YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase. - Wikidata - awgldk - TriplyDB

YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase.

YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase.

http://www.wikidata.org/entity/Q35182665

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Crystal structure of the dimer of two essentialSalmonella typhimuriumproteins, YgjD & YeaZ and calorimetric evidence for the formation of a ternary YgjD-YeaZ-YjeE complex Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside NMR-based Structural Analysis of Threonylcarbamoyl-AMP Synthase and Its Substrate Interactions.Specific RNA-protein interactions detected with saturation transfer difference NMR Structure-function analysis of Sua5 protein reveals novel functional motifs required for the biosynthesis of the universal t6A tRNA modification.

P2860

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P2860

YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase.

http://www.wikidata.org/entity/Q35182665

description

2011 nî lūn-bûn

@nan

2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase.

@ast

YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase.

@en

type

label

YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase.

@ast

YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase.

@en

prefLabel

YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase.

@ast

YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase.

@en

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YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase

@en

P2093

Manal A Swairjo

http://www.w3.org/2001/XMLSchema#string

Paul F Agris

http://www.w3.org/2001/XMLSchema#string

Victoria Jones

http://www.w3.org/2001/XMLSchema#string

Yann Bilbille

http://www.w3.org/2001/XMLSchema#string

P2860

Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection

Improvement of reading frame maintenance is a common function for several tRNA modifications.

Post-transcriptional nucleotide modification and alternative folding of RNA

Hypermodified nucleosides in the anticodon of tRNALys stabilize a canonical U-turn structure

Functional anticodon architecture of human tRNALys3 includes disruption of intraloop hydrogen bonding by the naturally occurring amino acid modification, t6A

The structure of theyrdCgene product fromEscherichia colireveals a new fold and suggests a role in RNA binding

Anticodon domain modifications contribute order to tRNA for ribosome-mediated codon binding

RNA-Protein Mutually Induced Fit: STRUCTURE OF ESCHERICHIA COLI ISOPENTENYL-tRNA TRANSFERASE IN COMPLEX WITH tRNA(Phe)

Snapshots of Dynamics in Synthesizing N 6 -Isopentenyladenosine at the tRNA Anticodon

Stabilization of the anticodon stem-loop of tRNALys,3 by an A+-C base-pair and by pseudouridine

P304

1678-1687

http://www.w3.org/2001/XMLSchema#string

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scholarly article

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10.1261/RNA.2592411

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9

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17

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Kimberly A Harris

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2011-07-20T00:00:00Z

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51508035

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21775474

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3162333

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