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English
Homology model of the dengue 2 virus NS3 protease: putative interactions with both substrate and NS2B cofactor.
scientific article published on May 1999
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scholarly article
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Europe PubMed Central
PubMed publication ID
10355763
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10355763%20AND%20SRC:MED&resulttype=core&format=json
retrieved
8 December 2019
title
Homology model of the dengue 2 virus NS3 protease: putative interactions with both substrate and NS2B cofactor
(English)
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stated in
Europe PubMed Central
PubMed publication ID
10355763
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10355763%20AND%20SRC:MED&resulttype=core&format=json
retrieved
8 December 2019
main subject
Dengue virus
1 reference
inferred from
title
dengue NS2B-NS3 protease
1 reference
based on heuristic
inferred from abstract
author
Paul R Young
series ordinal
4
1 reference
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Europe PubMed Central
PubMed publication ID
10355763
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10355763%20AND%20SRC:MED&resulttype=core&format=json
retrieved
8 December 2019
author name string
Brinkworth RI
series ordinal
1
1 reference
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Europe PubMed Central
PubMed publication ID
10355763
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10355763%20AND%20SRC:MED&resulttype=core&format=json
retrieved
8 December 2019
Fairlie DP
series ordinal
2
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Europe PubMed Central
PubMed publication ID
10355763
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10355763%20AND%20SRC:MED&resulttype=core&format=json
retrieved
8 December 2019
Leung D
series ordinal
3
1 reference
stated in
Europe PubMed Central
PubMed publication ID
10355763
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10355763%20AND%20SRC:MED&resulttype=core&format=json
retrieved
8 December 2019
language of work or name
English
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publication date
1 May 1999
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stated in
Europe PubMed Central
PubMed publication ID
10355763
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10355763%20AND%20SRC:MED&resulttype=core&format=json
retrieved
8 December 2019
published in
Journal of General Virology
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Europe PubMed Central
PubMed publication ID
10355763
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10355763%20AND%20SRC:MED&resulttype=core&format=json
retrieved
8 December 2019
volume
80 ( Pt 5)
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Europe PubMed Central
PubMed publication ID
10355763
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10355763%20AND%20SRC:MED&resulttype=core&format=json
retrieved
8 December 2019
page(s)
1167-1177
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Europe PubMed Central
PubMed publication ID
10355763
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10355763%20AND%20SRC:MED&resulttype=core&format=json
retrieved
8 December 2019
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Hepatitis C virus-encoded nonstructural protein NS4A has versatile functions in viral protein processing
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Mutagenesis of the yellow fever virus NS2B protein: effects on proteolytic processing, NS2B-NS3 complex formation, and viral replication
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Flavivirus premembrane protein cleavage and spike heterodimer secretion require the function of the viral proteinase NS3.
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The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site
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Primary structure of the West Nile flavivirus genome region coding for all nonstructural proteins
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Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide
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In vitro synthesis of West Nile virus proteins indicates that the amino-terminal segment of the NS3 protein contains the active centre of the protease which cleaves the viral polyprotein after multiple basic amino acids
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Cotranslational membrane insertion of the serine proteinase precursor NS2B-NS3(Pro) of dengue virus type 2 is required for efficient in vitro processing and is mediated through the hydrophobic regions of NS2B.
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Gene mapping and positive identification of the non-structural proteins NS2A, NS2B, NS3, NS4B and NS5 of the flavivirus Kunjin and their cleavage sites
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Evidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-bound host protease in the endoplasmic reticulum
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Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion
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Enhancement of hepatitis C virus NS3 proteinase activity by association with NS4A-specific synthetic peptides: identification of sequence and critical residues of NS4A for the cofactor activity
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Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins
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Assessment of protein models with three-dimensional profiles
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N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases
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The nucleotide sequence of dengue type 4 virus: analysis of genes coding for nonstructural proteins
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Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein
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Ultrastructure of Kunjin virus-infected cells: colocalization of NS1 and NS3 with double-stranded RNA, and of NS2B with NS3, in virus-induced membrane structures
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Cleavage at a novel site in the NS4A region by the yellow fever virus NS2B-3 proteinase is a prerequisite for processing at the downstream 4A/4B signalase site
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In vitro processing of dengue virus type 2 nonstructural proteins NS2A, NS2B, and NS3
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27 December 2022
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27 December 2022
Deletion analysis of dengue virus type 4 nonstructural protein NS2B: identification of a domain required for NS2B-NS3 protease activity
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27 December 2022
A central region in the hepatitis C virus NS4A protein allows formation of an active NS3-NS4A serine proteinase complex in vivo and in vitro
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27 December 2022
ChemInform Abstract: Towards Protein Surface Mimetics
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27 December 2022
Mimicking extended conformations of protease substrates
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27 December 2022
Characterization of the hepatitis C virus-encoded serine proteinase: determination of proteinase-dependent polyprotein cleavage sites
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Semantic Scholar
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retrieved
27 December 2022
Identifiers
DOI
10.1099/0022-1317-80-5-1167
1 reference
stated in
Europe PubMed Central
PubMed publication ID
10355763
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10355763%20AND%20SRC:MED&resulttype=core&format=json
retrieved
8 December 2019
PubMed publication ID
10355763
1 reference
stated in
Europe PubMed Central
PubMed publication ID
10355763
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10355763%20AND%20SRC:MED&resulttype=core&format=json
retrieved
8 December 2019
ResearchGate publication ID
12942697
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