PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
22772751-4	2012	Regarding the partial reactions catalysed by SsEF-1alpha the effect produced by ppGpp on the affinity for aa-tRNA was lower than that measured in the presence of GTP but higher than that for GDP.	Guanosine Triphosphate	162-165	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	45-56
22772751-4	2012	Regarding the partial reactions catalysed by SsEF-1alpha the effect produced by ppGpp on the affinity for aa-tRNA was lower than that measured in the presence of GTP but higher than that for GDP.	Guanosine Diphosphate	191-194	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	45-56
22772751-6	2012	Furthermore, ppGpp inhibited the intrinsic GTPase of SsEF-1alpha with a competitive behaviour.	Guanosine Tetraphosphate	13-18	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	53-64
18267133-3	2008	Thermal denaturation of both the GDP-bound (SsEF-1 alpha*.GDP) and the ligand-free (nfSsEF-1 alpha) forms was investigated by means of circular dichroism and fluorescence measurements, over the 4.0-7.5 pH interval.	Guanosine Diphosphate	33-36	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	44-56
19375481-4	2009	The affinity for guanosine nucleotides was almost identical to that exhibited by wild-type SsEF-1alpha; vice versa, the GDP exchange rate was one order of magnitude faster on the mutated elongation factor, a property partially restored when the exchange reaction was analysed in the presence of the magnesium ions chelating agent EDTA.	guanosine nucleotides	17-38	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	91-102
19375481-4	2009	The affinity for guanosine nucleotides was almost identical to that exhibited by wild-type SsEF-1alpha; vice versa, the GDP exchange rate was one order of magnitude faster on the mutated elongation factor, a property partially restored when the exchange reaction was analysed in the presence of the magnesium ions chelating agent EDTA.	Magnesium	299-308	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	91-102
19375481-4	2009	The affinity for guanosine nucleotides was almost identical to that exhibited by wild-type SsEF-1alpha; vice versa, the GDP exchange rate was one order of magnitude faster on the mutated elongation factor, a property partially restored when the exchange reaction was analysed in the presence of the magnesium ions chelating agent EDTA.	Edetic Acid	330-334	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	91-102
21924318-1	2012	The effect of pulvomycin on the biochemical and fluorescence spectroscopic properties of the archaeal elongation factor 1alpha from Sulfolobus solfataricus (SsEF-1alpha), the functional analog of eubacterial EF-Tu, was investigated.	pulvomycin	14-24	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	157-168
21924318-3	2012	The effect of the antibiotic on the partial reactions catalysed by SsEF-1alpha indicated that pulvomycin was able to decrease the affinity of the elongation factor toward aa-tRNA only in the presence of GTP, to an extent similar to that measured in the presence of GDP.	pulvomycin	94-104	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	67-78
21924318-7	2012	This finding was confirmed by the protection against chemical denaturation of SsEF-1alpha, observed in the presence of pulvomycin.	pulvomycin	119-129	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	78-89
16411747-2	2006	Indeed, the atypical shape of the protein structure and the unusual living conditions of the host organism prompted us to analyze the effect of urea and guanidine hydrochloride (GuHCl) on the GDP complex of the enzyme (SsEF-1alpha x GDP) by fluorescence and circular dichroism.	Urea	144-148	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	219-230
16411747-2	2006	Indeed, the atypical shape of the protein structure and the unusual living conditions of the host organism prompted us to analyze the effect of urea and guanidine hydrochloride (GuHCl) on the GDP complex of the enzyme (SsEF-1alpha x GDP) by fluorescence and circular dichroism.	Guanidine	153-176	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	219-230
