A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P.
about
Neisseria meningitidis Translation Elongation Factor P and Its Active-Site Arginine Residue Are Essential for Cell ViabilityHigh-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 PStall no more at polyproline stretches with the translation elongation factors EF-P and IF-5A.tRNAPro -mediated downregulation of elongation factor P is required for mgtCBR expression during Salmonella infection.eIF5A Functions Globally in Translation Elongation and Termination.Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-PEvolutionary analysis of polyproline motifs in Escherichia coli reveals their regulatory role in translation.The role of polyproline motifs in the histidine kinase EnvZ.
P2860
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P2860
A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
2014年论文
@zh
2014年论文
@zh-cn
name
A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P.
@en
type
label
A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P.
@en
prefLabel
A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P.
@en
P2093
P2860
P50
P1433
P1476
A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P.
@en
P2093
Allen Buskirk
Christopher J Woolstenhulme
Kai Virumäe
Kirsten Jung
P2860
P304
P356
10.1016/J.CELREP.2014.09.008
P577
2014-10-09T00:00:00Z