Evidence map›Paper›PMID 33036230›Full record

ArticleInternational journal of molecular sciences2020

Crystal Structure of Non-Structural Protein 10 from Severe Acute Respiratory Syndrome Coronavirus-2.

Annika Rogstam, Maria Nyblom, Signe Christensen, Celeste Sele, Vladimir O Talibov, Therese Lindvall, Anna Andersson Rasmussen, Ingemar André, Zoë Fisher, Wolfgang Knecht and 1 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.4field-weighted citation impact, top 4% 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

32 citing papers in PubMed, 66 citations in OpenAlex.

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  20. Overview of SARS-CoV-2 genome-encoded proteins.Science China. Life sciences · 2022
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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

11 authors at 3 institutions in 2 countries.

Annika RogstamDepartment of Biology & Lund Protein Production Platform, Lund University, Sölvegatan 35, 22362 Lund, Sweden.
Maria NyblomDepartment of Biology & Lund Protein Production Platform, Lund University, Sölvegatan 35, 22362 Lund, Sweden.
Signe ChristensenDepartment of Biochemistry and Structural Biology, Lund University, Naturvetarvägen 26, 22241 Lund, Sweden.
Celeste SeleDepartment of Biology & Lund Protein Production Platform, Lund University, Sölvegatan 35, 22362 Lund, Sweden.
Vladimir O TalibovBioMax, MAX IV Laboratory, Fotongatan 2, 22484 Lund, Sweden.ORCID 0000-0002-1135-2744
Therese LindvallDepartment of Biology & Lund Protein Production Platform, Lund University, Sölvegatan 35, 22362 Lund, Sweden.
Anna Andersson RasmussenDepartment of Biology & Lund Protein Production Platform, Lund University, Sölvegatan 35, 22362 Lund, Sweden.
Ingemar AndréDepartment of Biochemistry and Structural Biology, Lund University, Naturvetarvägen 26, 22241 Lund, Sweden.
Zoë FisherDepartment of Biology & Lund Protein Production Platform, Lund University, Sölvegatan 35, 22362 Lund, Sweden.ORCID 0000-0001-8287-0269
Wolfgang KnechtDepartment of Biology & Lund Protein Production Platform, Lund University, Sölvegatan 35, 22362 Lund, Sweden.
Frank KozielskiSchool of Pharmacy, University College London, 29-39 Brunswick Square, London WC1N 1AX, UK.ORCID 0000-0001-6096-9102
Lund University · SEMAX IV Laboratory · SEUniversity College London · GB

Funding

European Spallation Source ERIC projects related to COVID-19Lund University Lund Protein Production Platform (LP3)Medical Research Council MC_PC_19054
6 · The paper itself

Abstract

Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2), causing Coronavirus Disease 19 (COVID-19), emerged at the end of 2019 and quickly spread to cause a global pandemic with severe socio-economic consequences. The early sequencing of its RNA genome revealed its high similarity to SARS, likely to have originated from bats. The SARS-CoV-2 non-structural protein 10 (nsp10) displays high sequence similarity with its SARS homologue, which binds to and stimulates the 3'-to-5' exoribonuclease and the 2'-O-methlytransferase activities of nsps 14 and 16, respectively. Here, we report the biophysical characterization and 1.6 Å resolution structure of the unbound form of nsp10 from SARS-CoV-2 and compare it to the structures of its SARS homologue and the complex-bound form with nsp16 from SARS-CoV-2. The crystal structure and solution behaviour of nsp10 will not only form the basis for understanding the role of SARS-CoV-2 nsp10 as a central player of the viral RNA capping apparatus, but will also serve as a basis for the development of inhibitors of nsp10, interfering with crucial functions of the replication-transcription complex and virus replication.

Indexed as

Molecular Dynamics SimulationBinding SitesCrystallography, X-RayProtein BindingS-AdenosylmethionineSequence HomologyViral Nonstructural ProteinsViral Regulatory and Accessory ProteinsZinc FingersORF1ab polyprotein, SARS-CoV-2S-AdenosylmethionineViral Nonstructural ProteinsViral Regulatory and Accessory ProteinsCOVID-19non-structural proteinsnsp10replication–transcription complexRNA capping machinerySARS CoV-2

Identifiers

PMID33036230
PMCPMC7583907
OpenAlexW3091637359

What OpenQuestion holds

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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.