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dc.contributor.authorSolbak, Sara M
dc.contributor.authorReksten, Tove R
dc.contributor.authorWray, Victor
dc.contributor.authorBruns, Karsten
dc.contributor.authorHorvli, Ole
dc.contributor.authorRaae, Arnt J
dc.contributor.authorHenklein, Petra
dc.contributor.authorHenklein, Peter
dc.contributor.authorRöder, Rene
dc.contributor.authorMitzner, David
dc.contributor.authorSchubert, Ulrich
dc.contributor.authorFossen, Torgils
dc.date.accessioned2011-03-09T10:13:45Z
dc.date.available2011-03-09T10:13:45Z
dc.date.issued2010
dc.identifier.citationThe intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding. 2010, 10:31 BMC Struct. Biol.en
dc.identifier.issn1472-6807
dc.identifier.pmid20920334
dc.identifier.doi10.1186/1472-6807-10-31
dc.identifier.urihttp://hdl.handle.net/10033/124027
dc.description.abstractCyclophilin A (CypA) represents a potential target for antiretroviral therapy since inhibition of CypA suppresses human immunodeficiency virus type 1 (HIV-1) replication, although the mechanism through which CypA modulates HIV-1 infectivity still remains unclear. The interaction of HIV-1 viral protein R (Vpr) with the human peptidyl prolyl isomerase CypA is known to occur in vitro and in vivo. However, the nature of the interaction of CypA with Pro-35 of N-terminal Vpr has remained undefined.
dc.language.isoenen
dc.subject.meshCyclophilin Aen
dc.subject.meshHumansen
dc.subject.meshKineticsen
dc.subject.meshNuclear Magnetic Resonance, Biomolecularen
dc.subject.meshPeptidylprolyl Isomeraseen
dc.subject.meshProlineen
dc.subject.meshProtein Bindingen
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionizationen
dc.subject.meshSurface Plasmon Resonanceen
dc.subject.meshVirus Replicationen
dc.subject.meshvpr Gene Products, Human Immunodeficiency Virusen
dc.titleThe intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding.en
dc.typeArticleen
dc.contributor.departmentDepartment of Chemistry, University of Bergen, N-5007 Bergen, Norway.en
dc.identifier.journalBMC structural biologyen
refterms.dateFOA2018-06-12T22:46:27Z
html.description.abstractCyclophilin A (CypA) represents a potential target for antiretroviral therapy since inhibition of CypA suppresses human immunodeficiency virus type 1 (HIV-1) replication, although the mechanism through which CypA modulates HIV-1 infectivity still remains unclear. The interaction of HIV-1 viral protein R (Vpr) with the human peptidyl prolyl isomerase CypA is known to occur in vitro and in vivo. However, the nature of the interaction of CypA with Pro-35 of N-terminal Vpr has remained undefined.


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