	Adenosine Diphosphate	86-89	eukaryotic translation elongation factor 2	Homo sapiens	176-206
22139586-1	2012	Diphtheria toxin (DT) and its N-terminal fragment A (FA) catalyse the transfer of the ADP-ribose moiety of nicotinamide adenine dinucleotide (NAD) into a covalent linkage with eukaryotic elongation factor 2 (eEF2).	Adenosine Diphosphate	86-89	eukaryotic translation elongation factor 2	Homo sapiens	208-212
22139586-1	2012	Diphtheria toxin (DT) and its N-terminal fragment A (FA) catalyse the transfer of the ADP-ribose moiety of nicotinamide adenine dinucleotide (NAD) into a covalent linkage with eukaryotic elongation factor 2 (eEF2).	Ribose	90-96	eukaryotic translation elongation factor 2	Homo sapiens	176-206
22139586-1	2012	Diphtheria toxin (DT) and its N-terminal fragment A (FA) catalyse the transfer of the ADP-ribose moiety of nicotinamide adenine dinucleotide (NAD) into a covalent linkage with eukaryotic elongation factor 2 (eEF2).	Ribose	90-96	eukaryotic translation elongation factor 2	Homo sapiens	208-212
22139586-1	2012	Diphtheria toxin (DT) and its N-terminal fragment A (FA) catalyse the transfer of the ADP-ribose moiety of nicotinamide adenine dinucleotide (NAD) into a covalent linkage with eukaryotic elongation factor 2 (eEF2).	NAD	107-140	eukaryotic translation elongation factor 2	Homo sapiens	176-206
22139586-1	2012	Diphtheria toxin (DT) and its N-terminal fragment A (FA) catalyse the transfer of the ADP-ribose moiety of nicotinamide adenine dinucleotide (NAD) into a covalent linkage with eukaryotic elongation factor 2 (eEF2).	NAD	107-140	eukaryotic translation elongation factor 2	Homo sapiens	208-212
22139586-1	2012	Diphtheria toxin (DT) and its N-terminal fragment A (FA) catalyse the transfer of the ADP-ribose moiety of nicotinamide adenine dinucleotide (NAD) into a covalent linkage with eukaryotic elongation factor 2 (eEF2).	NAD	142-145	eukaryotic translation elongation factor 2	Homo sapiens	176-206
22139586-1	2012	Diphtheria toxin (DT) and its N-terminal fragment A (FA) catalyse the transfer of the ADP-ribose moiety of nicotinamide adenine dinucleotide (NAD) into a covalent linkage with eukaryotic elongation factor 2 (eEF2).	NAD	142-145	eukaryotic translation elongation factor 2	Homo sapiens	208-212
22308030-3	2012	Upon exposure to hypoxia, phosphorylation of eEF2 at Thr(56) occurred rapidly (&lt;15 min) and resulted in modest translational arrest, a fundamental homeostatic response to hypoxia that spares ATP and thus facilitates cell survival.	Adenosine Triphosphate	194-197	eukaryotic translation elongation factor 2	Homo sapiens	45-49
22308030-5	2012	Furthermore, eEF2 phosphorylation was mimicked by prolyl hydroxylase (PHD) inhibition with dimethyloxalylglycine or by selective PHD2 siRNA silencing but was independent of hypoxia-inducible factor alpha stabilization.	oxalylglycine	91-112	eukaryotic translation elongation factor 2	Homo sapiens	13-17
22157746-4	2012	Here, we demonstrate that the RNA-binding protein, cytoplasmic polyadenylation element binding protein (CPEB)2, interacts with the elongation factor, eEF2, to reduce eEF2/ribosome-triggered GTP hydrolysis in vitro and slow down peptide elongation of CPEB2-bound RNA in vivo.	Guanosine Triphosphate	190-193	eukaryotic translation elongation factor 2	Homo sapiens	150-154
22157746-4	2012	Here, we demonstrate that the RNA-binding protein, cytoplasmic polyadenylation element binding protein (CPEB)2, interacts with the elongation factor, eEF2, to reduce eEF2/ribosome-triggered GTP hydrolysis in vitro and slow down peptide elongation of CPEB2-bound RNA in vivo.	Guanosine Triphosphate	190-193	eukaryotic translation elongation factor 2	Homo sapiens	166-170
22158625-5	2012	High glucose stimulated mTORC1 to promote key events in the initiation and elongation phases of mRNA translation: binding of eIF4A to eIF4G, reduction in PDCD4 expression and inhibition of its binding to eIF4A, eEF2 kinase phosphorylation, and dephosphorylation of eEF2; these events were inhibited by NaHS.	Glucose	5-12	eukaryotic translation elongation factor 2	Homo sapiens	211-215
22158625-5	2012	High glucose stimulated mTORC1 to promote key events in the initiation and elongation phases of mRNA translation: binding of eIF4A to eIF4G, reduction in PDCD4 expression and inhibition of its binding to eIF4A, eEF2 kinase phosphorylation, and dephosphorylation of eEF2; these events were inhibited by NaHS.	Glucose	5-12	eukaryotic translation elongation factor 2	Homo sapiens	265-269
22158625-5	2012	High glucose stimulated mTORC1 to promote key events in the initiation and elongation phases of mRNA translation: binding of eIF4A to eIF4G, reduction in PDCD4 expression and inhibition of its binding to eIF4A, eEF2 kinase phosphorylation, and dephosphorylation of eEF2; these events were inhibited by NaHS.	sodium bisulfide	302-306	eukaryotic translation elongation factor 2	Homo sapiens	211-215
21875114-7	2011	Further investigation indicated that mitochondrial respiration inhibitors such as 1 and rotenone induced the rapid hyperphosphorylation and inhibition of translation initiation factor eIF2alpha and elongation factor eEF2.	Rotenone	88-96	eukaryotic translation elongation factor 2	Homo sapiens	216-220
22020937-0	2011	1-Benzyl-3-cetyl-2-methylimidazolium iodide (NH125) induces phosphorylation of eukaryotic elongation factor-2 (eEF2): a cautionary note on the anticancer mechanism of an eEF2 kinase inhibitor.	NH 125	0-43	eukaryotic translation elongation factor 2	Homo sapiens	111-115
22020937-0	2011	1-Benzyl-3-cetyl-2-methylimidazolium iodide (NH125) induces phosphorylation of eukaryotic elongation factor-2 (eEF2): a cautionary note on the anticancer mechanism of an eEF2 kinase inhibitor.	NH 125	0-43	eukaryotic translation elongation factor 2	Homo sapiens	170-174
22020937-0	2011	1-Benzyl-3-cetyl-2-methylimidazolium iodide (NH125) induces phosphorylation of eukaryotic elongation factor-2 (eEF2): a cautionary note on the anticancer mechanism of an eEF2 kinase inhibitor.	NH 125	45-50	eukaryotic translation elongation factor 2	Homo sapiens	111-115
22020937-0	2011	1-Benzyl-3-cetyl-2-methylimidazolium iodide (NH125) induces phosphorylation of eukaryotic elongation factor-2 (eEF2): a cautionary note on the anticancer mechanism of an eEF2 kinase inhibitor.	NH 125	45-50	eukaryotic translation elongation factor 2	Homo sapiens	170-174
22020937-14	2011	We also explored signal transduction pathways leading to NH125-induced eEF2 phosphorylation.	NH 125	57-62	eukaryotic translation elongation factor 2	Homo sapiens	71-75
21945617-1	2011	Elongation factor-2 kinase (eEF-2 kinase, also known as calmodulin-dependent protein kinase III), is a unique calcium/calmodulin-dependent enzyme that inhibits protein synthesis by phosphorylating and inactivating elongation factor-2 (eEF-2).	Calcium	110-117	eukaryotic translation elongation factor 2	Homo sapiens	214-233
21945617-1	2011	Elongation factor-2 kinase (eEF-2 kinase, also known as calmodulin-dependent protein kinase III), is a unique calcium/calmodulin-dependent enzyme that inhibits protein synthesis by phosphorylating and inactivating elongation factor-2 (eEF-2).	Calcium	110-117	eukaryotic translation elongation factor 2	Homo sapiens	28-33
22911754-6	2012	This targeting resulted in a substantial decrease in eEF2 phosphorylation in the tumors, and led to the inhibition of tumor growth, the induction of apoptosis and the sensitization of tumors to the chemotherapy agent doxorubicin.	Doxorubicin	217-228	eukaryotic translation elongation factor 2	Homo sapiens	53-57
22121028-3	2012	For 10-200 kDa cellular proteins, the Bis-Tris-HCl system showed a higher resolving power in a 2-D fluorescence DIGE analysis of certain phosphoproteins, e.g. histone H3 (15 kDa) and elongation factor 2 (95 kDa).	bis-tris-hcl	38-50	eukaryotic translation elongation factor 2	Homo sapiens	183-202
21554491-8	2011	In an in vitro study, silencing of eEF2 expression increased mitochondrial elongation, cellular autophagy and cisplatin sensitivity.	Cisplatin	110-119	eukaryotic translation elongation factor 2	Homo sapiens	35-39
21746787-15	2011	These data indicate that the increase in myofibrillar MPS for C+P could, potentially, be mediated through p70S6K, downstream of mTOR, which in turn may suppress the rise in eEF2 on translation elongation.	Carbon	62-63	eukaryotic translation elongation factor 2	Homo sapiens	173-177
21426346-3	2011	Our lab has previously shown that treatment with the facilitating neurotransmitter, 5-hydroxytryptamine (5-HT), causes a target of rapamycin complex 1-mediated decrease in phosphorylation of eukaryotic elongation factor 2 (eEF2) within the neurites of sensory neurons involved in LTF.	Serotonin	84-103	eukaryotic translation elongation factor 2	Homo sapiens	191-221
21132439-6	2011	Compared with pretest, in the posttest basal eukaryotic elongation factor 2 (eEF2) phosphorylation was elevated in CHO (P &lt; 0.05), but not in F. In the pretest, exercise increased the degree of eEF2 phosphorylation about twofold (P &lt; 0.05), and values returned to baseline within the 4 h recovery period in each group.	CAV protocol	115-118	eukaryotic translation elongation factor 2	Homo sapiens	45-75
21132439-6	2011	Compared with pretest, in the posttest basal eukaryotic elongation factor 2 (eEF2) phosphorylation was elevated in CHO (P &lt; 0.05), but not in F. In the pretest, exercise increased the degree of eEF2 phosphorylation about twofold (P &lt; 0.05), and values returned to baseline within the 4 h recovery period in each group.	CAV protocol	115-118	eukaryotic translation elongation factor 2	Homo sapiens	77-81
21132439-7	2011	However, in the posttest dephosphorylation of eEF2 was negated after recovery in CHO, but not in F. Independent of the dietary condition training enhanced the basal phosphorylation status of Phospholamban at Thr(17), 5"-AMP-activated protein kinase alpha (AMPKalpha), and Acetyl CoA carboxylase beta (ACCbeta), and abolished the exercise-induced increase of AMPKalpha and ACCbeta (P &lt; 0.05).	CAV protocol	81-84	eukaryotic translation elongation factor 2	Homo sapiens	46-50
21132439-8	2011	In conclusion, training in the fasted state, compared with identical training with ample carbohydrate intake, facilitates post-exercise dephosphorylation of eEF2.	Carbohydrates	89-101	eukaryotic translation elongation factor 2	Homo sapiens	157-161
21677641-6	2011	We find that the ketamine-mediated blockade of NMDAR at rest deactivates eukaryotic elongation factor 2 (eEF2) kinase (also called CaMKIII), resulting in reduced eEF2 phosphorylation and de-suppression of translation of brain-derived neurotrophic factor.	Ketamine	17-25	eukaryotic translation elongation factor 2	Homo sapiens	84-103
21677641-6	2011	We find that the ketamine-mediated blockade of NMDAR at rest deactivates eukaryotic elongation factor 2 (eEF2) kinase (also called CaMKIII), resulting in reduced eEF2 phosphorylation and de-suppression of translation of brain-derived neurotrophic factor.	Ketamine	17-25	eukaryotic translation elongation factor 2	Homo sapiens	105-109
21677641-6	2011	We find that the ketamine-mediated blockade of NMDAR at rest deactivates eukaryotic elongation factor 2 (eEF2) kinase (also called CaMKIII), resulting in reduced eEF2 phosphorylation and de-suppression of translation of brain-derived neurotrophic factor.	Ketamine	17-25	eukaryotic translation elongation factor 2	Homo sapiens	162-166
21426346-3	2011	Our lab has previously shown that treatment with the facilitating neurotransmitter, 5-hydroxytryptamine (5-HT), causes a target of rapamycin complex 1-mediated decrease in phosphorylation of eukaryotic elongation factor 2 (eEF2) within the neurites of sensory neurons involved in LTF.	Serotonin	84-103	eukaryotic translation elongation factor 2	Homo sapiens	223-227
21426346-5	2011	We show that the Aplysia eEF2K orthologue contains an S6 kinase phosphorylation site and that a serine-to-alanine mutation at this site blocks the ability of 5-HT to decrease eEF2 phosphorylation in neurites.	Alanine	106-113	eukaryotic translation elongation factor 2	Homo sapiens	25-29
20708687-0	2010	Identification of eukaryotic elongation factor-2 as a novel cellular target of lithium and glycogen synthase kinase-3.	Lithium	79-86	eukaryotic translation elongation factor 2	Homo sapiens	18-48
21307130-4	2011	Suppression of MK-2206-induced autophagy by eEF-2 silencing was accompanied by a promotion of apoptotic cell death.	MK 2206	15-22	eukaryotic translation elongation factor 2	Homo sapiens	44-49
21112387-5	2011	Here, we show that under conditions where cell growth is limited by Mg(2+) availability, TRPM7 via its kinase mediates enhanced Thr56 phosphorylation of eEF2.	magnesium ion	68-74	eukaryotic translation elongation factor 2	Homo sapiens	153-157
20708687-3	2010	Proteomic analysis identified eukaryotic elongation factor-2 (eEF-2) as a cellular target of lithium.	Lithium	93-100	eukaryotic translation elongation factor 2	Homo sapiens	30-60
20708687-3	2010	Proteomic analysis identified eukaryotic elongation factor-2 (eEF-2) as a cellular target of lithium.	Lithium	93-100	eukaryotic translation elongation factor 2	Homo sapiens	62-67
20708687-5	2010	In cells, lithium decreased eEF-2 phosphorylation at its key inhibitory site, threonine 56, and blocked the enhancement of eEF-2 phosphorylation normally coupled with stress conditions such as nutrient and serum deprivation.	Lithium	10-17	eukaryotic translation elongation factor 2	Homo sapiens	28-33
20708687-5	2010	In cells, lithium decreased eEF-2 phosphorylation at its key inhibitory site, threonine 56, and blocked the enhancement of eEF-2 phosphorylation normally coupled with stress conditions such as nutrient and serum deprivation.	Lithium	10-17	eukaryotic translation elongation factor 2	Homo sapiens	123-128
20708687-5	2010	In cells, lithium decreased eEF-2 phosphorylation at its key inhibitory site, threonine 56, and blocked the enhancement of eEF-2 phosphorylation normally coupled with stress conditions such as nutrient and serum deprivation.	Threonine	78-87	eukaryotic translation elongation factor 2	Homo sapiens	28-33
20708687-8	2010	In summary, unexpectedly eEF-2 is activated by both lithium and GSK-3, whereas, lithium treatment and inhibition of GSK-3 have opposing effects on eEF-2.	Lithium	52-59	eukaryotic translation elongation factor 2	Homo sapiens	25-30
20708687-8	2010	In summary, unexpectedly eEF-2 is activated by both lithium and GSK-3, whereas, lithium treatment and inhibition of GSK-3 have opposing effects on eEF-2.	Lithium	80-87	eukaryotic translation elongation factor 2	Homo sapiens	147-152
20410930-8	2010	In addition, we constructed a DT-A-resistant human cell line by introducing a human elongation factor 2 mutant into HEK293T cells.	diphtheria toxin fragment A	30-34	eukaryotic translation elongation factor 2	Homo sapiens	84-103
20817065-6	2010	Indeed, after a 15 min exposure to glutamate a transient increase in elongation factor 2 phosphorylation has been reported, an effect mediated through the activation of the elongation factor 2 kinase.	Glutamic Acid	35-44	eukaryotic translation elongation factor 2	Homo sapiens	69-88
19702335-6	2009	The upregulation of Seryl-aminoacyl-tRNA-synthetase and Eef2 was sensitive to the mTOR inhibitor rapamycin, as determined by Western blot.	Sirolimus	97-106	eukaryotic translation elongation factor 2	Homo sapiens	56-60
19765649-6	2010	Resveratrol inhibited high glucose-induced changes in association of eIF4E with eIF4G, phosphorylation of eIF4E, eEF2, eEF2 kinase and, p70S6 kinase, indicating that it affects important events in both initiation and elongation phases of mRNA translation.	Resveratrol	0-11	eukaryotic translation elongation factor 2	Homo sapiens	113-117
19472338-7	2009	The complex of GFPN-EF1 and EF2-GFPC was purified from cells using metal-ion chelate chromatography and the temperature dependence of GFP fluorescence was found to be calcium dependent.	Metals	67-72	eukaryotic translation elongation factor 2	Homo sapiens	28-36
19625063-10	2009	However, chemotherapy mediated TRAIL sensitization was mimicked by low concentrations of H(2)O(2), which resulted in the phosphorylation of translation EF2 and decreased the expression of several short half-life, anti-apoptotic proteins, including FLIP(S), XIAP and survivin.	Hydrogen Peroxide	89-97	eukaryotic translation elongation factor 2	Homo sapiens	152-155
19406104-5	2009	Inhibition of mTOR by rapamycin notably increased the level of phosphorylated eEF2 in infected cells.	Sirolimus	22-31	eukaryotic translation elongation factor 2	Homo sapiens	78-82
