Evidence map›Paper›PMID 20671029›Full record

ArticleNucleic acids research2010

Cooperative translocation enhances the unwinding of duplex DNA by SARS coronavirus helicase nsP13.

Na-Ra Lee, Hyun-Mi Kwon, Kkothanahreum Park, Sangtaek Oh, Yong-Joo Jeong, Dong-Eun Kim

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
1.5field-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

60 citing papers in PubMed, 92 citations in OpenAlex.

  1. Review
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  15. The stalk domain of SARS-CoV-2 NSP13 is essential for its helicase activity.Biochemical and biophysical research communications · 2022
    Article
  16. Article
  17. Structural biology of SARS-CoV-2: open the door for novel therapies.Signal transduction and targeted therapy · 2022
    Review
  18. Review
  19. Review
  20. Metal Complexes as Antiviral Agents for SARS-CoV-2.Chembiochem : a European journal of chemical biology · 2021
    Review
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 3 institutions in 1 country.

Na-Ra LeeDepartment of Bio and Nanochemistry, Kookmin University, Seoul 136-702, Republic of Korea.
Hyun-Mi Kwon
Kkothanahreum Park
Sangtaek Oh
Yong-Joo Jeong
Dong-Eun Kim
Kookmin University · KRInje University · KRKonkuk University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SARS coronavirus encodes non-structural protein 13 (nsP13), a nucleic acid helicase/NTPase belonging to superfamily 1 helicase, which efficiently unwinds both partial-duplex RNA and DNA. In this study, unwinding of DNA substrates that had different duplex lengths and 5'-overhangs was examined under single-turnover reaction conditions in the presence of excess enzyme. The amount of DNA unwound decreased significantly as the length of the duplex increased, indicating a poor in vitro processivity. However, the quantity of duplex DNA unwound increased as the length of the single-stranded 5'-tail increased for the 50-bp duplex. This enhanced processivity was also observed for duplex DNA that had a longer single-stranded gap in between. These results demonstrate that nsP13 requires the presence of a long 5'-overhang to unwind longer DNA duplexes. In addition, enhanced DNA unwinding was observed for gapped DNA substrates that had a 5'-overhang, indicating that the translocated nsP13 molecules pile up and the preceding helicase facilitate DNA unwinding. Together with the propensity of oligomer formation of nsP13 molecules, we propose that the cooperative translocation by the functionally interacting oligomers of the helicase molecules loaded onto the 5'-overhang account for the observed enhanced processivity of DNA unwinding.

Indexed as

DNADNA HelicasesKineticsSevere acute respiratory syndrome-related coronavirusViral Nonstructural ProteinsDNADNA HelicasesViral Nonstructural Proteins

Identifiers

PMID20671029
PMCPMC2995068
OpenAlexW2030429617

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.