Detection and in-cell selectivity profiling of the full-length West Nile virus NS2B/NS3 serine protease using membrane-anchored fluorescent substrates (Q42995620)

From Wikidata

Jump to navigation Jump to search

scientific article published in May 2010

Language	Label	Description	Also known as
English	Detection and in-cell selectivity profiling of the full-length West Nile virus NS2B/NS3 serine protease using membrane-anchored fluorescent substrates	scientific article published in May 2010

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

Detection and in-cell selectivity profiling of the full-length West Nile virus NS2B/NS3 serine protease using membrane-anchored fluorescent substrates (English)

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

West Nile virus

0 references

author name string

Stephanie A Condotta

1

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

Morgan M Martin

2

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

Martine Boutin

3

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

François Jean

4

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

language of work or name

1 reference

based on heuristic

inferred from title

publication date

1 May 2010

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

391

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

5

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

549-559

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

Functional characterization of cis and trans activity of the Flavivirus NS2B-NS3 protease.

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

The molecular biology of West Nile Virus: a new invader of the western hemisphere

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Nucleotide sequence of the 5'-terminal untranslated part of the genome of the flavivirus West Nile virus

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Sequence analysis of the viral core protein and the membrane-associated proteins V1 and NV2 of the flavivirus West Nile virus and of the genome sequence for these proteins

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Primary structure of the West Nile flavivirus genome region coding for all nonstructural proteins

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Flavivirus genome organization, expression, and replication

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Site-directed mutagenesis and kinetic studies of the West Nile Virus NS3 protease identify key enzyme-substrate interactions.

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Insights to substrate binding and processing by West Nile Virus NS3 protease through combined modeling, protease mutagenesis, and kinetic studies

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Generation and characterization of proteolytically active and highly stable truncated and full-length recombinant West Nile virus NS3.

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Mutagenesis of the West Nile virus NS2B cofactor domain reveals two regions essential for protease activity

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

West Nile Virus NS2B/NS3 protease as an antiviral target

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

The Two-component NS2B-NS3 Proteinase Represses DNA Unwinding Activity of the West Nile Virus NS3 Helicase

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

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.

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Effects of detergents on the West Nile virus protease activity

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Enzymatic characterization of membrane-associated hepatitis C virus NS3-4A heterocomplex serine protease activity expressed in human cells

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

The antiviral protein, viperin, localizes to lipid droplets via its N-terminal amphipathic alpha-helix

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Mutagenesis of conserved residues at the yellow fever virus 3/4A and 4B/5 dibasic cleavage sites: effects on cleavage efficiency and polyprotein processing

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Single-cell resolution imaging of membrane-anchored hepatitis C virus NS3/4A protease activity

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Enzymatic characterization and homology model of a catalytically active recombinant West Nile virus NS3 protease

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Structure-based mutagenesis identifies important novel determinants of the NS2B cofactor of the West Nile virus two-component NS2B-NS3 proteinase

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Nucleotide sequence of yellow fever virus: implications for flavivirus gene expression and evolution

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Serpin mechanism of hepatitis C virus nonstructural 3 (NS3) protease inhibition: induced fit as a mechanism for narrow specificity

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

On the size of the active site in proteases. I. Papain

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Cleavage targets and the D-arginine-based inhibitors of the West Nile virus NS3 processing proteinase

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Expression and purification of a two-component flaviviral proteinase resistant to autocleavage at the NS2B–NS3 junction region

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Cleavage preference distinguishes the two-component NS2B–NS3 serine proteinases of Dengue and West Nile viruses

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Switching the Substrate Specificity of the Two-Component NS2B-NS3 Flavivirus Proteinase by Structure-Based Mutagenesis

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Architecture of the flaviviral replication complex. Protease, nuclease, and detergents reveal encasement within double-layered membrane compartments

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

The carboxy-terminal part of the NS 3 protein of the West Nile Flavivirus can be isolated as a soluble protein after proteolytic cleavage and represents an RNA-stimulated NTPase

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Description of a procedure which allows isolation of viral nonstructural proteins from BHK vertebrate cells infected with the West Nile flavivirus in a state which allows their direct chemical characterization

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Regulation of the late events in flavivirus protein processing and maturation

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Structure of the immature dengue virus at low pH primes proteolytic maturation

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Purified NS2B/NS3 serine protease of dengue virus type 2 exhibits cofactor NS2B dependence for cleavage of substrates with dibasic amino acids in vitro

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases

1 reference

https://api.crossref.org/works/10.1515%2FBC.2010.051

21 January 2018

Identifiers

10.1515/BC.2010.051

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

12 November 2017

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q42995620&oldid=1976284998"