19472338-7	2009	The complex of GFPN-EF1 and EF2-GFPC was purified from cells using metal-ion chelate chromatography and the temperature dependence of GFP fluorescence was found to be calcium dependent.	Calcium	167-174	eukaryotic translation elongation factor 2	Homo sapiens	28-36
19244119-3	2009	The induction of autophagy by 2-DG was associated with activation of elongation factor-2 kinase (eEF-2 kinase), a structurally and functionally unique enzyme that phosphorylates eEF-2, leading to loss of affinity of this elongation factor for the ribosome and to termination of protein elongation.	Deoxyglucose	30-34	eukaryotic translation elongation factor 2	Homo sapiens	97-102
19360331-5	2009	Knockdown of eEF2 by eEF2-specific short-hairpin RNA (shEF2) inhibited cancer cell growth in two gastric cancer cell lines, AZ-521 and MKN28, and one colon cancer cell line, SW620.	az-521	124-130	eukaryotic translation elongation factor 2	Homo sapiens	13-17
19360331-5	2009	Knockdown of eEF2 by eEF2-specific short-hairpin RNA (shEF2) inhibited cancer cell growth in two gastric cancer cell lines, AZ-521 and MKN28, and one colon cancer cell line, SW620.	az-521	124-130	eukaryotic translation elongation factor 2	Homo sapiens	21-25
19360331-5	2009	Knockdown of eEF2 by eEF2-specific short-hairpin RNA (shEF2) inhibited cancer cell growth in two gastric cancer cell lines, AZ-521 and MKN28, and one colon cancer cell line, SW620.	mkn28	135-140	eukaryotic translation elongation factor 2	Homo sapiens	13-17
19360331-5	2009	Knockdown of eEF2 by eEF2-specific short-hairpin RNA (shEF2) inhibited cancer cell growth in two gastric cancer cell lines, AZ-521 and MKN28, and one colon cancer cell line, SW620.	mkn28	135-140	eukaryotic translation elongation factor 2	Homo sapiens	21-25
19143494-4	2009	GCAP1 binds functionally to Mg(2+) at EF2 (DeltaH(EF2) = 4.3 kcal/mol, and K(EF2) = 0.7 mM) required for RetGC activation.	magnesium ion	28-34	eukaryotic translation elongation factor 2	Homo sapiens	50-53
19143494-4	2009	GCAP1 binds functionally to Mg(2+) at EF2 (DeltaH(EF2) = 4.3 kcal/mol, and K(EF2) = 0.7 mM) required for RetGC activation.	magnesium ion	28-34	eukaryotic translation elongation factor 2	Homo sapiens	50-53
19143494-4	2009	GCAP1 binds functionally to Mg(2+) at EF2 (DeltaH(EF2) = 4.3 kcal/mol, and K(EF2) = 0.7 mM) required for RetGC activation.	magnesium ion	28-34	eukaryotic translation elongation factor 2	Homo sapiens	38-41
19143494-5	2009	Ca(2+) and/or Mg(2+) binding to GCAP1 dramatically alters DSC and NMR spectra, indicating metal-induced protein conformational changes in EF2, EF3, and EF4.	magnesium ion	14-20	eukaryotic translation elongation factor 2	Homo sapiens	138-141
19143494-5	2009	Ca(2+) and/or Mg(2+) binding to GCAP1 dramatically alters DSC and NMR spectra, indicating metal-induced protein conformational changes in EF2, EF3, and EF4.	Metals	90-95	eukaryotic translation elongation factor 2	Homo sapiens	138-141
18706914-4	2008	Calcium binding to S100B causes a conformational change involving movement of helix III in the second calcium-binding site (EF2) that exposes a hydrophobic surface enabling interactions with other proteins such as tubulin and Ndr kinase.	Calcium	0-7	eukaryotic translation elongation factor 2	Homo sapiens	124-127
19008222-4	2009	The N-domain consists of EF1 and EF2 in a closed conformation with Mg2+ bound at EF1.	magnesium ion	67-71	eukaryotic translation elongation factor 2	Homo sapiens	33-36
18768473-4	2008	Our data indicate that although exogenous ROS inhibit mTOR, eIF2alpha, and eEF2, mTOR and eEF2 were largely refractory to ROS generated under moderate hypoxia (0.5% O(2)).	Reactive Oxygen Species	42-45	eukaryotic translation elongation factor 2	Homo sapiens	75-79
19137259-5	2009	While the AMPK/eEF-2K/eEF-2 pathway appears to function in adaptation to physiological fluctuations in ATP levels in the mutant cells, the ER stress signified by constitutive protein synthesis inhibition through eIF-2alpha-mediated repression of translation initiation may have pathobiochemical consequences.	Adenosine Triphosphate	103-106	eukaryotic translation elongation factor 2	Homo sapiens	15-20
18706914-4	2008	Calcium binding to S100B causes a conformational change involving movement of helix III in the second calcium-binding site (EF2) that exposes a hydrophobic surface enabling interactions with other proteins such as tubulin and Ndr kinase.	Calcium	102-109	eukaryotic translation elongation factor 2	Homo sapiens	124-127
18706914-7	2008	A series of tryptophan substitutions near the dimer interface and the EF2 calcium-binding site were studied by fluorescence spectroscopy and showed biphasic unfolding curves.	Calcium	74-81	eukaryotic translation elongation factor 2	Homo sapiens	70-73
18384084-2	2008	Most S100 proteins are dimeric, with each monomer containing two EF-hand calcium-binding sites (EF1, EF2).	Calcium	73-80	eukaryotic translation elongation factor 2	Homo sapiens	101-104
18712774-0	2008	Lopinavir impairs protein synthesis and induces eEF2 phosphorylation via the activation of AMP-activated protein kinase.	Lopinavir	0-9	eukaryotic translation elongation factor 2	Homo sapiens	48-52
18712774-8	2008	To verify this connection, myocytes were treated with the AMPK inhibitor compound C. Compound C blocked eEF2K and eEF2 phosphorylation, demonstrating that LPV affects eEF2 activity via an AMPK-eEF2K dependent pathway.	Lopinavir	155-158	eukaryotic translation elongation factor 2	Homo sapiens	104-108
18712774-8	2008	To verify this connection, myocytes were treated with the AMPK inhibitor compound C. Compound C blocked eEF2K and eEF2 phosphorylation, demonstrating that LPV affects eEF2 activity via an AMPK-eEF2K dependent pathway.	Lopinavir	155-158	eukaryotic translation elongation factor 2	Homo sapiens	114-118
18712774-9	2008	In contrast, incubation of myocytes with rottlerin suppressed eEF2K, but not eEF2 phosphorylation, suggesting that eEF2 can be regulated independent of eEF2K.	rottlerin	41-50	eukaryotic translation elongation factor 2	Homo sapiens	62-66
18384084-4	2008	Although several three dimensional structures of S100 proteins are available in the calcium-free (apo-) state it has been observed that these structures appear to adopt a wide range of conformations in the EF2 site with respect to the positioning of helix III, the helix that undergoes the most dramatic calcium-induced conformational change.	Calcium	304-311	eukaryotic translation elongation factor 2	Homo sapiens	206-209
18384084-10	2008	This shows that calcium binding to the S100 proteins causes not only a conformational change but results in a tighter distribution of helices within the EF2 calcium binding site required for target protein interactions.	Calcium	16-23	eukaryotic translation elongation factor 2	Homo sapiens	153-156
18384084-10	2008	This shows that calcium binding to the S100 proteins causes not only a conformational change but results in a tighter distribution of helices within the EF2 calcium binding site required for target protein interactions.	Calcium	157-164	eukaryotic translation elongation factor 2	Homo sapiens	153-156
18684057-2	2008	Denileukin diftitox specifically binds to IL-2 receptors on the cell membrane, is internalized via receptor-mediated endocytosis and inhibits protein synthesis by ADP ribosylation of elongation factor 2, resulting in cell death.	diftitox	11-19	eukaryotic translation elongation factor 2	Homo sapiens	183-202
18644383-1	2008	In an attempt to understand ribosome-induced GTP hydrolysis on eEF2, we determined a 12.6-A cryo-electron microscopy reconstruction of the eEF2-bound 80S ribosome in the presence of aluminum tetrafluoride and GDP, with aluminum tetrafluoride mimicking the gamma-phosphate during hydrolysis.	Guanosine Triphosphate	45-48	eukaryotic translation elongation factor 2	Homo sapiens	63-67
18644383-1	2008	In an attempt to understand ribosome-induced GTP hydrolysis on eEF2, we determined a 12.6-A cryo-electron microscopy reconstruction of the eEF2-bound 80S ribosome in the presence of aluminum tetrafluoride and GDP, with aluminum tetrafluoride mimicking the gamma-phosphate during hydrolysis.	Guanosine Triphosphate	45-48	eukaryotic translation elongation factor 2	Homo sapiens	139-143
18644383-1	2008	In an attempt to understand ribosome-induced GTP hydrolysis on eEF2, we determined a 12.6-A cryo-electron microscopy reconstruction of the eEF2-bound 80S ribosome in the presence of aluminum tetrafluoride and GDP, with aluminum tetrafluoride mimicking the gamma-phosphate during hydrolysis.	tetrafluoroaluminate	182-204	eukaryotic translation elongation factor 2	Homo sapiens	63-67
18644383-1	2008	In an attempt to understand ribosome-induced GTP hydrolysis on eEF2, we determined a 12.6-A cryo-electron microscopy reconstruction of the eEF2-bound 80S ribosome in the presence of aluminum tetrafluoride and GDP, with aluminum tetrafluoride mimicking the gamma-phosphate during hydrolysis.	tetrafluoroaluminate	182-204	eukaryotic translation elongation factor 2	Homo sapiens	139-143
18644383-1	2008	In an attempt to understand ribosome-induced GTP hydrolysis on eEF2, we determined a 12.6-A cryo-electron microscopy reconstruction of the eEF2-bound 80S ribosome in the presence of aluminum tetrafluoride and GDP, with aluminum tetrafluoride mimicking the gamma-phosphate during hydrolysis.	Guanosine Diphosphate	209-212	eukaryotic translation elongation factor 2	Homo sapiens	139-143
18644383-1	2008	In an attempt to understand ribosome-induced GTP hydrolysis on eEF2, we determined a 12.6-A cryo-electron microscopy reconstruction of the eEF2-bound 80S ribosome in the presence of aluminum tetrafluoride and GDP, with aluminum tetrafluoride mimicking the gamma-phosphate during hydrolysis.	tetrafluoroaluminate	219-241	eukaryotic translation elongation factor 2	Homo sapiens	139-143
18644383-1	2008	In an attempt to understand ribosome-induced GTP hydrolysis on eEF2, we determined a 12.6-A cryo-electron microscopy reconstruction of the eEF2-bound 80S ribosome in the presence of aluminum tetrafluoride and GDP, with aluminum tetrafluoride mimicking the gamma-phosphate during hydrolysis.	gamma-phosphate	256-271	eukaryotic translation elongation factor 2	Homo sapiens	139-143
18577697-4	2008	The phosphorylation of PKB Ser(473) and p70(S6k) Thr(389) increased concomitantly with insulin, but whereas raising insulin to 30 mU/l increased the phosphorylation of mTOR Ser(2448), 4E-BP1 Thr(37/46), or GSK3beta Ser(9) and decreased that of eEF2 Thr(56), higher insulin doses to 72 and 167 mU/l did not augment these latter responses.	Serine	27-30	eukaryotic translation elongation factor 2	Homo sapiens	244-248
18460012-0	2008	The diphthamide modification on elongation factor-2 renders mammalian cells resistant to ricin.	diphthamide	4-15	eukaryotic translation elongation factor 2	Homo sapiens	32-51
18460012-1	2008	Diphthamide is a post-translational derivative of histidine in protein synthesis elongation factor-2 (eEF-2) that is present in all eukaryotes with no known normal physiological role.	diphthamide	0-11	eukaryotic translation elongation factor 2	Homo sapiens	81-100
18460012-1	2008	Diphthamide is a post-translational derivative of histidine in protein synthesis elongation factor-2 (eEF-2) that is present in all eukaryotes with no known normal physiological role.	Histidine	50-59	eukaryotic translation elongation factor 2	Homo sapiens	81-100
18583986-3	2008	One loop moves to form a solvent cover for the active site of the enzyme and reaches towards the target residue (diphthamide) in eEF2 forming an important hydrogen bond.	diphthamide	113-124	eukaryotic translation elongation factor 2	Homo sapiens	129-133
18583986-3	2008	One loop moves to form a solvent cover for the active site of the enzyme and reaches towards the target residue (diphthamide) in eEF2 forming an important hydrogen bond.	Hydrogen	155-163	eukaryotic translation elongation factor 2	Homo sapiens	129-133
18337751-9	2008	Inactivation of eEF2K by cdc2 may serve to keep eEF2 active during mitosis (where calcium levels rise) and thereby permit protein synthesis to proceed in mitotic cells.	Calcium	82-89	eukaryotic translation elongation factor 2	Homo sapiens	16-20
18188169-4	2008	We show that sal induces phosphorylation of the translation elongation factor eukaryotic translation elongation factor 2 (eEF-2), an event that depends on eEF-2 kinase (eEF-2K).	salubrinal	13-16	eukaryotic translation elongation factor 2	Homo sapiens	78-120
18188169-4	2008	We show that sal induces phosphorylation of the translation elongation factor eukaryotic translation elongation factor 2 (eEF-2), an event that depends on eEF-2 kinase (eEF-2K).	salubrinal	13-16	eukaryotic translation elongation factor 2	Homo sapiens	122-127
18199453-7	2008	Our NMR data suggest that Mg(2+) binds to EF2 and EF3, thereby classifying them as structural sites, whereas EF4 is a Ca(2+)-specific or regulatory site.	magnesium ion	26-32	eukaryotic translation elongation factor 2	Homo sapiens	42-45
18199453-8	2008	This was further corroborated using an EF2/EF3-disabled mutant, which binds only Ca(2+) and not Mg(2+).	magnesium ion	96-102	eukaryotic translation elongation factor 2	Homo sapiens	39-42
17164244-0	2007	Alcohol regulates eukaryotic elongation factor 2 phosphorylation via an AMP-activated protein kinase-dependent mechanism in C2C12 skeletal myocytes.	Alcohols	0-7	eukaryotic translation elongation factor 2	Homo sapiens	18-48
18941619-1	2008	The sordarin family of compounds, characterized by a unique tetracyclic diterpene core including a norbornene system, inhibits protein synthesis in fungi by stabilizing the ribosome/EF2 complex.	sordarin	4-12	eukaryotic translation elongation factor 2	Homo sapiens	182-185
17947356-8	2008	Consistent with this idea, we also found that direct stimulation of PKC with the phorbol ester phorbol 12-myristate 13-acetate induced eEF2 dephosphorylation.	Phorbol Esters	81-94	eukaryotic translation elongation factor 2	Homo sapiens	135-139
17947356-8	2008	Consistent with this idea, we also found that direct stimulation of PKC with the phorbol ester phorbol 12-myristate 13-acetate induced eEF2 dephosphorylation.	Tetradecanoylphorbol Acetate	95-126	eukaryotic translation elongation factor 2	Homo sapiens	135-139
17893044-0	2007	Doxorubicin generates a proapoptotic phenotype by phosphorylation of elongation factor 2.	Doxorubicin	0-11	eukaryotic translation elongation factor 2	Homo sapiens	69-88
17893044-4	2007	In this study, we found that doxorubicin caused strong and sustained phosphorylation of elongation factor 2 (EF-2), which interferes with protein elongation.	Doxorubicin	29-40	eukaryotic translation elongation factor 2	Homo sapiens	88-107
17893044-4	2007	In this study, we found that doxorubicin caused strong and sustained phosphorylation of elongation factor 2 (EF-2), which interferes with protein elongation.	Doxorubicin	29-40	eukaryotic translation elongation factor 2	Homo sapiens	109-113
17893044-9	2007	In conclusion, our data suggest that free radicals can affect the phosphorylation of EF-2 resulting in a net loss of short-half-life proteins such as cFLIP(S) and XIAP, leaving a cell more vulnerable to apoptotic stimuli.	Free Radicals	37-50	eukaryotic translation elongation factor 2	Homo sapiens	85-89
17477546-3	2007	Ricin toxin A-chain (RTA) and pokeweed antiviral protein (PAP) catalyze the release of adenine from a specific adenosine on a stem-tetraloop (GAGA) sequence at the elongation factor (eEF2) binding site of the 28S subunit of eukaryotic ribosomes, thereby arresting translation.	Adenine	87-94	eukaryotic translation elongation factor 2	Homo sapiens	183-187
17477546-3	2007	Ricin toxin A-chain (RTA) and pokeweed antiviral protein (PAP) catalyze the release of adenine from a specific adenosine on a stem-tetraloop (GAGA) sequence at the elongation factor (eEF2) binding site of the 28S subunit of eukaryotic ribosomes, thereby arresting translation.	Adenosine	111-120	eukaryotic translation elongation factor 2	Homo sapiens	183-187
17164244-8	2007	Compound C, an inhibitor of AMPK, suppressed the effects of EtOH on eEF2 phosphorylation but had no effect on eEF2K, indicating that AMPK regulates eEF2 independent of eEF2K.	Ethanol	60-64	eukaryotic translation elongation factor 2	Homo sapiens	68-72
17164244-9	2007	Finally, EtOH decreased protein phosphatase 2A activity when either eEF2 or AMPK was used as the substrate.	Ethanol	9-13	eukaryotic translation elongation factor 2	Homo sapiens	68-72
