About: From SARS to MERS: crystallographic studies on coronaviral proteases enable antiviral drug design

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About: From SARS to MERS: crystallographic studies on coronaviral proteases enable antiviral drug design 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	From SARS to MERS: crystallographic studies on coronaviral proteases enable antiviral drug design
Creator	Hilgenfeld, Rolf
source	Medline; PMC
abstract	This review focuses on the important contributions that macromolecular crystallography has made over the past 12 years to elucidating structures and mechanisms of the essential proteases of coronaviruses, the main protease (M(pro)) and the papain‐like protease (PL(pro)). The role of X‐ray crystallography in structure‐assisted drug discovery against these targets is discussed. Aspects dealt with in this review include the emergence of the SARS coronavirus in 2002–2003 and of the MERS coronavirus 10 years later and the origins of these viruses. The crystal structure of the free SARS coronavirus M(pro) and its dependence on pH is discussed, as are efforts to design inhibitors on the basis of these structures. The mechanism of maturation of the enzyme from the viral polyprotein is still a matter of debate. The crystal structure of the SARS coronavirus PL(pro) and its complex with ubiquitin is also discussed, as is its orthologue from MERS coronavirus. Efforts at predictive structure‐based inhibitor development for bat coronavirus M(pro)s to increase the preparedness against zoonotic transmission to man are described as well. The paper closes with a brief discussion of structure‐based discovery of antivirals in an academic setting.
has issue date	2014-08-11(xsd:dateTime)
bibo:doi	10.1111/febs.12936
bibo:pmid	25039866
has license	no-cc
sha1sum (hex)	ee4812c2c845d1962fb49adc742493f12541336e
schema:url	https://doi.org/10.1111/febs.12936
resource representing a document's title	From SARS to MERS: crystallographic studies on coronaviral proteases enable antiviral drug design
has PubMed Central identifier	PMC7163996
has PubMed identifier	25039866
schema:publication	FEBS J
resource representing a document's body	covid:ee4812c2c845d1962fb49adc742493f12541336e#body_text
is schema:about of	named entity 'antiviral drug' named entity 'human coronavirus' named entity 'clade' named entity 'polyprotein' named entity 'SARS-CoV' named entity 'Nsp3' named entity 'oxyanion' named entity 'toxicity' named entity 'MERS-CoV' named entity 'SARS-CoV' named entity 'enzyme' named entity 'crystal structure' named entity 'nitrogen' named entity 'triazoles' named entity 'monomer' named entity 'bat' named entity 'acidic pH' named entity 'MERS-CoV' named entity 'small-molecule' named entity 'peptide' named entity 'zoonotic transmission' named entity 'protease' named entity 'enzyme' named entity 'human coronavirus' named entity 'isatin' named entity 'protein' named entity 'zinc ion' named entity 'enzyme' named entity 'polypeptide chain' named entity 'thrombin' named entity 'N-terminal' named entity 'virus' named entity 'peptidomimetic' named entity 'proteolytic' named entity 'host cells' named entity 'protease' named entity 'epidemic' named entity 'papain' named entity 'X-ray crystallography' named entity 'SARS-CoV' named entity 'chronic disease' named entity 'protease' named entity 'intermediate hosts' named entity 'protease inhibitors' named entity 'SARS-CoV' named entity 'SARS-CoV' named entity 'virus' named entity 'chymotrypsin' named entity 'X-ray crystallography' named entity 'protease' named entity 'SARS-CoV' named entity 'SARS-CoV' named entity 'lysine' named entity 'SARS-CoV' named entity 'MERS-CoV' named entity 'coronaviruses' named entity 'protease' named entity 'coronavirus' named entity 'peptidomimetics' named entity 'genome' named entity 'Cys' named entity 'cysteine' named entity 'glycine' named entity 'polyprotein' named entity 'coronavirus' named entity 'polyprotein' named entity 'SARS coronavirus' named entity 'red arrows' named entity 'SARS-CoV' named entity 'Nsp3' named entity 'virologists' named entity 'Pfizer' named entity 'genome' named entity 'peptide' named entity '229E' named entity 'protease' named entity 'enzyme' named entity 'transcription' named entity 'substrate-binding site' named entity 'coronavirus' named entity 'MERS-CoV'

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