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   1  off-target binding to proteins such as PKR (RNA-activated protein kinase).                          
     2 luding the expression of the double-stranded-RNA-activated protein kinase.                           
     3 lpha subunit of eIF-2 by the double-stranded RNA-activated protein kinase.                           
     4 tor-1 (IRF-1) but not IRF-2, double-stranded RNA-activated protein kinase, and inducible nitric-oxide
     5 ndent protein kinase II, and double-stranded RNA-activated protein kinase as the enzymes responsible 
     6 or of the interferon-induced double-stranded RNA-activated protein kinase, as induced during ER stres
     7 nly 200 ng (3 pmol) of human double-stranded RNA-activated protein kinase expressed in a mutant strai
     8 enzymes, viperin, ISG20, and double-stranded-RNA-activated protein kinase, inhibited steps in viral p
     9 a (eIF2alpha) kinase or PKR (double-stranded RNA-activated protein kinase)-like endoplasmic reticulum
    10 g caused weak stimulation of double-stranded RNA-activated protein kinase-like endoplasmic reticulum-
    11 ion of PERK-eIF2alpha (PERK: double-stranded RNA-activated protein kinase-like ER kinase; eIF2alpha: 
    12 ibroblasts deficient in the ER stress kinase RNA-activated protein kinase-like ER-resident kinase (PE
    13 s replication in control and double-stranded RNA-activated protein kinase-null MEFs indicated that th
    14  innate immune response, the double-stranded RNA activated protein kinase PKR phosphorylates the tran
    15 f sequence homology with the double-stranded RNA-activated protein kinase PKR and its substrate, the 
    16 ined the involvement of double stranded (ds) RNA-activated protein kinase PKR in tunicamycin-induced 
  
  
  
  
  
    22 anslation inhibition through double-stranded RNA-activated protein kinase (PKR) and also through a ne
    23 iting autophosphorylation of double-stranded RNA-activated protein kinase (PKR) and blocking phosphor
    24 nterferon (IFN)-induced double-stranded (ds) RNA-activated protein kinase (PKR) and is an important r
    25 both the interferon-induced, double-stranded-RNA-activated protein kinase (PKR) and the endoribonucle
  
    27  of the interferon-inducible double-stranded RNA-activated protein kinase (PKR) has been reported in 
    28 ole of interferon-inducible, double-stranded RNA-activated protein kinase (PKR) in the induction of a
    29 cognized nuclear function of double-stranded RNA-activated protein kinase (PKR) in the pathogenesis o
    30 or of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a cellular protein
  
    32 he interferon (IFN)-induced, double-stranded RNA-activated protein kinase (PKR) mediates the antivira
    33    In contrast, induction of double-stranded RNA-activated protein kinase (PKR) mRNA and protein by I
  
    35 ent or overexpression of the double-stranded RNA-activated protein kinase (PKR) significantly increas
    36 he interferon (IFN)-induced, double-stranded RNA-activated protein kinase (PKR) via the PKR eukaryoti
    37 lated, whereas expression of double-stranded RNA-activated protein kinase (PKR) was decreased by 55% 
  
    39 rt, we provide evidence that double-stranded RNA-activated protein kinase (PKR), a stress kinase, is 
    40 ein family that includes the double-stranded RNA-activated protein kinase (PKR), Drosophila Staufen a
    41 latory factor 1 (IRF-1), the double-stranded RNA-activated protein kinase (PKR), or RNase L (RNase L)
    42 ess responses, including the double-stranded RNA-activated protein kinase (PKR)-like endoplasmic reti
    43 zyme 1alpha (IRE1alpha), and double-stranded RNA-activated protein kinase (PKR)-like ER kinase (PERK)
  
  
  
  
  
  
    50 that the interferon-induced, double-stranded RNA-activated protein kinase, PKR, is responsible for re
  
  
  
    54 in kinase 3 [MAPK3], MAP3K8, double-stranded RNA-activated protein kinase [PRKR], and MAP2K4), and of
  
    56 nensis activates macrophage double-stranded, RNA-activated protein kinase R (PKR) to promote parasite
    57  viral nonstructural proteins independent of RNA-activated protein kinase R and replication of HBoV1 
  
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