Evidence map›Paper›PMID 34542936›Full record

ArticleChembiochem : a European journal of chemical biology2021

On the Weak Binding and Spectroscopic Signature of SARS-CoV-2 nsp14 Interaction with RNA.

Ayaz Hassan, Graziela C Sedenho, Phelipe A M Vitale, Mona N Oliviera, Frank N Crespilho

Open access · bronzeAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.9field-weighted citation impact, top 22% 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

2 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. On the Weak Binding and Spectroscopic Signature of SARS-CoV-2 nsp14 Interaction with RNA.Chembiochem : a European journal of chemical biology · 2021
    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 at 2 institutions in 1 country.

Ayaz HassanDepartment of Physical Chemistry, São Carlos Institute of Chemistry, University of São Paulo, Av. Trabalhador São Carlense, 400 - Parque Arnold Schimidt, São Carlos, SP, 13566-590, Brazil.ORCID 0000-0003-3842-5883
Graziela C SedenhoDepartment of Physical Chemistry, São Carlos Institute of Chemistry, University of São Paulo, Av. Trabalhador São Carlense, 400 - Parque Arnold Schimidt, São Carlos, SP, 13566-590, Brazil.ORCID 0000-0001-8696-5978
Phelipe A M VitaleBiolinker, Av. Prof. Lineu Prestes, Cietec - Butantã, São Paulo, SP, 05508-000, Brazil.
Mona N OlivieraBiolinker, Av. Prof. Lineu Prestes, Cietec - Butantã, São Paulo, SP, 05508-000, Brazil.
Frank N CrespilhoDepartment of Physical Chemistry, São Carlos Institute of Chemistry, University of São Paulo, Av. Trabalhador São Carlense, 400 - Parque Arnold Schimidt, São Carlos, SP, 13566-590, Brazil.ORCID 0000-0003-4830-652X
Universidade de São Paulo · BRCentro de Inovação, Empreendedorismo e Tecnologia · BR

Funding

BioMicS Group (São Carlos Institute of Chemistry, University of São Paulo)CAPES-PNPD 88887.358060/2019-00Coordinating Agency for Advanced Training of Graduate Personnel (CAPES)MeDiCo Network CAPES Brazil 88881.504532/2020-01National Council of Scientific and Technological Development (CNPq) 305486/2019-5São Paulo Research Foundation (FAPESP) 18/22214-6São Paulo Research Foundation (FAPESP) 19/12053-8São Paulo Research Foundation (FAPESP) 19/15333-1São Paulo Research Foundation (FAPESP) 2020/04796-8
6 · The paper itself

Abstract

The SARS-CoV-2 non-structural protein 14 (nsp14), known as exoribonuclease is encoded from the large polyprotein of viral genome and is a major constituent of the transcription replication complex (TRC) machinery of the viral RNA synthesis. This protein is highly conserved among the coronaviruses and is a potential target for the development of a therapeutic drug. Here, we report the SARS-CoV-2 nsp14 expression, show its structural characterization, and ss-RNA exonuclease activity through vibrational and electronic spectroscopies. The deconvolution of amide-I band in the FTIR spectrum of the protein revealed a composition of 35 % α-helix and 25 % β-sheets. The binding between protein and RNA is evidenced from the spectral changes in the amide-I region of the nsp14, showing protein conformational changes during the binding process. A value of 20.60±3.81 mol L

Indexed as

ExoribonucleasesProtein BindingProtein ConformationRNA, ViralSARS-CoV-2Spectrophotometry, UltravioletSpectroscopy, Fourier Transform InfraredViral Nonstructural ProteinsExoribonucleasesNSP14 protein, SARS-CoV-2RNA, ViralViral Nonstructural Proteinsmicro-FTIR spectroscopynon-structural proteinsnsp14RNASARS-CoV-2

Identifiers

PMID34542936
PMCPMC8653059
OpenAlexW3200980383

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.