BI-2 destabilizes HIV-1 cores during infection and Prevents Binding of CPSF6 to the HIV-1 Capsid
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1742-4690
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
-
online resource.
- Bibliographic citation
-
BI-2 destabilizes HIV-1 cores during infection and Prevents Binding of CPSF6 to the HIV-1 Capsid ; volume:11 ; number:1 ; day:11 ; month:12 ; year:2014 ; pages:1-7 ; date:12.2014
Retrovirology ; 11, Heft 1 (11.12.2014), 1-7, 12.2014
- Creator
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Fricke, Thomas
- Contributor
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Buffone, Cindy
Opp, Silvana
Valle-Casuso, Jose
Diaz-Griffero, Felipe
SpringerLink (Online service)
- DOI
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10.1186/s12977-014-0120-x
- URN
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urn:nbn:de:1111-2016080732729
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:50 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Fricke, Thomas
- Buffone, Cindy
- Opp, Silvana
- Valle-Casuso, Jose
- Diaz-Griffero, Felipe
- SpringerLink (Online service)
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The HIV-1 capsid and reverse transcription
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The immature HIV-1 capsid and its assembly
Extreme genetic fragility of the HIV-1 capsid
Electrostatic repulsion regulates hiv-1 capsid hexamer plasticity and assembling capacities into core-like structures
The HIV capsid mimics karyopherin engagement of FG-nucleoporins
Passage of the HIV capsid cracks the nuclear pore
Highly conserved serine residue 40 in HIV-1 p6 regulates capsid processing and virus core assembly
Highly conserved serine residue 40 in HIV-1 p6 regulates capsid processing and virus core assembly
Rotten to the core: antivirals targeting the HIV-1 capsid core
Curvature Concentrations on the HIV-1 Capsid
The HIV-1 capsid and reverse transcription
MxB binds to the HIV-1 core and prevents the uncoating process of HIV-1
HIV-1 capsid variability: viral exploitation and evasion of capsid-binding molecules
The immature HIV-1 capsid and its assembly
Extreme genetic fragility of the HIV-1 capsid
Electrostatic repulsion regulates hiv-1 capsid hexamer plasticity and assembling capacities into core-like structures
The HIV capsid mimics karyopherin engagement of FG-nucleoporins
Passage of the HIV capsid cracks the nuclear pore
Highly conserved serine residue 40 in HIV-1 p6 regulates capsid processing and virus core assembly