Conserved C-terminal threonine of hepatitis C virus NS3 regulates autoproteolysis and prevents product inhibition (Q36942703)

17 August 2017

Conserved C-terminal threonine of hepatitis C virus NS3 regulates autoproteolysis and prevents product inhibition (English)

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17 August 2017

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Wenyan Wang

1

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17 August 2017

Frederick C Lahser

2

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17 August 2017

MinKyung Yi

3

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17 August 2017

Jacquelyn Wright-Minogue

4

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17 August 2017

Ellen Xia

5

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17 August 2017

Patricia C Weber

6

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17 August 2017

Stanley M Lemon

7

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17 August 2017

Bruce A Malcolm

8

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17 August 2017

language of work or name

English

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publication date

1 January 2004

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17 August 2017

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17 August 2017

78

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2

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17 August 2017

700-709

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describes a project that uses

17 August 2017

ImageQuant

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11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC368748/fullTextXML

based on heuristic

inferred from PubMed Central ID database lookup

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

29 September 2017

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Activity of purified hepatitis C virus protease NS3 on peptide substrates

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29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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27 June 2018

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27 June 2018

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Mechanistic role of an NS4A peptide cofactor with the truncated NS3 protease of hepatitis C virus: elucidation of the NS4A stimulatory effect via kinetic analysis and inhibitor mapping

27 June 2018

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27 June 2018

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27 June 2018

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Substrate specificity of the hepatitis C virus serine protease NS3.

4 September 2018

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4 September 2018

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4 September 2018

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4 September 2018

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4 September 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/14694101

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1128/JVI.78.2.700-709.2004

1 reference

17 August 2017

1 reference

17 August 2017

1 reference