16411747-2	2006	Indeed, the atypical shape of the protein structure and the unusual living conditions of the host organism prompted us to analyze the effect of urea and guanidine hydrochloride (GuHCl) on the GDP complex of the enzyme (SsEF-1alpha x GDP) by fluorescence and circular dichroism.	Guanidine	178-183	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	219-230
16411747-2	2006	Indeed, the atypical shape of the protein structure and the unusual living conditions of the host organism prompted us to analyze the effect of urea and guanidine hydrochloride (GuHCl) on the GDP complex of the enzyme (SsEF-1alpha x GDP) by fluorescence and circular dichroism.	Guanosine Diphosphate	192-195	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	219-230
16411747-2	2006	Indeed, the atypical shape of the protein structure and the unusual living conditions of the host organism prompted us to analyze the effect of urea and guanidine hydrochloride (GuHCl) on the GDP complex of the enzyme (SsEF-1alpha x GDP) by fluorescence and circular dichroism.	Guanosine Diphosphate	233-236	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	219-230
16411747-5	2006	Moreover, the chemically induced unfolding process of both SsEF-1alpha x GDP and nfSsEF-1alpha is fully reversible.	Guanosine Diphosphate	73-76	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	59-70
16411747-6	2006	Both SsEF-1alpha forms exhibit remarkable stability against urea, but they do not display a strong resistance to the denaturing action of GuHCl.	Urea	60-64	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	5-16
16407071-5	2006	Conformations of the two switch regions involved in GTP binding are similar to those encountered in an EF1A:GTP:Phe-tRNA(Phe) complex.	Guanosine Triphosphate	52-55	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	103-107
16407071-5	2006	Conformations of the two switch regions involved in GTP binding are similar to those encountered in an EF1A:GTP:Phe-tRNA(Phe) complex.	Guanosine Triphosphate	108-111	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	103-107
16407071-5	2006	Conformations of the two switch regions involved in GTP binding are similar to those encountered in an EF1A:GTP:Phe-tRNA(Phe) complex.	Phenylalanine	112-115	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	103-107
16407071-5	2006	Conformations of the two switch regions involved in GTP binding are similar to those encountered in an EF1A:GTP:Phe-tRNA(Phe) complex.	Phenylalanine	121-124	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	103-107
15157096-5	2004	Furthermore, nucleotide exchange experiments carried out on a truncated form of SsEF-1alpha, consisting only of the nucleotide binding domain, demonstrate that the low affinity of SsEF-1alpha.GDP for Mg(2+) is due to the local architecture of the active site and does not depend on the presence of the other two domains.	Guanosine Diphosphate	192-195	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	180-191
15290325-1	2004	The thiazolyl-peptide antibiotic GE2270A, an inhibitor of the elongation factor Tu from Escherichia coli (EcEF-Tu), was used to study the effects produced in the biochemical properties of the archaeal functional analogue elongation factor 1alpha from Sulfolobus solfataricus (SsEF-1alpha).	thiazolyl	4-13	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	276-287
15290325-2	2004	GE2270A did not substantially affect the poly(U)-directed-polyPhe incorporation catalyzed by SsEF-1alpha and the formation of the ternary complex SsEF-1alpha.GTP.Phe-tRNAPhe.	Guanosine Triphosphate	158-161	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	146-157
15290325-2	2004	GE2270A did not substantially affect the poly(U)-directed-polyPhe incorporation catalyzed by SsEF-1alpha and the formation of the ternary complex SsEF-1alpha.GTP.Phe-tRNAPhe.	phe-trnaphe	162-173	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	146-157
15290325-3	2004	On the other hand, the antibiotic was able to increase the GDP/GTP exchange rate of SsEF-1alpha; nevertheless, this improvement was not associated with an increase in the catalytic activity of the enzyme.	Guanosine Diphosphate	59-62	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	84-95
