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1 protein synthesis caused by inactivation of elongation factor 2.
2 ptide is identical to residues 581 to 589 of elongation factor 2.
3 nslocates to the cytosol and ADP-ribosylates elongation factor 2.
4 ocates into the cytosol where it inactivates elongation factor 2.
5 synthesis by ADP-ribosylation of eukaryotic elongation factor 2.
6 ible for the trimethylation of lysine 509 on elongation factor 2.
7 re toxin to reach the cytosol and inactivate elongation factor 2.
8 bosyltransferase activity against eukaryotic elongation factor 2.
9 found in archaeal and eukaryotic translation elongation factor 2.
10 single amino acid substitution in eukaryotic elongation factor 2.
11 NAD-dependent ADP-ribosylation of eukaryotic elongation factor 2.
12 sleep-related gene encoding the translation elongation factor 2.
13 ding of the C domain of DT to its substrate, elongation factor-2.
14 cells via ADP-ribosylation of the eukaryotic elongation factor-2.
15 inase in turn phosphorylates and inactivates elongation factor-2, a key mediator of ribosomal transfe
16 tresses on the phosphorylation of eukaryotic elongation factor 2 also differed: oxidative stress elic
17 reduced phosphorylation levels of eukaryotic elongation factor 2 and also requires the presence of el
18 ation but increases the association of human elongation factor 2 and human heterogeneous nuclear ribo
19 catalyzed the ADP-ribosylation of eukaryotic elongation factor 2 and inhibited protein synthesis.
22 tes and inactivates eukaryotic translational elongation factor-2, and thus can modulate the rate of p
23 osomal protein S4, malate dehydrogenase, and elongation factor 2, as well as two novel parasite prote
24 tep in the posttranslational modification of elongation factor-2 at His(715) that yields diphthamide,
25 4 resulted in increased dephosphorylation of elongation factor 2, but had no effect on phosphorylatio
26 kills by ADP-ribosylation of the translation elongation factor 2, but many of the host factors requir
28 (P < 0.05) and phosphorylation of eukaryotic elongation factor 2 decreased (P < 0.05) after exercise
29 esent on archaeal and eukaryotic translation elongation factor 2, diphthamide represents one of the m
30 regions of endogenous eukaryotic translation elongation factor 2 (eEF-2) gene] using the Clustered Re
31 y increase the phosphorylation of eukaryotic elongation factor 2 (eEF-2) in extracts of NIH3T3 cells.
32 demonstrated that the activity of eukaryotic elongation factor 2 (eEF-2) kinase was markedly increase
35 ulin-dependent phosphorylation of eukaryotic elongation factor-2 (eEF-2) by eukaryotic elongation fac
36 d autophagy, whereas silencing of eukaryotic elongation factor-2 (eEF-2) kinase, a protein synthesis
37 induced the phosphorylation of a eukaryotic elongation factor-2 (eEF-2) kinase, radiation sensitivit
38 eased level of phosphorylation of eukaryotic elongation factor-2 (eEF-2) was observed in the brains a
39 at phosphorylates and inactivates eukaryotic elongation factor 2 (eEF2 kinase; eEF2K) is subject to m
40 in 1 (4EBP1 Thr37/46; 14 +/- 3%), eukaryotic elongation factor 2 (eEF2 Thr56; -47 +/- 4%), extracellu
44 an target of rapamycin (mTOR) and eukaryotic elongation factor 2 (eEF2) in the mPFC, effects recently
46 diphthamide on human eukaryotic translation elongation factor 2 (eEF2) is the target of ADP ribosyla
47 kade of NMDAR at rest deactivates eukaryotic elongation factor 2 (eEF2) kinase (also called CaMKIII),
48 roteasome-targeted degradation of eukaryotic elongation factor 2 (eEF2) kinase and activation of the
49 MDA receptors at rest deactivates eukaryotic elongation factor 2 (eEF2) kinase, resulting in reduced
50 an inhibitory phosphorylation of eukaryotic elongation factor 2 (eEF2) kinase, which in turn promote
53 elongation is phosphorylation of eukaryotic elongation factor 2 (eEF2) on threonine 56 (T56) by eEF2
55 ing protein (Tbp) and eukaryotic translation elongation factor 2 (Eef2) were not affected by inflamma
56 increasing the phosphorylation of eukaryotic elongation factor 2 (eEF2), a key component of the trans
