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Article

The activity of topoisomerase I is modulated by large T antigen during unwinding of the SV40 origin.

The Journal of biological chemistry - 7 Aug 1998

Simmons D T, Roy R, Chen L, Gai D, Trowbridge P W

Abstract excerpt

When simian virus 40 (SV40) large T antigen binds to the virus origin of replication, it forms a double hexamer that functions as a helicase to unwind the DNA bidirectionally. We demonstrate in this report that T antigen can unwind and release an origin DNA single strand of less than full length in the presence of purified human topoisomerase I. The sites nicked by topoisomerase I in the strands released by T...

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

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Source

Identifiers

PMID: 9685392
DOI: 10.1074/jbc.273.32.20390

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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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The activity of topoisomerase I is modulated by large T antigen during unwinding of the SV40 origin.PMID 9685392Read ↗

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