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Article

Analysis of the VPg-proteinase (NIa) encoded by tobacco etch potyvirus: effects of mutations on subcellular transport, proteolytic processing, and genome amplification.

Journal of virology - 1 Oct 1996

Schaad M C, Haldeman-Cahill R, Cronin S, Carrington J C

Abstract excerpt

A mutational analysis was conducted to investigate the functions of the tobacco etch potyvirus VPg-proteinase (NIa) protein in vivo. The NIa N-terminal domain contains the VPg attachment site, whereas the C-terminal domain contains a picornavirus 3C-like proteinase. Cleavage at an internal site separating the two domains occurs in a subset of NIa molecules. The majority of NIa molecules in TEV-infected cells...

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Source

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Identifiers

PMID: 8794348
DOI: 10.1128/JVI.70.10.7039-7048.1996
PMCID: PMC190754

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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.

Related research

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Analysis of the VPg-proteinase (NIa) encoded by tobacco etch potyvirus: effects of mutations on subcellular transport, proteolytic processing, and genome amplification.PMID 8794348Read ↗

Evidence that the potyvirus P1 proteinase functions in trans as an accessory factor for genome amplification.Semantic proximity Read ↗

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Potyviral NIa proteinase, a proteinase with novel deoxyribonuclease activity.Semantic proximity Read ↗

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