15290325-3	2004	On the other hand, the antibiotic was able to increase the GDP/GTP exchange rate of SsEF-1alpha; nevertheless, this improvement was not associated with an increase in the catalytic activity of the enzyme.	Guanosine Triphosphate	63-66	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	84-95
15157096-2	2004	Along this line, it has been demonstrated that, in contrast to EF-Tu, Sulfolobus solfataricus EF-1alpha in complex with GDP (SsEF-1alpha.GDP) does not bind Mg(2+), when the ion is present in the crystallization medium at moderate concentration (5 mM).	Guanosine Diphosphate	120-123	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	94-103
15157096-2	2004	Along this line, it has been demonstrated that, in contrast to EF-Tu, Sulfolobus solfataricus EF-1alpha in complex with GDP (SsEF-1alpha.GDP) does not bind Mg(2+), when the ion is present in the crystallization medium at moderate concentration (5 mM).	Guanosine Diphosphate	120-123	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	125-136
15157096-2	2004	Along this line, it has been demonstrated that, in contrast to EF-Tu, Sulfolobus solfataricus EF-1alpha in complex with GDP (SsEF-1alpha.GDP) does not bind Mg(2+), when the ion is present in the crystallization medium at moderate concentration (5 mM).	Guanosine Diphosphate	137-140	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	94-103
15157096-2	2004	Along this line, it has been demonstrated that, in contrast to EF-Tu, Sulfolobus solfataricus EF-1alpha in complex with GDP (SsEF-1alpha.GDP) does not bind Mg(2+), when the ion is present in the crystallization medium at moderate concentration (5 mM).	Guanosine Diphosphate	137-140	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	125-136
15157096-3	2004	To further investigate the role that magnesium plays in the exchange process of EF-1alpha and to check the ability of SsEF-1alpha.GDP to bind the ion, we have determined the crystal structure of SsEF-1alpha.GDP in the presence of a nonphysiological concentration (100 mM) of Mg(2+).	Magnesium	37-46	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	80-89
15157096-3	2004	To further investigate the role that magnesium plays in the exchange process of EF-1alpha and to check the ability of SsEF-1alpha.GDP to bind the ion, we have determined the crystal structure of SsEF-1alpha.GDP in the presence of a nonphysiological concentration (100 mM) of Mg(2+).	Magnesium	37-46	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	195-206
15157096-3	2004	To further investigate the role that magnesium plays in the exchange process of EF-1alpha and to check the ability of SsEF-1alpha.GDP to bind the ion, we have determined the crystal structure of SsEF-1alpha.GDP in the presence of a nonphysiological concentration (100 mM) of Mg(2+).	Guanosine Diphosphate	130-133	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	118-129
15157096-3	2004	To further investigate the role that magnesium plays in the exchange process of EF-1alpha and to check the ability of SsEF-1alpha.GDP to bind the ion, we have determined the crystal structure of SsEF-1alpha.GDP in the presence of a nonphysiological concentration (100 mM) of Mg(2+).	Guanosine Diphosphate	130-133	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	195-206
15157096-3	2004	To further investigate the role that magnesium plays in the exchange process of EF-1alpha and to check the ability of SsEF-1alpha.GDP to bind the ion, we have determined the crystal structure of SsEF-1alpha.GDP in the presence of a nonphysiological concentration (100 mM) of Mg(2+).	Guanosine Diphosphate	207-210	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	118-129
15157096-3	2004	To further investigate the role that magnesium plays in the exchange process of EF-1alpha and to check the ability of SsEF-1alpha.GDP to bind the ion, we have determined the crystal structure of SsEF-1alpha.GDP in the presence of a nonphysiological concentration (100 mM) of Mg(2+).	Guanosine Diphosphate	207-210	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	195-206
