Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F.
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Biochemical characterization of the ATPase and helicase activity of UAP56, an essential pre-mRNA splicing and mRNA export factorStructural basis for the enhancement of eIF4A helicase activity by eIF4G.Identification of differential proteins in nasopharyngeal carcinoma cells with p53 silence by proteome analysisStimulation of mammalian translation initiation factor eIF4A activity by a small molecule inhibitor of eukaryotic translation.mRNA decay during herpes simplex virus (HSV) infections: protein-protein interactions involving the HSV virion host shutoff protein and translation factors eIF4H and eIF4A.Ddx42p--a human DEAD box protein with RNA chaperone activities.Phosphorylation of eucaryotic translation initiation factor 4B Ser422 is modulated by S6 kinasesA novel function of the MA-3 domains in transformation and translation suppressor Pdcd4 is essential for its binding to eukaryotic translation initiation factor 4AHerpes simplex virus virion host shutoff protein is stimulated by translation initiation factors eIF4B and eIF4HTranslational control by a small RNA: dendritic BC1 RNA targets the eukaryotic initiation factor 4A helicase mechanismDead-box proteins: a family affair--active and passive players in RNP-remodelingThe organization and regulation of mRNA-protein complexesMechanical Signaling in the Pathophysiology of Critical Illness MyopathyTranslational Control of the HIV Unspliced Genomic RNA'Ribozoomin'--translation initiation from the perspective of the ribosome-bound eukaryotic initiation factors (eIFs)DEAD-box helicases as integrators of RNA, nucleotide and protein bindingRNA helicase proteins as chaperones and remodelersA ribonucleoprotein complex protects the interleukin-6 mRNA from degradation by distinct herpesviral endonucleasesStructural evidence for consecutive Hel308-like modules in the spliceosomal ATPase Brr2Structure of the Tandem MA-3 Region of Pdcd4 Protein and Characterization of Its Interactions with eIF4A and eIF4GStructural Analysis of the DAP5 MIF4G Domain and Its Interaction with eIF4AStructural integrity of the PCI domain of eIF3a/TIF32 is required for mRNA recruitment to the 43S pre-initiation complexesInvestigation of the conserved glutamate immediately following the DEAD box in eukaryotic translation initiation factor 4AI.Characterization of Saccharomyces cerevisiae Npa2p (Urb2p) reveals a low-molecular-mass complex containing Dbp6p, Npa1p (Urb1p), Nop8p, and Rsa3p involved in early steps of 60S ribosomal subunit biogenesisCofactor-dependent specificity of a DEAD-box protein.Yeast eIF4B binds to the head of the 40S ribosomal subunit and promotes mRNA recruitment through its N-terminal and internal repeat domainsNtr1 activates the Prp43 helicase to trigger release of lariat-intron from the spliceosomeCharacterization of the essential activities of Saccharomyces cerevisiae Mtr4p, a 3'->5' helicase partner of the nuclear exosome.The DEAD-box protein Dbp2 functions with the RNA-binding protein Yra1 to promote mRNP assembly.The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis.What Is the Impact of mRNA 5' TL Heterogeneity on Translational Start Site Selection and the Mammalian Cellular Phenotype?Human eukaryotic initiation factor 4G (eIF4G) protein binds to eIF3c, -d, and -e to promote mRNA recruitment to the ribosomeQuantitative studies of mRNA recruitment to the eukaryotic ribosomeeIF4F: a retrospectiveA mechanistic overview of translation initiation in eukaryotesStructural insight of human DEAD-box protein rck/p54 into its substrate recognition with conformational changesThe transformation suppressor Pdcd4 is a novel eukaryotic translation initiation factor 4A binding protein that inhibits translationThe mechanism of eukaryotic translation initiation and principles of its regulationPhosphorylation of eukaryotic translation initiation factor 4B (EIF4B) by open reading frame 45/p90 ribosomal S6 kinase (ORF45/RSK) signaling axis facilitates protein translation during Kaposi sarcoma-associated herpesvirus (KSHV) lytic replicationInteraction between the NH2-terminal domain of eIF4A and the central domain of eIF4G modulates RNA-stimulated ATPase activity.
P2860
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P2860
Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F.
@ast
Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F.
@en
type
label
Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F.
@ast
Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F.
@en
prefLabel
Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F.
@ast
Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F.
@en
P2093
P356
P1476
Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F.
@en
P2093
Merrick WC
Richter NJ
Rogers GW Jr
P304
30914-30922
P356
10.1074/JBC.M100157200
P407
P577
2001-06-19T00:00:00Z