Evidence map›Paper›PMID 32161317›Full record

ArticleScientific reports2020

A high ATP concentration enhances the cooperative translocation of the SARS coronavirus helicase nsP13 in the unwinding of duplex RNA.

Kyoung-Jin Jang, Seonghwan Jeong, Dong Young Kang, Nipin Sp, Young Mok Yang, Dong-Eun Kim

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed, 1 pooled it
2.8field-weighted citation impact, top 6% 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

67 citing papers in PubMed, 1 synthesis or guideline pooled it, 119 citations in OpenAlex.

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  13. An iron-sulfur cluster in the zinc-binding domain of the SARS-CoV-2 helicase modulates its RNA-binding and -unwinding activities.Proceedings of the National Academy of Sciences of the United States of America · 2023
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7 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

Kyoung-Jin JangDepartment of Bioscience and Biotechnology, Konkuk University, Seoul, 05029, Republic of Korea.
Seonghwan JeongDepartment of Bioscience and Biotechnology, Konkuk University, Seoul, 05029, Republic of Korea.
Dong Young KangDepartment of Pathology, School of Medicine, Institute of Biomedical Science and Technology (IBST), Konkuk University, Seoul, 05029, Republic of Korea.
Nipin SpDepartment of Pathology, School of Medicine, Institute of Biomedical Science and Technology (IBST), Konkuk University, Seoul, 05029, Republic of Korea.
Young Mok YangDepartment of Pathology, School of Medicine, Institute of Biomedical Science and Technology (IBST), Konkuk University, Seoul, 05029, Republic of Korea. ymyang@kku.ac.kr.
Dong-Eun KimDepartment of Bioscience and Biotechnology, Konkuk University, Seoul, 05029, Republic of Korea. kimde@konkuk.ac.kr.
Konkuk University · KR

Funding

National Research Foundation of Korea 2018R1C1B6006146
6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus nonstructural protein 13 (SCV nsP13), a superfamily 1 helicase, plays a central role in viral RNA replication through the unwinding of duplex RNA and DNA with a 5' single-stranded tail in a 5' to 3' direction. Despite its putative role in viral RNA replication, nsP13 readily unwinds duplex DNA by cooperative translocation. Herein, nsP13 exhibited different characteristics in duplex RNA unwinding than that in duplex DNA. nsP13 showed very poor processivity on duplex RNA compared with that on duplex DNA. More importantly, nsP13 inefficiently unwinds duplex RNA by increasing the 5'-ss tail length. As the concentration of nsP13 increased, the amount of unwound duplex DNA increased and that of unwound duplex RNA decreased. The accumulation of duplex RNA/nsP13 complexes increased as the concentration of nsP13 increased. An increased ATP concentration in the unwinding of duplex RNA relieved the decrease in duplex RNA unwinding. Thus, nsP13 has a strong affinity for duplex RNA as a substrate for the unwinding reaction, which requires increased ATPs to processively unwind duplex RNA. Our results suggest that duplex RNA is a preferred substrate for the helicase activity of nsP13 than duplex DNA at high ATP concentrations.

Indexed as

Adenosine TriphosphateDNADNA-Binding ProteinsDNA HelicasesDNA, Single-StrandedDNA, ViralHydrolysisKineticsMethyltransferasesProtein BindingRNA-Binding ProteinsRNA, Double-StrandedRNA HelicasesRNA, ViralSevere acute respiratory syndrome-related coronavirusSubstrate SpecificityAdenosine TriphosphateDNADNA-Binding ProteinsDNA HelicasesDNA, Single-StrandedDNA, ViralMethyltransferasesNsp13 protein, SARS-CoVRNA-Binding ProteinsRNA, Double-StrandedRNA HelicasesRNA, ViralViral Nonstructural Proteins

Identifiers

PMID32161317
PMCPMC7066239
OpenAlexW3012042245

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.