Hypusine-containing protein eIF5A promotes translation elongation
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Post-translational modification by β-lysylation is required for activity of Escherichia coli elongation factor P (EF-P)Agmatidine, a modified cytidine in the anticodon of archaeal tRNA(Ile), base pairs with adenosine but not with guanosineOne-Carbon Metabolism in Prostate Cancer: The Role of Androgen SignalingTranslational development of difluoromethylornithine (DFMO) for the treatment of neuroblastomaSerine, glycine and one-carbon units: cancer metabolism in full circleeIF5A isoforms and cancer: two brothers for two functions?Metabolic reprogramming and metabolic dependency in T cellsLost in translation: endoplasmic reticulum stress and the decline of β-cell health in diabetes mellitusPrinciples of translational control: an overviewFormation of the First Peptide Bond: The Structure of EF-P Bound to the 70S RibosomePoxA, YjeK, and Elongation Factor P Coordinately Modulate Virulence and Drug Resistance in Salmonella entericaA paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor PCrystal Structure of Hypusine-Containing Translation Factor eIF5A Bound to a Rotated Eukaryotic RibosomeNutrients and the Pkh1/2 and Pkc1 protein kinases control mRNA decay and P-body assembly in yeastFertility and polarized cell growth depends on eIF5A for translation of polyproline-rich formins in Saccharomyces cerevisiae.Eukaryotic translation initiation factor (eIF) 5A stimulates protein synthesis in Saccharomyces cerevisiaeStm1p alters the ribosome association of eukaryotic elongation factor 3 and affects translation elongationDom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay.Allosteric activation of trypanosomatid deoxyhypusine synthase by a catalytically dead paralogA structural domain mediates attachment of ethanolamine phosphoglycerol to eukaryotic elongation factor 1A in Trypanosoma bruceiDeoxyhypusine hydroxylase from Plasmodium vivax, the neglected human malaria parasite: molecular cloning, expression and specific inhibition by the 5-LOX inhibitor zileutonCPEB2-eEF2 interaction impedes HIF-1α RNA translationA novel mouse model for inhibition of DOHH-mediated hypusine modification reveals a crucial function in embryonic development, proliferation and oncogenic transformationTranslation initiation factors eIF3 and HCR1 control translation termination and stop codon read-through in yeast cellsNeisseria meningitidis Translation Elongation Factor P and Its Active-Site Arginine Residue Are Essential for Cell ViabilityDeoxyhypusine synthase promotes differentiation and proliferation of T helper type 1 (Th1) cells in autoimmune diabetesProteomic Analysis of Copper-Binding Proteins in Excess Copper-Stressed Roots of Two Rice (Oryza sativa L.) Varieties with Different Cu Tolerances.Inhibition of deoxyhypusine synthase enhances islet {beta} cell function and survival in the setting of endoplasmic reticulum stress and type 2 diabetesThe unique hypusine modification of eIF5A promotes islet beta cell inflammation and dysfunction in mice.Maternal protein-energy malnutrition during early pregnancy in sheep impacts the fetal ornithine cycle to reduce fetal kidney microvascular development.Characterization of a eukaryotic translation initiation factor 5A homolog from Tamarix androssowii involved in plant abiotic stress tolerance.eIF5A promotes translation elongation, polysome disassembly and stress granule assemblyMicroRNA-434-3p regulates age-related apoptosis through eIF5A1 in the skeletal muscle.A profusion of upstream open reading frame mechanisms in polyamine-responsive translational regulation.Predicting the pathway involved in post-translational modification of elongation factor P in a subset of bacterial species.Biochemical quantitation of the eIF5A hypusination in Arabidopsis thaliana uncovers ABA-dependent regulationFunctional significance of eIF5A and its hypusine modification in eukaryotesInhibition of eukaryotic translation elongation by cycloheximide and lactimidomycin.The role of polyamines in supporting growth of mammalian cells is mediated through their requirement for translation initiation and elongationTranslational regulation of HIV-1 replication by HIV-1 Rev cellular cofactors Sam68, eIF5A, hRIP, and DDX3.
