About: Differential domain structure stability of the severe acute respiratory syndrome coronavirus papain-like protease

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

About: Differential domain structure stability of the severe acute respiratory syndrome coronavirus papain-like 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	Differential domain structure stability of the severe acute respiratory syndrome coronavirus papain-like protease
Creator	Chou, Chi-Yuan Cheng, Shu-Chun Chou, Ya-Wen Lai, Hsing-Yi
Source	Elsevier; Medline; PMC
abstract	Abstract Papain-like protease (PLpro) from severe acute respiratory syndrome (SARS) coronavirus is one of the two proteases involved in the proteolytic processing of the virion polyproteins. In addition, PLpro shows significant in vitro deubiquitinating and de-ISGylating activities. All these findings demonstrated the multifunctional nature of the PLpro. Here we report the sensitivity of PLpro to denaturant urea. An increase in urea concentration induced a reversible biphasic unfolding of the enzyme. Differently, the unfolding of the catalytic triad region located within the palm and thumb domains followed a monophasic unfolding curve. Further observations suggest that the zinc-binding domain may start to unfold during the first transition. An 80% lost of its enzymatic activity at a urea concentration lower than 1M showed a close correlation with unfolding of the zinc-binding domain. The enzyme was also characterized in terms of hydrophobicity and size-and-shape distribution. We have demonstrated that PLpro displayed differential domain structure stability and molten globule state in its folding. These studies will not only assist in our understanding of the folding of this viral enzyme, but also that of other deubiquitinating enzymes with a similar scaffold.
has issue date	2012-04-15(xsd:dateTime)
bibo:doi	10.1016/j.abb.2012.02.015
bibo:pmid	22391227
has license	els-covid
sha1sum (hex)	9e5703d577f7e8f824906685a970ad5c5e2e1ce4
schema:url	https://doi.org/10.1016/j.abb.2012.02.015
resource representing a document's title	Differential domain structure stability of the severe acute respiratory syndrome coronavirus papain-like protease
has PubMed Central identifier	PMC7094420
has PubMed identifier	22391227
schema:publication	Archives of Biochemistry and Biophysics
resource representing a document's body	covid:9e5703d577f7e8f824906685a970ad5c5e2e1ce4#body_text
is schema:about of	named entity 'STABILITY' named entity 'PROTEASE' named entity 'correlation' named entity 'denaturant' named entity 'enzymes' named entity 'hydrophobicity' named entity 'located' named entity 'scaffold' named entity 'severe acute respiratory syndrome (SARS)' named entity 'HAVE' named entity 'SHAPE' named entity 'ADDITION' named entity 'PAPAIN' named entity 'OUR' named entity 'LOWER' named entity 'PROTEASE' named entity '80%' named entity 'FOLDING' named entity 'INDUCED' named entity 'CORRELATION' named entity 'PALM' named entity 'SCAFFOLD' named entity 'FOLLOWED' named entity 'CORONAVIRUS' named entity 'DOMAIN STRUCTURE' named entity 'ACTIVITIES' named entity 'SIZE' named entity 'PAPAIN' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME' named entity 'CHARACTERIZED' named entity 'IN VITRO' named entity 'DEUBIQUITINATING' named entity 'SIGNIFICANT' named entity 'THESE' named entity 'LOST' named entity 'DIFFERENTIAL' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS' named entity 'SIMILAR' named entity 'ONE OF' named entity 'START' named entity 'ITS' named entity 'PROTEOLYTIC PROCESSING' named entity 'BUT' named entity 'REPORT' named entity 'DOMAIN' named entity 'BINDING' named entity 'TRANSITION' named entity 'INCREASE' named entity 'CURVE' named entity 'UNFOLDING' named entity 'STATE' named entity 'DIFFERENTIAL' named entity 'NATURE' named entity 'ENZYME' named entity 'POLYPROTEINS' named entity 'ZINC' named entity 'LIKE' named entity 'SENSITIVITY' named entity 'PROTEASES' named entity 'REGION' named entity 'STABILITY' named entity 'MOLTEN GLOBULE' named entity 'HYDROPHOBICITY' named entity 'BIPHASIC' named entity 'LIKE' named entity 'MONOPHASIC' named entity 'SUGGEST' named entity 'OBSERVATIONS' named entity 'UREA' named entity 'ENZYMATIC ACTIVITY' named entity 'VIRAL' named entity 'DEMONSTRATED' named entity 'HERE' named entity 'DISTRIBUTION' named entity 'TERMS' named entity 'CLOSE' named entity 'DISPLAYED' named entity 'INVOLVED'

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