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1 y modulating the activity of double-stranded RNA-dependent protein kinase.
2 se R-motif exons of the interferon-inducible RNA-dependent protein kinase.
3 veal the existence in nuclear extracts of an RNA-dependent protein kinase activity that hyperphosphor
4 S, was dependent on CD14 activity but not on RNA-dependent protein kinase and could be inhibited by a
5 igoadenylate synthetase, and double-stranded-RNA-dependent protein kinase as well as those coding for
6 investigated the role of the double-stranded RNA-dependent protein kinase gene (pkr) in the regulatio
7 feron-alpha --> upward arrow double-stranded RNA-dependent protein kinase --> downward arrow c-Myc --
8 eta mRNA was MyD88- and PKR (double-stranded RNA-dependent protein kinase)-independent, but TIRAP (To
9 n [IFN-beta], IFN-gamma, protein Mx1 GTPase, RNA-dependent protein kinase, inducible nitric oxide syn
11 , so we monitored the activity of PERK [PKR (RNA-dependent protein kinase)-like ER kinase (EIF2AK3)],
12 c translation initiator factor 2alpha kinase RNA-dependent protein kinase-like ER kinase (PERK) allow
13 tx1 activated the proximal ER stress sensors RNA-dependent protein kinase-like ER kinase and inositol
14 led by the activation of ER stress-inducible RNA-dependent protein kinase-like ER-integral (PERK) eIF
15 e anti-viral response, e.g., double-stranded RNA-dependent protein kinase, myxovirus resistance prote
16 a and IL-18 - as well as the double-stranded-RNA-dependent protein kinase pathway and RNaseL pathway,
17 nd inhibit activation of the double-stranded RNA-dependent protein kinase PKR in cell-free systems, a
21 d autophosphorylation of the double-stranded RNA-dependent protein kinase PKR leading to phosphorylat
22 nterestingly, absence of the double-stranded RNA-dependent protein kinase PKR led to a profound defec
23 d to be effective in blocking binding to the RNA-dependent protein kinase PKR, a cytoplasmic dsRNA-bi
28 is study quantified constitutive and induced RNA-dependent protein kinase (PKR) activation in Fanconi
29 gamma, and the activation of double-stranded RNA-dependent protein kinase (PKR) and eukaryotic initia
31 through the increase of the double-stranded RNA-dependent protein kinase (PKR) and following inactiv
32 olyinosinic-polycytidylic acid activated the RNA-dependent protein kinase (PKR) and induced significa
33 specific adenosine deaminase (ADAR1) and the RNA-dependent protein kinase (PKR) are both interferon-i
35 virus 1 (HSV-1) results in the activation of RNA-dependent protein kinase (PKR) but that the alpha su
36 tranded RNA, which activates double-stranded RNA-dependent protein kinase (PKR) by mimicking viral in
37 re, we provide evidence that double-stranded RNA-dependent protein kinase (PKR) can respond to nutrie
39 study, the role of the double-stranded (ds) RNA-dependent protein kinase (PKR) in macrophage activat
40 repressed expression of the double-stranded RNA-dependent protein kinase (PKR) in the promonocytic U
43 h herpes simplex virus 1 the double-stranded RNA-dependent protein kinase (PKR) is activated but phos
51 ed upon virus infection, the double-stranded RNA-dependent protein kinase (PKR) is best known for tri
53 situation and show that the double-stranded RNA-dependent protein kinase (PKR) is involved in the lo
54 we provide evidence that the double-stranded RNA-dependent protein kinase (PKR) is not required for v
57 red that viperin, ISG20, and double-stranded RNA-dependent protein kinase (PKR) noncytolytically inhi
60 e interferon-inducible, double-stranded (ds) RNA-dependent protein kinase (PKR) regulates protein syn
61 N-terminal kinase (JNK) and double-stranded RNA-dependent protein kinase (PKR) to induce autophagy w
62 The gene encoding the interferon-inducible, RNA-dependent protein kinase (PKR) was isolated as lambd
64 promotes the degradation of double-stranded RNA-dependent protein kinase (PKR), and it suppresses ho
65 d in an elevation in an IFN-responsive gene, RNA-dependent protein kinase (PKR), but not 2',5'-oligoa
66 the human eIF2alpha kinase, double-stranded-RNA-dependent protein kinase (PKR), impeded growth of S.
67 e proteasomal degradation of double-stranded RNA-dependent protein kinase (PKR), little is known abou
68 eIF-2alpha kinases including double-stranded RNA-dependent protein kinase (PKR), which has been recen
69 da7 induces andactivates the double-stranded RNA-dependent protein kinase (PKR), which leads to phosp
70 itro transcripts containing uridine activate RNA-dependent protein kinase (PKR), which then phosphory
71 the role of the ER resident protein kinase, RNA-dependent protein kinase (PKR)-like ER kinase (PERK)
72 ured cells due to their inability to prevent RNA-dependent protein kinase (PKR)-mediated inhibition o
73 ansgenic mouse strain in which double-strand RNA-dependent protein kinase (PKR)-mediated phosphorylat
82 here we identify a role for double-stranded RNA-dependent protein kinase (PKR, also known as EIF2AK2
83 RNA-specific adenosine deaminase [ADAR1] and RNA-dependent protein kinase [PKR]) in a tissue-specific
84 rt that in HeLa cells, activation of a PERK (RNA-dependent protein kinase [PKR]-like ER kinase)-eIF2a
85 in vitro with and inhibits the IFN-induced, RNA-dependent protein kinase, PKR, and that NS5A interac
87 plication indicated that the double-stranded RNA-dependent protein kinase, PKR, exerted some early an
88 -terminal region of the double-stranded (ds) RNA-dependent protein kinase, PKR, has been shown to med
89 is now apparent that the double-stranded (ds)RNA-dependent protein kinase, PKR, is a regulator of div
90 have shown recently that the double-stranded RNA-dependent protein kinase, PKR, is involved in transl
91 ctor 2 (eIF2alpha) by the interferon-induced RNA-dependent protein kinase, PKR, leads to inhibition o
93 tRNA2-1 and down-regulate the phosphorylated RNA-dependent protein kinase (pPKR), whose activity has
94 ulated gene products such as double-stranded RNA-dependent protein kinase R (PKR), 2',5'-oligoadenyla
97 t restored in the absence of double-stranded RNA-dependent protein kinase, RNase L, or IFN-alpha/beta
98 pkr gene encoding the interferon-inducible, RNA-dependent protein kinase was isolated as lambda phag
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