About: Characterization of the cleavage of signal peptide at the C-terminus of hepatitis C virus core protein by signal peptide peptidase

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

About: Characterization of the cleavage of signal peptide at the C-terminus of hepatitis C virus core protein by signal peptide peptidase 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	Characterization of the cleavage of signal peptide at the C-terminus of hepatitis C virus core protein by signal peptide peptidase
Creator	Lo, Shih-Yen Ma, Hsin-Chieh Hsieh, Yi-Ching Ku, Yi-Yung
Source	Medline; PMC
abstract	Production of hepatitis C virus (HCV) core protein requires the cleavages of polyprotein by signal peptidase and signal peptide peptidase (SPP). Cleavage of signal peptide at the C-terminus of HCV core protein by SPP was characterized in this study. The spko mutant (mutate a.a. 189–193 from ASAYQ to PPFPF) is more efficient than the A/F mutant (mutate a.a 189 and 191 from A to F) in blocking the cleavage of signal peptide by signal peptidase. The cleavage efficiency of SPP is inversely proportional to the length of C-terminal extension of the signal peptide: the longer the extension, the less efficiency the cleavage is. Thus, reducing the length of C-terminal extension of signal peptide by signal peptidase cleavage could facilitate further cleavage by SPP. The recombinant core protein fused with signal peptide from the C-terminus of p7 protein, but not those from the C-termini of E1 and E2, could be cleaved by SPP. Therefore, the sequence of the signal peptide is important but not the sole determinant for its cleavage by SPP. Replacement of the HCV core protein E.R.-associated domain (a.a. 120–150) with the E.R.-associated domain (a.a.1–50) of SARS-CoV membrane protein results in the failure of cleavage of this recombinant protein by SPP, though this protein still is E.R.-associated. This result suggests that not only E.R.-association but also specific protein sequence is important for the HCV core protein signal peptide cleavage by SPP. Thus, our results suggest that both sequences of the signal peptide and the E.R.-associated domain are important for the signal peptide cleavage of HCV core protein by SPP. Electronic Supplementary MaterialThe online version of this article (doi: 10.1007/s11373-006-9127-1) contains supplementary material, which is available to authorized users.
has issue date	2007-01-20(xsd:dateTime)
bibo:doi	10.1007/s11373-006-9127-1
bibo:pmid	17237979
has license	no-cc
sha1sum (hex)	d1b81e5a1b204e350f125b9f4f6781dbe1668dfb
schema:url	https://doi.org/10.1007/s11373-006-9127-1
resource representing a document's title	Characterization of the cleavage of signal peptide at the C-terminus of hepatitis C virus core protein by signal peptide peptidase
has PubMed Central identifier	PMC7088784
has PubMed identifier	17237979
schema:publication	J Biomed Sci
resource representing a document's body	covid:d1b81e5a1b204e350f125b9f4f6781dbe1668dfb#body_text
is schema:about of	named entity 'SIGNAL PEPTIDE PEPTIDASE' named entity 'IMPORTANT' named entity '28A' named entity 'C-TERMINAL' named entity 'RECOMBINANT PROTEIN' named entity 'CLEAVED' named entity 'PROPORTIONAL' named entity 'RESULTS' named entity 'PRODUCTION' named entity 'CHARACTERIZATION' named entity 'ITS' named entity 'POLYPROTEIN' named entity 'ASSOCIATED' named entity 'EFFICIENT' named entity 'SIGNAL PEPTIDE' named entity 'MEMBRANE PROTEIN' named entity 'CLEAVAGE' named entity 'SPP' named entity 'BLOCKING' named entity 'CORE PROTEIN' named entity 'REDUCING' named entity 'STUDY' named entity 'SUGGEST' named entity 'ASSOCIATION' named entity 'RECOMBINANT' named entity 'SIGNAL PEPTIDE CLEAVAGE' named entity 'RESULT' named entity '120' named entity 'SIGNAL PEPTIDASE' named entity 'VIRUS CORE PROTEIN' named entity 'CLEAVAGE' named entity 'SIGNAL PEPTIDE' named entity 'FAILURE' named entity 'C-TERMINUS' named entity 'PROTEIN FUSED' named entity 'REPLACEMENT' named entity 'PROTEIN ' named entity 'PROTEIN SEQUENCE' named entity 'HEPATITIS C VIRUS' named entity 'COULD BE' named entity 'PROTEIN' named entity 'C-TERMINUS' named entity 'BUT' named entity 'EXTENSION OF' named entity 'LENGTH' named entity '189' named entity 'SPECIFIC PROTEIN' named entity 'DETERMINANT' named entity 'HEPATITIS C VIRUS CORE' named entity 'CHARACTERIZED' named entity 'SOLE' named entity '50%' named entity 'SEQUENCE' named entity 'EFFICIENCY' named entity 'MUTANT' named entity '150' named entity 'HCV' named entity 'SIGNAL PEPTIDE PEPTIDASE' named entity 'FUSED WITH' named entity 'PROTEIN ' named entity 'SEQUENCES' named entity 'EXTENSION' named entity '191' named entity 'DOMAIN' named entity 'OUR' named entity 'SARS-COV' named entity 'PROTEIN E' covid:arg/d1b81e5a1b204e350f125b9f4f6781dbe1668dfb named entity 'cleavage' named entity 'signal peptide' named entity 'SPP' named entity 'SPP' named entity 'signal peptide' named entity 'signal peptide cleavage' named entity 'HCV' named entity 'E.R.' named entity 'core protein' named entity 'C-terminus'

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