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About:
Characterization of ubiquitin and ubiquitin-like-protein isopeptidase activities
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schema:ScholarlyArticle
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wasabi.inria.fr
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Type:
Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
has title
Characterization of ubiquitin and ubiquitin-like-protein isopeptidase activities
Creator
Leach, Craig
Nicholson, Benjamin
Tian, Xufan
Bernal, Alejandro
Shanks, John
Mattern, Michael
Wilkinson, Keith
Butt, Tauseef
Francis, Dana
Goldenberg, Seth
Kodrasov, Matthew
Sterner, David
Source
Medline; PMC
abstract
Conjugation or deconjugation of ubiquitin (Ub) or ubiquitin-like proteins (UBLs) to or from cellular proteins is a multifaceted and universal means of regulating cellular physiology, controlling the lifetime, localization, and activity of many critical proteins. Deconjugation of Ub or UBL from proteins is performed by a class of proteases called isopeptidases. Herein is described a readily quantifiable novel isopeptidase assay platform consisting of Ub or UBL fused to the reporter enzyme phospholipase A(2) (PLA(2)). Isopeptidase activity releases PLA(2), which cleaves its substrate, generating a signal that is linear with deubiquitylase (DUB) concentration and is able to discriminate DUB, deSUMOylase, deNEDDylase, and deISGylase activities. The power and sensitivity of the UBL-PLA(2) assay are demonstrated by its ability to differentiate the contrasting deISGylase and DUB activities of two coronavirus proteases: severe acute respiratory syndrome papain-like protease (SARS-CoV PLpro) and NL63 CoV papain-like protease 2 (PLP2). Furthermore, direct comparisons with the current Ub-7-amino-4-methylcoumarin (Ub-AMC) assay demonstrated that the Ub-PLA(2) assay is an effective tool for characterizing modulators of isopeptidase activity. This observation was expanded by profiling the inhibitory activity of the nonselective isopeptidase inhibitor NSC 632839 against DUBs and deSUMOylases. Taken together, these studies illustrate the utility of the reporter-based approach to measuring isopeptidase activity.
has issue date
2008-06-01
(
xsd:dateTime
)
bibo:doi
10.1110/ps.083450408
bibo:pmid
18424514
has license
green-oa
sha1sum (hex)
a61e5889417eb9962a005eadfba3c9d28e73a9af
schema:url
https://doi.org/10.1110/ps.083450408
resource representing a document's title
Characterization of ubiquitin and ubiquitin-like-protein isopeptidase activities
has PubMed Central identifier
PMC2386736
has PubMed identifier
18424514
schema:publication
Protein Science
resource representing a document's body
covid:a61e5889417eb9962a005eadfba3c9d28e73a9af#body_text
is
schema:about
of
named entity 'called'
named entity 'proteases'
named entity 'power'
named entity 'This'
named entity 'activities'
named entity 'severe acute respiratory syndrome'
named entity 'DUB'
named entity 'ACTIVITIES'
named entity 'ISOPEPTIDASE'
named entity 'PROTEASES'
named entity 'TOOL'
named entity 'THESE'
named entity 'PROTEASE 2'
named entity 'QUANTIFIABLE'
named entity 'REGULATING'
named entity 'NSC 632839'
named entity 'REPORTER'
named entity 'INHIBITOR'
named entity 'MEASURING'
named entity 'LIKE'
named entity 'DISCRIMINATE'
named entity 'REPORTER ENZYME'
named entity 'MODULATORS'
named entity 'FUSED TO'
named entity 'CRITICAL'
named entity 'A CLASS'
named entity 'PROTEASE'
named entity 'DESCRIBED'
named entity 'CHARACTERIZATION'
named entity 'UBIQUITIN'
named entity 'LIKE'
named entity 'PROTEIN '
named entity 'CURRENT'
named entity 'SENSITIVITY'
named entity 'PERFORMED BY'
named entity 'DIFFERENTIATE'
named entity 'DEUBIQUITYLASE'
named entity 'SEVERE ACUTE RESPIRATORY SYNDROME'
named entity 'GENERATING'
named entity 'PAPAIN'
named entity 'CONTRASTING'
named entity 'SIGNAL'
named entity 'CELLULAR PHYSIOLOGY'
named entity 'MEANS'
named entity 'BASED'
named entity 'CORONAVIRUS'
named entity 'MULTIFACETED'
named entity 'UNIVERSAL'
named entity 'CONCENTRATION'
named entity 'CLEAVES'
named entity 'STUDIES'
named entity 'LIFETIME'
named entity 'ISOPEPTIDASE'
named entity 'ITS'
named entity 'ACTIVITIES'
named entity 'SUBSTRATE'
named entity 'PHOSPHOLIPASE A 2'
named entity 'OBSERVATION'
named entity 'IS A'
named entity 'PLA'
named entity 'DEMONSTRATED'
named entity 'NOVEL'
named entity 'RELEASES'
named entity 'CONJUGATION'
named entity '7-AMINO-4-METHYLCOUMARIN'
named entity 'APPROACH'
named entity 'UBL'
named entity 'TAKEN'
named entity 'POWER'
named entity 'CONTROLLING'
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