Evidence map›Paper›PMID 32304108›Full record

ArticleProtein science : a publication of the Protein Society2020

Crystal structure of Nsp15 endoribonuclease NendoU from SARS-CoV-2.

Youngchang Kim, Robert Jedrzejczak, Natalia I Maltseva, Mateusz Wilamowski, Michael Endres, Adam Godzik, Karolina Michalska, Andrzej Joachimiak

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 212 papers.

0numbers the graph read from it
0cells of the map it votes in
212citing papers in PubMed
26.2field-weighted citation impact, top 1% 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

212 citing papers in PubMed, 365 citations in OpenAlex.

  1. Review
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  9. SARS-CoV-2 nsp15 enhances viral virulence by subverting host antiviral defenses.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Functional implications of hexameric dynamics in SARS-CoV-2 Nsp15.Protein science : a publication of the Protein Society · 2025
    Article
  11. Article
  12. Anti-interferon armamentarium of human coronaviruses.Cellular and molecular life sciences : CMLS · 2025
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

152 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

8 authors at 3 institutions in 1 country.

Youngchang KimCenter for Structural Genomics of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, Illinois, USA.ORCID https://orcid.org/0000-0002-1610-4889
Robert JedrzejczakCenter for Structural Genomics of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, Illinois, USA.
Natalia I MaltsevaCenter for Structural Genomics of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, Illinois, USA.
Mateusz WilamowskiCenter for Structural Genomics of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, Illinois, USA.
Michael EndresStructural Biology Center, X-ray Science Division, Argonne National Laboratory, Argonne, Illinois, USA.
Adam GodzikBiomedical Sciences, University of California Riverside, Riverside, California, USA.
Karolina MichalskaCenter for Structural Genomics of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, Illinois, USA.
Andrzej JoachimiakCenter for Structural Genomics of Infectious Diseases, Consortium for Advanced Science and Engineering, University of Chicago, Chicago, Illinois, USA.ORCID https://orcid.org/0000-0003-2535-6209
Argonne National Laboratory · USUniversity of California, Riverside · USUniversity of Illinois Chicago · US

Funding

NIAID NIH HHS HHSN272201700060CU.S. Department of Energy (DOE) Office of Science DE-AC02-06CH11357
6 · The paper itself

Abstract

Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) is rapidly spreading around the world. There is no existing vaccine or proven drug to prevent infections and stop virus proliferation. Although this virus is similar to human and animal SARS-CoVs and Middle East Respiratory Syndrome coronavirus (MERS-CoVs), the detailed information about SARS-CoV-2 proteins structures and functions is urgently needed to rapidly develop effective vaccines, antibodies, and antivirals. We applied high-throughput protein production and structure determination pipeline at the Center for Structural Genomics of Infectious Diseases to produce SARS-CoV-2 proteins and structures. Here we report two high-resolution crystal structures of endoribonuclease Nsp15/NendoU. We compare these structures with previously reported homologs from SARS and MERS coronaviruses.

Indexed as

Amino Acid SequenceBetacoronavirusCatalytic DomainCloning, MolecularCrystallography, X-RayEndoribonucleasesEscherichia coliGene ExpressionGenetic VectorsHumansMiddle East Respiratory Syndrome CoronavirusModels, MolecularOligonucleotidesProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandEndoribonucleasesnidoviral uridylate-specific endoribonucleaseOligonucleotidesRecombinant ProteinsViral Nonstructural ProteinsCOVID-19crystal structureendoribonucleaseEndoU familyNendoUNsp15SARS-CoV-2

Identifiers

PMID32304108
PMCPMC7264519
OpenAlexW3017291089

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.