Evidence map›Paper›PMID 38956874›Full record

ArticleHGG advances2024

A model organism pipeline provides insight into the clinical heterogeneity of TARS1 loss-of-function variants.

Rebecca Meyer-Schuman, Allison R Cale, Jennifer A Pierluissi, Kira E Jonatzke, Young N Park, Guy M Lenk, Stephanie N Oprescu, Marina A Grachtchouk, Andrzej A Dlugosz, Asim A Beg and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in HGG advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Rebecca Meyer-SchumanDepartment of Human Genetics, University of Michigan, Ann Arbor, MI, USA.
Allison R CaleDepartment of Human Genetics, University of Michigan, Ann Arbor, MI, USA.
Jennifer A PierluissiDepartment of Human Genetics, University of Michigan, Ann Arbor, MI, USA.
Kira E JonatzkeDepartment of Human Genetics, University of Michigan, Ann Arbor, MI, USA.
Young N ParkDepartment of Human Genetics, University of Michigan, Ann Arbor, MI, USA.
Guy M LenkDepartment of Human Genetics, University of Michigan, Ann Arbor, MI, USA.
Stephanie N OprescuDepartment of Human Genetics, University of Michigan, Ann Arbor, MI, USA.
Marina A GrachtchoukDepartment of Dermatology, University of Michigan, Ann Arbor, MI, USA.
Andrzej A DlugoszDepartment of Dermatology, University of Michigan, Ann Arbor, MI, USA; Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA; Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.
Asim A BegNeuroscience Graduate Program, University of Michigan, Ann Arbor, MI, USA.
Miriam H MeislerDepartment of Human Genetics, University of Michigan, Ann Arbor, MI, USA; Department of Neurology, University of Michigan, Ann Arbor, MI, USA.
Anthony AntonellisDepartment of Human Genetics, University of Michigan, Ann Arbor, MI, USA; Department of Neurology, University of Michigan, Ann Arbor, MI, USA. Electronic address: antonell@umich.edu.

Funding

PREDOCTORAL TRAINING IN GENETICST32GM007544 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MORAN, JOHN V. · 1985 to 2022
$11.3M
University of Michigan Skin Biology and Diseases Resource-based CenterP30AR075043 · NIAMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Johann Eli Gudjonsson · 2019 to 2026
$6.6M
Defining the Role of Aminoacyl-tRNA Synthetases in Human Health and DiseaseR35GM136441 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Anthony Antonellis · 2020 to 2026
$2.8M
NIAMS NIH HHS P30 AR075043NIGMS NIH HHS R35 GM136441NIGMS NIH HHS T32 GM007544
6 · The paper itself

Abstract

Aminoacyl-tRNA synthetases (ARSs) are ubiquitously expressed, essential enzymes that complete the first step of protein translation: ligation of amino acids to cognate tRNAs. Genes encoding ARSs have been implicated in myriad dominant and recessive phenotypes, the latter often affecting multiple tissues but with frequent involvement of the central and peripheral nervous systems, liver, and lungs. Threonyl-tRNA synthetase (TARS1) encodes the enzyme that ligates threonine to tRNA

Indexed as

Caenorhabditis elegansSaccharomyces cerevisiaeThreonine-tRNA LigaseAnimalsDisease Models, AnimalHumansLoss of Function MutationMiceMutation, MissensePhenotypeThreonine-tRNA Ligaseaminoacyl-tRNA synthetasesMendelian diseaseprotein translationrecessive diseasethreoninethreonyl-tRNA synthetase

Identifiers

PMID38956874
PMCPMC11284558

What OpenQuestion holds

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Registered trials

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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.