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Article

New details of HCV NS3/4A proteinase functionality revealed by a high-throughput cleavage assay.

PloS one - 1 Jan 2012

Shiryaev Sergey A, Thomsen Elliot R, Cieplak Piotr, Chudin Eugene, Cheltsov Anton V, Chee Mark S, Kozlov Igor A, Strongin Alex Y

Abstract excerpt

BACKGROUND: The hepatitis C virus (HCV) genome encodes a long polyprotein, which is processed by host cell and viral proteases to the individual structural and non-structural (NS) proteins. HCV NS3/4A serine proteinase (NS3/4A) is a non-covalent heterodimer of the N-terminal, ∼180-residue portion of the 631-residue NS3 protein with the NS4A co-factor. NS3/4A cleaves the polyprotein sequence at four specific...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 22558217
DOI: 10.1371/journal.pone.0035759
PMCID: PMC3338790

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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