Evidence map›Paper›PMID 33594727›Full record

ArticleProtein science : a publication of the Protein Society2021

Nonstructural protein 7 and 8 complexes of SARS-CoV-2.

Changhui Zhang, Li Li, Jun He, Cheng Chen, Dan Su

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
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  5. Review
  6. Article
  7. Article
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  9. Article
  10. Article
  11. Article
  12. Structural biology of SARS-CoV-2: open the door for novel therapies.Signal transduction and targeted therapy · 2022
    Review
  13. Article
  14. Nonstructural protein 7 and 8 complexes of SARS-CoV-2.Protein science : a publication of the Protein Society · 2021
    Article
  15. Review Devil's tools: SARS-CoV-2 antagonists against innate immunity.Current research in virological science · 2021
    Review
  16. 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

5 authors.

Changhui ZhangState Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center for Biotherapy, Chengdu, China.ORCID 0000-0002-7630-7426
Li LiState Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center for Biotherapy, Chengdu, China.ORCID 0000-0001-5997-3075
Jun HeCAS Key Laboratory of Regenerative Biology, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, China.
Cheng ChenSchool of Life Sciences, Tianjin University, Tianjin, China.
Dan SuState Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center for Biotherapy, Chengdu, China.ORCID 0000-0002-1059-5226

Funding

National Key Research and Development Program of China 2017YFA0505903National Natural Science Foundation of China 2018YFC1312300Special Research Fund on COVID-19 of Sichuan Province 2020YFS0010The Urgent Project on COVID-19 of West China Hospital, Sichuan University HX-2019-nCoV-044
6 · The paper itself

Abstract

The pandemic outbreak of coronavirus disease 2019 (COVID-19) across the world has led to millions of infection cases and caused a global public health crisis. Current research suggests that SARS-CoV-2 is a highly contagious coronavirus that spreads rapidly through communities. To understand the mechanisms of viral replication, it is imperative to investigate coronavirus viral replicase, a huge protein complex comprising up to 16 viral nonstructural and associated host proteins, which is the most promising antiviral target for inhibiting viral genome replication and transcription. Recently, several components of the viral replicase complex in SARS-CoV-2 have been solved to provide a basis for the design of new antiviral therapeutics. Here, we report the crystal structure of the SARS-CoV-2 nsp7+8 tetramer, which comprises two copies of each protein representing nsp7's full-length and the C-terminus of nsp8 owing to N-terminus proteolysis during the process of crystallization. We also identified a long helical extension and highly flexible N-terminal domain of nsp8, which is preferred for interacting with single-stranded nucleic acids.

Indexed as

Coronavirus RNA-Dependent RNA PolymeraseCOVID-19Crystallography, X-RayHumansModels, MolecularProtein ConformationProtein DomainsProtein MultimerizationSARS-CoV-2Viral Nonstructural ProteinsCoronavirus RNA-Dependent RNA PolymeraseNS8 protein, SARS-CoV-2ORF1ab polyprotein, SARS-CoV-2Viral Nonstructural ProteinsCOVID-19nsp7nsp7+8 complexnsp8SARS-CoV-2

Identifiers

PMID33594727
PMCPMC7980517

What OpenQuestion holds

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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.