Structural disorder in expanding the functionome of aminoacyl-tRNA synthetases. - Wikidata - awgldk - TriplyDB

Structural disorder in expanding the functionome of aminoacyl-tRNA synthetases.

Structural disorder in expanding the functionome of aminoacyl-tRNA synthetases.

http://www.wikidata.org/entity/Q37196704

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Infection-specific phosphorylation of glutamyl-prolyl tRNA synthetase induces antiviral immunity.The GAIT translational control system.

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Structural disorder in expanding the functionome of aminoacyl-tRNA synthetases.

http://www.wikidata.org/entity/Q37196704

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article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on September 2013

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

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name

Structural disorder in expanding the functionome of aminoacyl-tRNA synthetases.

@en

Structural disorder in expanding the functionome of aminoacyl-tRNA synthetases.

@nl

type

label

Structural disorder in expanding the functionome of aminoacyl-tRNA synthetases.

@en

Structural disorder in expanding the functionome of aminoacyl-tRNA synthetases.

@nl

prefLabel

Structural disorder in expanding the functionome of aminoacyl-tRNA synthetases.

@en

Structural disorder in expanding the functionome of aminoacyl-tRNA synthetases.

@nl

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J.CHEMBIOL.2013.07.013

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Chemistry and Biology

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Structural disorder in expanding the functionome of aminoacyl-tRNA synthetases.

@en

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Xiang-Lei Yang

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P2860

Two distinct cytokines released from a human aminoacyl-tRNA synthetase

Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life

Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway

Crystal structures and biochemical analyses suggest a unique mechanism and role for human glycyl-tRNA synthetase in Ap4A homeostasis

The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex

Crystal structure of a human aminoacyl-tRNA synthetase cytokine

Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process

Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains

Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity

Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex

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1093-1099

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scholarly article

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10.1016/J.CHEMBIOL.2013.07.013

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9

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20

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2013-09-01T00:00:00Z

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24054183

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3782743

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