15157096-5	2004	Furthermore, nucleotide exchange experiments carried out on a truncated form of SsEF-1alpha, consisting only of the nucleotide binding domain, demonstrate that the low affinity of SsEF-1alpha.GDP for Mg(2+) is due to the local architecture of the active site and does not depend on the presence of the other two domains.	Guanosine Diphosphate	192-195	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	80-91
15157096-5	2004	Furthermore, nucleotide exchange experiments carried out on a truncated form of SsEF-1alpha, consisting only of the nucleotide binding domain, demonstrate that the low affinity of SsEF-1alpha.GDP for Mg(2+) is due to the local architecture of the active site and does not depend on the presence of the other two domains.	magnesium ion	200-206	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	80-91
15157096-5	2004	Furthermore, nucleotide exchange experiments carried out on a truncated form of SsEF-1alpha, consisting only of the nucleotide binding domain, demonstrate that the low affinity of SsEF-1alpha.GDP for Mg(2+) is due to the local architecture of the active site and does not depend on the presence of the other two domains.	magnesium ion	200-206	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	180-191
12463746-1	2002	Valine 114 in the D(109)AAILVVA sequence of elongation factor 1alpha from the archaeon Sulfolobus solfataricus (SsEF-1alpha) was substituted with an acidic (V114E), basic (V114K), or cavity-forming (V114A) residue, and the effects on the biochemical properties of the factor were investigated.	Valine	0-6	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	112-123
12463746-2	2002	This sequence is well-conserved among most of eukaryal and eubacterial counterparts, and in the three-dimensional structure of SsEF-1alpha, V114 is located in a hydrophobic pocket near the first GDP-binding consensus sequence G(13)XXXXGK[T,S] [Vitagliano, L., Masullo, M., Sica, F., Zagari, A., and Bocchini, V. (2001) EMBO J.	Guanosine Diphosphate	195-198	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	127-138
12463746-5	2002	In fact, although they exhibited a rate in poly(Phe) incorporation almost identical to that of SsEF-1alpha, V114K and V114A exhibited an affinity for GDP and GTP higher and a capability to bind heterologous aa-tRNA stronger than that elicited by SsEF-1alpha but similar to that of eubacterial EF-Tu.	Guanosine Triphosphate	158-161	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	95-106
12463746-8	2002	Interestingly, the decreased intrinsic GTPase activity of V114E was partially restored by kirromycin, an effect already observed for the G13A mutant of SsEF-1alpha [Masullo, M., Cantiello, P., de Paola, B., Catanzano, F., Arcari, P., and Bocchini, V. (2002) Biochemistry 41, 628-633].	mocimycin	90-100	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	152-163
11683622-1	2001	Elongation factor 1alpha from the hyperthermophilic archaeon Sulfolobus solfataricus (SsEF-1alpha) carries the aminoacyl tRNA to the ribosome; it binds GDP or GTP, and it is also endowed with an intrinsic GTPase activity that is triggered in vitro by NaCl at molar concentrations [Masullo, M., De Vendittis, E., and Bocchini, V. (1994) J. Biol.	Guanosine Diphosphate	152-155	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	86-97
11781103-10	2002	Surprisingly, the decreased intrinsic GTPase(Na) of G13ASsEF-1 alpha can be partially restored by kirromycin, an effect not found for SsEF-1 alpha wt.	mocimycin	98-108	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	56-68
11683622-8	2001	The thermal stability of the SsEF-1alpha*GDP complex was significantly reduced when the GDP was replaced with Gpp(NH)p or in the presence of NaBr or NH4Cl, whereas a lower destabilizing effect was provoked by NaCl and KCl.	Guanylyl Imidodiphosphate	110-118	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	29-40