17164244-10	2007	Thus, this later action may partially account for the increased phosphorylation of eEF2 in response to EtOH and the observed sensitivity of AMPK to rapamycin and PD98059 treatments.	Ethanol	103-107	eukaryotic translation elongation factor 2	Homo sapiens	83-87
17164244-10	2007	Thus, this later action may partially account for the increased phosphorylation of eEF2 in response to EtOH and the observed sensitivity of AMPK to rapamycin and PD98059 treatments.	Sirolimus	148-157	eukaryotic translation elongation factor 2	Homo sapiens	83-87
17187762-0	2007	Calcium-induced synergistic inhibition of a translational factor eEF2 in nerve growth cones.	Calcium	0-7	eukaryotic translation elongation factor 2	Homo sapiens	65-69
17187762-3	2007	While phosphorylated eEF2 was weakly distributed in advancing growth cones, eEF2 phosphorylation was increased by high potassium-evoked calcium influx.	Potassium	119-128	eukaryotic translation elongation factor 2	Homo sapiens	76-80
17187762-3	2007	While phosphorylated eEF2 was weakly distributed in advancing growth cones, eEF2 phosphorylation was increased by high potassium-evoked calcium influx.	Calcium	136-143	eukaryotic translation elongation factor 2	Homo sapiens	76-80
17187762-6	2007	Moreover, calcium elevation decreased total eEF2 in growth cones.	Calcium	10-17	eukaryotic translation elongation factor 2	Homo sapiens	44-48
17187762-7	2007	Since phosphorylated eEF2 inhibits mRNA translation, calcium elevation appears to inhibit mRNA translation in growth cones by a synergistic mechanism involving regulation of EF2K, S6K, and eEF2 itself.	Calcium	53-60	eukaryotic translation elongation factor 2	Homo sapiens	189-193
17164244-10	2007	Thus, this later action may partially account for the increased phosphorylation of eEF2 in response to EtOH and the observed sensitivity of AMPK to rapamycin and PD98059 treatments.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	162-169	eukaryotic translation elongation factor 2	Homo sapiens	83-87
17164244-11	2007	Collectively, the induction of eEF2 phosphorylation by EtOH is controlled by an increase in AMPK and a decrease in protein phosphatase 2A activity.	Ethanol	55-59	eukaryotic translation elongation factor 2	Homo sapiens	31-35
17164244-2	2007	In the present study incubation of C2C12 myocytes with 100 mm EtOH decreased protein synthesis while markedly increasing the phosphorylation of eukaryotic elongation factor 2 (eEF2), a key component of the translation machinery.	Ethanol	62-66	eukaryotic translation elongation factor 2	Homo sapiens	144-174
17164244-2	2007	In the present study incubation of C2C12 myocytes with 100 mm EtOH decreased protein synthesis while markedly increasing the phosphorylation of eukaryotic elongation factor 2 (eEF2), a key component of the translation machinery.	Ethanol	62-66	eukaryotic translation elongation factor 2	Homo sapiens	176-180
17164244-3	2007	Both mTOR and MEK pathways were found to play a role in regulating the effect of EtOH on eEF2 phosphorylation.	Ethanol	81-85	eukaryotic translation elongation factor 2	Homo sapiens	89-93
17164244-4	2007	Rapamycin, an inhibitor of mammalian target of rapamycin, and the MEK inhibitor PD98059 blocked the EtOH-induced phosphorylation of eEF2, whereas the p38 MAPK inhibitor SB202190 had no effect.	Sirolimus	0-9	eukaryotic translation elongation factor 2	Homo sapiens	132-136
17164244-4	2007	Rapamycin, an inhibitor of mammalian target of rapamycin, and the MEK inhibitor PD98059 blocked the EtOH-induced phosphorylation of eEF2, whereas the p38 MAPK inhibitor SB202190 had no effect.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	80-87	eukaryotic translation elongation factor 2	Homo sapiens	132-136
17164244-4	2007	Rapamycin, an inhibitor of mammalian target of rapamycin, and the MEK inhibitor PD98059 blocked the EtOH-induced phosphorylation of eEF2, whereas the p38 MAPK inhibitor SB202190 had no effect.	Ethanol	100-104	eukaryotic translation elongation factor 2	Homo sapiens	132-136
17164244-5	2007	Unexpectedly, EtOH decreased the phosphorylation and activity of the eEF2 upstream regulator eEF2 kinase.	Ethanol	14-18	eukaryotic translation elongation factor 2	Homo sapiens	69-73
16901746-0	2006	Site-specific mutagenesis of the histidine precursor of diphthamide in the human elongation factor-2 gene confers resistance to diphtheria toxin.	Histidine	33-42	eukaryotic translation elongation factor 2	Homo sapiens	81-100
16817779-4	2006	HNP1 (human neutrophil protein 1) inhibited DT- or ETA-mediated ADP-ribosylation of eEF2 (eukaryotic elongation factor 2) and protected HeLa cells against DT- or ETA-induced cell death.	Adenosine Diphosphate	64-67	eukaryotic translation elongation factor 2	Homo sapiens	90-120
17665640-0	2007	Endogenous ADP-ribosylation of eukaryotic elongation factor 2 and its 32 kDa tryptic fragment.	Adenosine Diphosphate	11-14	eukaryotic translation elongation factor 2	Homo sapiens	31-61
17665640-2	2007	The binding of free ADP-ribose and endogenous transferase-dependent ADP-ribosylation were distinct reactions for eEF-2, as indicated by different findings.	Adenosine Diphosphate	20-23	eukaryotic translation elongation factor 2	Homo sapiens	113-118
17665640-2	2007	The binding of free ADP-ribose and endogenous transferase-dependent ADP-ribosylation were distinct reactions for eEF-2, as indicated by different findings.	Adenosine Diphosphate	68-71	eukaryotic translation elongation factor 2	Homo sapiens	113-118
17665640-3	2007	Incubation of eEF-2 tryptic fragment 32/33 kDa (32F) with NAD was ADP-ribosylated and gave rise to the covalent binding of ADP-ribose to eEF-2.	NAD	58-61	eukaryotic translation elongation factor 2	Homo sapiens	14-19
17665640-3	2007	Incubation of eEF-2 tryptic fragment 32/33 kDa (32F) with NAD was ADP-ribosylated and gave rise to the covalent binding of ADP-ribose to eEF-2.	NAD	58-61	eukaryotic translation elongation factor 2	Homo sapiens	137-142
17665640-3	2007	Incubation of eEF-2 tryptic fragment 32/33 kDa (32F) with NAD was ADP-ribosylated and gave rise to the covalent binding of ADP-ribose to eEF-2.	Adenosine Diphosphate	66-69	eukaryotic translation elongation factor 2	Homo sapiens	14-19
17665640-3	2007	Incubation of eEF-2 tryptic fragment 32/33 kDa (32F) with NAD was ADP-ribosylated and gave rise to the covalent binding of ADP-ribose to eEF-2.	Adenosine Diphosphate	66-69	eukaryotic translation elongation factor 2	Homo sapiens	137-142
17665640-3	2007	Incubation of eEF-2 tryptic fragment 32/33 kDa (32F) with NAD was ADP-ribosylated and gave rise to the covalent binding of ADP-ribose to eEF-2.	Adenosine Diphosphate Ribose	123-133	eukaryotic translation elongation factor 2	Homo sapiens	14-19
17665640-3	2007	Incubation of eEF-2 tryptic fragment 32/33 kDa (32F) with NAD was ADP-ribosylated and gave rise to the covalent binding of ADP-ribose to eEF-2.	Adenosine Diphosphate Ribose	123-133	eukaryotic translation elongation factor 2	Homo sapiens	137-142
17510559-0	2007	"In vitro" protective effect of a hydrophilic vitamin E analogue on the decrease in levels of elongation factor 2 in conditions of oxidative stress.	Vitamin E	46-55	eukaryotic translation elongation factor 2	Homo sapiens	94-113
17510559-3	2007	eEF-2 is extremely sensitive to oxidative stress caused mainly by lipid peroxidant compounds such as cumene hydroperoxide (CH).	cumene hydroperoxide	101-121	eukaryotic translation elongation factor 2	Homo sapiens	0-5
17510559-3	2007	eEF-2 is extremely sensitive to oxidative stress caused mainly by lipid peroxidant compounds such as cumene hydroperoxide (CH).	cumene hydroperoxide	123-125	eukaryotic translation elongation factor 2	Homo sapiens	0-5
17510559-4	2007	OBJECTIVE: The purpose of this study was to determine whether the antioxidant Trolox prevents the effect of CH on the levels of hepatic eEF-2.	6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid	78-84	eukaryotic translation elongation factor 2	Homo sapiens	136-141
17510559-7	2007	RESULTS: The results show that Trolox at certain doses prevents the decrease in the level of eEF-2 caused by CH.	6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid	31-37	eukaryotic translation elongation factor 2	Homo sapiens	93-98
16817779-4	2006	HNP1 (human neutrophil protein 1) inhibited DT- or ETA-mediated ADP-ribosylation of eEF2 (eukaryotic elongation factor 2) and protected HeLa cells against DT- or ETA-induced cell death.	Adenosine Diphosphate	64-67	eukaryotic translation elongation factor 2	Homo sapiens	84-88
16901746-1	2006	Protein synthesis elongation factor 2 (EF-2) from eukaryotes contains a conserved post-translationally modified histidine residue known as diphthamide.	diphthamide	139-150	eukaryotic translation elongation factor 2	Homo sapiens	39-43
16901746-4	2006	Using site-specific mutagenesis of the histidine precursor of diphthamide, the histidine residue of codon 715 in human EF-2 cDNA was substituted with one of four amino acid residue codons: leucine, methionine, asparagine or glutamine.	Histidine	39-48	eukaryotic translation elongation factor 2	Homo sapiens	119-123
16901746-4	2006	Using site-specific mutagenesis of the histidine precursor of diphthamide, the histidine residue of codon 715 in human EF-2 cDNA was substituted with one of four amino acid residue codons: leucine, methionine, asparagine or glutamine.	diphthamide	62-73	eukaryotic translation elongation factor 2	Homo sapiens	119-123
16901746-4	2006	Using site-specific mutagenesis of the histidine precursor of diphthamide, the histidine residue of codon 715 in human EF-2 cDNA was substituted with one of four amino acid residue codons: leucine, methionine, asparagine or glutamine.	Histidine	79-88	eukaryotic translation elongation factor 2	Homo sapiens	119-123
16901746-4	2006	Using site-specific mutagenesis of the histidine precursor of diphthamide, the histidine residue of codon 715 in human EF-2 cDNA was substituted with one of four amino acid residue codons: leucine, methionine, asparagine or glutamine.	Methionine	198-208	eukaryotic translation elongation factor 2	Homo sapiens	119-123
16901746-4	2006	Using site-specific mutagenesis of the histidine precursor of diphthamide, the histidine residue of codon 715 in human EF-2 cDNA was substituted with one of four amino acid residue codons: leucine, methionine, asparagine or glutamine.	Asparagine	210-220	eukaryotic translation elongation factor 2	Homo sapiens	119-123
16901746-4	2006	Using site-specific mutagenesis of the histidine precursor of diphthamide, the histidine residue of codon 715 in human EF-2 cDNA was substituted with one of four amino acid residue codons: leucine, methionine, asparagine or glutamine.	Glutamine	224-233	eukaryotic translation elongation factor 2	Homo sapiens	119-123
16901746-0	2006	Site-specific mutagenesis of the histidine precursor of diphthamide in the human elongation factor-2 gene confers resistance to diphtheria toxin.	diphthamide	56-67	eukaryotic translation elongation factor 2	Homo sapiens	81-100
16901746-1	2006	Protein synthesis elongation factor 2 (EF-2) from eukaryotes contains a conserved post-translationally modified histidine residue known as diphthamide.	Histidine	112-121	eukaryotic translation elongation factor 2	Homo sapiens	18-37
16901746-1	2006	Protein synthesis elongation factor 2 (EF-2) from eukaryotes contains a conserved post-translationally modified histidine residue known as diphthamide.	Histidine	112-121	eukaryotic translation elongation factor 2	Homo sapiens	39-43
16901746-1	2006	Protein synthesis elongation factor 2 (EF-2) from eukaryotes contains a conserved post-translationally modified histidine residue known as diphthamide.	diphthamide	139-150	eukaryotic translation elongation factor 2	Homo sapiens	18-37
15994961-0	2005	Farnesyltransferase inhibitor SCH66336 induces rapid phosphorylation of eukaryotic translation elongation factor 2 in head and neck squamous cell carcinoma cells.	lonafarnib	30-38	eukaryotic translation elongation factor 2	Homo sapiens	72-114
16142694-0	2006	Endogenous ADP-ribosylation for eukaryotic elongation factor 2: evidence of two different sites and reactions.	Adenosine Diphosphate	11-14	eukaryotic translation elongation factor 2	Homo sapiens	43-62
16142694-4	2006	Free ADP-ribose could bind to elongation factor 2 previously subjected to ADP-ribosylation by diphtheria toxin or endogenous transferase.	Adenosine Diphosphate Ribose	5-15	eukaryotic translation elongation factor 2	Homo sapiens	30-49
16142694-6	2006	The ADP-ribosyl-elongation factor 2 adduct which formed upon binding of free ADP-ribose was resistant to neutral NH2OH, but decomposed almost completely upon treatment with NaOH.	Adenosine Diphosphate Ribose	77-87	eukaryotic translation elongation factor 2	Homo sapiens	16-35
16142694-6	2006	The ADP-ribosyl-elongation factor 2 adduct which formed upon binding of free ADP-ribose was resistant to neutral NH2OH, but decomposed almost completely upon treatment with NaOH.	Hydroxylamine	113-118	eukaryotic translation elongation factor 2	Homo sapiens	16-35
16142694-6	2006	The ADP-ribosyl-elongation factor 2 adduct which formed upon binding of free ADP-ribose was resistant to neutral NH2OH, but decomposed almost completely upon treatment with NaOH.	Sodium Hydroxide	173-177	eukaryotic translation elongation factor 2	Homo sapiens	16-35
16469450-2	2006	Not all oxidants affect eEF-2, which is extremely sensitive to oxidative stress caused mainly by lipid peroxidant compounds such as cumene hydroperoxide and t-butyl hydroperoxide.	cumene hydroperoxide	132-152	eukaryotic translation elongation factor 2	Homo sapiens	24-29
16469450-2	2006	Not all oxidants affect eEF-2, which is extremely sensitive to oxidative stress caused mainly by lipid peroxidant compounds such as cumene hydroperoxide and t-butyl hydroperoxide.	tert-Butylhydroperoxide	157-178	eukaryotic translation elongation factor 2	Homo sapiens	24-29
16469450-4	2006	In this "in vitro" study, we show the effect of three of these aldehydes on the levels of hepatic eEF-2.	Aldehydes	63-72	eukaryotic translation elongation factor 2	Homo sapiens	98-103
16483933-8	2006	Together, eIF2alpha, eEF2, and mTOR inhibition represent important HIF-independent mechanisms of energy conservation that promote survival under low O2 conditions.	Oxygen	149-151	eukaryotic translation elongation factor 2	Homo sapiens	21-25
16171514-6	2005	Whereas eEF2 phosphorylation levels altered by BDNF were inhibited by rapamycin, eEF1A phosphorylation was not affected by rapamycin or PD98059, a mitogen-activated protein kinase kinase (MEK) inhibitor.	Sirolimus	70-79	eukaryotic translation elongation factor 2	Homo sapiens	8-12
16180920-2	2005	In this study, the fast Fourier transform rigid-body docking algorithm ZDOCK has been employed for in silico reconstitution of the calcium binding protein calbindin D9k, from its two EF-hands subdomains, namely, EF1 (residues 1-43) and EF2 (residues 44-75).	Calcium	131-138	eukaryotic translation elongation factor 2	Homo sapiens	236-239
16405506-0	2006	2-Deoxyglucose and NMDA inhibit protein synthesis in neurons and regulate phosphorylation of elongation factor-2 by distinct mechanisms.	Deoxyglucose	0-14	eukaryotic translation elongation factor 2	Homo sapiens	93-112
16405506-0	2006	2-Deoxyglucose and NMDA inhibit protein synthesis in neurons and regulate phosphorylation of elongation factor-2 by distinct mechanisms.	N-Methylaspartate	19-23	eukaryotic translation elongation factor 2	Homo sapiens	93-112
16405506-3	2006	In the present study, we demonstrate that both NMDA and metabolic impairment by 2-deoxyglucose or inhibitors of mitochondrial respiration inhibit protein synthesis in cortical neurons through the phosphorylation of eukaryotic elongation factor (eEF-2), without any change in phosphorylation of initiation factor eIF-2alpha.	N-Methylaspartate	47-51	eukaryotic translation elongation factor 2	Homo sapiens	245-250
16405506-5	2006	Although NMDA decreases ATP levels in neurons, only the effects of 2-deoxyglucose on protein synthesis and phosphorylation of elongation factor eEF-2 were reversed by Na(+) pyruvate.	Deoxyglucose	67-81	eukaryotic translation elongation factor 2	Homo sapiens	144-149
16405506-5	2006	Although NMDA decreases ATP levels in neurons, only the effects of 2-deoxyglucose on protein synthesis and phosphorylation of elongation factor eEF-2 were reversed by Na(+) pyruvate.	na(+) pyruvate	167-181	eukaryotic translation elongation factor 2	Homo sapiens	144-149
16405506-8	2006	In conclusion, we provide evidence that protein synthesis can be inhibited by NMDA and metabolic deprivation by two distinct mechanisms involving, respectively, Ca(2+)-dependent and Ca(2+)-independent eEF-2 phosphorylation.	N-Methylaspartate	78-82	eukaryotic translation elongation factor 2	Homo sapiens	201-206
