Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3T3 cells.
about
New antiviral pathway that mediates hepatitis C virus replicon interferon sensitivity through ADAR1Human CPR (cell cycle progression restoration) genes impart a Far- phenotype on yeast cells.Regulation of interferon-induced protein kinase PKR: modulation of P58IPK inhibitory function by a novel protein, P52rIPKIdentification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational controlA new double-stranded RNA-binding protein that interacts with PKRThe Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKRRegulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha.Antiviral actions of interferonsAlpha interferon induces distinct translational control programs to suppress hepatitis C virus RNA replicationA herpesvirus genetic element which affects translation in the absence of the viral GADD34 functionIdentification of a 170-kDa protein over-expressed in lung cancersRAX, the PKR activator, sensitizes cells to inflammatory cytokines, serum withdrawal, chemotherapy, and viral infectionImpact of protein kinase PKR in cell biology: from antiviral to antiproliferative actionRegulation of ribonucleotide reductase M2 expression by the upstream AUGsAntiapoptotic and oncogenic potentials of hepatitis C virus are linked to interferon resistance by viral repression of the PKR protein kinasePKR-dependent mechanisms of gene expression from a subgenomic hepatitis C virus clone.Posttranscriptional control of gene expression in yeast.Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2.Protein kinase R modulates c-Fos and c-Jun signaling to promote proliferation of hepatocellular carcinoma with hepatitis C virus infectionA novel mouse model for inhibition of DOHH-mediated hypusine modification reveals a crucial function in embryonic development, proliferation and oncogenic transformationResistance to vesicular stomatitis virus infection requires a functional cross talk between the eukaryotic translation initiation factor 2alpha kinases PERK and PKRPERK and GCN2 contribute to eIF2alpha phosphorylation and cell cycle arrest after activation of the unfolded protein response pathwayUnfolding anti-tumor immunity: ER stress responses sculpt tolerogenic myeloid cells in cancerPhosphorylation of Eukaryotic Initiation Factor-2α during Stress and Encystation in Entamoeba Species.An oncogenic role for the phosphorylated h-subunit of human translation initiation factor eIF3Double-stranded RNA-dependent protein kinase is involved in 2-methoxyestradiol-mediated cell death of osteosarcoma cells.Inhibition of proliferation by PERK regulates mammary acinar morphogenesis and tumor formation.Loss of the eukaryotic initiation factor 3f in pancreatic cancer.Inhibition of eIF2alpha dephosphorylation inhibits ErbB2-induced deregulation of mammary acinar morphogenesisTranslational homeostasis: eukaryotic translation initiation factor 4E control of 4E-binding protein 1 and p70 S6 kinase activities.Double-stranded RNA-activated protein kinase mediates virus-induced apoptosis: a new role for an old actor.RNA interference in mammalian cells using siRNAs synthesized with T7 RNA polymerase.Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR.Translational control of viral gene expression in eukaryotesDouble-stranded-RNA-activated protein kinase PKR enhances transcriptional activation by tumor suppressor p53Inhibition of double-stranded RNA- and tumor necrosis factor alpha-mediated apoptosis by tetratricopeptide repeat protein and cochaperone P58(IPK)The protein kinase PKR: a molecular clock that sequentially activates survival and death programs.Increased expression of the dsRNA-activated protein kinase PKR in breast cancer promotes sensitivity to doxorubicinA role of the kinase mTOR in cellular transformation induced by the oncoproteins P3k and Akt.
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P2860
Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3T3 cells.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on August 1995
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Abrogation of translation init ...... ansformation of NIH 3T3 cells.
@en
Abrogation of translation init ...... ansformation of NIH 3T3 cells.
@nl
type
label
Abrogation of translation init ...... ansformation of NIH 3T3 cells.
@en
Abrogation of translation init ...... ansformation of NIH 3T3 cells.
@nl
prefLabel
Abrogation of translation init ...... ansformation of NIH 3T3 cells.
@en
Abrogation of translation init ...... ansformation of NIH 3T3 cells.
@nl
P2093
P2860
P1433
P1476
Abrogation of translation init ...... ransformation of NIH 3T3 cells
@en
P2093
A E Koromilas
J W Hershey
N Sonenberg
P2860
P304
P356
10.1002/J.1460-2075.1995.TB00052.X
P407
P577
1995-08-01T00:00:00Z