Evidence map›Paper›PMID 33892550›Full record

ArticleMathematical biosciences and engineering : MBE2021

Electrostatic features for nucleocapsid proteins of SARS-CoV and SARS-CoV-2.

Wenhan Guo, Yixin Xie, Alan E Lopez-Hernandez, Shengjie Sun, Lin Li

Open access · goldAbstract read
In one paragraph

Article in Mathematical biosciences and engineering : MBE, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
  5. Article
  6. Review
  7. SARS-CoV-2 Is an Electricity-Driven Virus.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. HIT web server: A hybrid method to improve electrostatic calculations for biomolecules.Computational and structural biotechnology journal · 2022
    Article
  15. Article
  16. 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 1 institution in 1 country.

Wenhan GuoComputational Science Program, University of Texas at El Paso, El Paso, TX 79968, USA.
Yixin XieComputational Science Program, University of Texas at El Paso, El Paso, TX 79968, USA.
Alan E Lopez-HernandezComputational Science Program, University of Texas at El Paso, El Paso, TX 79968, USA.
Shengjie SunComputational Science Program, University of Texas at El Paso, El Paso, TX 79968, USA.
Lin LiComputational Science Program, University of Texas at El Paso, El Paso, TX 79968, USA.
The University of Texas at El Paso · US

Funding

UTEP Border Biomedical Research CenterU54MD007592 · NIMHD · UNIVERSITY OF TEXAS EL PASO · PI Gabriel Andrew Frietze · 2019 to 2026
$35.1M
TCCG12MD007592 · NIMHD · UNIVERSITY OF TEXAS EL PASO · PI KIRKEN, ROBERT A. · 2012 to 2018
$19.4M
Developing and applying large-scale simulation approach to understand the mechanisms of kinesins' motilities along microtubulesSC1GM132043 · NIGMS · UNIVERSITY OF TEXAS EL PASO · PI LI, LIN · 2019 to 2022
$1.5M
NIGMS NIH HHS SC1 GM132043NIMHD NIH HHS G12 MD007592NIMHD NIH HHS U54 MD007592
6 · The paper itself

Abstract

COVID-19 is increasingly affecting human health and global economy. Understanding the fundamental mechanisms of Severe Acute Respiratory Syndrome CoronaVirus 2 (SARS-CoV-2) is highly demanded to develop treatments for COVID-19. SARS-CoV and SARS-CoV-2 share 92.06% identity in their N protein RBDs' sequences, which results in very similar structures. However, the SARS-CoV-2 is more easily to spread. Utilizing multi-scale computational approaches, this work studied the fundamental mechanisms of the nucleocapsid (N) proteins of SARS-CoV and SARS-CoV-2, including their stabilities and binding strengths with RNAs at different pH values. Electrostatic potential on the surfaces of N proteins show that both the N proteins of SARS-CoV and SARS-CoV-2 have dominantly positive potential to attract RNAs. The binding forces between SARS-CoV N protein and RNAs at different distances are similar to that of SARS-CoV-2, both in directions and magnitudes. The electric filed lines between N proteins and RNAs are also similar for both SARS-CoV and SARS-CoV-2. The folding energy and binding energy dependence on pH revealed that the best environment for N proteins to perform their functions with RNAs is the weak acidic environment.

Indexed as

COVID-19Nucleocapsid ProteinsHumansSARS-CoV-2Static ElectricityNucleocapsid ProteinsCOVID-19DelPhiDelPhiForceelectrostatic forceprotein-protein interactionsprotein-RNA/DNA interactionsSARS-CoVSARS-CoV-2

Identifiers

PMID33892550
PMCPMC8279046
OpenAlexW3135037854

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.