11683622-1	2001	Elongation factor 1alpha from the hyperthermophilic archaeon Sulfolobus solfataricus (SsEF-1alpha) carries the aminoacyl tRNA to the ribosome; it binds GDP or GTP, and it is also endowed with an intrinsic GTPase activity that is triggered in vitro by NaCl at molar concentrations [Masullo, M., De Vendittis, E., and Bocchini, V. (1994) J. Biol.	Guanosine Triphosphate	159-162	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	86-97
11683622-1	2001	Elongation factor 1alpha from the hyperthermophilic archaeon Sulfolobus solfataricus (SsEF-1alpha) carries the aminoacyl tRNA to the ribosome; it binds GDP or GTP, and it is also endowed with an intrinsic GTPase activity that is triggered in vitro by NaCl at molar concentrations [Masullo, M., De Vendittis, E., and Bocchini, V. (1994) J. Biol.	Sodium Chloride	251-255	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	86-97
11683622-8	2001	The thermal stability of the SsEF-1alpha*GDP complex was significantly reduced when the GDP was replaced with Gpp(NH)p or in the presence of NaBr or NH4Cl, whereas a lower destabilizing effect was provoked by NaCl and KCl.	sodium bromide	141-145	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	29-40
11683622-5	2001	The estimation of the secondary structure of the SsEF-1alpha*GDP complex, made by curve fitting of the amide I" band or by factor analysis of the amide I band, indicated a content of 34-36% alpha-helix, 35-40% beta-sheet, 14-19% turn, and 7% unordered structure.	Guanosine Diphosphate	61-64	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	49-60
11683622-8	2001	The thermal stability of the SsEF-1alpha*GDP complex was significantly reduced when the GDP was replaced with Gpp(NH)p or in the presence of NaBr or NH4Cl, whereas a lower destabilizing effect was provoked by NaCl and KCl.	Ammonium Chloride	149-154	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	29-40
11683622-8	2001	The thermal stability of the SsEF-1alpha*GDP complex was significantly reduced when the GDP was replaced with Gpp(NH)p or in the presence of NaBr or NH4Cl, whereas a lower destabilizing effect was provoked by NaCl and KCl.	Sodium Chloride	209-213	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	29-40
11683622-8	2001	The thermal stability of the SsEF-1alpha*GDP complex was significantly reduced when the GDP was replaced with Gpp(NH)p or in the presence of NaBr or NH4Cl, whereas a lower destabilizing effect was provoked by NaCl and KCl.	Potassium Chloride	218-221	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	29-40
11683622-10	2001	The data suggested that the sodium ion was responsible for the induction of the GTPase activity, whereas the anion modulated the enzymatic activity through destabilization of particular regions of SsEF-1alpha.	Sodium	28-34	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	197-208
11683622-11	2001	Finally, the infrared data suggested that, in particular region(s) of the polypeptide chain, the SsEF-1alpha*Gpp(NH)p complex possesses structural conformations which are different from those present in the SsEF-1alpha*GDP complex.	Guanosine Diphosphate	219-222	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	97-108
11683622-5	2001	The estimation of the secondary structure of the SsEF-1alpha*GDP complex, made by curve fitting of the amide I" band or by factor analysis of the amide I band, indicated a content of 34-36% alpha-helix, 35-40% beta-sheet, 14-19% turn, and 7% unordered structure.	Amides	103-108	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	49-60
11683622-5	2001	The estimation of the secondary structure of the SsEF-1alpha*GDP complex, made by curve fitting of the amide I" band or by factor analysis of the amide I band, indicated a content of 34-36% alpha-helix, 35-40% beta-sheet, 14-19% turn, and 7% unordered structure.	Amides	146-151	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	49-60
11683622-7	2001	On the other hand, the alpha-helix content of the SsEF-1alpha*GDP complex increased upon addition of salts, and the highest effect was produced by 5 M NaCl.	Guanosine Diphosphate	62-65	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	50-61
