About: Can Papain-like Protease Inhibitors Halt SARS-CoV-2 Replication?

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Can Papain-like Protease Inhibitors Halt SARS-CoV-2 Replication?
Creator	Maiti, Biplab
Source	PMC
abstract	[Image: see text] SARS-CoV-2 encoded papain-like protease (PLpro) harbors a labile Zn site (Cys(189)–X–X–Cys(192)–X(n)–Cys(224)–X–Cys(226)) and a classic catalytic site (Cys(111)–His(272)–Asp(286)), which play key roles for viral replication and hence represent promising drug targets. In this Viewpoint, both sulfur-based drugs and peptides-based inhibitors may block Cys residues in the catalytic and/or Zn site of CoV-2-PLpro, leading to dysfunction of CoV-2-PLpro and thereby halting viral replication.
has issue date	2020-08-04(xsd:dateTime)
bibo:doi	10.1021/acsptsci.0c00093
has license	no-cc
sha1sum (hex)	5628ddfa471c83d735e70e11dfbff924ba156522
schema:url	https://doi.org/10.1021/acsptsci.0c00093
resource representing a document's title	Can Papain-like Protease Inhibitors Halt SARS-CoV-2 Replication?
has PubMed Central identifier	PMC7409920
schema:publication	ACS Pharmacol Transl Sci
resource representing a document's body	covid:5628ddfa471c83d735e70e11dfbff924ba156522#body_text
is schema:about of	named entity 'Cys' named entity 'drugs' named entity 'key' named entity 'VIRAL REPLICATION' named entity 'PAPAIN' named entity '192' named entity 'block' named entity 'Cys' named entity 'PLpro' named entity 'Asp' named entity 'Cys' named entity 'catalytic site' named entity 'SARS-CoV-2' named entity 'SARS-CoV-2' named entity 'sulfur' named entity 'PLpro' named entity 'cysteine' named entity 'India' named entity 'catalytic site' named entity 'butyric acid' named entity 'SARS' named entity 'Cys' named entity 'PLpro' named entity 'binding domain' named entity 'benzothiazole' named entity 'motif' named entity 'catalytic site' named entity 'protease' named entity 'peptides' named entity 'substrate' named entity 'PLpro' named entity '3CLpro' named entity 'PLpro' named entity 'catalytic site' named entity 'antiviral activity' named entity 'viral replication' named entity 'ubiquitin' named entity 'virus' named entity 'drug target' named entity 'virus replication' named entity 'Cys' named entity 'amino acid' named entity 'crystal structure' named entity 'leucine' named entity 'enzyme' named entity 'host cell' named entity 'nsp3' named entity 'polyprotein' named entity 'FDA' named entity 'substrate' named entity 'DSF' named entity 'cleavage' named entity 'viral replication' named entity 'SARS-CoV-2' named entity 'COVID-19' named entity 'cysteine proteases' named entity 'chymotrypsin-like' named entity 'glycine' named entity 'Cys' named entity 'PLpro' named entity 'angiotensin-converting enzyme 2' named entity 'amino acid' named entity 'Cys' named entity 'virus' named entity 'ubiquitin' named entity 'virus' named entity 'Cys' named entity 'nsp2' named entity 'viral replication' named entity 'severe acute respiratory syndrome coronavirus' named entity 'virus replication' named entity 'Cys' named entity 'substrate' named entity 'peptide' named entity 'therapeutic targets' named entity 'innate immune responses' named entity 'Sikkim' named entity 'ion' named entity 'ion' named entity 'PLpro' named entity 'DSF' named entity 'RNA synthesis' named entity 'transcription'

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