Evidence map›Paper›PMID 36753552›Full record

ArticleScience advances2023

The binding mode of orphan glycyl-tRNA synthetase with tRNA supports the synthetase classification and reveals large domain movements.

Lu Han, Zhiteng Luo, Yingchen Ju, Bingyi Chen, Taotao Zou, Junjian Wang, Jun Xu, Qiong Gu, Xiang-Lei Yang, Paul Schimmel and 1 more

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2023. 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
2.5field-weighted citation impact, top 11% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
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  3. Architecture ofProceedings of the National Academy of Sciences of the United States of America · 2025
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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

11 authors at 2 institutions in 2 countries.

Lu HanGuangdong Provincial Key Laboratory of Chiral Molecule and Drug Discovery, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, China.ORCID 0000-0003-3076-7483
Zhiteng LuoGuangdong Provincial Key Laboratory of Chiral Molecule and Drug Discovery, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, China.
Yingchen JuGuangdong Provincial Key Laboratory of Chiral Molecule and Drug Discovery, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, China.ORCID 0000-0003-2626-1914
Bingyi ChenGuangdong Provincial Key Laboratory of Chiral Molecule and Drug Discovery, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, China.ORCID 0000-0002-5231-6643
Taotao ZouGuangdong Provincial Key Laboratory of Chiral Molecule and Drug Discovery, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, China.ORCID 0000-0001-9129-4398
Junjian WangGuangdong Provincial Key Laboratory of Chiral Molecule and Drug Discovery, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, China.ORCID 0000-0002-5328-2908
Jun XuResearch Center for Drug Discovery, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, China.ORCID 0000-0002-1075-0337
Qiong GuResearch Center for Drug Discovery, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, China.ORCID 0000-0001-6011-3697
Xiang-Lei YangDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0003-2554-084X
Paul SchimmelDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0002-0448-022X
Huihao ZhouGuangdong Provincial Key Laboratory of Chiral Molecule and Drug Discovery, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, China.ORCID 0000-0002-9675-5007
Sun Yat-sen University · CNScripps Research Institute · US

Funding

Link extracellular function of tRNA synthetase with pathological mechanism of diseaseR35GM139627 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI YANG, XIANG-LEI · 2021 to 2025
$2.3M
NIGMS NIH HHS R35 GM139627
6 · The paper itself

Abstract

As a class of essential enzymes in protein translation, aminoacyl-transfer RNA (tRNA) synthetases (aaRSs) are organized into two classes of 10 enzymes each, based on two conserved active site architectures. The (αβ)

Indexed as

Amino Acyl-tRNA SynthetasesGlycine-tRNA LigaseCatalytic DomainLigasesRNA, TransferAmino Acyl-tRNA SynthetasesGlycine-tRNA LigaseLigasesRNA, Transfer

Identifiers

PMID36753552
PMCPMC9908026
OpenAlexW4319458893

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.