11683622-7	2001	On the other hand, the alpha-helix content of the SsEF-1alpha*GDP complex increased upon addition of salts, and the highest effect was produced by 5 M NaCl.	Sodium Chloride	151-155	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	50-61
11683622-8	2001	The thermal stability of the SsEF-1alpha*GDP complex was significantly reduced when the GDP was replaced with Gpp(NH)p or in the presence of NaBr or NH4Cl, whereas a lower destabilizing effect was provoked by NaCl and KCl.	Guanosine Diphosphate	41-44	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	29-40
11683622-8	2001	The thermal stability of the SsEF-1alpha*GDP complex was significantly reduced when the GDP was replaced with Gpp(NH)p or in the presence of NaBr or NH4Cl, whereas a lower destabilizing effect was provoked by NaCl and KCl.	Guanosine Diphosphate	88-91	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	29-40
11574461-6	2001	Finally, structural comparisons of SsEF- 1alpha.GDP with yeast EF-1alpha in complex with the nucleotide exchange factor EF-1beta shows that a dramatic rearrangement of the overall structure of EF-1alpha occurs during the nucleotide exchange.	Guanosine Diphosphate	48-51	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	35-47
11574461-6	2001	Finally, structural comparisons of SsEF- 1alpha.GDP with yeast EF-1alpha in complex with the nucleotide exchange factor EF-1beta shows that a dramatic rearrangement of the overall structure of EF-1alpha occurs during the nucleotide exchange.	Guanosine Diphosphate	48-51	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	193-202
9473450-5	1998	recSsEF-1beta and Y54HSsEF-1beta were both able to catalyze the GDP/GTP exchange on SsEF-1alpha as observed with the wild-type SsEF-1beta.	Guanosine Triphosphate	68-71	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	84-95
10998062-1	2000	The archaeal Sulfolobus solfataricus elongation factor 1alpha (SsEF-1alpha) bound to GTP or to its analogue guanyl-5"-yl imido diphosphate [Gpp(NH)p] formed a ternary complex with either Escherichia coli Val-tRNAVal or Saccharomyces cerevisiae Phe-tRNAPhe as demonstrated by gel-shift and gel-filtration experiments.	Guanosine Triphosphate	85-88	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	63-74
10998062-1	2000	The archaeal Sulfolobus solfataricus elongation factor 1alpha (SsEF-1alpha) bound to GTP or to its analogue guanyl-5"-yl imido diphosphate [Gpp(NH)p] formed a ternary complex with either Escherichia coli Val-tRNAVal or Saccharomyces cerevisiae Phe-tRNAPhe as demonstrated by gel-shift and gel-filtration experiments.	guanyl-5"-yl imido diphosphate	108-138	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	63-74
10998062-1	2000	The archaeal Sulfolobus solfataricus elongation factor 1alpha (SsEF-1alpha) bound to GTP or to its analogue guanyl-5"-yl imido diphosphate [Gpp(NH)p] formed a ternary complex with either Escherichia coli Val-tRNAVal or Saccharomyces cerevisiae Phe-tRNAPhe as demonstrated by gel-shift and gel-filtration experiments.	Guanylyl Imidodiphosphate	140-148	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	63-74
10998062-11	2000	As already observed with eukaryal EF-1alpha, SsEF-1alpha in its GDP-bound form was also able to protect the ester bond of aminoacyl-tRNA, even though with a 10-fold lower efficiency compared with SsEF-1alphaz.rad;Gpp(NH)p. The overall results indicated that the archaeal elongation factor 1alpha shares several properties with eukaryal EF-1alpha but not with eubacterial EF-Tu.	Guanosine Diphosphate	64-67	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	45-56
10998062-11	2000	As already observed with eukaryal EF-1alpha, SsEF-1alpha in its GDP-bound form was also able to protect the ester bond of aminoacyl-tRNA, even though with a 10-fold lower efficiency compared with SsEF-1alphaz.rad;Gpp(NH)p. The overall results indicated that the archaeal elongation factor 1alpha shares several properties with eukaryal EF-1alpha but not with eubacterial EF-Tu.	Guanosine Diphosphate	64-67	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	47-56
