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The effect of dimerizing domains and basic residues on in vitro and in vivo assembly of Mason-Pfizer monkey virus and Human immunodeficiency virus

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    0342386 - ÚOCHB 2011 RIV US eng J - Journal Article
    Böhmová, Karolína - Hadravová, Romana - Štokrová, Jitka - Tůma, R. - Ruml, T. - Pichová, Iva - Rumlová, Michaela
    The effect of dimerizing domains and basic residues on in vitro and in vivo assembly of Mason-Pfizer monkey virus and Human immunodeficiency virus.
    Journal of Virology. Roč. 84, č. 4 (2010), s. 1977-1988. ISSN 0022-538X. E-ISSN 1098-5514
    R&D Projects: GA MŠMT 1M0508; GA ČR GA204/09/1388
    Grant - others:EUROCORES(XE) ERAS-CT-2003-980409
    Institutional research plan: CEZ:AV0Z40550506
    Keywords : Mason-Pfizer Monkey Virus * Human Immunodeficiency Virus * assembly * NC
    Subject RIV: CC - Organic Chemistry
    Impact factor: 5.189, year: 2010

    In the present work we focus on the contribution of NC to the oligomerization of CA leading to assembly of Mason-Pfizer monkey virus (M-PMV) and HIV-1. Analyzing in vitro assembly of substitution and deletion mutants of .delta.ProCANC we identified a “spacer-like” sequence (NC15) at the M-PMV NC N-terminus. This NC15 domain is indispensable for the assembly and cannot be substituted with oligomerization domains of GCN4 or CREB proteins.
    Permanent Link: http://hdl.handle.net/11104/0185134

     
     
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