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1 bits the translation initiation factor eIF2 (eukaryotic initiation factor 2).
2 vent phosphorylation of the alpha-subunit of eukaryotic initiation factor 2.
3 sphorylation of PKR and the alpha subunit of eukaryotic initiation factor 2.
4  the phosphorylation of the alpha-subunit of eukaryotic initiation factor 2.
5 s of phosphorylation of the alpha subunit of eukaryotic initiation factor 2.
6 esis by phosphorylating the alpha subunit of eukaryotic initiation factor-2.
7                            Tat competes with eukaryotic initiation factor 2, a well-characterized sub
8                           Phosphorylation of eukaryotic initiation factor 2 alpha (eIF-2 alpha) is ty
9 t the hepatic heme-regulated inhibitor (HRI)-eukaryotic initiation factor 2 alpha (eIF2 alpha) kinase
10 spond to cellular stress by deactivating the eukaryotic initiation factor 2 alpha (eIF2alpha) or othe
11             PKR's pro-apoptotic role through eukaryotic initiation factor 2 alpha (eIF2alpha) phospho
12 d by attenuating protein translation through eukaryotic initiation factor 2 alpha (eIF2alpha) phospho
13                    Active PKR phosphorylates eukaryotic initiation factor 2 alpha and leads to inhibi
14  both with capsid-induced phosphorylation of eukaryotic initiation factor 2 alpha and with capsid-med
15  In 2014, scientists discovered mutations in eukaryotic initiation factor 2 alpha kinase 4 (EIF2AK4)
16 ation with polysomes likewise depends on the eukaryotic initiation factor 2 alpha kinase 4, which ass
17 nhibited PKR, we observed a reduced level of eukaryotic initiation factor 2 alpha subunit (eIF2alpha)
18 gative effect characterized by deficiency of eukaryotic initiation factor 2 alpha subunit phosphoryla
19 which can be repressed by phosphorylation of eukaryotic initiation factor 2 alpha-subunit (eIF2alpha)
20 age of procaspase-12, and phosphorylation of eukaryotic initiation factor-2 alpha in a human dopamine
21 suppresses protein synthesis by inactivating eukaryotic initiation factor 2-alpha (eIF2-alpha), to ex
22 imed T cells demonstrated phosphorylation of eukaryotic initiation factor 2-alpha (eIF2alpha), a 'col
23 IPK but was dependent on the presence of the eukaryotic initiation factor 2-alpha homology region, ma
24 st-in-class, small molecule inhibitor of the eukaryotic initiation factor 2-alpha kinase 3 (EIF2AK3)
25 s in phosphorylation of the alpha subunit of eukaryotic initiation factor 2 and NF-kappaB activity at
26 trol nonderepressible 2), phosphorylation of eukaryotic initiation factor 2, and increased synthesis
27                                              Eukaryotic initiation factor 2-associated glycoprotein,
28 onine aminopeptidase 2, which is the same as eukaryotic initiation factor 2-associated glycoprotein,
29  the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 causes translating mRNAs
30 -like ER kinase)-eIF2alpha (alpha subunit of eukaryotic initiation factor 2)-dependent pathway by Sub
31  that can phosphorylate the alpha subunit of eukaryotic initiation factor 2 (eIF-2alpha) and inhibit
32  the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF-2alpha) by activated
33      Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF-2alpha) is a well-ch
34 ctivity, and suppresses the alpha subunit of eukaryotic initiation factor 2 (eIF-2alpha) phosphorylat
35 oxia-associated increase in alpha subunit of eukaryotic initiation factor 2 (eIF-2alpha) phosphorylat
36 ke ER kinase (PERK) and the alpha subunit of eukaryotic initiation factor 2 (eIF-2alpha), as well as
37 irect substrate of PKR, the alpha subunit of eukaryotic initiation factor 2 (eIF-2alpha), was equally
38 ating the alpha subunit of protein synthesis eukaryotic initiation factor 2 (eIF-2alpha).
39 m the serum-starved cells phosphorylated the eukaryotic initiation factor-2 (eIF-2) alpha-subunit.
40      Phosphorylation of the alpha subunit of eukaryotic initiation factor-2 (eIF-2) is a well charact
41 e to cellular stresses by phosphorylation of eukaryotic initiation factor-2 (eIF-2).
42 GCN2 phosphorylation of the alpha subunit of eukaryotic initiation factor-2 (eIF-2).
43 g to phosphorylation of the alpha subunit of eukaryotic initiation factor-2 (eIF-2alpha) and inhibiti
44 s by phosphorylation of the alpha subunit of eukaryotic initiation factor-2 (eIF-2alpha).
45 phorylates the translation initiation factor eukaryotic initiation factor 2 (eIF2) and thereby inhibi
46            During translation initiation the eukaryotic initiation factor 2 (eIF2) forms a ternary co
47 family of protein kinases that phosphorylate eukaryotic initiation factor 2 (eIF2) in coordinating st
48                                              Eukaryotic initiation factor 2 (eIF2) is a central regul
49                                              Eukaryotic initiation factor 2 (eIF2) is a key integrato
50                           Phosphorylation of eukaryotic initiation factor 2 (eIF2) is an important me
51 that phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2) is fundamental to
52 ISR) via sensing amino acid depletion by the eukaryotic initiation factor 2 (eIF2) kinase GCN2.
53  repression of the p53 protein by the CUGBP1-eukaryotic initiation factor 2 (eIF2) repressor complex.
