Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.
about
Structure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosomeA novel mouse model for inhibition of DOHH-mediated hypusine modification reveals a crucial function in embryonic development, proliferation and oncogenic transformationNeisseria meningitidis Translation Elongation Factor P and Its Active-Site Arginine Residue Are Essential for Cell ViabilityThe hypusine-containing translation factor eIF5A.Elongation factor P and modifying enzyme PoxA are necessary for virulence of Shigella flexneri.Translation initiation rate determines the impact of ribosome stalling on bacterial protein synthesis.Genome-wide analyses and functional classification of proline repeat-rich proteins: potential role of eIF5A in eukaryotic evolutionProtein Hydroxylation Catalyzed by 2-Oxoglutarate-dependent Oxygenases.The bacterial translation stress response.The non-canonical hydroxylase structure of YfcM reveals a metal ion-coordination motif required for EF-P hydroxylation.Predicting the minimal translation apparatus: lessons from the reductive evolution of mollicutes.The large ribosomal subunit protein L9 enables the growth of EF-P deficient cells and enhances small subunit maturationArginine-rhamnosylation as new strategy to activate translation elongation factor PBiological Relevance and Therapeutic Potential of the Hypusine Modification System.Evidence for a Negative Cooperativity between eIF5A and eEF2 on Binding to the Ribosome(R)-β-lysine-modified elongation factor P functions in translation elongation.Nascent peptides that block protein synthesis in bacteria.Divergent protein motifs direct elongation factor P-mediated translational regulation in Salmonella enterica and Escherichia coli.High-precision analysis of translational pausing by ribosome profiling in bacteria lacking EFP.Translation Control of Swarming Proficiency in Bacillus subtilis by 5-Amino-pentanolylated Elongation Factor PeIF5A promotes translation of polyproline motifs.Distinct XPPX sequence motifs induce ribosome stalling, which is rescued by the translation elongation factor EF-PUniformity of Peptide Release Is Maintained by Methylation of Release Factors.Deciphering the Translation Initiation Factor 5A Modification Pathway in Halophilic Archaea.Molecular evolution of protein-RNA mimicry as a mechanism for translational controleIF5A and EF-P: two unique translation factors are now traveling the same road.Stall no more at polyproline stretches with the translation elongation factors EF-P and IF-5A.Regulation of bacterial gene expression by ribosome stalling and rescuing.Modifying the maker: Oxygenases target ribosome biology.Hydroxylation and translational adaptation to stress: some answers lie beyond the STOP codon.A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P.Maintenance of protein synthesis reading frame by EF-P and m(1)G37-tRNA.Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-PTranslational stalling at polyproline stretches is modulated by the sequence context upstream of the stall site.Elongation factor-P at the crossroads of the host-endosymbiont interface.Crystallization and preliminary X-ray crystallographic analysis of YfcM: an important factor for EF-P hydroxylation.Essential structural elements in tRNA(Pro) for EF-P-mediated alleviation of translation stalling.EF-P dependent pauses integrate proximal and distal signals during translation.EF-P is essential for rapid synthesis of proteins containing consecutive proline residues.Elongation factor P: Function and effects on bacterial fitness.
P2860
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P2860
Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.
description
2012 nî lūn-bûn
@nan
2012 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.
@ast
Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.
@en
Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.
@nl
type
label
Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.
@ast
Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.
@en
Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.
@nl
prefLabel
Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.
@ast
Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.
@en
Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.
@nl
P2860
P50
P921
P356
P1476
Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.
@en
P2093
Kai Virumäe
P2860
P2888
P304
P356
10.1038/NCHEMBIO.1001
P577
2012-06-17T00:00:00Z