Neddylation requires glycyl-tRNA synthetase to protect activated E2. - Test2 - elhamkhani - TriplyDB

Neddylation requires glycyl-tRNA synthetase to protect activated E2.

Neddylation requires glycyl-tRNA synthetase to protect activated E2.

http://www.wikidata.org/entity/Q37150065

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Emerging Mechanisms of Aminoacyl-tRNA Synthetase Mutations in Recessive and Dominant Human Disease.Predicting the pathogenicity of aminoacyl-tRNA synthetase mutations.Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.The role of tRNA synthetases in neurological and neuromuscular disorders.Reversible lysine acetylation regulates nuclear translocation of TyrRS to counteract genotoxic oxidative stress.Protein neddylation and its alterations in human cancers for targeted therapy.Plexin-Semaphorin Signaling Modifies Neuromuscular Defects in a Drosophila Model of Peripheral Neuropathy.

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Neddylation requires glycyl-tRNA synthetase to protect activated E2.

http://www.wikidata.org/entity/Q37150065

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 27 June 2016

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Neddylation requires glycyl-tRNA synthetase to protect activated E2.

@en

Neddylation requires glycyl-tRNA synthetase to protect activated E2.

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type

label

Neddylation requires glycyl-tRNA synthetase to protect activated E2.

@en

Neddylation requires glycyl-tRNA synthetase to protect activated E2.

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prefLabel

Neddylation requires glycyl-tRNA synthetase to protect activated E2.

@en

Neddylation requires glycyl-tRNA synthetase to protect activated E2.

@nl

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Nature Structural & Molecular Biology

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Neddylation requires glycyl-tRNA synthetase to protect activated E2.

@en

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Janelle Lauer

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

Litao Sun

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

Patrick R Griffin

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

Qian Zhang

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

Xiang-Lei Yang

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

Yi Shi

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

Ze Liu

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

Zhongying Mo

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

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Charcot-Marie-Tooth-linked mutant GARS is toxic to peripheral neurons independent of wild-type GARS levels

Structure of a RING E3 trapped in action reveals ligation mechanism for the ubiquitin-like protein NEDD8

A unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8

Two E3 ubiquitin ligases, SCF-Skp2 and DDB1-Cul4, target human Cdt1 for proteolysis.

Long-range structural effects of a Charcot-Marie-Tooth disease-causing mutation in human glycyl-tRNA synthetase

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

E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification

A new NEDD8-ligating system for cullin-4A

Characterization of NEDD8, a developmentally down-regulated ubiquitin-like protein

Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V.

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730-737

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scholarly article

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10.1038/NSMB.3250

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8

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23

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2016-06-27T00:00:00Z

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27348078

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4972647

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