Evidence map›Paper›PMID 35097139›Full record

ArticleMolecular biology research communications2021

Analysis and comparison of physiochemical properties, mutations and glycosylation patterns between RNA polymerase and membrane protein of SARS-CoV and SARS-CoV-2.

Mandana Behbahani, Parisa Rabiei, Hassan Mohabatkar

Open access · greenAbstract read
In one paragraph

Article in Molecular biology research communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 49% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

3 authors at 2 institutions in 1 country.

Mandana BehbahaniDepartment of Biotechnology, Faculty of Biological Science and Technology, University of Isfahan, Isfahan, Iran.
Parisa RabieiDepartment of Biotechnology, Faculty of Biological Science and Technology, University of Isfahan, Isfahan, Iran.
Hassan MohabatkarDepartment of Biotechnology, Faculty of Biological Science and Technology, University of Isfahan, Isfahan, Iran.
University of Isfahan · IRIsfahan University of Technology · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SARS-CoV-2 is a member of β-genus of the coronavirus subfamily, alongside the virus that causes SARS (Severe Acute Respiratory Syndrome). As implied by their names, SARS-CoV-2 and SARS-CoV genome sequences have close kinship (about 79% genomic sequence similarity). In the current research, sequence-based physiochemical properties of RNA polymerase and membrane glycoprotein of SARS-CoV-2 and SARS-CoV were compared. In addition, impacts of substitution mutations on stability and glycosylation patterns of these proteins were studied. In comparison of physiochemical features of membrane and RNA polymerase proteins, only instability index of membrane protein was difference between SARS-CoV and SARS-CoV-2. Mutation analysis showed increase in stability of RNA polymerase and decrease in stability of membrane protein in SARS-CoV-2. Glycosylation pattern analysis showed glycosylation enhancement in both membrane and RNA polymerase proteins of SARS-CoV-2 in comparison to SARS-CoV. In conclusion, more glycosylation and stability of SARS-CoV-2 RNA polymerase could be one of the reasons of high pathogenicity property and host immune system evasion of SARS-CoV-2.

Indexed as

BetacoronavirusCOVID-19GlycosylationMEME motifsSubstitution mutation

Identifiers

PMID35097139
PMCPMC8798276
OpenAlexW4210748288

What OpenQuestion holds

Textmetadata
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.