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1 rom ADP-ribosylation of elongation factor 2 (EF-2).
2 croM), and no Ca(2+) binding was detected at EF-2.
3 enzymes such as elongation factor 1alpha and EF-2.
4 ep, via phosphorylation/dephosphorylation of EF-2.
5 tase-2A, the principal phosphatase acting on EF-2.
6 ti-EF-3 interaction by EF-1 alpha but not by EF-2.
7 nition of the ADP-ribose acceptor substrate, EF-2.
8 h appears to be presented for recognition by EF-2.
10 lcium ions to the second and third EF-hands (EF-2 and EF-3) of recoverin leads to the extrusion of th
13 ell-shaped dose-response curve, whereas when EF-2 and ribosomes were in equimolar concentrations sord
14 to abolish high-affinity calcium binding to EF-2 and thereby trap the myristoylated protein with cal
15 otes phosphorylation of elongation factor-2 (EF-2) and prostacyclin production, but not phosphorylati
18 for EF-2, it is demonstrated that DB blocks EF-2 binding to pre-translocative ribosome.EF-1alpha com
24 and it was shown previously that DB prevents EF-2-dependent translocation in partial reaction models
27 for protein synthesis (elongation factor-2 [EF-2], eukaryotic initiation factor-4AII, and transcript
29 on the ribosome-dependent GTPase activity of EF-2 from Candida albicans in the absence of any other c
31 eate functional domains that control chicken EF-2 gene transcription, the 5'-flanking region of the c
35 toxin-mediated ADP-ribosylation to assay for EF-2, it is demonstrated that DB blocks EF-2 binding to
38 and in vivo and suggest that destruction of EF-2 kinase may be an important cytotoxic mechanism of t
39 viability of glioma cells, the expression of EF-2 kinase protein, and the interaction between Hsp90 a
40 ein phosphatase-1 nor calmodulin kinase III (EF-2 kinase) activity was affected under these condition
45 lines for 24-48 h of GA or 17-AAG disrupted EF-2-kinase/Hsp90 interactions as measured by coimmunopr
46 h of hydrophobic residues formed by EF-1 and EF-2 (Leu24, Trp27, Phe31, Phe45, Phe48, Phe49, Tyr81, V
51 high glucose led to a marked stimulation of EF-2 phosphorylation, consistent with the possibility th
60 lucose promoted a rapid dephosphorylation of EF-2 that was complete in 10 min and maintained over the
61 ds NAD and catalyzes the ADP-ribosylation of EF-2, the crystal structure of DT in complex with NAD ha
62 ingly, glucose-mediated dephosphorylation of EF-2 was completely blocked by the mitochondrial respira
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