(Q45764108)

15 December 2017

title

Substrate specificity of the hepatitis C virus serine protease NS3. (English)

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15 December 2017

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Raffaele De Francesco

5

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15 December 2017

Anna Tramontano

4

object named as

Tramontano A

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15 December 2017

Urbani A

1

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15 December 2017

Bianchi E

2

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15 December 2017

Narjes F

3

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15 December 2017

Steinkühler C

6

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Pessi A

7

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language of work or name

English

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publication date

1 April 1997

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15 December 2017

Journal of Biological Chemistry

published in

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15 December 2017

volume

272

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issue

14

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15 December 2017

page(s)

9204-9209

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15 December 2017

The hepatitis C virus encodes a serine protease involved in processing of the putative nonstructural proteins from the viral polyprotein precursor

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

Processing of hepatitis C viral polyprotein in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

A central hydrophobic domain of the hepatitis C virus NS4A protein is necessary and sufficient for the activation of the NS3 protease

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

In vitro studies on the activation of the hepatitis C virus NS3 proteinase by the NS4A cofactor.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

In vitro activity of hepatitis C virus protease NS3 purified from recombinant Baculovirus-infected Sf9 cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

Molecular model of the specificity pocket of the hepatitis C virus protease: implications for substrate recognition.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

Redesigning the substrate specificity of the hepatitis C virus NS3 protease.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

Substrate specificity of the NS3 serine proteinase of hepatitis C virus as determined by mutagenesis at the NS3/NS4A junction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

Bacterial expression and analysis of cleavage activity of HCV serine proteinase using recombinant and synthetic substrate.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

Recombinant baculovirus-expressed NS3 proteinase of hepatitis C virus shows activity in cell-based and in vitro assays

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

In vitro cleavage of hepatitis C virus polyprotein substrates by purified recombinant NS3 protease

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

In vivo and in vitro trans-cleavage activity of hepatitis C virus serine proteinase expressed by recombinant baculoviruses

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

Proteolytic activity of NS3 serine proteinase of hepatitis C virus efficiently expressed in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

Enzymatic characterization of purified NS3 serine proteinase of hepatitis C virus expressed in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

A continuous assay of hepatitis C virus protease based on resonance energy transfer depsipeptide substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

Structural basis of substrate specificity in the serine proteases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

Stimulation of the herpes simplex virus type I protease by antichaeotrophic salts

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

Substrate specificity of porcine renin: P1', P1, and P3 residues of renin substrates are crucial for activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

Distinct mechanisms contribute to stringent substrate specificity of tissue-type plasminogen activator

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.14.9204

21 January 2018

Identifiers

DOI

10.1074/JBC.272.14.9204

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15 December 2017

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15 December 2017