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

Ubiquitously Expressed Proteins and Restricted Phenotypes: Exploring Cell-Specific Sensitivities to Impaired tRNA Charging.

Trends in genetics : TIG - 1 Feb 2020

Kuo Molly E, Antonellis Anthony

Abstract excerpt

Aminoacyl-tRNA synthetases (ARS) are ubiquitously expressed, essential enzymes that charge tRNA with cognate amino acids. Variants in genes encoding ARS enzymes lead to myriad human inherited diseases. First, missense alleles cause dominant peripheral neuropathy. Second, missense, nonsense, and frameshift alleles cause recessive multisystem disorders that differentially affect tissues depending on which ARS is...

Read the complete abstract on PubMed

Topics

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

Share to Alleles
Share to Amino Acids
Share to Amino Acyl-tRNA Synthetases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Predisposition to Disease

Share to Mutation

Share to Peripheral Nervous System Diseases

Share to Phenotype

Share to RNA, Transfer

Source

Open in PubMed Open full text

Identifiers

PMID: 31839378
DOI: 10.1016/j.tig.2019.11.007
PMCID: PMC6980692

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Ubiquitously Expressed Proteins and Restricted Phenotypes: Exploring Cell-Specific Sensitivities to Impaired tRNA Charging.PMID 31839378Read ↗

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

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

The Role of Nuclear-Encoded Mitochondrial tRNA Charging Enzymes in Human Inherited Disease.Semantic proximity Read ↗

Asparaginyl-tRNA synthetase (NARS1) variants implicated in dominant neurological phenotypes display dominant-negative properties.Semantic proximity Read ↗

Aminoacyl-tRNA synthetase deficiencies in search of common themes.Semantic proximity Read ↗

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

Aminoacyl-tRNA synthetase defects in neurological diseases.Semantic 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 ↗

Functional analyses of glycyl-tRNA synthetase mutations suggest a key role for tRNA-charging enzymes in peripheral axons.Semantic proximity Read ↗

Compound heterozygosity for loss-of-function GARS variants results in a multisystem developmental syndrome that includes severe growth retardation.Semantic proximity Read ↗

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