Evidence map›Paper›PMID 33475934›Full record

ArticleBiomolecular NMR assignments2021

Nicola Salvi, Luiza Mamigonian Bessa, Serafima Guseva, Aldo Camacho-Zarco, Damien Maurin, Laura Marino Perez, Anas Malki, Martin Hengesbach, Sophie Marianne Korn, Andreas Schlundt and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Biomolecular NMR assignments, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 42% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
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  4. Review
  5. 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

12 authors at 2 institutions in 2 countries.

Nicola SalviUniv. Grenoble Alpes, CNRS, CEA, IBS, 38000, Grenoble, France.ORCID http://orcid.org/0000-0003-1515-6908
Luiza Mamigonian BessaUniv. Grenoble Alpes, CNRS, CEA, IBS, 38000, Grenoble, France.
Serafima GusevaUniv. Grenoble Alpes, CNRS, CEA, IBS, 38000, Grenoble, France.
Aldo Camacho-ZarcoUniv. Grenoble Alpes, CNRS, CEA, IBS, 38000, Grenoble, France.
Damien MaurinUniv. Grenoble Alpes, CNRS, CEA, IBS, 38000, Grenoble, France.
Laura Marino PerezUniv. Grenoble Alpes, CNRS, CEA, IBS, 38000, Grenoble, France.
Anas MalkiUniv. Grenoble Alpes, CNRS, CEA, IBS, 38000, Grenoble, France.
Martin HengesbachInstitute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438, Frankfurt, Germany.ORCID http://orcid.org/0000-0001-9414-1602
Sophie Marianne KornInstitute for Molecular Biosciences, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 9, 60438, Frankfurt, Germany.ORCID http://orcid.org/0000-0003-3798-3277
Andreas SchlundtInstitute for Molecular Biosciences, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 9, 60438, Frankfurt, Germany.ORCID http://orcid.org/0000-0003-2254-7560
Harald SchwalbeInstitute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438, Frankfurt, Germany.ORCID http://orcid.org/0000-0001-5693-7909
Martin BlackledgeUniv. Grenoble Alpes, CNRS, CEA, IBS, 38000, Grenoble, France. martin.blackledge@ibs.fr.ORCID http://orcid.org/0000-0003-0935-721X
Centre National de la Recherche Scientifique · FRGoethe University Frankfurt · DE

Funding

Agence Nationale de la Recherche ANR-10-INBS-05-02Deutsche Forschungsgemeinschaft CRC902
6 · The paper itself

Abstract

The non-structural protein nsp3 from SARS-CoV-2 plays an essential role in the viral replication transcription complex. Nsp3a constitutes the N-terminal domain of nsp3, comprising a ubiquitin-like folded domain and a disordered acidic chain. This region of nsp3a has been linked to interactions with the viral nucleoprotein and the structure of double membrane vesicles. Here, we report the backbone resonance assignment of both domains of nsp3a. The study is carried out in the context of the international covid19-nmr consortium, which aims to characterize SARS-CoV-2 proteins and RNAs, providing for example NMR chemical shift assignments of the different viral components. Our assignment will provide the basis for the identification of inhibitors and further functional and interaction studies of this essential protein.

Indexed as

Magnetic Resonance SpectroscopyCarbon IsotopesCoronavirus Papain-Like ProteasesEscherichia coliHydrogenHydrogen-Ion ConcentrationNitrogen IsotopesPlasmidsProtein BindingProtein DomainsProtein Structure, SecondarySARS-CoV-2Carbon-13Carbon IsotopesCoronavirus Papain-Like ProteasesHydrogenNitrogen-15Nitrogen Isotopespapain-like protease, SARS-CoV-2Covid-19Intrinsically disordered proteinSARS-CoV-2Viral replication

Identifiers

PMID33475934
PMCPMC7819138
OpenAlexW3121851595

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.