Evidence map›Paper›PMID 32611767›Full record

ArticleThe Journal of biological chemistry2020

Hairpin RNA-induced conformational change of a eukaryotic-specific lysyl-tRNA synthetase extension and role of adjacent anticodon-binding domain.

Sheng Liu, Maryanne Refaei, Shuohui Liu, Aaron Decker, Jennifer M Hinerman, Andrew B Herr, Mike Howell, Karin Musier-Forsyth, Pearl Tsang

Open access · hybridAbstract read
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 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact, top 94% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Structural basis for aminoacylation of cellular modified tRNAbioRxiv : the preprint server for biology · 2024
    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

9 authors at 4 institutions in 1 country.

Sheng LiuDepartment of Chemistry, University of Cincinnati, Cincinnati, Ohio, USA.
Maryanne RefaeiDepartment of Chemistry, University of Cincinnati, Cincinnati, Ohio, USA.
Shuohui LiuDepartment of Chemistry and Biochemistry, Center for RNA Biology, Ohio State University, Columbus, Ohio, USA.
Aaron DeckerDepartment of Chemistry, University of Cincinnati, Cincinnati, Ohio, USA.
Jennifer M HinermanDepartment of Pediatrics, University of Cincinnati College of Medicine, Cincinnati, Ohio, USA; Division of Immunobiology, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio, USA.
Andrew B HerrDepartment of Pediatrics, University of Cincinnati College of Medicine, Cincinnati, Ohio, USA; Division of Immunobiology, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio, USA.
Mike HowellProtein Express, Inc., Cincinnati, Ohio, USA.
Karin Musier-ForsythDepartment of Chemistry and Biochemistry, Center for RNA Biology, Ohio State University, Columbus, Ohio, USA.
Pearl TsangDepartment of Chemistry, University of Cincinnati, Cincinnati, Ohio, USA. Electronic address: musier-forsyth.1@osu.edu.
The Ohio State University · USUniversity of Cincinnati · USCincinnati Children's Hospital Medical Center · USProtein Express (United States) · US

Funding

Cellular Factors Critical for Initiation of HIV-1 Reverse TranscriptaseR01AI150493 · NIAID · OHIO STATE UNIVERSITY · PI MUSIER-FORSYTH, KARIN M · 2020 to 2022
$1.2M
NIAID NIH HHS R01 AI150493
6 · The paper itself

Abstract

Human lysyl-tRNA synthetase (hLysRS) is essential for aminoacylation of tRNA

Indexed as

Models, MolecularRNA FoldingHumansLysine-tRNA LigaseMagnetic Resonance SpectroscopyProtein DomainsRNA, TransferLysine-tRNA LigaseRNA, Transferaminoacyl-tRNA synthetaseconformational changeconformational transitionfluorescence anisotropyintrinsically disorderedlysyl-tRNA synthetaseNMRN-terminal extensionnuclear magnetic resonance (NMR)RNA bindingsegmental protein labelingsortase A ligationtransfer RNA (tRNA)tRNALys

Identifiers

PMID32611767
PMCPMC7443506
OpenAlexW3039656760

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.