Blocking eIF4E-eIF4G interaction as a strategy to impair coronavirus replication.
about
Structure of the eukaryotic translation initiation factor eIF4E in complex with 4EGI-1 reveals an allosteric mechanism for dissociating eIF4GHigh throughput screening for small molecule enhancers of the interferon signaling pathway to drive next-generation antiviral drug discoveryViral and Cellular mRNA Translation in Coronavirus-Infected Cells.SARS coronavirus nsp1 protein induces template-dependent endonucleolytic cleavage of mRNAs: viral mRNAs are resistant to nsp1-induced RNA cleavageEukaryotic initiation factor 4F: a vulnerability of tumor cells.Targeting the eIF4F translation initiation complex: a critical nexus for cancer developmentMurine norovirus 1 (MNV1) replication induces translational control of the host by regulating eIF4E activity during infectionEmerging therapeutics targeting mRNA translationSevere acute respiratory syndrome coronavirus nsp1 facilitates efficient propagation in cells through a specific translational shutoff of host mRNA.Therapeutic interventions to disrupt the protein synthetic machinery in melanomaReselection of a genomic upstream open reading frame in mouse hepatitis coronavirus 5'-untranslated-region mutantsFunctional genomics reveals that tumors with activating phosphoinositide 3-kinase mutations are dependent on accelerated protein turnover.Tinkering with translation: protein synthesis in virus-infected cells.Non-canonical Translation in Plant RNA Viruses.Hippuristanol - A potent steroid inhibitor of eukaryotic initiation factor 4A.4EBP1/eIF4E and p70S6K/RPS6 axes play critical and distinct roles in hepatocarcinogenesis driven by AKT and N-Ras proto-oncogenes in mice.Comparative Proteome Analysis of Porcine Jejunum Tissues in Response to a Virulent Strain of Porcine Epidemic Diarrhea Virus and Its Attenuated Strain.Targeting Hsp27/eIF4E interaction with phenazine compound: a promising alternative for castration-resistant prostate cancer treatment.The p53 target gene TRIM22 directly or indirectly interacts with the translation initiation factor eIF4E and inhibits the binding of eIF4E to eIF4G.Beyond molecular tumor heterogeneity: protein synthesis takes control.Pancreatic tumours escape from translational control through 4E-BP1 loss.Cellular hnRNP A1 Interacts with Nucleocapsid Protein of Porcine Epidemic Diarrhea Virus and Impairs Viral Replication.
P2860
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P2860
Blocking eIF4E-eIF4G interaction as a strategy to impair coronavirus replication.
description
2011 nî lūn-bûn
@nan
2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Blocking eIF4E-eIF4G interaction as a strategy to impair coronavirus replication.
@ast
Blocking eIF4E-eIF4G interaction as a strategy to impair coronavirus replication.
@en
type
label
Blocking eIF4E-eIF4G interaction as a strategy to impair coronavirus replication.
@ast
Blocking eIF4E-eIF4G interaction as a strategy to impair coronavirus replication.
@en
prefLabel
Blocking eIF4E-eIF4G interaction as a strategy to impair coronavirus replication.
@ast
Blocking eIF4E-eIF4G interaction as a strategy to impair coronavirus replication.
@en
P2093
P2860
P356
P1433
P1476
Blocking eIF4E-eIF4G interaction as a strategy to impair coronavirus replication
@en
P2093
David R Hall
Jerry Pelletier
Marc Desforges
Pierre J Talbot
Regina Cencic
Sandor Vajda
P2860
P304
P356
10.1128/JVI.00078-11
P577
2011-04-20T00:00:00Z