P2860
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P248
Q24600333-E06D0CDD-925F-4A92-8CD8-D8A382A29CBAQ24625020-6D9F06EA-E362-4C04-B515-021A288B1C73Q26740548-11EBE816-10B4-49AE-AE14-872C9A9C1286Q26770306-23A6E2FE-080D-48D0-B47F-EA5F21331EBDQ26828610-6D7C4C65-F352-4559-877B-C5BF2CD155BCQ26830163-18AD7ECE-0A85-4434-8601-613A1A49F28BQ26864319-6E722A00-4951-492A-B379-6588F46FBCFAQ26864403-DD758392-6412-4053-9FAD-1FB3F3FA9A9DQ26995200-0FA06F68-B81C-4976-9838-CCD3CA65BA5DQ27657106-75CF479A-3B03-432E-BF71-6A48D5FEA2E8Q27663668-A95485D3-5416-4956-A609-DE4080F0A5C7Q27664126-05D23095-EF17-4E6F-AC8F-C4FC7DA048A5Q27704900-E063203B-C1DD-47A7-85A9-E844BF1F2B91Q27930050-C0423013-ABC9-4DD8-AF67-BEF924C7B8A7Q27932452-BE4DEC08-4ADA-4E2E-A590-07EFB068A49CQ27936637-AD964E71-9EAF-4BE4-BDE6-76C0D3B4FC1FQ27937056-53331045-C686-40B8-BEEE-C5FA41364D6BQ27937072-18907C55-D257-475F-A7B2-88A24BD9E7F4Q28119052-C241019A-DFA9-4B56-8F07-8F1E656BAEB2Q28473078-3508F5B9-2234-4A44-A99E-0E5E07059F1EQ28487727-7F358E50-C6AC-475B-9ED1-8D8B7EEC8145Q28509318-689526C1-31D6-4598-A970-3EC8A72340A9Q28510855-80E5BDAF-E11C-4E84-B615-4C8AB68F6478Q28535333-B08D1E64-8482-41BB-812C-7C3D40579660Q28553068-3774643A-6F7F-44CE-A9A5-63C3428BEE0EQ28586190-5BEEC471-C7EB-4006-AFC6-B5E39200C1F4Q30152943-94AE9832-5033-4F58-9818-1F5D81D1E196Q30429251-293111A0-230A-4729-98A6-6301E1985F29Q30435990-8807B71C-AAFD-422F-9961-FE63290FF41AQ30596717-D682B22C-8ED1-4610-9202-7B2BB0380142Q31077285-5159CF68-5A5C-476E-BEFF-E3A1D8C3C6FAQ33550797-80BA0179-A196-436F-9DF8-5D29A4104273Q33563502-F85F8C06-378F-4B0D-A981-E77F65924379Q33608811-E2FC9B8E-FFF3-42BE-8031-68A8396E4EE1Q33650393-A02C1F69-D9F9-4045-BAEB-9AFEFFE0D37AQ33658033-F8D9757A-D57E-40F8-9203-3733E6284AB4Q33691772-2118A30F-7AB4-4983-9A28-8D455E43DE83Q33699590-F3D33139-2E96-4B0C-86F0-082DC0FEEA8EQ33800179-FAAA00FD-E68C-48BE-80B5-EB106EC62B91Q33832420-F6A8D5C1-294A-4405-8877-F414BA3F9929
P2860
Hypusine-containing protein eIF5A promotes translation elongation
description
2009 nî lūn-bûn
@nan
2009 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Hypusine-containing protein eIF5A promotes translation elongation
@ast
Hypusine-containing protein eIF5A promotes translation elongation
@en
Hypusine-containing protein eIF5A promotes translation elongation.
@nl
type
label
Hypusine-containing protein eIF5A promotes translation elongation
@ast
Hypusine-containing protein eIF5A promotes translation elongation
@en
Hypusine-containing protein eIF5A promotes translation elongation.
@nl
altLabel
Hypusine-containing protein eIF5A promotes translation elongation
@en
prefLabel
Hypusine-containing protein eIF5A promotes translation elongation
@ast
Hypusine-containing protein eIF5A promotes translation elongation
@en
Hypusine-containing protein eIF5A promotes translation elongation.
@nl
P2093
P2860
P3181
P356
P1433
P1476
Hypusine-containing protein eIF5A promotes translation elongation
@en
P2093
Daniel E Eyler
Preeti Saini
Rachel Green
P2860
P2888
P304
P3181
P356
10.1038/NATURE08034
P407
P50
P577
2009-05-07T00:00:00Z
P5875
P6179
1026075248