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

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

Journal of neurochemistry - 1 May 2021

Zhang Han, Zhou Zhong-Wei, Sun Litao

Abstract excerpt

Charcot-Marie-Tooth disease (CMT) is one of the most common inherited neurodegenerative disorders with an increasing number of CMT-associated variants identified as causative factors, however, there has been no effective therapy for CMT to date. Aminoacyl-tRNA synthetases (aaRS) are essential enzymes in translation by charging amino acids onto their cognate tRNAs during protein synthesis. Dominant monoallelic...

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 Charcot-Marie-Tooth Disease
Share to Disease Models, Animal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 33236345
DOI: 10.1111/jnc.15249
PMCID: PMC8247414

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Aminoacyl-tRNA synthetases in Charcot-Marie-Tooth disease: A gain or a loss?PMID 33236345Read ↗

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

Searching for non-canonical functions of aminoacyl-tRNA synthases based on mutations carried by Charcot-Marie-Tooth patientsSemantic proximity Read ↗

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

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

Associations between Neurological Diseases and Mutations in the Human Glycyl-tRNA Synthetase.Semantic proximity Read ↗

Aminoacyl-tRNA synthetases: Structure, function, and drug discovery.Semantic proximity Read ↗

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

Deficient activity of alanyl-tRNA synthetase underlies an autosomal recessive syndrome of progressive microcephaly, hypomyelination, and epileptic encephalopathy.Semantic proximity Read ↗

Heterozygous Seryl-tRNA Synthetase 1 Variants Cause Charcot-Marie-Tooth Disease.Semantic proximity Read ↗

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

CMT2N-causing aminoacylation domain mutants enable Nrp1 interaction with AlaRS.Semantic proximity Read ↗

Hypermorphic and hypomorphic AARS alleles in patients with CMT2N expand clinical and molecular heterogeneities.Semantic proximity Read ↗

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