about
Tracking a refined eIF4E-binding motif reveals Angel1 as a new partner of eIF4EMultifunctional roles of leader protein of foot-and-mouth disease viruses in suppressing host antiviral responsesInsights into the Biology of IRES Elements through Riboproteomic ApproachesGemin5 Binds to the Survival Motor Neuron mRNA to Regulate SMN ExpressionStructural insights into Gemin5-guided selection of pre-snRNAs for snRNP assemblyIdentification of gemin5 as a novel 7-methylguanosine cap-binding proteinThe RNA-binding protein Gemin5 binds directly to the ribosome and regulates global translationExploring IRES region accessibility by interference of foot-and-mouth disease virus infectivity.eIF4E: new family members, new binding partners, new roles.RNA structural elements of hepatitis C virus controlling viral RNA translation and the implications for viral pathogenesis.The Gemin associates of survival motor neuron are required for motor function in Drosophila.Unraveling regulation and new components of human P-bodies through a protein interaction framework and experimental validationAn unbiased proteomics approach to identify human cytomegalovirus RNA-associated proteins.Spinal muscular atrophy: the role of SMN in axonal mRNA regulation.Candidate RNA structures for domain 3 of the foot-and-mouth-disease virus internal ribosome entry site.RNA structure: new messages in translation, replication and disease. Workshop on the role of RNA structures in the translation of viral and cellular RNAs.RNA-binding proteins impacting on internal initiation of translation.Synthetic biology: tools to design, build, and optimize cellular processes.The pathogenesis of foot-and-mouth disease II: viral pathways in swine, small ruminants, and wildlife; myotropism, chronic syndromes, and molecular virus-host interactions.Hepatitis C viral protein translation: mechanisms and implications in developing antivirals.Gemin5: A Multitasking RNA-Binding Protein Involved in Translation Control.Structural basis for the biological relevance of the invariant apical stem in IRES-mediated translation.Magnesium-dependent folding of a picornavirus IRES element modulates RNA conformation and eIF4G interaction.Genome-wide identification of mRNAs associated with the protein SMN whose depletion decreases their axonal localization.Identification of RNA-protein interaction networks involved in the norovirus life cycle.Gemin5 proteolysis reveals a novel motif to identify L protease targets.Identification of novel non-canonical RNA-binding sites in Gemin5 involved in internal initiation of translation.Tailoring the switch from IRES-dependent to 5'-end-dependent translation with the RNase P ribozyme.G3BP1 interacts directly with the FMDV IRES and negatively regulates translation.Local RNA flexibility perturbation of the IRES element induced by a novel ligand inhibits viral RNA translation.Gemin5 promotes IRES interaction and translation control through its C-terminal region.Alternative Mechanisms to Initiate Translation in Eukaryotic mRNAs.Evolutionary conserved motifs constrain the RNA structure organization of picornavirus IRES.Insights into Structural and Mechanistic Features of Viral IRES Elements.The landscape of the non-canonical RNA-binding site of Gemin5 unveils a feedback loop counteracting the negative effect on translation.A novel function for the survival motoneuron protein as a translational regulator
P2860
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P2860
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
A novel role for Gemin5 in mRNA translation.
@en
A novel role for Gemin5 in mRNA translation.
@nl
type
label
A novel role for Gemin5 in mRNA translation.
@en
A novel role for Gemin5 in mRNA translation.
@nl
prefLabel
A novel role for Gemin5 in mRNA translation.
@en
A novel role for Gemin5 in mRNA translation.
@nl
P2093
P2860
P356
P1476
A novel role for Gemin5 in mRNA translation.
@en
P2093
Almudena Pacheco
Jorge Ramajo
Noemí Fernández
Sonia López de Quinto
P2860
P304
P356
10.1093/NAR/GKN979
P577
2008-12-09T00:00:00Z