(Q28377012)

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Inhibition of hepatitis C virus NS2/3 processing by NS4A peptides. Implications for control of viral processing

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Inhibition of hepatitis C virus NS2/3 processing by NS4A peptides. Implications for control of viral processing (English)

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P L Darke

1

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A R Jacobs

series ordinal

2

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L Waxman

series ordinal

3

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L C Kuo

series ordinal

4

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language of work or name

English

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publication date

3 December 1999

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published in

Journal of Biological Chemistry

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volume

274

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issue

49

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page(s)

34511-4

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cites work

An assay for circulating antibodies to a major etiologic virus of human non-A, non-B hepatitis

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.274.49.34511

retrieved

21 January 2018

Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.274.49.34511

retrieved

21 January 2018

Genetic organization and diversity of the hepatitis C virus

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.274.49.34511

retrieved

21 January 2018

A second hepatitis C virus-encoded proteinase

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.274.49.34511

retrieved

21 January 2018

Expression, identification and subcellular localization of the proteins encoded by the hepatitis C viral genome

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.274.49.34511

retrieved

21 January 2018

Molecular biology of the hepatitis C viruses: implications for diagnosis, development and control of viral disease

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.274.49.34511

retrieved

21 January 2018

Proteolytic processing and membrane association of putative nonstructural proteins of hepatitis C virus

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Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.274.49.34511

retrieved

21 January 2018

Processing of hepatitis C viral polyprotein in Escherichia coli

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.274.49.34511

retrieved

21 January 2018

Analysis of NS3-mediated processing of the hepatitis C virus non-structural region in vitro

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stated in

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.274.49.34511

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21 January 2018

Mechanism of autoproteolysis at the NS2-NS3 junction of the hepatitis C virus polyprotein

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reference URL

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21 January 2018

Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide

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stated in

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.274.49.34511

retrieved

21 January 2018

Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: A 2.2 Å resolution structure in a hexagonal crystal form

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stated in

Crossref

reference URL

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retrieved

21 January 2018

The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site

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stated in

Crossref

reference URL

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21 January 2018

High-level expression of soluble protein in Escherichia coli using a His6-tag and maltose-binding-protein double-affinity fusion system.

1 reference

stated in

Crossref

reference URL

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21 January 2018

Complex formation between the hepatitis C virus serine protease and a synthetic NS4A cofactor peptide

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.274.49.34511

retrieved

21 January 2018

Modulation of hepatitis C virus NS3 protease and helicase activities through the interaction with NS4A

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.274.49.34511

retrieved

21 January 2018

Viral cysteine proteinases

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stated in

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.274.49.34511

retrieved

21 January 2018

Identifiers

DOI

10.1074/JBC.274.49.34511

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PubMed publication ID

10574908

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(Q28377012)

Inhibition of hepatitis C virus NS2/3 processing by NS4A peptides. Implications for control of viral processing

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