Dengue protease activity: the structural integrity and interaction of NS2B with NS3 protease and its potential as a drug target (Q39354663)

11 September 2017

Dengue protease activity: the structural integrity and interaction of NS2B with NS3 protease and its potential as a drug target (English)

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11 September 2017

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Nicole J Moreland

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Siew Pheng Lim

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Siew P Lim

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author name string

Wai Y Phong

1

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11 September 2017

Daying Wen

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11 September 2017

Prasad N Paradkar

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11 September 2017

Subhash G Vasudevan

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11 September 2017

1 October 2011

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11 September 2017

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11 September 2017

31

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11 September 2017

5

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11 September 2017

399-409

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Dengue: the risk to developed and developing countries

11 September 2017

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https://api.crossref.org/works/10.1042%2FBSR20100142

Flavivirus genome organization, expression, and replication

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

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.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBSR20100142

Mutagenesis of the yellow fever virus NS2A/2B cleavage site: effects on proteolytic processing, viral replication, and evidence for alternative processing of the NS2A protein

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

Dengue 2 virus NS2B and NS3 form a stable complex that can cleave NS3 within the helicase domain

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

Processing of nonstructural proteins NS4A and NS4B of dengue 2 virus in vitro and in vivo

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

Flavivirus premembrane protein cleavage and spike heterodimer secretion require the function of the viral proteinase NS3.

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

Regulation of the late events in flavivirus protein processing and maturation

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

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

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

Functional profiling of recombinant NS3 proteases from all four serotypes of dengue virus using tetrapeptide and octapeptide substrate libraries.

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus.

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

Structural evidence for regulation and specificity of flaviviral proteases and evolution of theFlaviviridaefold

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

Structure of West Nile virus NS3 protease: ligand stabilization of the catalytic conformation

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

NMR Analysis of the Dynamic Exchange of the NS2B Cofactor between Open and Closed Conformations of the West Nile Virus NS2B-NS3 Protease

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBSR20100142

Serotype-Specific Structural Differences in the Protease-Cofactor Complexes of the Dengue Virus Family

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBSR20100142

Activation of dengue protease autocleavage at the NS2B–NS3 junction by recombinant NS3 and GST–NS2B fusion proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBSR20100142

On-column protein refolding for crystallization

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

High affinity human antibody fragments to dengue virus non-structural protein 3

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

Yellow fever virus NS3 protease: peptide-inhibition studies.

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

On a mouse monoclonal antibody that neutralizes all four dengue virus serotypes

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

Identification of residues in the dengue virus type 2 NS2B cofactor that are critical for NS3 protease activation

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

Mechanism of NS2B-Mediated Activation of NS3pro in Dengue Virus: Molecular Dynamics Simulations and Bioassays

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

The active essential CFNS3d protein complex

21 January 2018

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https://api.crossref.org/works/10.1042%2FBSR20100142

Crystal Structure of the NS3 Protease-Helicase from Dengue Virus

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBSR20100142

A multigene analysis of the phylogenetic relationships among the flaviviruses (Family: Flaviviridae) and the evolution of vector transmission

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBSR20100142

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBSR20100142

Novel dengue virus-specific NS2B/NS3 protease inhibitor, BP2109, discovered by a high-throughput screening assay

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBSR20100142

21 January 2018

Identifiers

DOI

10.1042/BSR20100142

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11 September 2017

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