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Article

The host-pathogen interaction of human cyclophilin A and HIV-1 Vpr requires specific N-terminal and novel C-terminal domains.

BMC structural biology - 20 Dec 2011

Solbak Sara M Ø, Wray Victor, Horvli Ole, Raae Arnt J, Flydal Marte I, Henklein Petra, Henklein Peter, Nimtz Manfred, Schubert Ulrich, Fossen Torgils

Abstract excerpt

BACKGROUND: Cyclophilin A (CypA) represents a potential key molecule in future antiretroviral therapy since inhibition of CypA suppresses human immunodeficiency virus type 1 (HIV-1) replication. CypA interacts with the virus proteins Capsid (CA) and Vpr, however, the mechanism through which CypA influences HIV-1 infectivity still remains unclear. RESULTS: Here the interaction of full-length HIV-1 Vpr with the...

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Identifiers

PMID: 22185200
DOI: 10.1186/1472-6807-11-49
PMCID: PMC3269379

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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The host-pathogen interaction of human cyclophilin A and HIV-1 Vpr requires specific N-terminal and novel C-terminal domains.PMID 22185200Read ↗

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