An N-terminal domain helical motif of Prototype Foamy Virus Gag with dual functions essential for particle egress and viral infectivity
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1742-4690
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Anmerkungen
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online resource.
- Erschienen in
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An N-terminal domain helical motif of Prototype Foamy Virus Gag with dual functions essential for particle egress and viral infectivity ; volume:10 ; number:1 ; day:25 ; month:4 ; year:2013 ; pages:1-14 ; date:12.2013
Retrovirology ; 10, Heft 1 (25.4.2013), 1-14, 12.2013
- Urheber
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Reh, Juliane
- Beteiligte Personen und Organisationen
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Stange, Annett
Götz, Anne
Rönitz, Marlene
Große, Arend
Lindemann, Dirk
SpringerLink (Online service)
- DOI
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10.1186/1742-4690-10-45
- URN
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urn:nbn:de:1111-2016080729560
- Rechteinformation
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:49 MESZ
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Beteiligte
- Reh, Juliane
- Stange, Annett
- Götz, Anne
- Rönitz, Marlene
- Große, Arend
- Lindemann, Dirk
- SpringerLink (Online service)
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A purine-rich element in foamy virus pol regulates env splicing and gag/pol expression
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Mutagenesis of N-terminal residues of feline foamy virus Gag reveals entirely distinct functions during capsid formation, particle assembly, Gag processing and budding
Nuclear Localization of Foamy Virus Gag Precursor Protein
Reactivity of primate sera to foamy virus Gag and Bet proteins
Molecular mechanisms by which HERV-K Gag interferes with HIV-1 Gag assembly and particle infectivity
Prototype foamy virus gag nuclear localization and glycine-arginine box functions revised
Orthoretroviral-like prototype foamy virus gag-pol expression is compatible with viral replication
Novel prototype foamy virus Gag interactions with lost cell kinases important for virus entry
Determination of the relative amounts of Gag and Pol proteins in foamy virus particles
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Gags Gags Gags
A purine-rich element in foamy virus pol regulates env splicing and gag/pol expression
An N-terminal domain helical motif of Prototype Foamy Virus Gag with dual functions essential for particle egress and viral infectivity
Mutagenesis of N-terminal residues of feline foamy virus Gag reveals entirely distinct functions during capsid formation, particle assembly, Gag processing and budding
Nuclear Localization of Foamy Virus Gag Precursor Protein
Reactivity of primate sera to foamy virus Gag and Bet proteins
Molecular mechanisms by which HERV-K Gag interferes with HIV-1 Gag assembly and particle infectivity
Prototype foamy virus gag nuclear localization and glycine-arginine box functions revised
Orthoretroviral-like prototype foamy virus gag-pol expression is compatible with viral replication
Novel prototype foamy virus Gag interactions with lost cell kinases important for virus entry
Determination of the relative amounts of Gag and Pol proteins in foamy virus particles
N-terminal foamy virus Gag domains and individual residues are critical for capsid assembly and interaction with the unique Env leader protein Elp for Env-dependent budding
Gags Gags Gags