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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.
9 t the hepatic heme-regulated inhibitor (HRI)-eukaryotic initiation factor 2 alpha (eIF2 alpha) kinase
11 y converging at serine-51 phosphorylation on eukaryotic initiation factor 2 alpha (eIF2alpha) and act
12 spond to cellular stress by deactivating the eukaryotic initiation factor 2 alpha (eIF2alpha) or othe
14 d by attenuating protein translation through eukaryotic initiation factor 2 alpha (eIF2alpha) phospho
16 both with capsid-induced phosphorylation of eukaryotic initiation factor 2 alpha and with capsid-med
17 In 2014, scientists discovered mutations in eukaryotic initiation factor 2 alpha kinase 4 (EIF2AK4)
18 ation with polysomes likewise depends on the eukaryotic initiation factor 2 alpha kinase 4, which ass
19 at AKT1 protein loss led to the induction of eukaryotic initiation factor 2 alpha subunit (eIF2alpha)
20 nhibited PKR, we observed a reduced level of eukaryotic initiation factor 2 alpha subunit (eIF2alpha)
21 gative effect characterized by deficiency of eukaryotic initiation factor 2 alpha subunit phosphoryla
23 which can be repressed by phosphorylation of eukaryotic initiation factor 2 alpha-subunit (eIF2alpha)
24 age of procaspase-12, and phosphorylation of eukaryotic initiation factor-2 alpha in a human dopamine
25 suppresses protein synthesis by inactivating eukaryotic initiation factor 2-alpha (eIF2-alpha), to ex
26 imed T cells demonstrated phosphorylation of eukaryotic initiation factor 2-alpha (eIF2alpha), a 'col
27 IPK but was dependent on the presence of the eukaryotic initiation factor 2-alpha homology region, ma
28 st-in-class, small molecule inhibitor of the eukaryotic initiation factor 2-alpha kinase 3 (EIF2AK3)
29 s in phosphorylation of the alpha subunit of eukaryotic initiation factor 2 and NF-kappaB activity at
30 trol nonderepressible 2), phosphorylation of eukaryotic initiation factor 2, and increased synthesis
32 onine aminopeptidase 2, which is the same as eukaryotic initiation factor 2-associated glycoprotein,
33 ticulum resident kinase)/eIF2a (a subunit of eukaryotic initiation factor 2) axis of the ISR is stron
34 the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 causes translating mRNAs
35 -like ER kinase)-eIF2alpha (alpha subunit of eukaryotic initiation factor 2)-dependent pathway by Sub
36 that can phosphorylate the alpha subunit of eukaryotic initiation factor 2 (eIF-2alpha) and inhibit
37 the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF-2alpha) by activated
39 ctivity, and suppresses the alpha subunit of eukaryotic initiation factor 2 (eIF-2alpha) phosphorylat
40 oxia-associated increase in alpha subunit of eukaryotic initiation factor 2 (eIF-2alpha) phosphorylat
41 ke ER kinase (PERK) and the alpha subunit of eukaryotic initiation factor 2 (eIF-2alpha), as well as
42 irect substrate of PKR, the alpha subunit of eukaryotic initiation factor 2 (eIF-2alpha), was equally
44 m the serum-starved cells phosphorylated the eukaryotic initiation factor-2 (eIF-2) alpha-subunit.
48 g to phosphorylation of the alpha subunit of eukaryotic initiation factor-2 (eIF-2alpha) and inhibiti
50 t, we address the role of phosphorylation of eukaryotic initiation factor 2 (eIF2) and attendant gene
51 phorylates the translation initiation factor eukaryotic initiation factor 2 (eIF2) and thereby inhibi
53 family of protein kinases that phosphorylate eukaryotic initiation factor 2 (eIF2) in coordinating st
58 that phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2) is fundamental to
60 repression of the p53 protein by the CUGBP1-eukaryotic initiation factor 2 (eIF2) repressor complex.
62 Ai) in a ternary complex (TC) with GTP-bound eukaryotic initiation factor 2 (eIF2) to the small (40S)
63 rotein kinase R (PKR), which inactivates the eukaryotic initiation factor 2 (eIF2) translation initia
64 rged transfer RNA induces phosphorylation of eukaryotic initiation factor 2 (eIF2) via the GC nondere
65 ar domains that can regulate the activity of eukaryotic initiation factor 2 (eIF2), a critical transl
68 48S ribosomal complexes on the IRES requires eukaryotic initiation factor 2 (eIF2), eIF3, eIF4A, and
69 ludes an early initiation complex containing eukaryotic initiation factor 2 (eIF2), GTP, and methioni
70 effector, the translation initiation complex eukaryotic initiation factor 2 (eIF2), have a profound i
71 and eukaryotes-initiation factor 2 (IF2) and eukaryotic initiation factor 2 (eIF2), respectively.