15994961-4	2005	We showed that SCH66336 induced phosphorylation (inactivation) of eukaryotic translation elongation factor 2 (eEF2), an important molecule for protein synthesis, as early as 3 hours after SCH66336 administration.	lonafarnib	188-196	eukaryotic translation elongation factor 2	Homo sapiens	66-108
15994961-4	2005	We showed that SCH66336 induced phosphorylation (inactivation) of eukaryotic translation elongation factor 2 (eEF2), an important molecule for protein synthesis, as early as 3 hours after SCH66336 administration.	lonafarnib	188-196	eukaryotic translation elongation factor 2	Homo sapiens	110-114
15994961-6	2005	Paradoxically, activation of eEF2 kinase (eEF2K), the only known kinase that regulates eEF2, was observed only at 12 hours after SCH66336 treatment.	lonafarnib	129-137	eukaryotic translation elongation factor 2	Homo sapiens	29-33
15994961-8	2005	Our data suggest that inhibition of protein synthesis through inactivation of eEF2 is a novel mechanism of SCH66336-mediated growth inhibition and that this effect is independent of ras-MEK/p70S6K-eEF2K signaling cascades.	lonafarnib	107-115	eukaryotic translation elongation factor 2	Homo sapiens	78-82
15994961-4	2005	We showed that SCH66336 induced phosphorylation (inactivation) of eukaryotic translation elongation factor 2 (eEF2), an important molecule for protein synthesis, as early as 3 hours after SCH66336 administration.	lonafarnib	15-23	eukaryotic translation elongation factor 2	Homo sapiens	66-108
15994961-4	2005	We showed that SCH66336 induced phosphorylation (inactivation) of eukaryotic translation elongation factor 2 (eEF2), an important molecule for protein synthesis, as early as 3 hours after SCH66336 administration.	lonafarnib	15-23	eukaryotic translation elongation factor 2	Homo sapiens	110-114
15882069-1	2005	S100B is a dimeric Ca(2+)-binding protein that undergoes a 90 +/- 3 degrees rotation of helix 3 in the typical EF-hand domain (EF2) upon the addition of calcium.	Calcium	153-160	eukaryotic translation elongation factor 2	Homo sapiens	127-130
15709741-8	2005	Light-dependent activation of beta(2)-AR leading to Galphas signaling was observed only for the EF2 chimera, and its activation was further enhanced by replacements of the other loops.	galphas	52-59	eukaryotic translation elongation factor 2	Homo sapiens	96-99
15746104-4	2005	By contrast, only two Ca(2+) bind to DREAM in the presence of physiological levels of Mg(2+) for both wild-type and D150N, suggesting that EF-2 binds constitutively to Mg(2+).	magnesium ion	86-92	eukaryotic translation elongation factor 2	Homo sapiens	139-143
15746104-4	2005	By contrast, only two Ca(2+) bind to DREAM in the presence of physiological levels of Mg(2+) for both wild-type and D150N, suggesting that EF-2 binds constitutively to Mg(2+).	magnesium ion	168-174	eukaryotic translation elongation factor 2	Homo sapiens	139-143
15746104-12	2005	We propose that Mg(2+) binding at EF-2 may structurally bridge DREAM to DNA targets and that Ca(2+)-induced protein dimerization disrupts DNA binding.	magnesium ion	16-22	eukaryotic translation elongation factor 2	Homo sapiens	34-38
15637051-0	2005	Gene trap mutagenesis-based forward genetic approach reveals that the tumor suppressor OVCA1 is a component of the biosynthetic pathway of diphthamide on elongation factor 2.	diphthamide	139-150	eukaryotic translation elongation factor 2	Homo sapiens	154-173
15637051-6	2005	We demonstrated direct evidence that the tumor suppressor OVCA1 is a component of the biosynthetic pathway of diphthamide on elongation factor 2, the target of bacterial ADP-ribosylating toxins.	diphthamide	110-121	eukaryotic translation elongation factor 2	Homo sapiens	125-144
15534876-6	2005	Cycloheximide addition after 4 h-pressure treatment suggested that the half-life of eEF-2 protein was shorter in pressurized cells.	Cycloheximide	0-13	eukaryotic translation elongation factor 2	Homo sapiens	84-89
15680246-5	2005	Pre-incubation of DTx with a 2000-fold excess of NAD, the natural substrate for the toxin"s ADP-ribosyltransferase (ADPrT) activity, inhibited the transfer of radiolabeled ADP-ribose to elongation factor 2 but had no effect on the degradation of radiolabeled DNA.	NAD	49-52	eukaryotic translation elongation factor 2	Homo sapiens	186-205
15680246-5	2005	Pre-incubation of DTx with a 2000-fold excess of NAD, the natural substrate for the toxin"s ADP-ribosyltransferase (ADPrT) activity, inhibited the transfer of radiolabeled ADP-ribose to elongation factor 2 but had no effect on the degradation of radiolabeled DNA.	Adenosine Diphosphate Ribose	172-182	eukaryotic translation elongation factor 2	Homo sapiens	186-205
14756556-3	2004	Diphtheria toxin catalyzes the ADP ribosylation of the diphthamide residue of eukaryotic elongation factor 2 (eEF-2).	Adenosine Diphosphate	31-34	eukaryotic translation elongation factor 2	Homo sapiens	110-115
15381153-4	2005	The investigation revealed that the endogenous ADP-ribosylation of eEF2 is complex and can take place in K562 cell lysates either under the action of endogenous transferase from [adenosine-14C]NAD or by direct binding of free [14C]ADP-ribose.	Adenosine	179-188	eukaryotic translation elongation factor 2	Homo sapiens	67-71
15381153-4	2005	The investigation revealed that the endogenous ADP-ribosylation of eEF2 is complex and can take place in K562 cell lysates either under the action of endogenous transferase from [adenosine-14C]NAD or by direct binding of free [14C]ADP-ribose.	Carbon-14	189-192	eukaryotic translation elongation factor 2	Homo sapiens	67-71
15381153-4	2005	The investigation revealed that the endogenous ADP-ribosylation of eEF2 is complex and can take place in K562 cell lysates either under the action of endogenous transferase from [adenosine-14C]NAD or by direct binding of free [14C]ADP-ribose.	Carbon-14	227-230	eukaryotic translation elongation factor 2	Homo sapiens	67-71
15381153-6	2005	Under standard culture conditions, in vivo labeling of eEF2 in the presence of [14C]adenosine was reversed to about 65% in the presence of diphtheria toxin and nicotinamide.	[14c]adenosine	79-93	eukaryotic translation elongation factor 2	Homo sapiens	55-59
15381153-6	2005	Under standard culture conditions, in vivo labeling of eEF2 in the presence of [14C]adenosine was reversed to about 65% in the presence of diphtheria toxin and nicotinamide.	Niacinamide	160-172	eukaryotic translation elongation factor 2	Homo sapiens	55-59
15381153-8	2005	On the other hand, H2O2-promoted oxidative stress gave rise to a nearly two-fold increase in the extent of in vivo labeling of eEF2.	Hydrogen Peroxide	19-23	eukaryotic translation elongation factor 2	Homo sapiens	127-131
15381153-10	2005	Oxidative stress specifically inhibited the subsequent binding of free ADP-ribose to eEF2.	Adenosine Diphosphate Ribose	71-81	eukaryotic translation elongation factor 2	Homo sapiens	85-89
15381153-11	2005	The results thus provide evidence that endogenous ADP-ribosylation of eEF2 can also take place by the binding of free ADP-ribose.	Adenosine Diphosphate	50-53	eukaryotic translation elongation factor 2	Homo sapiens	70-74
15381153-11	2005	The results thus provide evidence that endogenous ADP-ribosylation of eEF2 can also take place by the binding of free ADP-ribose.	Adenosine Diphosphate	118-121	eukaryotic translation elongation factor 2	Homo sapiens	70-74
15381153-11	2005	The results thus provide evidence that endogenous ADP-ribosylation of eEF2 can also take place by the binding of free ADP-ribose.	Ribose	122-128	eukaryotic translation elongation factor 2	Homo sapiens	70-74
15381153-12	2005	This nonenzymic reaction appears to account primarily for in vivo ADP-ribosylation of eEF2 under oxidative stress.	Adenosine Diphosphate	66-69	eukaryotic translation elongation factor 2	Homo sapiens	86-90
15125661-2	2004	The common toxic mechanism for these agents is mono-ADP-ribosylation of specific amino acids in G(s)(alpha), G(i)(alpha), and eEF-2 proteins, respectively, by the catalytic A chains of the toxins (CTA, PTA, and DTA).	mono-adp	47-55	eukaryotic translation elongation factor 2	Homo sapiens	126-131
15125661-2	2004	The common toxic mechanism for these agents is mono-ADP-ribosylation of specific amino acids in G(s)(alpha), G(i)(alpha), and eEF-2 proteins, respectively, by the catalytic A chains of the toxins (CTA, PTA, and DTA).	crotonic acid	197-200	eukaryotic translation elongation factor 2	Homo sapiens	126-131
15381153-0	2005	Effect of oxidative stress on in vivo ADP-ribosylation of eukaryotic elongation factor 2.	Adenosine Diphosphate	38-41	eukaryotic translation elongation factor 2	Homo sapiens	58-88
15381153-3	2005	In order to address this issue we investigated the in vivo ADP-ribosylation of eEF2 and the effect of oxidative stress thereon.	Adenosine Diphosphate	59-62	eukaryotic translation elongation factor 2	Homo sapiens	79-83
15341530-5	2004	We have cloned the 5"-terminal oligopyrimidine mRNA encoding eukaryotic elongation factor 2 and shown that serotonin increased its translation in synaptosomes.	Serotonin	107-116	eukaryotic translation elongation factor 2	Homo sapiens	72-91
15341530-8	2004	Serotonin application decreased eukaryotic elongation factor 2 phosphorylation in synaptosomes and in isolated neurites, and this was blocked by rapamycin.	Serotonin	0-9	eukaryotic translation elongation factor 2	Homo sapiens	43-62
15341530-8	2004	Serotonin application decreased eukaryotic elongation factor 2 phosphorylation in synaptosomes and in isolated neurites, and this was blocked by rapamycin.	Sirolimus	145-154	eukaryotic translation elongation factor 2	Homo sapiens	43-62
15024086-6	2004	Mutation of this site to alanine strongly attenuates the effects of insulin and rapamycin both on the binding of calmodulin to eEF2 kinase and on eEF2 kinase activity.	Alanine	25-32	eukaryotic translation elongation factor 2	Homo sapiens	127-131
15024086-6	2004	Mutation of this site to alanine strongly attenuates the effects of insulin and rapamycin both on the binding of calmodulin to eEF2 kinase and on eEF2 kinase activity.	Alanine	25-32	eukaryotic translation elongation factor 2	Homo sapiens	146-150
14709557-5	2004	AMPK also phosphorylates two other sites (Ser-78 and Ser-366) in eEF2 kinase in vitro.	Serine	42-45	eukaryotic translation elongation factor 2	Homo sapiens	65-69
14709557-5	2004	AMPK also phosphorylates two other sites (Ser-78 and Ser-366) in eEF2 kinase in vitro.	Serine	53-56	eukaryotic translation elongation factor 2	Homo sapiens	65-69
14709557-6	2004	We develop appropriate phosphospecific antisera and show that phosphorylation of Ser-398 in eEF2 kinase is enhanced in intact cells under a range of conditions that activate AMPK and increase the phosphorylation of eEF2.	Serine	81-84	eukaryotic translation elongation factor 2	Homo sapiens	92-96
14709557-6	2004	We develop appropriate phosphospecific antisera and show that phosphorylation of Ser-398 in eEF2 kinase is enhanced in intact cells under a range of conditions that activate AMPK and increase the phosphorylation of eEF2.	Serine	81-84	eukaryotic translation elongation factor 2	Homo sapiens	215-219
14756556-3	2004	Diphtheria toxin catalyzes the ADP ribosylation of the diphthamide residue of eukaryotic elongation factor 2 (eEF-2).	diphthamide	55-66	eukaryotic translation elongation factor 2	Homo sapiens	110-115
14756556-4	2004	The transition state of ADP ribosylation catalyzed by diphtheria toxin has been characterized by measuring a family of kinetic isotope effects using (3)H-, (14)C-, and (15)N-labeled NAD(+) with purified yeast eEF-2.	Adenosine Diphosphate	24-27	eukaryotic translation elongation factor 2	Homo sapiens	209-214
12891704-4	2003	Ninety-seven kiloDaltons eEF2 was found to coimmunoprecipitate in a salt-stable complex with p53.	Salts	68-72	eukaryotic translation elongation factor 2	Homo sapiens	25-29
12834812-0	2003	Cyclic AMP inhibits translation of cyclin D3 in T lymphocytes at the level of elongation by inducing eEF2-phosphorylation.	Cyclic AMP	0-10	eukaryotic translation elongation factor 2	Homo sapiens	101-105
12834812-4	2003	eEF2 promotes translation in its unphosphorylated form, and we observed a rapid phosphorylation of the eEF2-protein upon forskolin treatment.	Colforsin	121-130	eukaryotic translation elongation factor 2	Homo sapiens	0-4
12834812-4	2003	eEF2 promotes translation in its unphosphorylated form, and we observed a rapid phosphorylation of the eEF2-protein upon forskolin treatment.	Colforsin	121-130	eukaryotic translation elongation factor 2	Homo sapiens	103-107
12834812-5	2003	When using specific inhibitors of the eEF2-kinase prior to forskolin treatment, we were able to inhibit the increased phosphorylation of eEF2.	Colforsin	59-68	eukaryotic translation elongation factor 2	Homo sapiens	38-42
12920134-3	2003	Therefore, we tested the hypothesis that, as in liver, it could mediate the inhibition of protein synthesis by oxygen deprivation in heart by modulating the phosphorylation of eukaryotic elongation factor-2 (eEF2), which becomes inactive in its phosphorylated form.	Oxygen	111-117	eukaryotic translation elongation factor 2	Homo sapiens	176-206
12920134-3	2003	Therefore, we tested the hypothesis that, as in liver, it could mediate the inhibition of protein synthesis by oxygen deprivation in heart by modulating the phosphorylation of eukaryotic elongation factor-2 (eEF2), which becomes inactive in its phosphorylated form.	Oxygen	111-117	eukaryotic translation elongation factor 2	Homo sapiens	208-212
12891704-5	2003	The 97 kDa species was identified as eEF2, because it was (1) recognized by a polyclonal antiserum specific for eEF2, (2) ADP-ribosylated by diphtheria toxin (DT), and (3) radiolabeled by gamma-32P-azido-GTP and UV-irradiation.	Adenosine Diphosphate	122-125	eukaryotic translation elongation factor 2	Homo sapiens	37-41
12891704-5	2003	The 97 kDa species was identified as eEF2, because it was (1) recognized by a polyclonal antiserum specific for eEF2, (2) ADP-ribosylated by diphtheria toxin (DT), and (3) radiolabeled by gamma-32P-azido-GTP and UV-irradiation.	gamma-32p-azido-gtp	188-207	eukaryotic translation elongation factor 2	Homo sapiens	37-41
12891704-6	2003	p53 and eEF2 sedimented in sucrose gradients in both polyribosomal and subribosomal fractions.	Sucrose	27-34	eukaryotic translation elongation factor 2	Homo sapiens	8-12
12423334-5	2002	The kinase acting on eEF2 is an unusual and specific one, whose activity is dependent on calcium ions and calmodulin.	Calcium	89-96	eukaryotic translation elongation factor 2	Homo sapiens	21-25
12711611-3	2003	Binding of two Ca2+/monomer triggers translocation, although EF1, EF2, and EF3 are potentially able to bind calcium at micromolar concentrations.	Calcium	108-115	eukaryotic translation elongation factor 2	Homo sapiens	66-69
12711611-5	2003	Limited structural perturbations occur only in E124A-sorcin due to involvement of Glu-124 in a network of interactions that comprise the long D helix connecting EF3 to EF2.	Glutamic Acid	82-85	eukaryotic translation elongation factor 2	Homo sapiens	168-171
12270928-5	2002	The lack of requirement for NAD(+) to produce the toxin-eEF-2 complex demonstrates that the catalytic process is a random order mechanism, thereby disputing the current model.	NAD	28-34	eukaryotic translation elongation factor 2	Homo sapiens	56-61
12270928-7	2002	The ability of the toxin to bind eEF-2 with bound GTP/GDP was assessed using nonhydrolyzable analogues.	Guanosine Triphosphate	50-53	eukaryotic translation elongation factor 2	Homo sapiens	33-38
12270928-7	2002	The ability of the toxin to bind eEF-2 with bound GTP/GDP was assessed using nonhydrolyzable analogues.	Guanosine Diphosphate	54-57	eukaryotic translation elongation factor 2	Homo sapiens	33-38
12270928-8	2002	The results from the substrate binding and catalytic activity experiments indicate that PE24H is able to interact and bind with eEF-2 in all of its guanyl nucleotide-induced conformational states.	guanyl nucleotide	148-165	eukaryotic translation elongation factor 2	Homo sapiens	128-133
12171600-5	2002	In the present study we have examined the effects of the protein synthesis inhibitor anisomycin and tumour necrosis factor-alpha (TNF-alpha) on the phosphorylation of eEF2 kinase.	Anisomycin	85-95	eukaryotic translation elongation factor 2	Homo sapiens	167-171
