Evidence map›Paper›PMID 39487674›Full record

ReviewIUBMB life2025

Aminoacyl-tRNA synthetase defects in neurological diseases.

Hong Zhang, Jiqiang Ling

Abstract readReview
In one paragraph

Review in IUBMB life, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Hong ZhangDepartment of Cell Biology and Molecular Genetics, The University of Maryland, College Park, Maryland, USA.
Jiqiang LingDepartment of Cell Biology and Molecular Genetics, The University of Maryland, College Park, Maryland, USA.ORCID 0000-0003-4466-8304

Funding

Regulation and Physiological Roles of Translational FidelityR35GM136213 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI LING, JIQIANG · 2020 to 2024
$2.0M
NIGMS NIH HHS R35 GM136213NIGMS NIH HHS R35GM136213
6 · The paper itself

Abstract

Aminoacyl-tRNA synthetases (aaRSs) are essential enzymes to support protein synthesis in all organisms. Recent studies, empowered by advancements in genome sequencing, have uncovered an increasing number of disease-causing mutations in aaRSs. Monoallelic aaRS mutations typically lead to dominant peripheral neuropathies such as Charcot-Marie-Tooth (CMT) disease, whereas biallelic aaRS mutations often impair the central nervous system (CNS) and cause neurodevelopmental disorders. Here, we review recent progress in the disease onsets, molecular basis, and potential therapies for diseases caused by aaRS mutations, with a focus on biallelic mutations in cytoplasmic aaRSs.

Indexed as

Amino Acyl-tRNA SynthetasesCharcot-Marie-Tooth DiseaseMutationAnimalsHumansNervous System DiseasesAmino Acyl-tRNA Synthetasesaa‐tRNAdevelopmental delaymicrocephalytranslational defect

Identifiers

PMID39487674
PMCPMC11611227

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.