Evidence map›Paper›PMID 30282926›Full record

ArticleInternational journal of molecular sciences2018

Nucleic Acid-Dependent Structural Transition of the Intrinsically Disordered N-Terminal Appended Domain of Human Lysyl-tRNA Synthetase.

Soon Bin Kwon, Ji Eun Yu, Chan Park, Jiseop Lee, Baik L Seong

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Soon Bin KwonDepartment of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Korea. yunbin829@gmail.com.
Ji Eun YuDepartment of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Korea. 4-season-love@hanmail.net.
Chan ParkDepartment of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Korea. justies@naver.com.
Jiseop LeeDepartment of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Korea. tjqto7@naver.com.
Baik L SeongDepartment of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Korea. blseong@yonsei.ac.kr.
Yonsei University · KR

Funding

Ministry of Agriculture, Food and Rural Affairs 716002-7National Research Foundation of Korea NRF2015R1D1A4A01016640
6 · The paper itself

Abstract

Eukaryotic lysyl-tRNA synthetases (LysRS) have an N-terminal appended tRNA-interaction domain (RID) that is absent in their prokaryotic counterparts. This domain is intrinsically disordered and lacks stable structures. The disorder-to-order transition is induced by tRNA binding and has implications on folding and subsequent assembly into multi-tRNA synthetase complexes. Here, we expressed and purified RID from human LysRS (hRID) in

Indexed as

Protein Interaction Domains and MotifsHumansLysine-tRNA LigaseMutationNucleic AcidsProtein BindingProtein Structure, SecondaryRNA, TransferStructure-Activity RelationshipLysine-tRNA LigaseNucleic AcidsRNA, Transferaminoacyl-tRNA synthetasedisorder-helix transitionhRIDLysRS

Identifiers

PMID30282926
PMCPMC6213541
OpenAlexW2894771333

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.