12171600-6	2002	We demonstrate that Ser-359, Ser-366 and two novel sites (Ser-377 and Ser-396) are all phosphorylated in human epithelial KB cells, but only the phosphorylation of Ser-359 and Ser-377 increases in response to these agonists and correlates with the dephosphorylation (activation) of eEF2.	Serine	20-23	eukaryotic translation elongation factor 2	Homo sapiens	282-286
12171600-0	2002	Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and -insensitive pathways.	SB 203580	70-79	eukaryotic translation elongation factor 2	Homo sapiens	29-59
12171600-7	2002	Ser-377 is probably a substrate of MAPKAP-K2/K3 (mitogen-activated protein kinase-activated protein kinase 2/kinase 3) in cells, because eEF2 kinase is phosphorylated efficiently by these protein kinases in vitro and phosphorylation of this site, induced by TNF-alpha and low (but not high) concentrations of anisomycin, is prevented by SB 203580, which inhibits SAPK2a/p38, their "upstream" activator.	Serine	0-3	eukaryotic translation elongation factor 2	Homo sapiens	137-141
12171600-2	2002	Previous work showed that stress-activated protein kinase 4 (SAPK4, also called p38delta) inhibits eEF2 kinase in vitro by phosphorylating Ser-359, while ribosomal protein S6 kinases inhibit eEF2 kinase by phosphorylating Ser-366 [Knebel, Morrice and Cohen (2001) EMBO J.	Serine	139-142	eukaryotic translation elongation factor 2	Homo sapiens	99-103
12171600-7	2002	Ser-377 is probably a substrate of MAPKAP-K2/K3 (mitogen-activated protein kinase-activated protein kinase 2/kinase 3) in cells, because eEF2 kinase is phosphorylated efficiently by these protein kinases in vitro and phosphorylation of this site, induced by TNF-alpha and low (but not high) concentrations of anisomycin, is prevented by SB 203580, which inhibits SAPK2a/p38, their "upstream" activator.	Anisomycin	309-319	eukaryotic translation elongation factor 2	Homo sapiens	137-141
12171600-7	2002	Ser-377 is probably a substrate of MAPKAP-K2/K3 (mitogen-activated protein kinase-activated protein kinase 2/kinase 3) in cells, because eEF2 kinase is phosphorylated efficiently by these protein kinases in vitro and phosphorylation of this site, induced by TNF-alpha and low (but not high) concentrations of anisomycin, is prevented by SB 203580, which inhibits SAPK2a/p38, their "upstream" activator.	SB 203580	337-346	eukaryotic translation elongation factor 2	Homo sapiens	137-141
12171600-10	2002	Since the phosphorylation of Ser-377 does not inhibit eEF2 kinase in vitro, our results suggest that anisomycin or TNF-alpha inhibit eEF2 kinase via the phosphorylation of Ser-359.	Anisomycin	101-111	eukaryotic translation elongation factor 2	Homo sapiens	133-137
12171600-10	2002	Since the phosphorylation of Ser-377 does not inhibit eEF2 kinase in vitro, our results suggest that anisomycin or TNF-alpha inhibit eEF2 kinase via the phosphorylation of Ser-359.	Serine	172-175	eukaryotic translation elongation factor 2	Homo sapiens	133-137
11714909-9	2001	Detailed structural comparisons of sorcin with other members of PEF indicate that the EF-hand pair EF1-EF2 is likely to correspond to the two physiologically relevant calcium-binding sites and that the calcium-induced conformational change may be modest and localized within this pair of EF-hands.	Calcium	167-174	eukaryotic translation elongation factor 2	Homo sapiens	99-106
12194824-7	2002	In HEK293 cells, transfection of a dominant-negative AMPK construct abolished the oligomycin-induced inhibition of protein synthesis and eEF2 phosphorylation.	Oligomycins	82-92	eukaryotic translation elongation factor 2	Homo sapiens	137-141
12194824-8	2002	Lastly, eEF2 kinase, the kinase that phosphorylates eEF2, was activated in anoxic or AICA riboside-treated hepatocytes.	riboside	90-98	eukaryotic translation elongation factor 2	Homo sapiens	8-12
12194824-8	2002	Lastly, eEF2 kinase, the kinase that phosphorylates eEF2, was activated in anoxic or AICA riboside-treated hepatocytes.	riboside	90-98	eukaryotic translation elongation factor 2	Homo sapiens	52-56
11980481-4	2002	The cooperative binding of two calcium ions to the second and third EF-hands (EF-2 and EF-3) of recoverin leads to the extrusion of the fatty acid.	Calcium	31-38	eukaryotic translation elongation factor 2	Homo sapiens	78-82
11980481-4	2002	The cooperative binding of two calcium ions to the second and third EF-hands (EF-2 and EF-3) of recoverin leads to the extrusion of the fatty acid.	Fatty Acids	136-146	eukaryotic translation elongation factor 2	Homo sapiens	78-82
12379242-8	2002	NMDA treatment resulted in an increase in the phosphorylation of eEF-2 in the absence or presence of external Ca(2+).	N-Methylaspartate	0-4	eukaryotic translation elongation factor 2	Homo sapiens	65-70
11560506-7	2001	Increased levels of eEF-2 phosphorylation in hibernators appear to be a component of the regulated shutdown of cellular functions that permits hibernating animals to tolerate severe reductions in cerebral blood flow and oxygen delivery capacity.	Oxygen	220-226	eukaryotic translation elongation factor 2	Homo sapiens	20-25
11500363-6	2001	eEF2K became phosphorylated at Ser359 and its substrate eEF2 became dephosphorylated (activated) when KB cells were exposed to anisomycin, an agonist that activates all SAPKs, including SAPK4/p38delta.	Anisomycin	127-137	eukaryotic translation elongation factor 2	Homo sapiens	0-4
11406481-5	2001	Protein phosphatase 2A (PP2A) inhibitors okadaic acid and fostriecin, but not the PP2B inhibitor FK506, attenuated ANG II-dependent dephosphorylation of eEF-2.	Okadaic Acid	41-53	eukaryotic translation elongation factor 2	Homo sapiens	153-158
11500364-2	2001	Insulin induces dephosphorylation of eEF2 and inactivation of eEF2 kinase, and these effects are blocked by rapamycin, which inhibits the mammalian target of rapamycin, mTOR.	Sirolimus	108-117	eukaryotic translation elongation factor 2	Homo sapiens	37-41
11500364-7	2001	In response to insulin-like growth factor 1, which activates p70 S6 kinase but not Erk, regulation of eEF2 is blocked by rapamycin.	Sirolimus	121-130	eukaryotic translation elongation factor 2	Homo sapiens	102-106
11498025-8	2001	With eIF2B and eEF2, both amino acids and glucose must be provided for insulin to regulate their activities.	Glucose	42-49	eukaryotic translation elongation factor 2	Homo sapiens	15-19
11498025-12	2001	eEF2 kinase is phosphorylated by p70 S6 kinase at Ser-366; this results in the inactivation of eEF2 kinase, especially at low (micromolar) Ca concentrations.	Serine	50-53	eukaryotic translation elongation factor 2	Homo sapiens	0-4
11406481-5	2001	Protein phosphatase 2A (PP2A) inhibitors okadaic acid and fostriecin, but not the PP2B inhibitor FK506, attenuated ANG II-dependent dephosphorylation of eEF-2.	fostriecin	58-68	eukaryotic translation elongation factor 2	Homo sapiens	153-158
11406481-7	2001	The effect of ANG II on eEF-2 dephosphorylation was also blocked by LY-29004 (1-20 nM), suggesting a role for phosphoinositide 3-kinase, but the mammalian target rapamycin inhibitor rapamycin (10--100 nM) had no effect.	ly-29004	68-76	eukaryotic translation elongation factor 2	Homo sapiens	24-29
11171059-0	2001	Phosphorylation of elongation factor-2 kinase on serine 499 by cAMP-dependent protein kinase induces Ca2+/calmodulin-independent activity.	Serine	49-55	eukaryotic translation elongation factor 2	Homo sapiens	19-38
11358819-9	2001	The ability of GA to inhibit the growth of glioma cells was abrogated by overexpressing EF-2 kinase.	geldanamycin	15-17	eukaryotic translation elongation factor 2	Homo sapiens	88-92
11358819-0	2001	Disruption of the EF-2 kinase/Hsp90 protein complex: a possible mechanism to inhibit glioblastoma by geldanamycin.	geldanamycin	101-113	eukaryotic translation elongation factor 2	Homo sapiens	18-22
11171059-0	2001	Phosphorylation of elongation factor-2 kinase on serine 499 by cAMP-dependent protein kinase induces Ca2+/calmodulin-independent activity.	Cyclic AMP	63-67	eukaryotic translation elongation factor 2	Homo sapiens	19-38
10551494-9	1999	Proliferating-cell nuclear antigen and c-myc mRNA concentrations and bromodeoxyuridine incorporation were decreased in the EF2-decoy group by medians of 73% [IQR 53-84], 70% [50-79], and 74% [56-83], respectively) but not in the scrambled-oligodeoxynucleotide group (p&lt;0.0001).	Bromodeoxyuridine	69-86	eukaryotic translation elongation factor 2	Homo sapiens	123-126
10637774-1	1999	The exchange of free guanine nucleotides with guanine nucleotides bound to elongation factor 2 (EF-2) and to the EF-2-ribosome complex, and the effect of ADP-ribosylation of the EF-2 thereon, were investigated by nitrocellulose filter assay.	Guanine Nucleotides	21-40	eukaryotic translation elongation factor 2	Homo sapiens	96-100
10637774-1	1999	The exchange of free guanine nucleotides with guanine nucleotides bound to elongation factor 2 (EF-2) and to the EF-2-ribosome complex, and the effect of ADP-ribosylation of the EF-2 thereon, were investigated by nitrocellulose filter assay.	Guanine Nucleotides	46-65	eukaryotic translation elongation factor 2	Homo sapiens	75-94
10637774-1	1999	The exchange of free guanine nucleotides with guanine nucleotides bound to elongation factor 2 (EF-2) and to the EF-2-ribosome complex, and the effect of ADP-ribosylation of the EF-2 thereon, were investigated by nitrocellulose filter assay.	Guanine Nucleotides	46-65	eukaryotic translation elongation factor 2	Homo sapiens	96-100
10637774-1	1999	The exchange of free guanine nucleotides with guanine nucleotides bound to elongation factor 2 (EF-2) and to the EF-2-ribosome complex, and the effect of ADP-ribosylation of the EF-2 thereon, were investigated by nitrocellulose filter assay.	Guanine Nucleotides	46-65	eukaryotic translation elongation factor 2	Homo sapiens	113-117
10637774-1	1999	The exchange of free guanine nucleotides with guanine nucleotides bound to elongation factor 2 (EF-2) and to the EF-2-ribosome complex, and the effect of ADP-ribosylation of the EF-2 thereon, were investigated by nitrocellulose filter assay.	Guanine Nucleotides	46-65	eukaryotic translation elongation factor 2	Homo sapiens	113-117
10637774-2	1999	Under the experimental conditions, stoichiometric amounts of guanine nucleotides were bound, in particular, to ternary complexes of EF-2 with biphasic kinetics.	Guanine Nucleotides	61-80	eukaryotic translation elongation factor 2	Homo sapiens	132-136
11181828-5	2001	H(2)O(2) stimulated the phosphorylation of both eIF-2alpha and eEF-2, in a time- and dose-dependent manner, suggesting that both the blockade of the elongation and of the initiation step are responsible for the H(2)O(2)-induced inhibition of protein synthesis.	Hydrogen Peroxide	0-8	eukaryotic translation elongation factor 2	Homo sapiens	63-68
11181828-5	2001	H(2)O(2) stimulated the phosphorylation of both eIF-2alpha and eEF-2, in a time- and dose-dependent manner, suggesting that both the blockade of the elongation and of the initiation step are responsible for the H(2)O(2)-induced inhibition of protein synthesis.	Hydrogen Peroxide	211-219	eukaryotic translation elongation factor 2	Homo sapiens	63-68
11181828-7	2001	In conclusion, H(2)O(2) inhibits protein translation in cortical neurons by a process that involves the phosphorylation of both eIF-2alpha and eEF-2 and the relative contribution of these two events depends on the duration of H(2)O(2) treatment.	Hydrogen Peroxide	15-23	eukaryotic translation elongation factor 2	Homo sapiens	143-148
11158355-1	2001	The sordarin class of natural products selectively inhibits fungal protein synthesis by impairing the function of eukaryotic elongation factor 2 (eEF2).	sordarin	4-12	eukaryotic translation elongation factor 2	Homo sapiens	146-150
11158355-2	2001	Mutations in Saccharomyces cerevisiae eEF2 or the ribosomal stalk protein rpP0 can confer resistance to sordarin, although eEF2 is the major determinant of sordarin specificity.	sordarin	104-112	eukaryotic translation elongation factor 2	Homo sapiens	38-42
11158355-3	2001	It has been shown previously that sordarin specifically binds S. cerevisiae eEF2 while there is no detectable binding to eEF2 from plants or mammals, despite the high level of amino acid sequence conservation among these proteins.	sordarin	34-42	eukaryotic translation elongation factor 2	Homo sapiens	76-80
11158355-5	2001	To investigate the basis of sordarin"s fungal selectivity, eEF2 has been cloned and characterized from several sordarin-sensitive and -insensitive fungal species.	sordarin	28-36	eukaryotic translation elongation factor 2	Homo sapiens	59-63
11158355-5	2001	To investigate the basis of sordarin"s fungal selectivity, eEF2 has been cloned and characterized from several sordarin-sensitive and -insensitive fungal species.	sordarin	111-119	eukaryotic translation elongation factor 2	Homo sapiens	59-63
11158355-7	2001	It is also shown that the corresponding residues at these positions in human eEF2 are sufficient to confer sordarin insensitivity to S. cerevisiae identical to that observed with mammalian eEF2.	sordarin	107-115	eukaryotic translation elongation factor 2	Homo sapiens	77-81
11158355-7	2001	It is also shown that the corresponding residues at these positions in human eEF2 are sufficient to confer sordarin insensitivity to S. cerevisiae identical to that observed with mammalian eEF2.	sordarin	107-115	eukaryotic translation elongation factor 2	Homo sapiens	189-193
11575162-0	2001	Elongation factor-2 phosphorylation and the regulation of protein synthesis by calcium.	Calcium	79-86	eukaryotic translation elongation factor 2	Homo sapiens	0-19
10949152-3	2000	Comparing different pH ranges in immobilized pH gradient-isoelectric focusing (IPG-IEF), a range of pH 3 - 10 and 4 - 9 resulted in a highly defined and reproducible resolution of six different EF-2 variants of all extracts in the first dimension.	2-Isopropoxyethanol	79-82	eukaryotic translation elongation factor 2	Homo sapiens	194-198
10949152-7	2000	By application of a second IPG indicator strip to the 2-D gel, they could be aligned with corresponding spots in a silver-stained 2-D separation of human myocardial tissue, revealing that the EF-2 variants belong to the group of low-abundance proteins.	2-Isopropoxyethanol	27-30	eukaryotic translation elongation factor 2	Homo sapiens	192-196
10949152-7	2000	By application of a second IPG indicator strip to the 2-D gel, they could be aligned with corresponding spots in a silver-stained 2-D separation of human myocardial tissue, revealing that the EF-2 variants belong to the group of low-abundance proteins.	Silver	115-121	eukaryotic translation elongation factor 2	Homo sapiens	192-196
10771424-6	2000	This, combined with previous observations that the helix in EF-2 (helix III) undergoes a large conformational change upon calcium binding, suggests that the C-terminal EF-hand (EF-2) plays a role as a trigger for Ca(2+)-induced conformational change.	Calcium	122-129	eukaryotic translation elongation factor 2	Homo sapiens	60-64
10771424-6	2000	This, combined with previous observations that the helix in EF-2 (helix III) undergoes a large conformational change upon calcium binding, suggests that the C-terminal EF-hand (EF-2) plays a role as a trigger for Ca(2+)-induced conformational change.	Calcium	122-129	eukaryotic translation elongation factor 2	Homo sapiens	177-181
10757982-3	2000	Inhibition of protein synthesis by DB in vitro also occurs at the elongation stage, and it was shown previously that DB prevents EF-2-dependent translocation in partial reaction models of protein synthesis.	didemnins	35-37	eukaryotic translation elongation factor 2	Homo sapiens	129-133
10757982-3	2000	Inhibition of protein synthesis by DB in vitro also occurs at the elongation stage, and it was shown previously that DB prevents EF-2-dependent translocation in partial reaction models of protein synthesis.	didemnins	117-119	eukaryotic translation elongation factor 2	Homo sapiens	129-133
10816814-4	2000	Similar structural changes induced by Ca2+ are also characteristic of the -EF2 mutant of recoverin whose second Ca(2+)-binding site is modified and cannot bind calcium ions.	Calcium	160-167	eukaryotic translation elongation factor 2	Homo sapiens	75-78
10816814-5	2000	The structural properties of the -EF3 and -EF2,3 mutants (whose third or simultaneously second and third Ca(2+)-binding sites, respectively, are modified and damaged) are practically indifferent to calcium ions.	Calcium	198-205	eukaryotic translation elongation factor 2	Homo sapiens	43-46
10567226-2	1999	Here, we demonstrate that their activation by insulin requires the presence, in the medium in which the cells are maintained, of both amino acids and glucose: insulin only induced activation of eIF2B and the dephosphorylation of eEF2 when cells were exposed to both types of nutrient.	Glucose	150-157	eukaryotic translation elongation factor 2	Homo sapiens	229-233