10998062-11	2000	As already observed with eukaryal EF-1alpha, SsEF-1alpha in its GDP-bound form was also able to protect the ester bond of aminoacyl-tRNA, even though with a 10-fold lower efficiency compared with SsEF-1alphaz.rad;Gpp(NH)p. The overall results indicated that the archaeal elongation factor 1alpha shares several properties with eukaryal EF-1alpha but not with eubacterial EF-Tu.	Esters	108-113	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	45-56
10998062-11	2000	As already observed with eukaryal EF-1alpha, SsEF-1alpha in its GDP-bound form was also able to protect the ester bond of aminoacyl-tRNA, even though with a 10-fold lower efficiency compared with SsEF-1alphaz.rad;Gpp(NH)p. The overall results indicated that the archaeal elongation factor 1alpha shares several properties with eukaryal EF-1alpha but not with eubacterial EF-Tu.	Esters	108-113	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	47-56
10493796-0	1999	A chimeric elongation factor containing the putative guanine nucleotide binding domain of archaeal EF-1 alpha and the M and C domains of eubacterial EF-Tu.	Guanine Nucleotides	53-71	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	99-109
10493796-1	1999	A recombinant chimeric elongation factor containing the region of EF-1 alpha from Sulfolobus solfataricus harboring the site for GDP and GTP binding and GTP hydrolysis (SsG) and domains M and C of Escherichia coli EF-Tu (EcMC) was studied.	Guanosine Diphosphate	129-132	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	66-76
10493796-1	1999	A recombinant chimeric elongation factor containing the region of EF-1 alpha from Sulfolobus solfataricus harboring the site for GDP and GTP binding and GTP hydrolysis (SsG) and domains M and C of Escherichia coli EF-Tu (EcMC) was studied.	Guanosine Triphosphate	137-140	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	66-76
10493796-1	1999	A recombinant chimeric elongation factor containing the region of EF-1 alpha from Sulfolobus solfataricus harboring the site for GDP and GTP binding and GTP hydrolysis (SsG) and domains M and C of Escherichia coli EF-Tu (EcMC) was studied.	Guanosine Triphosphate	153-156	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	66-76
9473450-5	1998	recSsEF-1beta and Y54HSsEF-1beta were both able to catalyze the GDP/GTP exchange on SsEF-1alpha as observed with the wild-type SsEF-1beta.	Guanosine Diphosphate	64-67	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	84-95
11574461-1	2001	The crystal structure of elongation factor 1alpha from the archaeon Sulfolobus solfataricus in complex with GDP (SsEF-1alpha.GDP) at 1.8 A resolution is reported.	Guanosine Diphosphate	108-111	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	113-124
11574461-1	2001	The crystal structure of elongation factor 1alpha from the archaeon Sulfolobus solfataricus in complex with GDP (SsEF-1alpha.GDP) at 1.8 A resolution is reported.	Guanosine Diphosphate	125-128	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	113-124
11574461-2	2001	As already known for the eubacterial elongation factor Tu, the SsEF-1alpha.GDP structure consists of three different structural domains.	Guanosine Diphosphate	75-78	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	63-74
11574461-4	2001	Furthermore, the residues that usually co-ordinate Mg(2+) through water molecules in the GTP-binding proteins, though conserved in SsEF-1alpha, are located quite far from the binding site.	Magnesium	51-53	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	131-142
11574461-4	2001	Furthermore, the residues that usually co-ordinate Mg(2+) through water molecules in the GTP-binding proteins, though conserved in SsEF-1alpha, are located quite far from the binding site.	Water	66-71	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	131-142
11574461-4	2001	Furthermore, the residues that usually co-ordinate Mg(2+) through water molecules in the GTP-binding proteins, though conserved in SsEF-1alpha, are located quite far from the binding site.	Guanosine Triphosphate	89-92	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	131-142
