Identification and characterization of a hitherto unknown nucleotide-binding domain and an intricate interdomain regulation in HflX-a ribosome binding GTPase.
about
Characterization of the autophosphorylation property of HflX, a ribosome-binding GTPase from Escherichia coliNovel MntR-independent mechanism of manganese homeostasis in Escherichia coli by the ribosome-associated protein HflX.The conserved GTPase HflX is a ribosome splitting factor that binds to the E-site of the bacterial ribosome.The putative Walker A and Walker B motifs of Rrp2 are required for the growth of Borrelia burgdorferi.Disassembly of the Staphylococcus aureus hibernating 100S ribosome by an evolutionarily conserved GTPase.The universally conserved GTPase HflX is an RNA helicase that restores heat-damaged ribosomes
P2860
Identification and characterization of a hitherto unknown nucleotide-binding domain and an intricate interdomain regulation in HflX-a ribosome binding GTPase.
description
2013 nî lūn-bûn
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2013年の論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年论文
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2013年论文
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2013年论文
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name
Identification and characteriz ...... flX-a ribosome binding GTPase.
@en
Identification and characteriz ...... flX-a ribosome binding GTPase.
@nl
type
label
Identification and characteriz ...... flX-a ribosome binding GTPase.
@en
Identification and characteriz ...... flX-a ribosome binding GTPase.
@nl
prefLabel
Identification and characteriz ...... flX-a ribosome binding GTPase.
@en
Identification and characteriz ...... flX-a ribosome binding GTPase.
@nl
P2093
P2860
P356
P1476
Identification and characteriz ...... flX-a ribosome binding GTPase.
@en
P2093
Balaji Prakash
Neha Vithani
Nikhil Jain
P2860
P304
P356
10.1093/NAR/GKT705
P407
P577
2013-08-16T00:00:00Z