72 mation of a specific ternary complex between eukaryotic initiation factor 2 (eIF2), the initiator met
73 e R that phosphorylates the alpha subunit of eukaryotic initiation factor 2 (eIF2), thus rendering eI
74 an Obg-family GTPase, has been implicated in eukaryotic initiation factor 2 (eIF2)-mediated translati
79 tion factor 1A stimulates 40S-binding of the eukaryotic initiation factor 2 (eIF2)/GTP/Met-tRNA(iMet)
80 nitiation is regulated by phosphorylation of eukaryotic initiation factor 2 (eIF2-P) that causes decr
81 mulate and activate Gcn2p phosphorylation of eukaryotic initiation factor-2 (eIF2) and the general am
83 During cellular stresses, phosphorylation of eukaryotic initiation factor-2 (eIF2) elicits gene expre
84 ly of protein kinases that phosphorylate the eukaryotic initiation factor-2 (eIF2) function in transl
86 t environmental stresses, phosphorylation of eukaryotic initiation factor-2 (eIF2) rapidly reduces pr
88 role of phosphorylation of the alpha-subunit eukaryotic initiation factor-2 (eIF2), and its attendant
91 onstrated the activation of the a subunit of eukaryotic initiation factor 2 (eIF2a) kinase GCN2 durin
92 phosphorylation of the alpha subunit of the eukaryotic initiation factor 2 (eIF2alpha) and inhibits
93 PKR phosphorylates the alpha-subunit of the eukaryotic initiation factor 2 (eIF2alpha) and inhibits
94 the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) and the conse
95 ases that phosphorylate the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) are activated
96 The phosphorylation of the alpha-subunit of eukaryotic initiation factor 2 (eIF2alpha) at a conserve
97 eticulum (ER) kinase (PERK)-alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) branch of the
98 ion, phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) by the interf
99 the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) in MEFs in an
100 ases that phosphorylate the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) in response t
101 the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) in response t
102 mRNA translation through phosphorylation of eukaryotic initiation factor 2 (eIF2alpha) is essential
103 Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) is known to b
104 anslation initiation factor alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) is known to o
105 the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) translation i
106 of protein kinase Gcn2, which phosphorylates eukaryotic initiation factor 2 (eIF2alpha) with attendan
107 yme that phosphorylates the alpha-subunit of eukaryotic initiation factor 2 (eIF2alpha), inhibiting t
108 phosphorylation of the alpha subunit of the eukaryotic initiation factor 2 (eIF2alpha), the cellular
116 nitiation factor eIF2alpha (alpha subunit of eukaryotic initiation factor 2), ensuring viral protein
118 w "privileged" translation despite inhibited eukaryotic initiation factor 2-guanosine triphosphate-in
119 eme-regulated kinase of the alpha subunit of eukaryotic initiation factor 2 (HRI) is activated in rab
120 eatic ER kinase, and its downstream effector eukaryotic initiation factor 2 in human leukemia (HL60)
121 sphorylation of PKR and the alpha subunit of eukaryotic initiation factor 2, indicating that K1L and
122 m activates the eIF-2alpha (alpha subunit of eukaryotic initiation factor 2) kinase PERK to transient
123 reduced glutathione, enhanced activation of eukaryotic initiation factor 2-mediated stress response,
124 ither protein kinase R, which phosphorylates eukaryotic initiation factor 2, nor oligoadenylate synth
125 Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 on serine 51 was not dete
126 orylation of both protein kinase R (PKR) and eukaryotic initiation factor 2 on the alpha-subunit in s
127 ranslation initiation via phosphorylation of eukaryotic initiation factor 2 on the alpha-subunit.
128 responses (AADR) such as phosphorylation of eukaryotic initiation factor 2 (p-eIF2) leading to incre
129 ntial effects of the APOL1-G1 variant on the eukaryotic initiation factor 2 pathway highlighted diffe
130 hared across the ages, corroborating similar eukaryotic initiation factor 2 phosphorylation responses
131 e in phosphorylation of the alpha subunit of eukaryotic initiation factor 2, requiring PKR-like endop
132 n 1976 to phosphorylate the alpha-subunit of eukaryotic initiation factor 2, revealing a new molecula
133 ts, independent of source of infection, with eukaryotic initiation factor 2 signaling being the most
134 ations also impaired autophosphorylation and eukaryotic initiation factor 2 subunit alpha (eIF2alpha)
135 (ER) cisternae, increased phosphorylation of eukaryotic initiation factor 2 subunit alpha (P-eIF2alph
137 ated PKR phosphorylates the alpha subunit of eukaryotic initiation factor 2, thereby inhibiting prote
138 ated PKR phosphorylates the alpha-subunit of eukaryotic initiation factor 2, thereby inhibiting prote
139 hosphorylation of the alpha-subunit of eIF2 (eukaryotic initiation factor 2), which inhibits its guan
140 translational control via phosphorylation of eukaryotic initiation factor 2, which is implicated in l
141 mitochondrial localization of phosphorylated eukaryotic initiation factor 2, which we show is suffici