58 also increased phosphorylation of eukaryotic elongation factor 2 (eEF2), a process known to inhibit p
59 and found that phosphorylation of eukaryotic elongation factor 2 (eEF2), a ribosomal translocase whos
60 ion (inactivation) of eukaryotic translation elongation factor 2 (eEF2), an important molecule for pr
61 6k), ribosomal protein S6 (rpS6), eukaryotic elongation factor 2 (eEF2), and eukaryotic initiation fa
62 es the involvement of eukaryotic translation elongation factor 2 (eEF2), the phosphorylation of which
63 f the diphthamide modification on eukaryotic elongation factor 2 (eEF2), we generated an eEF2 Gly(717
64 n this study, we demonstrate that eukaryotic elongation factor 2 (eEF2), which catalyzes the GTP-depe
65 controlled by phosphorylation of eukaryotic elongation factor 2 (eEF2), which inhibits its activity
66 ar target has been identified as translation elongation factor 2 (eEF2), which is responsible for the
72 receptor-dependent suppression of eukaryotic elongation factor-2 (eEF2) phosphorylation thus reversin
78 the endothelium, promotes phosphorylation of elongation factor-2 (EF-2) and prostacyclin production,
81 (4) genes responsible for protein synthesis (elongation factor-2 [EF-2], eukaryotic initiation factor
82 osttranslational modification on translation elongation factor 2 (EF2) in archaea and eukaryotes.
85 hibitor Exotoxin A (ToxA), which ribosylates elongation factor 2 (EF2), upregulates a significant sub
89 2 is unable to ADP ribosylate and inactivate elongation factor-2 (EF2), owing to a low level of DPH4
91 thetase, glutaminyl-transfer RNA synthetase, elongation factor 2, elongation factor 1delta, and eukar
93 ng vimentin, EH-domain-containing protein 2, elongation factor 2, glucose-regulated protein 78, trans
94 ene product, ribosomal protein S6, cyclin K, elongation factor-2, Grb2-associated protein 2, and othe
96 m nicotinamide adenine dinucleotide (NAD) to elongation factor-2 in eukaryotic cells, inhibiting prot
100 plitudes by reducing postsynaptic eukaryotic elongation factor 2 kinase (eEF2K) activity subsequent t
110 d higher levels of phosphorylated eukaryotic elongation factor 2 kinase than were observed in Mtm1 p.
111 des the activation of eukaryotic translation elongation factor 2 kinase with a consequent inhibition
112 ering RNA (siRNA) to eEF2 kinase (eukaryotic elongation factor 2 kinase) blocked the dendritic MAP1B
113 ivation and downregulation of the eukaryotic elongation factor 2 kinase, which normally inhibits tran
115 , rat, and Caenorhabditis elegans eukaryotic elongation factor-2 kinase (eEF-2 kinase) and found that
117 gy by 2-DG was associated with activation of elongation factor-2 kinase (eEF-2 kinase), a structurall
121 inase inhibitors against a mammalian enzyme, elongation factor-2 kinase (eEF-2K), and the effect of t
123 ic elongation factor-2 (eEF-2) by eukaryotic elongation factor-2 kinase (EF2K), which inhibits elonga
125 -2 kinase and a putative nematode eukaryotic elongation factor-2 kinase also encode the catalytic dom
126 gments of homology present in rat eukaryotic elongation factor-2 kinase and a putative nematode eukar
127 d neurotrophic factor expression, eukaryotic elongation factor-2 kinase function, and increased surfa
131 ot inhibit the phosphorylation of eukaryotic elongation factor 2 or augment subsequent expression of
132 chanism of action, inhibition of translation elongation factor 2 (PfEF2), led to progression of 2 (DD
133 city through ADP-ribosylation of translation elongation factor 2, predicated on binding to specific c
135 P dissociation inhibitor beta, ATP synthase, elongation factor 2, protein disulfide isomerase, nucleo
138 RNA reporter constructs with the 5'-TOP from elongation factor 2 showed decreased translational activ
139 osttranslational modification of translation elongation factor 2 that is conserved in all eukaryotes
140 d to interfere with binding of the substrate elongation factor 2 to the enzymatic active site of the
141 itor that impairs the function of eukaryotic elongation factor 2, whereas the rpl40a and rpl40b null
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