10551494-9	1999	Proliferating-cell nuclear antigen and c-myc mRNA concentrations and bromodeoxyuridine incorporation were decreased in the EF2-decoy group by medians of 73% [IQR 53-84], 70% [50-79], and 74% [56-83], respectively) but not in the scrambled-oligodeoxynucleotide group (p&lt;0.0001).	Oligodeoxyribonucleotides	239-259	eukaryotic translation elongation factor 2	Homo sapiens	123-126
10583753-2	1999	The Gram-negative, rod-shaped, sulphate-reducing strains MM6, EF2, FM2, and GF2 were isolated from drain water, and from drilling muds E, F, and G, respectively.	Sulfates	31-39	eukaryotic translation elongation factor 2	Homo sapiens	62-65
10486009-5	1999	The two domain IV regions (one of which comprises the ADP-ribosylatable site of EF-2) are almost certainly due to the artifactual alignment of insertion segments that are unique to Bacteria and to Archaea-Eucarya.	Adenosine Diphosphate	54-57	eukaryotic translation elongation factor 2	Homo sapiens	80-84
10583753-2	1999	The Gram-negative, rod-shaped, sulphate-reducing strains MM6, EF2, FM2, and GF2 were isolated from drain water, and from drilling muds E, F, and G, respectively.	Water	105-110	eukaryotic translation elongation factor 2	Homo sapiens	62-65
9845338-4	1998	Three-dimensional modelling of the new EF-2 sequences enabled the identification of amino acid residues that may be important for conferring low temperature activity and included greater structural flexibility produced by fewer salt bridges, less packed hydrophobic cores and the reduction of proline residues in loop structures.	Proline	293-300	eukaryotic translation elongation factor 2	Homo sapiens	39-43
10383444-8	1999	GCAP-2 differs from recoverin in that the calcium ion binds to EF-4 in addition to EF-2 and EF-3.	Calcium	42-49	eukaryotic translation elongation factor 2	Homo sapiens	83-87
10383444-9	1999	A prominent exposed patch of hydrophobic residues formed by EF-1 and EF-2 (Leu24, Trp27, Phe31, Phe45, Phe48, Phe49, Tyr81, Val82, Leu85, and Leu89) may serve as a target-binding site for the transmission of calcium signals to guanylyl cyclase.	Calcium	208-215	eukaryotic translation elongation factor 2	Homo sapiens	69-73
10350103-14	1999	In the CTP group, however, there is a stunning phenomenon (EF1: 54.9+/-6.9%; EF2: 50.8+/-8.5%; EF3: 57.7+/-7.7%) which does not occur in the CON group (EF1: 58.0+/-8.3%; EF2: 60.8+/-10.9%; EF3: 63.0+/-9.3%).	Captopril	7-10	eukaryotic translation elongation factor 2	Homo sapiens	77-80
10350103-14	1999	In the CTP group, however, there is a stunning phenomenon (EF1: 54.9+/-6.9%; EF2: 50.8+/-8.5%; EF3: 57.7+/-7.7%) which does not occur in the CON group (EF1: 58.0+/-8.3%; EF2: 60.8+/-10.9%; EF3: 63.0+/-9.3%).	Captopril	7-10	eukaryotic translation elongation factor 2	Homo sapiens	170-173
9637736-5	1998	The Ca2+ channel antagonist, nisoldipine, lowered [Ca2+]i and reduced eEF-2 phosphorylation by half but had no effect on amino acid incorporation.	Nisoldipine	29-40	eukaryotic translation elongation factor 2	Homo sapiens	70-75
9783263-3	1998	Proteolytic cleavage and disulfide bridge reduction in the DTA-DTB linker region of DTx are required for optimal ADP-ribosylation of elongation factor 2 (EF-2).	Disulfides	25-34	eukaryotic translation elongation factor 2	Homo sapiens	133-152
9783263-3	1998	Proteolytic cleavage and disulfide bridge reduction in the DTA-DTB linker region of DTx are required for optimal ADP-ribosylation of elongation factor 2 (EF-2).	Disulfides	25-34	eukaryotic translation elongation factor 2	Homo sapiens	154-158
9783263-3	1998	Proteolytic cleavage and disulfide bridge reduction in the DTA-DTB linker region of DTx are required for optimal ADP-ribosylation of elongation factor 2 (EF-2).	dta-dtb	59-66	eukaryotic translation elongation factor 2	Homo sapiens	133-152
9783263-3	1998	Proteolytic cleavage and disulfide bridge reduction in the DTA-DTB linker region of DTx are required for optimal ADP-ribosylation of elongation factor 2 (EF-2).	dta-dtb	59-66	eukaryotic translation elongation factor 2	Homo sapiens	154-158
9783263-3	1998	Proteolytic cleavage and disulfide bridge reduction in the DTA-DTB linker region of DTx are required for optimal ADP-ribosylation of elongation factor 2 (EF-2).	Adenosine Diphosphate	113-116	eukaryotic translation elongation factor 2	Homo sapiens	133-152
9783263-3	1998	Proteolytic cleavage and disulfide bridge reduction in the DTA-DTB linker region of DTx are required for optimal ADP-ribosylation of elongation factor 2 (EF-2).	Adenosine Diphosphate	113-116	eukaryotic translation elongation factor 2	Homo sapiens	154-158
9685370-4	1998	Here, we report on the roles of EF-2 and -3 in S-modulin function (calcium binding, membrane association, and inhibition of rhodopsin phosphorylation) by site-directed mutants (E85M and E121M).	Calcium	67-74	eukaryotic translation elongation factor 2	Homo sapiens	32-43
9637736-6	1998	The Ca2+ channel agonist, Bay K 8644, produced sustained elevations of [Ca2+]i that were associated with 25-50% increases in eEF-2 phosphorylation, but no changes in protein synthetic rates occurred.	3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester	26-36	eukaryotic translation elongation factor 2	Homo sapiens	125-130
9637736-10	1998	Addition of low concentrations of ionomycin, which do not lower ATP content, was associated with complex changes in [Ca2+]i that resembled alterations in eEF-2 phosphorylation.	Ionomycin	34-43	eukaryotic translation elongation factor 2	Homo sapiens	154-159
8692916-1	1996	The catalytic, or third domain of Pseudomonas exotoxin A (PEIII) catalyzes the transfer of ADP ribose from nicotinamide adenine dinucleotide (NAD) to elongation factor-2 in eukaryotic cells, inhibiting protein synthesis.	Adenosine Diphosphate Ribose	91-101	eukaryotic translation elongation factor 2	Homo sapiens	150-169
9452424-3	1998	We have identified the sordarins as selective inhibitors of fungal protein synthesis acting via a specific interaction with EF2 despite the high degree of amino acid sequence homology exhibited by EF2s from various eukaryotes.	sordarin	23-32	eukaryotic translation elongation factor 2	Homo sapiens	124-127
9452424-4	1998	In vitro reconstitution assays using purified components from human, yeast, and plant cells demonstrate that sordarin sensitivity is dependent on fungal EF2.	sordarin	109-117	eukaryotic translation elongation factor 2	Homo sapiens	153-156
9452424-6	1998	Sordarin blocks ribosomal translocation by stabilizing the fungal EF2-ribosome complex in a manner similar to that of fusidic acid.	sordarin	0-8	eukaryotic translation elongation factor 2	Homo sapiens	66-69
9452424-7	1998	The fungal specificity of the sordarins, along with a detailed understanding of its mechanism of action, make EF2 an attractive antifungal target.	sordarin	30-39	eukaryotic translation elongation factor 2	Homo sapiens	110-113
9193634-4	1997	Residues 39-46 of the active-site loop of the C-domain become disordered upon NAD-binding, suggesting a potential role for these residues in binding to elongation facor-2 (EF-2).	NAD	78-81	eukaryotic translation elongation factor 2	Homo sapiens	172-176
9133370-3	1997	Here we have examined in cortical neurons in culture the regulation by glutamate of phosphorylation of eukaryotic elongation factor-2 (eEF-2) by eEF-2 kinase, a Ca2+/calmodulin-dependent enzyme.	Glutamic Acid	71-80	eukaryotic translation elongation factor 2	Homo sapiens	103-133
9133370-3	1997	Here we have examined in cortical neurons in culture the regulation by glutamate of phosphorylation of eukaryotic elongation factor-2 (eEF-2) by eEF-2 kinase, a Ca2+/calmodulin-dependent enzyme.	Glutamic Acid	71-80	eukaryotic translation elongation factor 2	Homo sapiens	135-140
9133370-4	1997	Using a phosphorylation state-specific antibody, we show that glutamate, which triggers a large influx of Ca2+, enhances dramatically the phosphorylation of eEF-2.	Glutamic Acid	62-71	eukaryotic translation elongation factor 2	Homo sapiens	157-162
9133370-6	1997	A 30 min treatment with NMDA induced a transient phosphorylation of eEF-2 and delayed neuronal death.	N-Methylaspartate	24-28	eukaryotic translation elongation factor 2	Homo sapiens	68-73
9133370-8	1997	Thus, phosphorylation of eEF-2 and the resulting depression of protein translation may have protective effects against excitotoxicity and open new perspectives for understanding long-term effects of glutamate.	Glutamic Acid	199-208	eukaryotic translation elongation factor 2	Homo sapiens	25-30
9168436-3	1997	DTctGMCSF was specifically immunoreactive with antidiphtheria toxin and anti-GMCSF antiseras, and exhibited the characteristic catalytic activity of diphtheria toxin, catalyzing the in vitro ADP-ribosylation of purified elongation factor 2.	dtctgmcsf	0-9	eukaryotic translation elongation factor 2	Homo sapiens	220-239
9168436-3	1997	DTctGMCSF was specifically immunoreactive with antidiphtheria toxin and anti-GMCSF antiseras, and exhibited the characteristic catalytic activity of diphtheria toxin, catalyzing the in vitro ADP-ribosylation of purified elongation factor 2.	Adenosine Diphosphate	191-194	eukaryotic translation elongation factor 2	Homo sapiens	220-239
8692916-1	1996	The catalytic, or third domain of Pseudomonas exotoxin A (PEIII) catalyzes the transfer of ADP ribose from nicotinamide adenine dinucleotide (NAD) to elongation factor-2 in eukaryotic cells, inhibiting protein synthesis.	NAD	107-140	eukaryotic translation elongation factor 2	Homo sapiens	150-169
8692916-1	1996	The catalytic, or third domain of Pseudomonas exotoxin A (PEIII) catalyzes the transfer of ADP ribose from nicotinamide adenine dinucleotide (NAD) to elongation factor-2 in eukaryotic cells, inhibiting protein synthesis.	NAD	142-145	eukaryotic translation elongation factor 2	Homo sapiens	150-169
8641294-5	1996	Rapamycin, a macrolide immunosuppressant which blocks the signalling pathway leading to the stimulation of the 70/85 kDa ribosomal protein S6 kinases, substantially blocks the activation of elongation, the fall in eEF-2 phosphorylation and the decrease in eEF-2 kinase activity, suggesting that p7O S6 kinase (p70s6k) and eEF-2 kinase may tie on a common signalling pathway.	Sirolimus	0-9	eukaryotic translation elongation factor 2	Homo sapiens	214-219
8573568-2	1996	Specifically, the catalytic (C) domain of DT transfers the ADP-ribose group of NAD to elongation factor-2 (EF-2), rendering EF-2 inactive.	Adenosine Diphosphate	59-62	eukaryotic translation elongation factor 2	Homo sapiens	86-105
8617259-0	1996	Photoaffinity labeling of elongation factor-2 with 8-azido derivatives of GTP and ATP.	8-azido	51-58	eukaryotic translation elongation factor 2	Homo sapiens	26-45
8617259-0	1996	Photoaffinity labeling of elongation factor-2 with 8-azido derivatives of GTP and ATP.	Guanosine Triphosphate	74-77	eukaryotic translation elongation factor 2	Homo sapiens	26-45
8617259-0	1996	Photoaffinity labeling of elongation factor-2 with 8-azido derivatives of GTP and ATP.	Adenosine Triphosphate	82-85	eukaryotic translation elongation factor 2	Homo sapiens	26-45
8617259-3	1996	Photoincorporation of the radioactive GTP derivative into eEF-2 was prevented by the previous addition of GTP and GDP.	Guanosine Triphosphate	38-41	eukaryotic translation elongation factor 2	Homo sapiens	58-63
8617259-3	1996	Photoincorporation of the radioactive GTP derivative into eEF-2 was prevented by the previous addition of GTP and GDP.	Guanosine Triphosphate	106-109	eukaryotic translation elongation factor 2	Homo sapiens	58-63
8617259-3	1996	Photoincorporation of the radioactive GTP derivative into eEF-2 was prevented by the previous addition of GTP and GDP.	Guanosine Diphosphate	114-117	eukaryotic translation elongation factor 2	Homo sapiens	58-63
8573568-2	1996	Specifically, the catalytic (C) domain of DT transfers the ADP-ribose group of NAD to elongation factor-2 (EF-2), rendering EF-2 inactive.	Adenosine Diphosphate	59-62	eukaryotic translation elongation factor 2	Homo sapiens	107-111
8573568-2	1996	Specifically, the catalytic (C) domain of DT transfers the ADP-ribose group of NAD to elongation factor-2 (EF-2), rendering EF-2 inactive.	Ribose	63-69	eukaryotic translation elongation factor 2	Homo sapiens	86-105
8573568-2	1996	Specifically, the catalytic (C) domain of DT transfers the ADP-ribose group of NAD to elongation factor-2 (EF-2), rendering EF-2 inactive.	Ribose	63-69	eukaryotic translation elongation factor 2	Homo sapiens	107-111
8573568-2	1996	Specifically, the catalytic (C) domain of DT transfers the ADP-ribose group of NAD to elongation factor-2 (EF-2), rendering EF-2 inactive.	NAD	79-82	eukaryotic translation elongation factor 2	Homo sapiens	86-105
8573568-2	1996	Specifically, the catalytic (C) domain of DT transfers the ADP-ribose group of NAD to elongation factor-2 (EF-2), rendering EF-2 inactive.	NAD	79-82	eukaryotic translation elongation factor 2	Homo sapiens	107-111
8573568-3	1996	In order to investigate how the C-domain of DT binds NAD and catalyzes the ADP-ribosylation of EF-2, the crystal structure of DT in complex with NAD has been determined to 2.3 A resolution.	Adenosine Diphosphate	75-78	eukaryotic translation elongation factor 2	Homo sapiens	95-99
8573568-3	1996	In order to investigate how the C-domain of DT binds NAD and catalyzes the ADP-ribosylation of EF-2, the crystal structure of DT in complex with NAD has been determined to 2.3 A resolution.	NAD	145-148	eukaryotic translation elongation factor 2	Homo sapiens	95-99
8573568-6	1996	Residues 39-46 of the active-site loop of the C-domain become disordered upon NAD binding, suggesting a potential role for this loop in the recognition of the ADP-ribose acceptor substrate, EF-2.	NAD	78-81	eukaryotic translation elongation factor 2	Homo sapiens	190-194
8573568-6	1996	Residues 39-46 of the active-site loop of the C-domain become disordered upon NAD binding, suggesting a potential role for this loop in the recognition of the ADP-ribose acceptor substrate, EF-2.	Adenosine Diphosphate	159-162	eukaryotic translation elongation factor 2	Homo sapiens	190-194
8573568-6	1996	Residues 39-46 of the active-site loop of the C-domain become disordered upon NAD binding, suggesting a potential role for this loop in the recognition of the ADP-ribose acceptor substrate, EF-2.	Ribose	163-169	eukaryotic translation elongation factor 2	Homo sapiens	190-194
8562903-3	1995	The resulting diphtheria toxin-related cytokine fusion proteins, or fusion toxins bind to their respective receptors, are internalized by receptor-mediated endocytosis, and efficiently eliminate target cell populations by the adenosine diphosphate ribosylation of elongation factor 2.	Adenosine Diphosphate	226-247	eukaryotic translation elongation factor 2	Homo sapiens	264-283
7805855-1	1994	The intrinsic fluorescence emission spectrum of elongation factor EF-2 due to the 7 Trp residues was not modified after complete phosphorylation of the factor by the specific Ca2+/Calmodulin-dependent kinase III.	Tryptophan	84-87	eukaryotic translation elongation factor 2	Homo sapiens	66-70
7548224-3	1995	Differentiation of the HL-60 cells by all-trans retinoic acid resulted in a reduced growth rate and a marked decrease in the intracellular concentration of eEF-2.	Tretinoin	48-61	eukaryotic translation elongation factor 2	Homo sapiens	156-161
8822152-2	1995	Indeed, the cell-surface receptor-specific intoxication of neoplastic cells through the catalytic ADP-ribosylation of EF-2 is the prototype of a new class of biological response modifiers that may be generally applicable.	Adenosine Diphosphate	98-101	eukaryotic translation elongation factor 2	Homo sapiens	118-122
7999776-2	1994	eEF-2 was complexed to empty reassociated 80S ribosomes in the presence of the nonhydrolyzable GTP analogue GuoPP[CH2]P.	Guanosine Triphosphate	95-98	eukaryotic translation elongation factor 2	Homo sapiens	0-5
7805855-3	1994	Low concentrations of GTP had a smaller quenching effect on the fluorescence of phosphorylated EF-2 than on the fluorescence of unmodified EF-2, whereas GDP had exactly the same quenching effect on the fluorescence of both samples.	Guanosine Triphosphate	22-25	eukaryotic translation elongation factor 2	Homo sapiens	95-99
7999776-2	1994	eEF-2 was complexed to empty reassociated 80S ribosomes in the presence of the nonhydrolyzable GTP analogue GuoPP[CH2]P.	guanosine 5'-(beta,gamma-methylene)triphosphate	108-119	eukaryotic translation elongation factor 2	Homo sapiens	0-5
