About: Role of RNA Guanine Quadruplexes in Favoring the Dimerization of SARS Unique Domain in Coronaviruses

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Role of RNA Guanine Quadruplexes in Favoring the Dimerization of SARS Unique Domain in Coronaviruses Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Role of RNA Guanine Quadruplexes in Favoring the Dimerization of SARS Unique Domain in Coronaviruses
Creator	Barone, Giampaolo Franceś-Monerris, Antonio Garcı́a-Iriepa, Cristina Grandemange, Stephanie Hognon, Cećilia Marazzi, Marco Miclot, Tom Monari, Antonio Terenzi, Alessio
topic	covid:f0d2fe6c8a0729a16efe056552a7428b6d0ef458#this
source	Medline; PMC
abstract	[Image: see text] Coronaviruses may produce severe acute respiratory syndrome (SARS). As a matter of fact, a new SARS-type virus, SARS-CoV-2, is responsible for the global pandemic in 2020 with unprecedented sanitary and economic consequences for most countries. In the present contribution we study, by all-atom equilibrium and enhanced sampling molecular dynamics simulations, the interaction between the SARS Unique Domain and RNA guanine quadruplexes, a process involved in eluding the defensive response of the host thus favoring viral infection of human cells. Our results evidence two stable binding modes involving an interaction site spanning either the protein dimer interface or only one monomer. The free energy profile unequivocally points to the dimer mode as the thermodynamically favored one. The effect of these binding modes in stabilizing the protein dimer was also assessed, being related to its biological role in assisting the SARS viruses to bypass the host protective response. This work also constitutes a first step in the possible rational design of efficient therapeutic agents aiming at perturbing the interaction between SARS Unique Domain and guanine quadruplexes, hence enhancing the host defenses against the virus.
has issue date	2020-06-14(xsd:dateTime)
bibo:doi	10.1021/acs.jpclett.0c01097
bibo:pmid	32536162
has license	no-cc
sha1sum (hex)	f0d2fe6c8a0729a16efe056552a7428b6d0ef458
schema:url	https://doi.org/10.1021/acs.jpclett.0c01097
resource representing a document's title	Role of RNA Guanine Quadruplexes in Favoring the Dimerization of SARS Unique Domain in Coronaviruses
has PubMed Central identifier	PMC7331935
has PubMed identifier	32536162
schema:publication	J Phys Chem Lett
resource representing a document's body	covid:f0d2fe6c8a0729a16efe056552a7428b6d0ef458#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/f0d2fe6c8a0729a16efe056552a7428b6d0ef458
is schema:about of	named entity 'enhancing' named entity 'free energy' named entity 'bypass' named entity 'sampling' named entity 'points' named entity 'stable' named entity 'RELATED' named entity 'BINDING' named entity 'VIRUSES' named entity 'TYPE VIRUS' named entity 'VIRAL INFECTION' named entity 'ITS' named entity 'SITE' named entity 'INVOLVED' named entity 'EFFECT' named entity 'FAVORING' named entity 'PROFILE' named entity 'PRESENT' named entity 'CONTRIBUTION' named entity 'CONSEQUENCES' named entity 'INVOLVING' named entity 'POINTS' named entity 'MONOMER' named entity 'STABLE' named entity 'MATTER' named entity 'DIMER' named entity 'molecular dynamics' named entity 'economic' named entity 'fact' named entity 'RNA' named entity 'agents' named entity 'efficient' named entity 'interaction' named entity 'interaction' named entity 'human cells' named entity 'host defenses' named entity 'global pandemic' named entity 'SARS' named entity 'biological role' named entity 'viral infection' named entity 'free energy' named entity 'guanine' named entity 'SARS' named entity 'therapeutic agents' named entity 'dimer' named entity 'protein dimer' named entity 'protein dimer' named entity 'guanine' named entity 'SARS' named entity 'Dimerization' named entity 'Guanine' named entity 'viral infection' named entity 'RDF' named entity 'protein' named entity 'antiviral' named entity 'coronaviruses' named entity 'infection' named entity 'protein' named entity 'COVID-19 pandemic' named entity 'force field' named entity 'social distancing' named entity 'potential of mean force' named entity 'protein' named entity 'coronaviruses' named entity 'SARS' named entity 'SARS disease' named entity 'RMSD' named entity 'viruses' named entity 'cell survival' named entity 'noncovalent interactions' named entity 'radial distribution function'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software