NMR Analysis of the Dynamic Exchange of the NS2B Cofactor between Open and Closed Conformations of the West Nile Virus NS2B-NS3 Protease (Q27490417)

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NMR analysis of the dynamic exchange of the NS2B cofactor between open and closed conformations of the West Nile virus NS2B-NS3 protease

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English	NMR Analysis of the Dynamic Exchange of the NS2B Cofactor between Open and Closed Conformations of the West Nile Virus NS2B-NS3 Protease	scientific article	NMR analysis of the dynamic exchange of the NS2B cofactor between open and closed conformations of the West Nile virus NS2B-NS3 protease

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scholarly article

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14 February 2020

NMR analysis of the dynamic exchange of the NS2B cofactor between open and closed conformations of the West Nile virus NS2B-NS3 protease (English)

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14 February 2020

infectious disease

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West Nile virus

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5

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14 February 2020

Gottfried Otting

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14 February 2020

Subhash G Vasudevan

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Subhash G Vasudevan

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14 February 2020

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Xun-Cheng Su

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14 February 2020

Kiyoshi Ozawa

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14 February 2020

Ruhu Qi

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8 December 2009

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14 February 2020

PLoS Neglected Tropical Diseases

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14 February 2020

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14 February 2020

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14 February 2020

e561

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14 February 2020

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Creative Commons Attribution 4.0 International

8 December 2009

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April 2022 Public Data File from Crossref

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Discovery of a Non-Peptidic Inhibitor of West Nile Virus NS3 Protease by High-Throughput Docking

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2780355

20 March 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2780355

20 March 2017

Identification and Biochemical Characterization of Small-Molecule Inhibitors of West Nile Virus Serine Protease by a High-Throughput Screen

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2780355

20 March 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2780355

20 March 2017

Crystal Structure of the NS3 Protease-Helicase from Dengue Virus

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2780355

20 March 2017

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

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2780355

20 March 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2780355

20 March 2017

Origin of the West Nile virus responsible for an outbreak of encephalitis in the northeastern United States

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20 March 2017

Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

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20 March 2017

A fluorescence quenching assay to discriminate between specific and nonspecific inhibitors of dengue virus protease.

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29 September 2017

Flaviviral protease inhibitors identified by fragment-based library docking into a structure generated by molecular dynamics

1 reference

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29 September 2017

West Nile Virus NS2B/NS3 protease as an antiviral target

1 reference

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29 September 2017

Towards the design of antiviral inhibitors against flaviviruses: the case for the multifunctional NS3 protein from Dengue virus as a target

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29 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2780355

29 September 2017

HTS identifies novel and specific uncompetitive inhibitors of the two-component NS2B-NS3 proteinase of West Nile virus

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2780355

29 September 2017

The active essential CFNS3d protein complex

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29 September 2017

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

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29 September 2017

Identification and characterization of nonsubstrate based inhibitors of the essential dengue and West Nile virus proteases

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29 September 2017

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

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29 September 2017

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

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2 June 2018

Potent cationic inhibitors of West Nile virus NS2B/NS3 protease with serum stability, cell permeability and antiviral activity

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21 January 2018

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

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https://api.crossref.org/works/10.1371%2FJOURNAL.PNTD.0000561

21 January 2018

NMR study of complexes between low molecular mass inhibitors and the West Nile virus NS2B-NS3 protease

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21 January 2018

Optimization of an Escherichia coli system for cell-free synthesis of selectively N-labelled proteins for rapid analysis by NMR spectroscopy

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21 January 2018

Cell-free transcription/translation from PCR-amplified DNA for high-throughput NMR studies.

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21 January 2018

Identifiers

10.1371/JOURNAL.PNTD.0000561

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19997625%20AND%20SRC:MED&resulttype=core&format=json

14 February 2020

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19997625%20AND%20SRC:MED&resulttype=core&format=json

14 February 2020

1 reference

Europe PubMed Central

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14 February 2020

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