7805855-3	1994	Low concentrations of GTP had a smaller quenching effect on the fluorescence of phosphorylated EF-2 than on the fluorescence of unmodified EF-2, whereas GDP had exactly the same quenching effect on the fluorescence of both samples.	Guanosine Triphosphate	22-25	eukaryotic translation elongation factor 2	Homo sapiens	139-143
7805855-4	1994	These results suggest that phosphorylation of EF-2 decreased its affinity for GTP but not for GDP.	Guanosine Triphosphate	78-81	eukaryotic translation elongation factor 2	Homo sapiens	46-50
7805855-4	1994	These results suggest that phosphorylation of EF-2 decreased its affinity for GTP but not for GDP.	Guanosine Diphosphate	94-97	eukaryotic translation elongation factor 2	Homo sapiens	46-50
7805855-5	1994	Ability of phosphorylated EF-2 to form a ternary complex with ribosomes in the presence of a non-hydrolysable GTP analog and its ability to protect ribosomes against ricin-inactivation were both decreased to the same extent.	Guanosine Triphosphate	110-113	eukaryotic translation elongation factor 2	Homo sapiens	26-30
7805855-6	1994	The lower affinity of phosphorylated EF-2 for GTP could be responsible for a weaker and/or incorrect interaction of the factor with the ribosome, in particular with the ricin-site of the 28-S rRNA assumed to be involved in translocation initiation.	Guanosine Triphosphate	46-49	eukaryotic translation elongation factor 2	Homo sapiens	37-41
1323554-3	1992	The present evidence indicates that EF2 prebound to ribosomes is protected from phosphorylation, just as earlier evidence indicated that ribosome-bound EF2 is protected from ADP-ribosylation catalysed by diphtheria toxin.	Adenosine Diphosphate	174-177	eukaryotic translation elongation factor 2	Homo sapiens	36-39
7898455-2	1994	The enzyme transfers ADP-ribose from NAD to elongation factor 2, inactivating the factor and thus inhibiting in vitro protein synthesis.	Adenosine Diphosphate Ribose	21-31	eukaryotic translation elongation factor 2	Homo sapiens	44-63
7898455-2	1994	The enzyme transfers ADP-ribose from NAD to elongation factor 2, inactivating the factor and thus inhibiting in vitro protein synthesis.	NAD	37-40	eukaryotic translation elongation factor 2	Homo sapiens	44-63
1420308-1	1992	Incubation of 80S ribosomes with a substoichiometric amount of [alpha-32P]GTP and with eEF-2 resulted in the specific labeling of one ribosomal protein which migrated very close to the position of the acidic phosphoprotein P2 from the 60S subunit in two-dimensional isofocusing-SDS gel electrophoresis.	Sodium Dodecyl Sulfate	278-281	eukaryotic translation elongation factor 2	Homo sapiens	87-92
1331687-6	1992	The phosphorylation of EF-2 in control and Alzheimer"s disease (AD) brain was directly measured as the distribution of the four polypeptides on silver stained 2D gels.	Silver	144-150	eukaryotic translation elongation factor 2	Homo sapiens	23-27
1621096-4	1992	The related (paralogous) genes encoding elongation factor EF-2 and initiation factor IF-2 also lacked the 11-amino acid insert.	11-amino acid	106-119	eukaryotic translation elongation factor 2	Homo sapiens	58-89
8307162-3	1994	The novel protein kinase inhibitor rottlerin is shown to suppress eEF-2 phosphorylation with an IC50 of 5.3 microM.	rottlerin	35-44	eukaryotic translation elongation factor 2	Homo sapiens	66-71
8412369-0	1993	Phorbol ester PMA stimulates protein synthesis and increases the levels of active elongation factors EF-1 alpha and EF-2 in ageing human fibroblasts.	phorbol ester pma	0-17	eukaryotic translation elongation factor 2	Homo sapiens	116-120
8412369-2	1993	We have observed that a phorbol ester PMA stimulates protein synthesis and increases the amounts of active elongation factors, EF-1 alpha and EF-2 in cultured human fibroblasts MRC-5 undergoing ageing.	phorbol ester pma	24-41	eukaryotic translation elongation factor 2	Homo sapiens	142-146
8318952-4	1993	At the same time, the disassembly of actin microfilaments by cytochalasin D results also in the disappearance of eEF-2- carrying threads.	Cytochalasin D	61-75	eukaryotic translation elongation factor 2	Homo sapiens	113-118
1400500-5	1992	After binding of eEF-2 in complex with the non-hydrolyzable GTP analogue guanosine 5"-(beta, gamma-methylene)-triphosphate, most of the exposed bases in the 5 S rRNA were protected against both chemical and enzymatic modification.	Guanosine Triphosphate	60-63	eukaryotic translation elongation factor 2	Homo sapiens	17-22
1400500-5	1992	After binding of eEF-2 in complex with the non-hydrolyzable GTP analogue guanosine 5"-(beta, gamma-methylene)-triphosphate, most of the exposed bases in the 5 S rRNA were protected against both chemical and enzymatic modification.	guanosine 5'-(beta,gamma-methylene)triphosphate	73-122	eukaryotic translation elongation factor 2	Homo sapiens	17-22
1511751-0	1992	Reduced puromycin sensitivity of translocated polysomes after the addition of elongation factor 2 and non-hydrolysable GTP analogues.	Puromycin	8-17	eukaryotic translation elongation factor 2	Homo sapiens	78-97
1511751-1	1992	Treatment of reticulocyte polysomes with elongation factor eEF-2 and GTP led to an increased sensitivity of peptidyl-tRNA for puromycin as a result of the translocation from the ribosomal A-site to the P-site.	Puromycin	126-135	eukaryotic translation elongation factor 2	Homo sapiens	59-64
1511751-4	1992	The data suggest either that peptidyl-tRNA had re-translocated back to the A-site due to the higher affinity of eEF-2 for the pre-translocation than for the post-translocation ribosome, or that the eEF-2-GuoPP[CH2]P complex blocks the peptidyl-transferase activity.	guopp[ch2	204-213	eukaryotic translation elongation factor 2	Homo sapiens	198-203
1323554-3	1992	The present evidence indicates that EF2 prebound to ribosomes is protected from phosphorylation, just as earlier evidence indicated that ribosome-bound EF2 is protected from ADP-ribosylation catalysed by diphtheria toxin.	Adenosine Diphosphate	174-177	eukaryotic translation elongation factor 2	Homo sapiens	152-155
1742357-2	1991	By this method we showed that unmodified EF-2 formed a stable complex with GDP but not with GTP, whereas phosphorylated EF-2 and ADP-ribosylated + phosphorylated EF-2 formed stable complexes even in the absence of irradiation, with GTP but not GDP.	Guanosine Triphosphate	232-235	eukaryotic translation elongation factor 2	Homo sapiens	41-45
1353910-1	1992	The histidine residue at position 715 of elongation factor 2 (EF-2) is posttranslationally modified in a series of enzymatic reactions to 2-[3-carboxyamido-3-(trimethylammonio)-propyl]histidine, which has been given the trivial name diphthamide.	Histidine	4-13	eukaryotic translation elongation factor 2	Homo sapiens	62-66
1353910-1	1992	The histidine residue at position 715 of elongation factor 2 (EF-2) is posttranslationally modified in a series of enzymatic reactions to 2-[3-carboxyamido-3-(trimethylammonio)-propyl]histidine, which has been given the trivial name diphthamide.	diphthamide	138-193	eukaryotic translation elongation factor 2	Homo sapiens	41-60
1353910-1	1992	The histidine residue at position 715 of elongation factor 2 (EF-2) is posttranslationally modified in a series of enzymatic reactions to 2-[3-carboxyamido-3-(trimethylammonio)-propyl]histidine, which has been given the trivial name diphthamide.	diphthamide	138-193	eukaryotic translation elongation factor 2	Homo sapiens	62-66
1353910-1	1992	The histidine residue at position 715 of elongation factor 2 (EF-2) is posttranslationally modified in a series of enzymatic reactions to 2-[3-carboxyamido-3-(trimethylammonio)-propyl]histidine, which has been given the trivial name diphthamide.	diphthamide	233-244	eukaryotic translation elongation factor 2	Homo sapiens	41-60
1353910-1	1992	The histidine residue at position 715 of elongation factor 2 (EF-2) is posttranslationally modified in a series of enzymatic reactions to 2-[3-carboxyamido-3-(trimethylammonio)-propyl]histidine, which has been given the trivial name diphthamide.	diphthamide	233-244	eukaryotic translation elongation factor 2	Homo sapiens	62-66
1353910-2	1992	The diphthamide residue of EF-2 is the target site for ADP ribosylation by diphtheria toxin and Pseudomonas exotoxin A. ADP-ribosylated EF-2 does not function in protein synthesis.	diphthamide	4-15	eukaryotic translation elongation factor 2	Homo sapiens	27-31
1353910-2	1992	The diphthamide residue of EF-2 is the target site for ADP ribosylation by diphtheria toxin and Pseudomonas exotoxin A. ADP-ribosylated EF-2 does not function in protein synthesis.	diphthamide	4-15	eukaryotic translation elongation factor 2	Homo sapiens	136-140
1353910-3	1992	EF-2 that has not been posttranslationally modified at histidine 715 is resistant to ADP ribosylation by these toxins.	Histidine	55-64	eukaryotic translation elongation factor 2	Homo sapiens	0-4
1353910-3	1992	EF-2 that has not been posttranslationally modified at histidine 715 is resistant to ADP ribosylation by these toxins.	Adenosine Diphosphate	85-88	eukaryotic translation elongation factor 2	Homo sapiens	0-4
1353910-4	1992	In this report we show that a G-to-A transition in the first position of codon 717 of the EF-2 gene results in substitution of arginine for glycine and prevents addition of the side chain of diphthamide to histidine 715 of EF-2.	Arginine	127-135	eukaryotic translation elongation factor 2	Homo sapiens	90-94
1353910-4	1992	In this report we show that a G-to-A transition in the first position of codon 717 of the EF-2 gene results in substitution of arginine for glycine and prevents addition of the side chain of diphthamide to histidine 715 of EF-2.	Arginine	127-135	eukaryotic translation elongation factor 2	Homo sapiens	223-227
1353910-4	1992	In this report we show that a G-to-A transition in the first position of codon 717 of the EF-2 gene results in substitution of arginine for glycine and prevents addition of the side chain of diphthamide to histidine 715 of EF-2.	Glycine	140-147	eukaryotic translation elongation factor 2	Homo sapiens	90-94
1353910-4	1992	In this report we show that a G-to-A transition in the first position of codon 717 of the EF-2 gene results in substitution of arginine for glycine and prevents addition of the side chain of diphthamide to histidine 715 of EF-2.	Glycine	140-147	eukaryotic translation elongation factor 2	Homo sapiens	223-227
1353910-4	1992	In this report we show that a G-to-A transition in the first position of codon 717 of the EF-2 gene results in substitution of arginine for glycine and prevents addition of the side chain of diphthamide to histidine 715 of EF-2.	diphthamide	191-202	eukaryotic translation elongation factor 2	Homo sapiens	90-94
1353910-4	1992	In this report we show that a G-to-A transition in the first position of codon 717 of the EF-2 gene results in substitution of arginine for glycine and prevents addition of the side chain of diphthamide to histidine 715 of EF-2.	diphthamide	191-202	eukaryotic translation elongation factor 2	Homo sapiens	223-227
1353910-4	1992	In this report we show that a G-to-A transition in the first position of codon 717 of the EF-2 gene results in substitution of arginine for glycine and prevents addition of the side chain of diphthamide to histidine 715 of EF-2.	Histidine	206-215	eukaryotic translation elongation factor 2	Homo sapiens	90-94
1353910-4	1992	In this report we show that a G-to-A transition in the first position of codon 717 of the EF-2 gene results in substitution of arginine for glycine and prevents addition of the side chain of diphthamide to histidine 715 of EF-2.	Histidine	206-215	eukaryotic translation elongation factor 2	Homo sapiens	223-227
1730643-9	1992	In addition, yeast and mammalian EF-2 share identical sequences at two critical functional sites: (i) the domain containing the histidine residue that is modified to diphthamide and (ii) the threonine residue that is specifically phosphorylated in vivo in mammalian cells by calmodulin-dependent protein kinase III, also known as EF-2 kinase.	Histidine	128-137	eukaryotic translation elongation factor 2	Homo sapiens	33-37
1730643-9	1992	In addition, yeast and mammalian EF-2 share identical sequences at two critical functional sites: (i) the domain containing the histidine residue that is modified to diphthamide and (ii) the threonine residue that is specifically phosphorylated in vivo in mammalian cells by calmodulin-dependent protein kinase III, also known as EF-2 kinase.	diphthamide	166-177	eukaryotic translation elongation factor 2	Homo sapiens	33-37
1730643-9	1992	In addition, yeast and mammalian EF-2 share identical sequences at two critical functional sites: (i) the domain containing the histidine residue that is modified to diphthamide and (ii) the threonine residue that is specifically phosphorylated in vivo in mammalian cells by calmodulin-dependent protein kinase III, also known as EF-2 kinase.	Threonine	191-200	eukaryotic translation elongation factor 2	Homo sapiens	33-37
1519762-0	1992	High-resolution one-dimensional polyacrylamide gel isoelectric focusing of various forms of elongation factor-2.	polyacrylamide	32-46	eukaryotic translation elongation factor 2	Homo sapiens	92-111
1519762-1	1992	A system for analyzing covalent modifications of elongation factor-2 (eEF-2) by one-dimensional isoelectric focusing in slab polyacrylamide gels is described.	polyacrylamide	125-139	eukaryotic translation elongation factor 2	Homo sapiens	49-68
1519762-1	1992	A system for analyzing covalent modifications of elongation factor-2 (eEF-2) by one-dimensional isoelectric focusing in slab polyacrylamide gels is described.	polyacrylamide	125-139	eukaryotic translation elongation factor 2	Homo sapiens	70-75
1353910-0	1992	A mutation in codon 717 of the CHO-K1 elongation factor 2 gene prevents the first step in the biosynthesis of diphthamide.	diphthamide	110-121	eukaryotic translation elongation factor 2	Homo sapiens	38-57
1353910-1	1992	The histidine residue at position 715 of elongation factor 2 (EF-2) is posttranslationally modified in a series of enzymatic reactions to 2-[3-carboxyamido-3-(trimethylammonio)-propyl]histidine, which has been given the trivial name diphthamide.	Histidine	4-13	eukaryotic translation elongation factor 2	Homo sapiens	41-60
1742357-0	1991	Effect of ADP-ribosylation and phosphorylation on the interaction of elongation factor 2 with guanylic nucleotides.	Adenosine Diphosphate	10-13	eukaryotic translation elongation factor 2	Homo sapiens	69-88
1742357-2	1991	By this method we showed that unmodified EF-2 formed a stable complex with GDP but not with GTP, whereas phosphorylated EF-2 and ADP-ribosylated + phosphorylated EF-2 formed stable complexes even in the absence of irradiation, with GTP but not GDP.	Guanosine Diphosphate	75-78	eukaryotic translation elongation factor 2	Homo sapiens	41-45
1742357-2	1991	By this method we showed that unmodified EF-2 formed a stable complex with GDP but not with GTP, whereas phosphorylated EF-2 and ADP-ribosylated + phosphorylated EF-2 formed stable complexes even in the absence of irradiation, with GTP but not GDP.	Guanosine Triphosphate	232-235	eukaryotic translation elongation factor 2	Homo sapiens	120-124
1742357-2	1991	By this method we showed that unmodified EF-2 formed a stable complex with GDP but not with GTP, whereas phosphorylated EF-2 and ADP-ribosylated + phosphorylated EF-2 formed stable complexes even in the absence of irradiation, with GTP but not GDP.	Guanosine Triphosphate	232-235	eukaryotic translation elongation factor 2	Homo sapiens	120-124
1742357-2	1991	By this method we showed that unmodified EF-2 formed a stable complex with GDP but not with GTP, whereas phosphorylated EF-2 and ADP-ribosylated + phosphorylated EF-2 formed stable complexes even in the absence of irradiation, with GTP but not GDP.	Guanosine Diphosphate	244-247	eukaryotic translation elongation factor 2	Homo sapiens	41-45
1742357-2	1991	By this method we showed that unmodified EF-2 formed a stable complex with GDP but not with GTP, whereas phosphorylated EF-2 and ADP-ribosylated + phosphorylated EF-2 formed stable complexes even in the absence of irradiation, with GTP but not GDP.	Guanosine Diphosphate	244-247	eukaryotic translation elongation factor 2	Homo sapiens	120-124
1742357-2	1991	By this method we showed that unmodified EF-2 formed a stable complex with GDP but not with GTP, whereas phosphorylated EF-2 and ADP-ribosylated + phosphorylated EF-2 formed stable complexes even in the absence of irradiation, with GTP but not GDP.	Guanosine Diphosphate	244-247	eukaryotic translation elongation factor 2	Homo sapiens	120-124
