Evidence map›Paper›PMID 37687244›Full record

ArticleMolecules (Basel, Switzerland)2023

Docking and Molecular Dynamics Simulations Clarify Binding Sites for Interactions of Novel Marine Sulfated Glycans with SARS-CoV-2 Spike Glycoprotein.

Priyanka Samanta, Sushil K Mishra, Vitor H Pomin, Robert J Doerksen

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.1field-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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. 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

4 authors at 1 institution in 1 country.

Priyanka SamantaDepartment of BioMolecular Sciences, School of Pharmacy, University of Mississippi, University, MS 38677-1848, USA.ORCID 0000-0001-9127-5816
Sushil K MishraDepartment of BioMolecular Sciences, School of Pharmacy, University of Mississippi, University, MS 38677-1848, USA.ORCID 0000-0002-3080-9754
Vitor H PominDepartment of BioMolecular Sciences, School of Pharmacy, University of Mississippi, University, MS 38677-1848, USA.ORCID 0000-0002-5015-8880
Robert J DoerksenDepartment of BioMolecular Sciences, School of Pharmacy, University of Mississippi, University, MS 38677-1848, USA.ORCID 0000-0002-3789-1842
University of Mississippi · US

Funding

Tracking Glycosylation State with Fluorinated Glycosides ProbesP20GM130460 · NIGMS · UNIVERSITY OF MISSISSIPPI · PI Joshua S Sharp · 2020 to 2026
$17.9M
Disruption of CS/KSPG-Mediated Neuronal Outgrowth InhibitionR03NS110996 · NINDS · UNIVERSITY OF MISSISSIPPI · PI POMIN, VITOR HUGO · 2020 to 2020
$142k
NIGMS NIH HHS P20 GM130460NINDS NIH HHS R03 NS110996
6 · The paper itself

Abstract

The entry of SARS-CoV-2 into the host cell is mediated by its S-glycoprotein (SGP). Sulfated glycans bind to the SGP receptor-binding domain (RBD), which forms a ternary complex with its receptor angiotensin converting enzyme 2. Here, we have conducted a thorough and systematic computational study of the binding of four oligosaccharide building blocks from novel marine sulfated glycans (isolated from

Indexed as

COVID-19Molecular Dynamics SimulationBinding SitesHumansPolysaccharidesSARS-CoV-2Spike Glycoprotein, CoronavirusSulfatesPolysaccharidesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2Sulfatesbinding free energycryptic binding sitesglycosaminoglycansmolecular dockingmolecular dynamicsSARS-CoV-2 spike glycoprotein

Identifiers

PMID37687244
PMCPMC10490367
OpenAlexW4386418302

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.