About: An Antiviral Mechanism of Nitric Oxide Inhibition of a Viral Protease

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

About: An Antiviral Mechanism of Nitric Oxide Inhibition of a Viral Protease 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
has title	An Antiviral Mechanism of Nitric Oxide Inhibition of a Viral Protease
Creator	Hohenadl, Christine Saura, Marta Zaragoza, Carlos Lowenstein, Charles Lowenstein, John Mcmillan, Audrey Quick, Richard
Source	Elsevier; Medline; PMC
abstract	Abstract Although nitric oxide (NO) kills or inhibits the replication of a variety of intracellular pathogens, the antimicrobial mechanisms of NO are unknown. Here, we identify a viral protease as a target of NO. The life cycle of many viruses depends upon viral proteases that cleave viral polyproteins into individual polypeptides. NO inactivates the Coxsackievirus protease 3C, an enzyme necessary for the replication of Coxsackievirus. NO S-nitrosylates the cysteine residue in the active site of protease 3C, inhibiting protease activity and interrupting the viral life cycle. Substituting a serine residue for the active site cysteine renders protease 3C resistant to NO inhibition. Since cysteine proteases are critical for virulence or replication of many viruses, bacteria, and parasites, S-nitrosylation of pathogen cysteine proteases may be a general mechanism of antimicrobial host defenses.
has issue date	1999-01-01(xsd:dateTime)
bibo:doi	10.1016/s1074-7613(00)80003-5
bibo:pmid	10023767
has license	els-covid
sha1sum (hex)	e2cd9385b6fe84f42f1f6d0c99053c3ec6e2bcdb
schema:url	https://doi.org/10.1016/s1074-7613%2800%2980003-5
resource representing a document's title	An Antiviral Mechanism of Nitric Oxide Inhibition of a Viral Protease
has PubMed Central identifier	PMC7129050
has PubMed identifier	10023767
schema:publication	Immunity
resource representing a document's body	covid:e2cd9385b6fe84f42f1f6d0c99053c3ec6e2bcdb#body_text
is schema:about of	named entity 'REPLICATION' named entity 'MECHANISM' named entity 'inhibits' named entity 'Viral' named entity 'INOS' named entity 'VIRAL RNA' named entity 'ANTIVIRAL' named entity 'POLIOVIRUS' named entity 'NITRIC OXIDE' named entity 'INHIBITION' named entity 'COXSACKIEVIRUS' named entity 'IN VITRO' named entity 'VIRAL' named entity 'REDUCING' named entity 'PROTEASE' named entity 'PROTEIN SYNTHESIS' named entity 'EXOGENOUS' named entity 'IMPORTANT' named entity 'viral RNA' named entity 'Exogenous' named entity 'Nitrosylation' named entity 'active site' named entity 'spermine' named entity 'luminometer' named entity 'cysteine' named entity 'protease' named entity 'PCR' named entity 'cysteine' named entity 'interferon' named entity 'Picornaviruses' named entity 'cell lysates' named entity 'luciferase' named entity 'lipopolysaccharide' named entity 'viruses' named entity 'subcloned' named entity 'protease' named entity 'Cys' named entity 'Protease' named entity 'cysteine' named entity 'infection' named entity 'motif' named entity 'mutagenesis' named entity 'substrate' named entity 'luciferase' named entity 'active site' named entity 'RNA synthesis' named entity 'proteases' named entity 'protease' named entity 'macrophages' named entity 'protease' named entity 'macrophages' named entity 'protease' named entity 'serine' named entity 'penicillamine' named entity 'cleavage' named entity 'nitrite' named entity 'Mutating' named entity 'active site' named entity 'DTT' named entity 'dialyzed' named entity 'cleavage' named entity 'NONOate' named entity 'Active Site' named entity 'exogenous' named entity 'reaction mixture' named entity 'thiols' named entity 'polyprotein' named entity 'macrophages' named entity 'macrophages' named entity 'cysteine' named entity 'cysteine proteases' named entity 'immunoblot' named entity 'protease' named entity 'concentra' named entity 'LPS'

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 © 2009-2024 OpenLink Software