Evidence map›Paper›PMID 32817337›Full record

ArticleThe Journal of biological chemistry2020

Generation and validation of recombinant antibodies to study human aminoacyl-tRNA synthetases.

Charlotta Preger, Edvard Wigren, Elena Ossipova, Carolyn Marks, Johan Lengqvist, Camilla Hofström, Oskar Andersson, Per-Johan Jakobsson, Susanne Gräslund, Helena Persson

Open access · hybridAbstract readValidation Study
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. CD73RMD open · 2025
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  11. BRCA1 Antibodies Matter.International journal of biological sciences · 2021
    Article
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

10 authors at 3 institutions in 1 country.

Charlotta PregerStructural Genomics Consortium, Division of Rheumatology, Department of Medicine Solna, Karolinska Institutet, Karolinska University Hospital, Stockholm, Sweden.
Edvard WigrenStructural Genomics Consortium, Division of Rheumatology, Department of Medicine Solna, Karolinska Institutet, Karolinska University Hospital, Stockholm, Sweden.ORCID 0000-0002-7933-0939
Elena OssipovaStructural Genomics Consortium, Division of Rheumatology, Department of Medicine Solna, Karolinska Institutet, Karolinska University Hospital, Stockholm, Sweden.
Carolyn MarksStructural Genomics Consortium, Division of Rheumatology, Department of Medicine Solna, Karolinska Institutet, Karolinska University Hospital, Stockholm, Sweden.
Johan LengqvistPelago Bioscience AB, Solna, Sweden.
Camilla HofströmScience for Life Laboratory, Drug Discovery and Development, Stockholm, Sweden.
Oskar AnderssonScience for Life Laboratory, Drug Discovery and Development, Stockholm, Sweden.
Per-Johan JakobssonStructural Genomics Consortium, Division of Rheumatology, Department of Medicine Solna, Karolinska Institutet, Karolinska University Hospital, Stockholm, Sweden.ORCID 0000-0001-7665-9715
Susanne GräslundStructural Genomics Consortium, Division of Rheumatology, Department of Medicine Solna, Karolinska Institutet, Karolinska University Hospital, Stockholm, Sweden helena.persson@scilifelab.se susanne.graslund@ki.se.
Helena PerssonScience for Life Laboratory, Drug Discovery and Development, Stockholm, Sweden helena.persson@scilifelab.se susanne.graslund@ki.se.ORCID 0000-0002-2965-0395
Karolinska University Hospital · SEScience for Life Laboratory · SEPelago Bioscience (Sweden) · SE

Funding

Wellcome TrustWellcome Trust 106169/ZZ14/Z
6 · The paper itself

Abstract

Aminoacyl-tRNA synthetases (aaRSs) have long been viewed as mere housekeeping proteins and have therefore often been overlooked in drug discovery. However, recent findings have revealed that many aaRSs have noncanonical functions, and several of the aaRSs have been linked to autoimmune diseases, cancer, and neurological disorders. Deciphering these roles has been challenging because of a lack of tools to enable their study. To help solve this problem, we have generated recombinant high-affinity antibodies for a collection of thirteen cytoplasmic and one mitochondrial aaRSs. Selected domains of these proteins were produced recombinantly in

Indexed as

Amino Acyl-tRNA SynthetasesSingle-Chain AntibodiesHumansRecombinant ProteinsAmino Acyl-tRNA SynthetasesRecombinant ProteinsSingle-Chain Antibodiesaminoacyl-tRNA synthetaseantibody validationantigenanti-synthetase syndromeautoimmune diseasemyositisphage displayrecombinant antibodiesrecombinant protein expressionscFv

Identifiers

PMID32817337
PMCPMC7549041
OpenAlexW3049247669

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.