Catalytically active Dengue virus NS3 protease forms aggregates that are separable by size exclusion chromatography. (Q40578147)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12135556%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

title

Catalytically active Dengue virus NS3 protease forms aggregates that are separable by size exclusion chromatography (English)

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11 November 2019

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dengue NS2B-NS3 protease

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inferred from abstract

author

David P. Fairlie

3

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12135556%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

Paul R Young

4

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11 November 2019

Jennifer L. Martin

5

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12135556%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

author name string

Tracy L Arakaki

1

1 reference

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11 November 2019

Ning-Xia Fang

2

1 reference

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11 November 2019

publication date

1 July 2002

1 reference

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Protein Expression and Purification

11 November 2019

published in

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11 November 2019

volume

25

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11 November 2019

issue

2

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11 November 2019

page(s)

241-247

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Cleavage of the dengue virus polyprotein at the NS3/NS4A and NS4B/NS5 junctions is mediated by viral protease NS2B-NS3, whereas NS4A/NS4B may be processed by a cellular protease

11 November 2019

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS1046-5928%2802%2900005-0

7 January 2021

Analyses of the terminal sequences of West Nile virus structural proteins and of the in vitro translation of these proteins allow the proposal of a complete scheme of the proteolytic cleavages involved in their synthesis

1 reference

https://api.crossref.org/works/10.1016%2FS1046-5928%2802%2900005-0

7 January 2021

Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins

1 reference

https://api.crossref.org/works/10.1016%2FS1046-5928%2802%2900005-0

7 January 2021

Dengue virus NS3 serine protease. Crystal structure and insights into interaction of the active site with substrates by molecular modeling and structural analysis of mutational effects

1 reference

https://api.crossref.org/works/10.1016%2FS1046-5928%2802%2900005-0

7 January 2021

Crystal structure of Dengue virus NS3 protease in complex with a Bowman-Birk inhibitor: implications for flaviviral polyprotein processing and drug design

1 reference

https://api.crossref.org/works/10.1016%2FS1046-5928%2802%2900005-0

7 January 2021

Homology model of the dengue 2 virus NS3 protease: putative interactions with both substrate and NS2B cofactor.

1 reference

https://api.crossref.org/works/10.1016%2FS1046-5928%2802%2900005-0

7 January 2021

Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2B co-factor, small peptide substrates, and inhibitors.

1 reference

https://api.crossref.org/works/10.1016%2FS1046-5928%2802%2900005-0

7 January 2021

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/10.1016%2FS1046-5928%2802%2900005-0

7 January 2021

Measurement of protein using bicinchoninic acid

1 reference

https://api.crossref.org/works/10.1016%2FS1046-5928%2802%2900005-0

7 January 2021

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/10.1016%2FS1046-5928%2802%2900005-0

7 January 2021

10.1016/S1046-5928(02)00005-0

Identifiers

DOI

1 reference

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release_igahuxbabbfhhpymvnstf6qizi

11 November 2019

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/igahuxbabbfhhpymvnstf6qizi

24 November 2022

mapped directly with Wikidata item

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