Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Peripheral neuropathy via mutant tRNA synthetases: Inhibition of protein translation provides a possible explanation.

BioEssays : news and reviews in molecular, cellular and developmental biology - 1 Sept 2016

Storkebaum Erik

Abstract excerpt

Recent evidence indicates that inhibition of protein translation may be a common pathogenic mechanism for peripheral neuropathy associated with mutant tRNA synthetases (aaRSs). aaRSs are enzymes that ligate amino acids to their cognate tRNA, thus catalyzing the first step of translation. Dominant mutations in five distinct aaRSs cause Charcot-Marie-Tooth (CMT) peripheral neuropathy, characterized by...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acyl-tRNA Synthetases
Share to Axons
Share to Charcot-Marie-Tooth Disease

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Disease Models, Animal

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 27352040
DOI: 10.1002/bies.201600052
PMCID: PMC5094542

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Peripheral neuropathy via mutant tRNA synthetases: Inhibition of protein translation provides a possible explanation.PMID 27352040Read ↗

Emerging mechanisms of aminoacyl-tRNA synthetase mutations in recessive and dominant human disease.Semantic proximity Read ↗

Impaired protein translation in Drosophila models for Charcot-Marie-Tooth neuropathy caused by mutant tRNA synthetases.Semantic proximity Read ↗

An assessment of mechanisms underlying peripheral axonal degeneration caused by aminoacyl-tRNA synthetase mutations.Semantic proximity Read ↗

To charge or not to charge: mechanistic insights into neuropathy-associated tRNA synthetase mutations.Semantic proximity Read ↗

Aminoacyl-tRNA synthetases in Charcot-Marie-Tooth disease: A gain or a loss?Semantic proximity Read ↗

Aminoacyl-tRNA synthetase defects in neurological diseases.Semantic proximity Read ↗

CMT-associated mutations in glycyl- and tyrosyl-tRNA synthetases exhibit similar pattern of toxicity and share common genetic modifiers in Drosophila.Semantic proximity Read ↗

Drosophila Models for Charcot-Marie-Tooth Neuropathy Related to Aminoacyl-tRNA Synthetases.Semantic proximity Read ↗

The role of aminoacyl-tRNA synthetases in genetic diseases.Semantic proximity Read ↗

Aminoacyl tRNA synthetases and their connections to disease.Semantic proximity Read ↗

Human aminoacyl-tRNA synthetases in diseases of the nervous system.Semantic proximity Read ↗

Transfer RNA and small molecule therapeutics for aminoacyl-tRNA synthetase diseases.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.