1742357-4	1991	Prior ADP-ribosylation of EF-2 increased its ability to the phosphorylated.	Adenosine Diphosphate	6-9	eukaryotic translation elongation factor 2	Homo sapiens	26-30
1742357-5	1991	These results show that the structures of the two domains containing diphtamide 715 and the phosphorylatable threonines (between Ala 51 and Arg 60) are interdependent; modifications of these residues induce different conformational changes of EF-2 which alter the interactions of the factor with guanylic nucleotides as well with ribosomes.	diphtamide	69-79	eukaryotic translation elongation factor 2	Homo sapiens	243-247
1742357-5	1991	These results show that the structures of the two domains containing diphtamide 715 and the phosphorylatable threonines (between Ala 51 and Arg 60) are interdependent; modifications of these residues induce different conformational changes of EF-2 which alter the interactions of the factor with guanylic nucleotides as well with ribosomes.	Threonine	109-119	eukaryotic translation elongation factor 2	Homo sapiens	243-247
1742357-5	1991	These results show that the structures of the two domains containing diphtamide 715 and the phosphorylatable threonines (between Ala 51 and Arg 60) are interdependent; modifications of these residues induce different conformational changes of EF-2 which alter the interactions of the factor with guanylic nucleotides as well with ribosomes.	Alanine	129-132	eukaryotic translation elongation factor 2	Homo sapiens	243-247
1742357-5	1991	These results show that the structures of the two domains containing diphtamide 715 and the phosphorylatable threonines (between Ala 51 and Arg 60) are interdependent; modifications of these residues induce different conformational changes of EF-2 which alter the interactions of the factor with guanylic nucleotides as well with ribosomes.	Arginine	140-143	eukaryotic translation elongation factor 2	Homo sapiens	243-247
2037599-1	1991	We have used variations in the trypsin sensitivity of eukaryotic protein synthesis elongation factor 2 (eEF-2) to probe for structural alterations induced by phosphorylation, ribosomal binding, or guanosine nucleotides.	guanosine nucleotides	197-218	eukaryotic translation elongation factor 2	Homo sapiens	54-102
2037599-1	1991	We have used variations in the trypsin sensitivity of eukaryotic protein synthesis elongation factor 2 (eEF-2) to probe for structural alterations induced by phosphorylation, ribosomal binding, or guanosine nucleotides.	guanosine nucleotides	197-218	eukaryotic translation elongation factor 2	Homo sapiens	104-109
34715032-0	2021	Safety, pharmacokinetics, and antimalarial activity of the novel plasmodium eukaryotic translation elongation factor 2 inhibitor M5717: a first-in-human, randomised, placebo-controlled, double-blind, single ascending dose study and volunteer infection study.	DDD107498	129-134	eukaryotic translation elongation factor 2	Homo sapiens	76-118
1989969-7	1991	This effect resulted from inhibition of the binding of elongation factors EF-1 alpha and EF-2 to ribosomes and of the associated GTP hydrolysis.	Guanosine Triphosphate	129-132	eukaryotic translation elongation factor 2	Homo sapiens	89-93
2311763-1	1990	Elongation factor 2 (EF-2), ADP-ribosylated in vitro by the A-fragment of diphtheria toxin, can (in the presence of GMPPCP) form stable complexes with ribosomes regardless of whether the ribosomes are empty or carrying poly(U) and Phe-tRNA in the A-site.	5'-guanylylmethylenebisphosphonate	116-122	eukaryotic translation elongation factor 2	Homo sapiens	0-19
2311763-1	1990	Elongation factor 2 (EF-2), ADP-ribosylated in vitro by the A-fragment of diphtheria toxin, can (in the presence of GMPPCP) form stable complexes with ribosomes regardless of whether the ribosomes are empty or carrying poly(U) and Phe-tRNA in the A-site.	5'-guanylylmethylenebisphosphonate	116-122	eukaryotic translation elongation factor 2	Homo sapiens	21-25
2311763-1	1990	Elongation factor 2 (EF-2), ADP-ribosylated in vitro by the A-fragment of diphtheria toxin, can (in the presence of GMPPCP) form stable complexes with ribosomes regardless of whether the ribosomes are empty or carrying poly(U) and Phe-tRNA in the A-site.	Poly U	219-226	eukaryotic translation elongation factor 2	Homo sapiens	0-19
2311763-1	1990	Elongation factor 2 (EF-2), ADP-ribosylated in vitro by the A-fragment of diphtheria toxin, can (in the presence of GMPPCP) form stable complexes with ribosomes regardless of whether the ribosomes are empty or carrying poly(U) and Phe-tRNA in the A-site.	Poly U	219-226	eukaryotic translation elongation factor 2	Homo sapiens	21-25
2311763-1	1990	Elongation factor 2 (EF-2), ADP-ribosylated in vitro by the A-fragment of diphtheria toxin, can (in the presence of GMPPCP) form stable complexes with ribosomes regardless of whether the ribosomes are empty or carrying poly(U) and Phe-tRNA in the A-site.	Phenylalanine	231-234	eukaryotic translation elongation factor 2	Homo sapiens	0-19
2311763-1	1990	Elongation factor 2 (EF-2), ADP-ribosylated in vitro by the A-fragment of diphtheria toxin, can (in the presence of GMPPCP) form stable complexes with ribosomes regardless of whether the ribosomes are empty or carrying poly(U) and Phe-tRNA in the A-site.	Phenylalanine	231-234	eukaryotic translation elongation factor 2	Homo sapiens	21-25
2244994-4	1990	The 95% limits of agreement between Ionometer EF2 and flame photometry were for potassium -0.29 and 0.43 mmol/l and for sodium -5.0 and 2.89 mmol/l, respectively.	Potassium	80-89	eukaryotic translation elongation factor 2	Homo sapiens	46-49
2318846-1	1990	The effect of ADP-ribosylation on the function of eukaryotic elongation factor 2 (EF-2) was investigated by kinetic analysis of the EF-2-catalyzed hydrolysis of GTP in the presence of ribosomes and by direct determination of the affinity of the modified factor for the ribosome.	Adenosine Diphosphate	14-17	eukaryotic translation elongation factor 2	Homo sapiens	61-80
2318846-1	1990	The effect of ADP-ribosylation on the function of eukaryotic elongation factor 2 (EF-2) was investigated by kinetic analysis of the EF-2-catalyzed hydrolysis of GTP in the presence of ribosomes and by direct determination of the affinity of the modified factor for the ribosome.	Adenosine Diphosphate	14-17	eukaryotic translation elongation factor 2	Homo sapiens	82-86
2318846-1	1990	The effect of ADP-ribosylation on the function of eukaryotic elongation factor 2 (EF-2) was investigated by kinetic analysis of the EF-2-catalyzed hydrolysis of GTP in the presence of ribosomes and by direct determination of the affinity of the modified factor for the ribosome.	Adenosine Diphosphate	14-17	eukaryotic translation elongation factor 2	Homo sapiens	132-136
2318846-1	1990	The effect of ADP-ribosylation on the function of eukaryotic elongation factor 2 (EF-2) was investigated by kinetic analysis of the EF-2-catalyzed hydrolysis of GTP in the presence of ribosomes and by direct determination of the affinity of the modified factor for the ribosome.	Guanosine Triphosphate	161-164	eukaryotic translation elongation factor 2	Homo sapiens	61-80
2318846-1	1990	The effect of ADP-ribosylation on the function of eukaryotic elongation factor 2 (EF-2) was investigated by kinetic analysis of the EF-2-catalyzed hydrolysis of GTP in the presence of ribosomes and by direct determination of the affinity of the modified factor for the ribosome.	Guanosine Triphosphate	161-164	eukaryotic translation elongation factor 2	Homo sapiens	82-86
2318846-1	1990	The effect of ADP-ribosylation on the function of eukaryotic elongation factor 2 (EF-2) was investigated by kinetic analysis of the EF-2-catalyzed hydrolysis of GTP in the presence of ribosomes and by direct determination of the affinity of the modified factor for the ribosome.	Guanosine Triphosphate	161-164	eukaryotic translation elongation factor 2	Homo sapiens	132-136
2318846-2	1990	Under conditions where the concentration of EF-2 was rate-limiting, the ADP-ribosylation reduced the maximum rate of GTP hydrolysis and the second order rate constant Kcat/Km by approximately 50%.	Adenosine Diphosphate	72-75	eukaryotic translation elongation factor 2	Homo sapiens	44-48
2318846-2	1990	Under conditions where the concentration of EF-2 was rate-limiting, the ADP-ribosylation reduced the maximum rate of GTP hydrolysis and the second order rate constant Kcat/Km by approximately 50%.	Guanosine Triphosphate	117-120	eukaryotic translation elongation factor 2	Homo sapiens	44-48
2318846-4	1990	The affinity of EF-2 for the pretranslocation type of ribosomes was reduced by 2 orders of magnitude after ADP-ribosylation.	Adenosine Diphosphate	107-110	eukaryotic translation elongation factor 2	Homo sapiens	16-20
34853469-3	2021	Although numerous studies point to critical roles for both the conserved eukaryotic posttranslational modification diphthamide in eEF2 and tRNA modifications in supporting the accuracy of translocation, detailed molecular mechanisms describing their specific functions are poorly understood.	diphthamide	115-126	eukaryotic translation elongation factor 2	Homo sapiens	130-134
35609420-0	2022	The natural bicyclic hexapeptide RA-VII is a novel inhibitor of the eukaryotic translocase eEF2.	RA VII	33-39	eukaryotic translation elongation factor 2	Homo sapiens	91-95
34767248-6	2022	Sordarin inhibits protein synthesis at the elongation step of the translational cycle, acting on eukaryotic translation elongation factor 2.	sordarin	0-8	eukaryotic translation elongation factor 2	Homo sapiens	97-139
34507998-1	2021	Diphthamide, a modification found only on translation elongation factor 2 (EF2), was proposed to suppress -1 frameshifting in translation.	diphthamide	0-11	eukaryotic translation elongation factor 2	Homo sapiens	75-78
34107382-5	2021	Pioglitazone was able to also protect against high glucose-induced elevations in maladaptive ER stress markers and increase the adaptive unfolded protein response (UPR) by inhibiting mTORC1-eEF2 protein translation machinery.	Pioglitazone	0-12	eukaryotic translation elongation factor 2	Homo sapiens	190-194
35609420-4	2022	Biochemical functional assays showed that RA-VII inhibits poly(U)-dependent polyphenylalanine synthesis in the presence of animal elongation factors eEF1A and eEF2.	RA VII	42-48	eukaryotic translation elongation factor 2	Homo sapiens	159-163
35609420-4	2022	Biochemical functional assays showed that RA-VII inhibits poly(U)-dependent polyphenylalanine synthesis in the presence of animal elongation factors eEF1A and eEF2.	Poly U	58-65	eukaryotic translation elongation factor 2	Homo sapiens	159-163
35609420-4	2022	Biochemical functional assays showed that RA-VII inhibits poly(U)-dependent polyphenylalanine synthesis in the presence of animal elongation factors eEF1A and eEF2.	polyphenylalanine	76-93	eukaryotic translation elongation factor 2	Homo sapiens	159-163
35609420-6	2022	A filter binding assay demonstrated that RA-VII markedly enhances the binding affinity of eEF2 for GTP, but not for GDP, and prevents exchange of GTP in the eEF2-GTP complex, even after addition of a large excess of GTP/GDP.	Radium	41-43	eukaryotic translation elongation factor 2	Homo sapiens	90-94
35609420-6	2022	A filter binding assay demonstrated that RA-VII markedly enhances the binding affinity of eEF2 for GTP, but not for GDP, and prevents exchange of GTP in the eEF2-GTP complex, even after addition of a large excess of GTP/GDP.	Radium	41-43	eukaryotic translation elongation factor 2	Homo sapiens	157-161
35609420-6	2022	A filter binding assay demonstrated that RA-VII markedly enhances the binding affinity of eEF2 for GTP, but not for GDP, and prevents exchange of GTP in the eEF2-GTP complex, even after addition of a large excess of GTP/GDP.	Guanosine Triphosphate	99-102	eukaryotic translation elongation factor 2	Homo sapiens	90-94
35609420-6	2022	A filter binding assay demonstrated that RA-VII markedly enhances the binding affinity of eEF2 for GTP, but not for GDP, and prevents exchange of GTP in the eEF2-GTP complex, even after addition of a large excess of GTP/GDP.	Guanosine Triphosphate	146-149	eukaryotic translation elongation factor 2	Homo sapiens	157-161
35609420-6	2022	A filter binding assay demonstrated that RA-VII markedly enhances the binding affinity of eEF2 for GTP, but not for GDP, and prevents exchange of GTP in the eEF2-GTP complex, even after addition of a large excess of GTP/GDP.	Guanosine Triphosphate	162-165	eukaryotic translation elongation factor 2	Homo sapiens	157-161
35609420-6	2022	A filter binding assay demonstrated that RA-VII markedly enhances the binding affinity of eEF2 for GTP, but not for GDP, and prevents exchange of GTP in the eEF2-GTP complex, even after addition of a large excess of GTP/GDP.	Guanosine Triphosphate	216-219	eukaryotic translation elongation factor 2	Homo sapiens	90-94
35609420-6	2022	A filter binding assay demonstrated that RA-VII markedly enhances the binding affinity of eEF2 for GTP, but not for GDP, and prevents exchange of GTP in the eEF2-GTP complex, even after addition of a large excess of GTP/GDP.	Guanosine Triphosphate	216-219	eukaryotic translation elongation factor 2	Homo sapiens	157-161
35609420-6	2022	A filter binding assay demonstrated that RA-VII markedly enhances the binding affinity of eEF2 for GTP, but not for GDP, and prevents exchange of GTP in the eEF2-GTP complex, even after addition of a large excess of GTP/GDP.	Guanosine Diphosphate	220-223	eukaryotic translation elongation factor 2	Homo sapiens	90-94
35609420-6	2022	A filter binding assay demonstrated that RA-VII markedly enhances the binding affinity of eEF2 for GTP, but not for GDP, and prevents exchange of GTP in the eEF2-GTP complex, even after addition of a large excess of GTP/GDP.	Guanosine Diphosphate	220-223	eukaryotic translation elongation factor 2	Homo sapiens	157-161
35609420-7	2022	Limited proteolysis experiments indicated that RA-VII prevents the digestion of eEF2 in the presence of either GTP or GMPPCP, but not with GDP.	RA VII	47-53	eukaryotic translation elongation factor 2	Homo sapiens	80-84
35609420-7	2022	Limited proteolysis experiments indicated that RA-VII prevents the digestion of eEF2 in the presence of either GTP or GMPPCP, but not with GDP.	Guanosine Triphosphate	111-114	eukaryotic translation elongation factor 2	Homo sapiens	80-84
35609420-7	2022	Limited proteolysis experiments indicated that RA-VII prevents the digestion of eEF2 in the presence of either GTP or GMPPCP, but not with GDP.	5'-guanylylmethylenebisphosphonate	118-124	eukaryotic translation elongation factor 2	Homo sapiens	80-84
35609420-9	2022	These results suggest that RA-VII tightly stabilizes the GTP eEF2 complex structure, which is able to bind to the ribosomal functional site, but seems to suppress normal turnover of eEF2 after translocation.	Radium	27-29	eukaryotic translation elongation factor 2	Homo sapiens	61-65
35609420-9	2022	These results suggest that RA-VII tightly stabilizes the GTP eEF2 complex structure, which is able to bind to the ribosomal functional site, but seems to suppress normal turnover of eEF2 after translocation.	Radium	27-29	eukaryotic translation elongation factor 2	Homo sapiens	182-186
35609420-9	2022	These results suggest that RA-VII tightly stabilizes the GTP eEF2 complex structure, which is able to bind to the ribosomal functional site, but seems to suppress normal turnover of eEF2 after translocation.	Guanosine Triphosphate	57-60	eukaryotic translation elongation factor 2	Homo sapiens	61-65
35609420-9	2022	These results suggest that RA-VII tightly stabilizes the GTP eEF2 complex structure, which is able to bind to the ribosomal functional site, but seems to suppress normal turnover of eEF2 after translocation.	Guanosine Triphosphate	57-60	eukaryotic translation elongation factor 2	Homo sapiens	182-186
35609420-10	2022	The properties of RA-VII make it a novel ligand for probing the action of eEF2 in the process of translocation on the ribosome.	Radium	18-21	eukaryotic translation elongation factor 2	Homo sapiens	74-78
35176139-6	2022	Furthermore, the interaction of LDHA and eEF2 was dependent on NADH, a coenzyme of LDHA.	NAD	63-67	eukaryotic translation elongation factor 2	Homo sapiens	41-45
35176139-7	2022	NADH-competitive inhibitors of LDHA could release eEF2 from the LDHA pool, up-regulate translation and enhance MK maturation in vitro.	NAD	0-4	eukaryotic translation elongation factor 2	Homo sapiens	50-54