The non-canonical hydroxylase structure of YfcM reveals a metal ion-coordination motif required for EF-P hydroxylation.
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Neisseria meningitidis Translation Elongation Factor P and Its Active-Site Arginine Residue Are Essential for Cell ViabilityStall no more at polyproline stretches with the translation elongation factors EF-P and IF-5A.Modifying the maker: Oxygenases target ribosome biology.The role of polyproline motifs in the histidine kinase EnvZ.
P2860
The non-canonical hydroxylase structure of YfcM reveals a metal ion-coordination motif required for EF-P hydroxylation.
description
2014 nî lūn-bûn
@nan
2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
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
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2014年论文
@wuu
name
The non-canonical hydroxylase ...... quired for EF-P hydroxylation.
@ast
The non-canonical hydroxylase ...... quired for EF-P hydroxylation.
@en
The non-canonical hydroxylase ...... quired for EF-P hydroxylation.
@nl
type
label
The non-canonical hydroxylase ...... quired for EF-P hydroxylation.
@ast
The non-canonical hydroxylase ...... quired for EF-P hydroxylation.
@en
The non-canonical hydroxylase ...... quired for EF-P hydroxylation.
@nl
prefLabel
The non-canonical hydroxylase ...... quired for EF-P hydroxylation.
@ast
The non-canonical hydroxylase ...... quired for EF-P hydroxylation.
@en
The non-canonical hydroxylase ...... quired for EF-P hydroxylation.
@nl
P2093
P2860
P50
P356
P1476
The non-canonical hydroxylase ...... quired for EF-P hydroxylation.
@en
P2093
Andrei Rajkovic
Kan Kobayashi
Michael Ibba
Osamu Nureki
Owen E Branson
Ryuichiro Ishitani
P2860
P304
12295-12305
P356
10.1093/NAR/GKU898
P407
P577
2014-10-01T00:00:00Z