About: Structure-based drug repositioning over the human TMPRSS2 protease domain: search for chemical probes able to repress SARS-CoV-2 Spike protein cleavages

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About: Structure-based drug repositioning over the human TMPRSS2 protease domain: search for chemical probes able to repress SARS-CoV-2 Spike protein cleavages Goto Sponge NotDistinct Permalink

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	Structure-based drug repositioning over the human TMPRSS2 protease domain: search for chemical probes able to repress SARS-CoV-2 Spike protein cleavages
Creator	Decroly, Etienne Khatib, Abdel-Majid Singh, Natesh Villoutreix, Bruno
Source	Elsevier; Medline; PMC
abstract	In December 2019, a new coronavirus was identified in the Hubei province of central china and named SARS-CoV-2. This new virus induces COVID-19, a severe respiratory disease with high death rate. A putative target to interfere with the virus is the host transmembrane serine protease family member II (TMPRSS2). This enzyme is critical for the entry of coronaviruses into human cells by cleaving and activating the spike protein (S) of SARS-CoV-2. Repositioning approved, investigational and experimental drugs on the serine protease domain of TMPRSS2 could thus be valuable. There is no experimental structure for TMPRSS2 but it is possible to develop quality structural models for the serine protease domain using comparative modeling strategies as such domains are highly structurally conserved. Beside the TMPRSS2 catalytic site, we predicted on our structural models a main exosite that could be important for the binding of protein partners and/or substrates. To block the catalytic site or the exosite of TMPRSS2 we used structure-based virtual screening computations and two different collections of approved, investigational and experimental drugs. We propose a list of 156 molecules that could bind to the catalytic site and 100 compounds that may interact with the exosite. These small molecules should now be tested in vitro to gain novel insights over the roles of TMPRSS2 or as starting point for the development of second generation analogs.
has issue date	2020-07-28(xsd:dateTime)
bibo:doi	10.1016/j.ejps.2020.105495
bibo:pmid	32730844
has license	no-cc
sha1sum (hex)	e96d3e3d4fc1e908dd8c573f11b80f86cf95b07f
schema:url	https://doi.org/10.1016/j.ejps.2020.105495
resource representing a document's title	Structure-based drug repositioning over the human TMPRSS2 protease domain: search for chemical probes able to repress SARS-CoV-2 Spike protein cleavages
has PubMed Central identifier	PMC7384984
has PubMed identifier	32730844
schema:publication	Eur J Pharm Sci
resource representing a document's body	covid:e96d3e3d4fc1e908dd8c573f11b80f86cf95b07f#body_text
is schema:about of	named entity 'original' named entity 'long' named entity 're-use' named entity 'COVID-19' named entity 'original source' named entity 'protease' named entity 'Structure-based' named entity '3.5' named entity 'pneumonia' named entity 'protein' named entity 'camostat' named entity 'serine protease' named entity 'serine protease' named entity 'peptides' named entity 'Ramachandran plot' named entity 'Cell entry' named entity 'binding pocket' named entity 'PDB' named entity 'proteases' named entity 'structural analysis' named entity 'binding pockets' named entity 'FDA' named entity 'virtual screening' named entity 'TMPRSS2' named entity 'coronaviruses' named entity 'peptide' named entity 'TMPRSS2' named entity 'exosite' named entity 'TMPRSS2' named entity 'drug repositioning' named entity 'thrombin' named entity 'TMPRSS2' named entity 'membrane fusion' named entity 'approved drugs' named entity 'solvent' named entity 'small molecules' named entity 'solvent' named entity 'adverse drug reactions' named entity 'transmissibility' named entity 'China' named entity 'AutoDock Vina' named entity 'TMPRSS2' named entity 'Villarreal' named entity 'catalytic triad' named entity 'ChEMBL' named entity 'protein' named entity 'DrugBank' named entity 'Protein' named entity 'thrombin' named entity 'protein-protein interactions' named entity 'hydrogen atoms' named entity 'infection' named entity 'kallikrein' named entity 'bioactive compounds' named entity 'enzyme' named entity 'TMPRSS2' named entity 'MAFFT' named entity 'structure-based' named entity 'co-crystal' named entity 'SARS-CoV-2' named entity 'SARS-CoV-2' named entity 'cofactors' named entity 'TMPRSS2' named entity 'heparin' named entity 'TMPRSS2' named entity 'AutoDock Vina' named entity 'stereochemical' named entity 'binding pocket' named entity 'small molecules' named entity 'TMPRSS2' named entity 'TMPRSS2' named entity 'thrombin' named entity 'serine protease inhibitors' named entity 'camostat' named entity 'heparin' named entity 'serine protease inhibitors' named entity 'Nero' named entity 'exosite'

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