eIF5A binds to translational machinery components and affects translation in yeast
about
Posttranslational synthesis of hypusine: evolutionary progression and specificity of the hypusine modificationMutational analyses of human eIF5A-1--identification of amino acid residues critical for eIF5A activity and hypusine modificationCrystal Structure of Hypusine-Containing Translation Factor eIF5A Bound to a Rotated Eukaryotic RibosomeHypusine-containing protein eIF5A promotes translation elongationDimerization of the yeast eukaryotic translation initiation factor 5A requires hypusine and is RNA dependent.Utp25p, a nucleolar Saccharomyces cerevisiae protein, interacts with U3 snoRNP subunits and affects processing of the 35S pre-rRNA.Fertility and polarized cell growth depends on eIF5A for translation of polyproline-rich formins in Saccharomyces cerevisiae.Yeast ribosomal protein L40 assembles late into precursor 60 S ribosomes and is required for their cytoplasmic maturationIdentification of metabolic pathways expressed by Pichia anomala Kh6 in the presence of the pathogen Botrytis cinerea on apple: new possible targets for biocontrol improvementThe unique hypusine modification of eIF5A promotes islet beta cell inflammation and dysfunction in mice.eIF5A promotes translation elongation, polysome disassembly and stress granule assemblyMicroRNA-434-3p regulates age-related apoptosis through eIF5A1 in the skeletal muscle.Functional significance of eIF5A and its hypusine modification in eukaryotesTranslational regulation of HIV-1 replication by HIV-1 Rev cellular cofactors Sam68, eIF5A, hRIP, and DDX3.eIF5A facilitates translation termination globally and promotes the elongation of many non polyproline-specific tripeptide sequencesEvidence for conformational changes in the yeast deoxyhypusine hydroxylase Lia1 upon iron displacement from its active site.Proteomic analysis of Apis cerana and Apis mellifera larvae fed with heterospecific royal jelly and by CSBV challenge.Inhibition of HIV-1 gene expression by Ciclopirox and Deferiprone, drugs that prevent hypusination of eukaryotic initiation factor 5A.The hypusine-containing translation factor eIF5A.Inactivation of eukaryotic initiation factor 5A (eIF5A) by specific acetylation of its hypusine residue by spermidine/spermine acetyltransferase 1 (SSAT1).Eukaryotic initiation factor 5A plays an essential role in luteinizing hormone receptor regulationProduction of active recombinant eIF5A: reconstitution in E.coli of eukaryotic hypusine modification of eIF5A by its coexpression with modifying enzymes.The deoxyhypusine synthase mutant dys1-1 reveals the association of eIF5A and Asc1 with cell wall integrity.Essential role of eIF5A-1 and deoxyhypusine synthase in mouse embryonic development.XPO1/CRM1 Inhibition Causes Antitumor Effects by Mitochondrial Accumulation of eIF5A.eIF5A interacts functionally with eEF2.Neuronal growth and survival mediated by eIF5A, a polyamine-modified translation initiation factor.Evidence for a Negative Cooperativity between eIF5A and eEF2 on Binding to the RibosomeThe elongation, termination, and recycling phases of translation in eukaryotes.Modulation of eIF5A expression using SNS01 nanoparticles inhibits NF-κB activity and tumor growth in murine models of multiple myeloma.Acetate reduces microglia inflammatory signaling in vitroHypusine modification for growth is the major function of spermidine in Saccharomyces cerevisiae polyamine auxotrophs grown in limiting spermidine.Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae.The eukaryote-specific N-terminal extension of ribosomal protein S31 contributes to the assembly and function of 40S ribosomal subunits.The Drosophila deoxyhypusine hydroxylase homologue nero and its target eIF5A are required for cell growth and the regulation of autophagy.The effect of hypusine modification on the intracellular localization of eIF5A.Structural modeling and mutational analysis of yeast eukaryotic translation initiation factor 5A reveal new critical residues and reinforce its involvement in protein synthesisUnique modifications of translation elongation factors.Translational control of eIF5A in various diseases.Phloem RNA-binding proteins as potential components of the long-distance RNA transport system.
P2860
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P2860
eIF5A binds to translational machinery components and affects translation in yeast
description
im Oktober 2006 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published on 07 August 2006
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в жовтні 2006
@uk
name
eIF5A binds to translational machinery components and affects translation in yeast
@en
eIF5A binds to translational machinery components and affects translation in yeast
@nl
type
label
eIF5A binds to translational machinery components and affects translation in yeast
@en
eIF5A binds to translational machinery components and affects translation in yeast
@nl
prefLabel
eIF5A binds to translational machinery components and affects translation in yeast
@en
eIF5A binds to translational machinery components and affects translation in yeast
@nl
P2093
P50
P1476
eIF5A binds to translational machinery components and affects translation in yeast
@en
P2093
Ana L C Maragno
Ana P B Gregio
Carlos A Mestriner
Cleslei F Zanelli
Suzanne Komili
P304
P356
10.1016/J.BBRC.2006.07.195
P407
P577
2006-08-07T00:00:00Z