AbstractIn Sulfolobus solfataricus the binding of the exchange factor 1β (SsEF-1β) to SsEF-1α·GDP displaces the nucleotide and the SsEF-1α·SsEF-1β complex is formed. The complex itself is stable, but it dissociates upon the addition of GDP or Gpp(NH)p but not ATP. Since the rate of the formation of the SsEF-1α·SsEF-1β complex is significatively slower than the rate of the nucleotide exchange catalyzed by SsEF-1β it can be inferred that in vivo the GDP/GTP exchange reaction proceeds via an SsEF-1α–SsEF-1β interaction without involving the formation of a stable binary complex as an intermediate
The thiazolyl-peptide antibiotic GE2270A, an inhibitor of the elongation factor Tu from Escherichia ...
This review describes some features of the detailed structure-function relationship in two extremoph...
Nucleotide exchange in elongation factor Tu (EF-Tu) is catalyzed by elongation factor Ts (EF-Ts). Si...
In Sulfolobus solfataricus the binding of the exchange factor 1b (SsEF-1b) to SsEF-1aGDP displaces t...
AbstractIn Sulfolobus solfataricus the binding of the exchange factor 1β (SsEF-1β) to SsEF-1α·GDP di...
The crystal structure of elongation factor 1alpha from the archaeon Sulfolobus solfataricus in compl...
The elongation factor 1 beta (EF-1 beta), that in eukarya and archaea promotes the replacement of GD...
The elongation factor 2 from the thermoacidophilic archaeon Sulfolobus solfataricus (SsEF-2) binds [...
The archaeal Sulfolobus solfataricus elongation factor 1 alpha (SsEF-1 alpha) bound to GTP or to its...
A recombinant chimeric elongation factor containing the region of EF-1 alpha from Sulfolobus solfata...
Recent studies have shown that elongation factors extracted from archaea/eukarya and from eubacteria...
The D60A mutant of the elongation factor (EF) 1alpha from Sulfolobus solfataricus (Ss), was obtained...
The stability against chemical denaturants of the elongation factor EF-1A (SsEF-1A), a protein isola...
The present article reviews our recent work carried out on the translation elongation factors EF-1al...
The D60A mutant of the elongation factor (EF) 1alpha from Sulfolobus solfataricus (Ss), was obtained...
The thiazolyl-peptide antibiotic GE2270A, an inhibitor of the elongation factor Tu from Escherichia ...
This review describes some features of the detailed structure-function relationship in two extremoph...
Nucleotide exchange in elongation factor Tu (EF-Tu) is catalyzed by elongation factor Ts (EF-Ts). Si...
In Sulfolobus solfataricus the binding of the exchange factor 1b (SsEF-1b) to SsEF-1aGDP displaces t...
AbstractIn Sulfolobus solfataricus the binding of the exchange factor 1β (SsEF-1β) to SsEF-1α·GDP di...
The crystal structure of elongation factor 1alpha from the archaeon Sulfolobus solfataricus in compl...
The elongation factor 1 beta (EF-1 beta), that in eukarya and archaea promotes the replacement of GD...
The elongation factor 2 from the thermoacidophilic archaeon Sulfolobus solfataricus (SsEF-2) binds [...
The archaeal Sulfolobus solfataricus elongation factor 1 alpha (SsEF-1 alpha) bound to GTP or to its...
A recombinant chimeric elongation factor containing the region of EF-1 alpha from Sulfolobus solfata...
Recent studies have shown that elongation factors extracted from archaea/eukarya and from eubacteria...
The D60A mutant of the elongation factor (EF) 1alpha from Sulfolobus solfataricus (Ss), was obtained...
The stability against chemical denaturants of the elongation factor EF-1A (SsEF-1A), a protein isola...
The present article reviews our recent work carried out on the translation elongation factors EF-1al...
The D60A mutant of the elongation factor (EF) 1alpha from Sulfolobus solfataricus (Ss), was obtained...
The thiazolyl-peptide antibiotic GE2270A, an inhibitor of the elongation factor Tu from Escherichia ...
This review describes some features of the detailed structure-function relationship in two extremoph...
Nucleotide exchange in elongation factor Tu (EF-Tu) is catalyzed by elongation factor Ts (EF-Ts). Si...