11574461-5	2001	[(3)H]GDP binding experiments confirm that Mg(2+) has only a marginal effect on the nucleotide exchange reaction of SsEF-1alpha, although essential to GTPase activity elicited by SsEF-1alpha.	magnesium ion	43-49	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	116-127
9030774-4	1997	The values of kcat and Km for GTP of the intrinsic GTPase of SsEF-1alpha triggered by 3.6 M NaCl were not affected by the deletions.	Guanosine Triphosphate	30-33	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	61-72
9030774-4	1997	The values of kcat and Km for GTP of the intrinsic GTPase of SsEF-1alpha triggered by 3.6 M NaCl were not affected by the deletions.	Sodium Chloride	92-96	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	61-72
9030774-7	1997	Remarkably, both Ss(GM)EF-1alpha and Ss(G)EF-1alpha were able to exchange [3H]GDP for GTP at a very high rate so that they were no more sensitive to the stimulatory effect of SsEF-1beta, which is the nucleotide exchange factor of SsEF-1alpha.	Tritium	75-77	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	23-32
9030774-7	1997	Remarkably, both Ss(GM)EF-1alpha and Ss(G)EF-1alpha were able to exchange [3H]GDP for GTP at a very high rate so that they were no more sensitive to the stimulatory effect of SsEF-1beta, which is the nucleotide exchange factor of SsEF-1alpha.	Tritium	75-77	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	42-51
9030774-7	1997	Remarkably, both Ss(GM)EF-1alpha and Ss(G)EF-1alpha were able to exchange [3H]GDP for GTP at a very high rate so that they were no more sensitive to the stimulatory effect of SsEF-1beta, which is the nucleotide exchange factor of SsEF-1alpha.	Guanosine Diphosphate	78-81	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	23-32
9030774-7	1997	Remarkably, both Ss(GM)EF-1alpha and Ss(G)EF-1alpha were able to exchange [3H]GDP for GTP at a very high rate so that they were no more sensitive to the stimulatory effect of SsEF-1beta, which is the nucleotide exchange factor of SsEF-1alpha.	Guanosine Diphosphate	78-81	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	42-51
9030774-7	1997	Remarkably, both Ss(GM)EF-1alpha and Ss(G)EF-1alpha were able to exchange [3H]GDP for GTP at a very high rate so that they were no more sensitive to the stimulatory effect of SsEF-1beta, which is the nucleotide exchange factor of SsEF-1alpha.	Guanosine Triphosphate	86-89	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	23-32
9030774-7	1997	Remarkably, both Ss(GM)EF-1alpha and Ss(G)EF-1alpha were able to exchange [3H]GDP for GTP at a very high rate so that they were no more sensitive to the stimulatory effect of SsEF-1beta, which is the nucleotide exchange factor of SsEF-1alpha.	Guanosine Triphosphate	86-89	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	42-51
8652615-6	1996	At 50 degrees C, at a concentration of SsEF-1 beta 5-fold higher than that of SsEF-1 alpha x [3H]GDP the rate of the exchange of [3H]GDP for GTP becomes about 160-fold faster.	Tritium	94-96	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	78-90
8652615-6	1996	At 50 degrees C, at a concentration of SsEF-1 beta 5-fold higher than that of SsEF-1 alpha x [3H]GDP the rate of the exchange of [3H]GDP for GTP becomes about 160-fold faster.	Tritium	130-132	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	78-90
8652615-6	1996	At 50 degrees C, at a concentration of SsEF-1 beta 5-fold higher than that of SsEF-1 alpha x [3H]GDP the rate of the exchange of [3H]GDP for GTP becomes about 160-fold faster.	Guanosine Diphosphate	97-100	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	78-90
8652615-6	1996	At 50 degrees C, at a concentration of SsEF-1 beta 5-fold higher than that of SsEF-1 alpha x [3H]GDP the rate of the exchange of [3H]GDP for GTP becomes about 160-fold faster.	Guanosine Triphosphate	141-144	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	78-90
8867895-3	1996	Upon induction with isopropyl beta-D-thiogalactopyranoside, the recombinant SsEF-1 alpha (recSsEF-1 alpha) was purified from the E. coli S-100 extract by a two-step procedure.	Isopropyl Thiogalactoside	20-58	ribosomal protein S18-alanine N-acetyltransferase	Saccharolobus solfataricus	76-88