54                  Protein translation through eukaryotic initiation factor 2 (EIF2) signaling, a pathw
55 rotein kinase R (PKR), which inactivates the eukaryotic initiation factor 2 (eIF2) translation initia
56 rged transfer RNA induces phosphorylation of eukaryotic initiation factor 2 (eIF2) via the GC nondere
57 ar domains that can regulate the activity of eukaryotic initiation factor 2 (eIF2), a critical transl
58                Activated GCN2 phosphorylates eukaryotic initiation factor 2 (eIF2), altering gene-spe
59                                              Eukaryotic initiation factor 2 (eIF2), eIF3, and eIF4F w
60 48S ribosomal complexes on the IRES requires eukaryotic initiation factor 2 (eIF2), eIF3, eIF4A, and
61 ludes an early initiation complex containing eukaryotic initiation factor 2 (eIF2), GTP, and methioni
62 effector, the translation initiation complex eukaryotic initiation factor 2 (eIF2), have a profound i
63 and eukaryotes-initiation factor 2 (IF2) and eukaryotic initiation factor 2 (eIF2), respectively.
64 mation of a specific ternary complex between eukaryotic initiation factor 2 (eIF2), the initiator met
65 e R that phosphorylates the alpha subunit of eukaryotic initiation factor 2 (eIF2), thus rendering eI
66 an Obg-family GTPase, has been implicated in eukaryotic initiation factor 2 (eIF2)-mediated translati
67 ough phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2).
68 tion of a key translation initiation factor, eukaryotic initiation factor 2 (eIF2).
69 tion factor 1A stimulates 40S-binding of the eukaryotic initiation factor 2 (eIF2)/GTP/Met-tRNA(iMet)
70 nitiation is regulated by phosphorylation of eukaryotic initiation factor 2 (eIF2-P) that causes decr
71 mulate and activate Gcn2p phosphorylation of eukaryotic initiation factor-2 (eIF2) and the general am
72                           Phosphorylation of eukaryotic initiation factor-2 (eIF2) by pancreatic eIF2
73 During cellular stresses, phosphorylation of eukaryotic initiation factor-2 (eIF2) elicits gene expre
74 ly of protein kinases that phosphorylate the eukaryotic initiation factor-2 (eIF2) function in transl
75                           Phosphorylation of eukaryotic initiation factor-2 (eIF2) is an important me
76 t environmental stresses, phosphorylation of eukaryotic initiation factor-2 (eIF2) rapidly reduces pr
77                           Phosphorylation of eukaryotic initiation factor-2 (eIF2) regulates general
78 role of phosphorylation of the alpha-subunit eukaryotic initiation factor-2 (eIF2), and its attendant
79  by a mechanism involving phosphorylation of eukaryotic initiation factor-2 (eIF2).
80                                              Eukaryotic initiation factor 2- (eIF2-) associated glyco
81  phosphorylation of the alpha subunit of the eukaryotic initiation factor 2 (eIF2alpha) and inhibits
82  PKR phosphorylates the alpha-subunit of the eukaryotic initiation factor 2 (eIF2alpha) and inhibits
83  the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) and the conse
84 ases that phosphorylate the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) are activated
85 ion, phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) by the interf
86  the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) in MEFs in an
87  the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) in response t
88  mRNA translation through phosphorylation of eukaryotic initiation factor 2 (eIF2alpha) is essential
89      Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) is known to b
90 anslation initiation factor alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) is known to o
91  the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) translation i
92 yme that phosphorylates the alpha-subunit of eukaryotic initiation factor 2 (eIF2alpha), inhibiting t
93  phosphorylation of the alpha subunit of the eukaryotic initiation factor 2 (eIF2alpha), the cellular
94 anslation initiation factor alpha subunit of eukaryotic initiation factor 2 (eIF2alpha).
95 ated phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha).
96 t on phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha).
97 ough phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha).
98 tion initiation factor, the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha).
99 ough phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha).
100                               The absence of eukaryotic initiation factor 2 from these complexes sugg
101 w "privileged" translation despite inhibited eukaryotic initiation factor 2-guanosine triphosphate-in
102 eme-regulated kinase of the alpha subunit of eukaryotic initiation factor 2 (HRI) is activated in rab
103 eatic ER kinase, and its downstream effector eukaryotic initiation factor 2 in human leukemia (HL60)
104 sphorylation of PKR and the alpha subunit of eukaryotic initiation factor 2, indicating that K1L and
105 m activates the eIF-2alpha (alpha subunit of eukaryotic initiation factor 2) kinase PERK to transient
106 ither protein kinase R, which phosphorylates eukaryotic initiation factor 2, nor oligoadenylate synth
107      Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 on serine 51 was not dete
108 orylation of both protein kinase R (PKR) and eukaryotic initiation factor 2 on the alpha-subunit in s
109 ranslation initiation via phosphorylation of eukaryotic initiation factor 2 on the alpha-subunit.
110  responses (AADR) such as phosphorylation of eukaryotic initiation factor 2 (p-eIF2) leading to incre
111 e in phosphorylation of the alpha subunit of eukaryotic initiation factor 2, requiring PKR-like endop
112 ts, independent of source of infection, with eukaryotic initiation factor 2 signaling being the most
113 ations also impaired autophosphorylation and eukaryotic initiation factor 2 subunit alpha (eIF2alpha)
114 (ER) cisternae, increased phosphorylation of eukaryotic initiation factor 2 subunit alpha (P-eIF2alph
115 nslational arrest through phosphorylation of eukaryotic initiation factor 2 subunit alpha.
116 ated PKR phosphorylates the alpha subunit of eukaryotic initiation factor 2, thereby inhibiting prote
117 ated PKR phosphorylates the alpha-subunit of eukaryotic initiation factor 2, thereby inhibiting prote
118 hosphorylation of the alpha-subunit of eIF2 (eukaryotic initiation factor 2), which inhibits its guan
119 translational control via phosphorylation of eukaryotic initiation factor 2, which is implicated in l

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