Arginine-rhamnosylation as new strategy to activate translation elongation factor P
about
Structure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosomeNeisseria meningitidis Translation Elongation Factor P and Its Active-Site Arginine Residue Are Essential for Cell ViabilityRibosome pausing, arrest and rescue in bacteria and eukaryotes.Cyclic Rhamnosylated Elongation Factor P Establishes Antibiotic Resistance in Pseudomonas aeruginosa.Mutagenesis and Functional Analysis of the Bacterial Arginine Glycosyltransferase Effector NleB1 from Enteropathogenic Escherichia coli.Evidence for a Negative Cooperativity between eIF5A and eEF2 on Binding to the RibosomeRelevance of the Axis Spermidine/eIF5A for Plant Growth and Development.Deciphering the Translation Initiation Factor 5A Modification Pathway in Halophilic Archaea.Synthesis of rhamnosylated arginine glycopeptides and determination of the glycosidic linkage in bacterial elongation factor P.Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first ArgRha specific antibody.Stall no more at polyproline stretches with the translation elongation factors EF-P and IF-5A.Non-canonical roles of tRNAs and tRNA mimics in bacterial cell biologyThe bacterial arginine glycosyltransferase effector NleB preferentially modifies Fas-associated death domain protein (FADD).Elongation Factor P Interactions with the Ribosome Are Independent of Pausing.Alternative synthesis and antibacterial evaluation of 1,5-dideoxy-1,5-imino-L-rhamnitol.Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-PElongation factor-P at the crossroads of the host-endosymbiont interface.Carbonyl reduction by YmfI in Bacillus subtilis prevents accumulation of an inhibitory EF-P modification state.Evolutionary analysis of polyproline motifs in Escherichia coli reveals their regulatory role in translation.Amino acid substrates impose polyamine, eIF5A, or hypusine requirement for peptide synthesis.Structural basis for the glycosyltransferase activity of the Salmonella effector SseK3.EF-P Posttranslational Modification Has Variable Impact on Polyproline Translation in Bacillus subtilis.The role of polyproline motifs in the histidine kinase EnvZ.Genome Structure of the Opportunistic Pathogen () and Identification of Putative Virulence Factors
P2860
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P2860
Arginine-rhamnosylation as new strategy to activate translation elongation factor P
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
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2015年论文
@zh-cn
name
Arginine-rhamnosylation as new strategy to activate translation elongation factor P
@ast
Arginine-rhamnosylation as new strategy to activate translation elongation factor P
@en
type
label
Arginine-rhamnosylation as new strategy to activate translation elongation factor P
@ast
Arginine-rhamnosylation as new strategy to activate translation elongation factor P
@en
prefLabel
Arginine-rhamnosylation as new strategy to activate translation elongation factor P
@ast
Arginine-rhamnosylation as new strategy to activate translation elongation factor P
@en
P2093
P2860
P50
P356
P1476
Arginine-rhamnosylation as new strategy to activate translation elongation factor P
@en
P2093
Eva C Keilhauer
Julia Gödeke
Jürgen Rohr
Kirsten Jung
Kristin Wuichet
Matthias Mann
Maximilian Fürst
Susanne Häussler
P2507
P2860
P2888
P304
P356
10.1038/NCHEMBIO.1751
P577
2015-02-16T00:00:00Z