Identification of essential domains for Escherichia coli tRNA(leu) aminoacylation and amino acid editing using minimalist RNA molecules.
about
Crystal structure of a human aminoacyl-tRNA synthetase cytokineA T-stem slip in human mitochondrial tRNALeu(CUN) governs its charging capacityStructural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetaseAn inserted region of leucyl-tRNA synthetase plays a critical role in group I intron splicing.Pre-transfer editing by class II prolyl-tRNA synthetase: role of aminoacylation active site in "selective release" of noncognate amino acids.Two distinct domains of the beta subunit of Aquifex aeolicus leucyl-tRNA synthetase are involved in tRNA binding as revealed by a three-hybrid selection.tRNA synthetase: tRNA aminoacylation and beyondThe determination of tRNALeu recognition nucleotides for Escherichia coli L/F transferaseCharacterization of benzoxaborole-based antifungal resistance mutations demonstrates that editing depends on electrostatic stabilization of the leucyl-tRNA synthetase editing cap.Changing identities: tRNA duplication and remolding within animal mitochondrial genomes.CP1-dependent partitioning of pretransfer and posttransfer editing in leucyl-tRNA synthetase.Disrupted tRNA Genes and tRNA Fragments: A Perspective on tRNA Gene Evolution.A counterintuitive Mg2+-dependent and modification-assisted functional folding of mitochondrial tRNAsA Flexible peptide tether controls accessibility of a unique C-terminal RNA-binding domain in leucyl-tRNA synthetases.Crucial role of the C-terminal domain of Mycobacterium tuberculosis leucyl-tRNA synthetase in aminoacylation and editing.Recognition of tRNALeu by Aquifex aeolicus leucyl-tRNA synthetase during the aminoacylation and editing steps.Highly conserved modified nucleosides influence Mg2+-dependent tRNA folding.The pathogenic U3271C human mitochondrial tRNA(Leu(UUR)) mutation disrupts a fragile anticodon stem.Tertiary structure base pairs between D- and TpsiC-loops of Escherichia coli tRNA(Leu) play important roles in both aminoacylation and editing.Human mitochondrial leucyl tRNA synthetase can suppress non cognate pathogenic mt-tRNA mutationsNatural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation.Leucyl-tRNA synthetase from the hyperthermophilic bacterium Aquifex aeolicus recognizes minihelices.The crystal structure of leucyl-tRNA synthetase complexed with tRNALeu in the post-transfer-editing conformation.Studying base pair open-close kinetics of tRNALeu by TROSY-based proton exchange NMR spectroscopy.Functional divergence of a unique C-terminal domain of leucyl-tRNA synthetase to accommodate its splicing and aminoacylation roles.Aminoacylation complex structures of leucyl-tRNA synthetase and tRNALeu reveal two modes of discriminator-base recognition
P2860
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P2860
Identification of essential domains for Escherichia coli tRNA(leu) aminoacylation and amino acid editing using minimalist RNA molecules.
description
2002 nî lūn-bûn
@nan
2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Identification of essential do ...... sing minimalist RNA molecules.
@ast
Identification of essential do ...... sing minimalist RNA molecules.
@en
type
label
Identification of essential do ...... sing minimalist RNA molecules.
@ast
Identification of essential do ...... sing minimalist RNA molecules.
@en
prefLabel
Identification of essential do ...... sing minimalist RNA molecules.
@ast
Identification of essential do ...... sing minimalist RNA molecules.
@en
P2093
P2860
P356
P1476
Identification of essential do ...... sing minimalist RNA molecules.
@en
P2093
Amy M Williams
Deana C Larkin
George E Fox
Susan A Martinis
P2860
P304
P356
10.1093/NAR/30.10.2103
P407
P577
2002-05-01T00:00:00Z