Mutation in the loop C-terminal to the cyclophilin A binding site of HIV-1 capsid protein disrupts proper virus assembly and infectivity
- 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
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online resource.
- Bibliographic citation
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Mutation in the loop C-terminal to the cyclophilin A binding site of HIV-1 capsid protein disrupts proper virus assembly and infectivity ; volume:4 ; number:1 ; day:19 ; month:3 ; year:2007 ; pages:1-8 ; date:12.2007
Retrovirology ; 4, Heft 1 (19.3.2007), 1-8, 12.2007
- Creator
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Abdurahman, Samir
- Contributor
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Höglund, Stefan
Höglund, Anders
Vahlne, Anders
SpringerLink (Online service)
- DOI
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10.1186/1742-4690-4-19
- URN
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urn:nbn:de:1111-201608071245
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:59 AM CEST
Data provider
This object is provided by:
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Abdurahman, Samir
- Höglund, Stefan
- Höglund, Anders
- Vahlne, Anders
- SpringerLink (Online service)
Other Objects (12)
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Functional analysis of the secondary HIV-1 capsid binding site in the host protein cyclophilin A
The highly polymorphic cyclophilin A-binding loop in HIV-1 capsid modulates viral resistance to MxB
Fast Magic‐Angle‐Spinning NMR Reveals the Evasive Hepatitis B Virus Capsid C‐Terminal Domain **
Fast magic‐angle‐spinning NMR reveals the evasive hepatitis B virus capsid C‐terminal domain**
Fast Magic‐Angle‐Spinning NMR Reveals the Evasive Hepatitis B Virus Capsid C‐Terminal Domain **
Stabilization of the β-hairpin in Mason-Pfizer monkey virus capsid protein- a critical step for infectivity
The infectivity of AAV9 is influenced by the specific location and extent of chemically modified capsid residues
Important roles of C-terminal residues in degradation of capsid protein of classical swine fever virus
Non‐Immunosuppressive Cyclophilin Inhibitors
Nicht‐immunsuppressive Cyclophilin‐Inhibitoren
Capsid and Infectivity in Virus Detection
Modulation of HIV-1 infectivity and cyclophilin A-dependence by Gag sequence and target cell type
Functional analysis of the secondary HIV-1 capsid binding site in the host protein cyclophilin A
The highly polymorphic cyclophilin A-binding loop in HIV-1 capsid modulates viral resistance to MxB
Fast Magic‐Angle‐Spinning NMR Reveals the Evasive Hepatitis B Virus Capsid C‐Terminal Domain **
Fast magic‐angle‐spinning NMR reveals the evasive hepatitis B virus capsid C‐terminal domain**
Fast Magic‐Angle‐Spinning NMR Reveals the Evasive Hepatitis B Virus Capsid C‐Terminal Domain **
Stabilization of the β-hairpin in Mason-Pfizer monkey virus capsid protein- a critical step for infectivity
The infectivity of AAV9 is influenced by the specific location and extent of chemically modified capsid residues
Important roles of C-terminal residues in degradation of capsid protein of classical swine fever virus
Non‐Immunosuppressive Cyclophilin Inhibitors
Nicht‐immunsuppressive Cyclophilin‐Inhibitoren
Capsid and Infectivity in Virus Detection
Modulation of HIV-1 infectivity and cyclophilin A-dependence by Gag sequence and target cell type
Functional analysis of the secondary HIV-1 capsid binding site in the host protein cyclophilin A
The highly polymorphic cyclophilin A-binding loop in HIV-1 capsid modulates viral resistance to MxB
Fast Magic‐Angle‐Spinning NMR Reveals the Evasive Hepatitis B Virus Capsid C‐Terminal Domain **
Fast magic‐angle‐spinning NMR reveals the evasive hepatitis B virus capsid C‐terminal domain**
Fast Magic‐Angle‐Spinning NMR Reveals the Evasive Hepatitis B Virus Capsid C‐Terminal Domain **
Stabilization of the β-hairpin in Mason-Pfizer monkey virus capsid protein- a critical step for infectivity
The infectivity of AAV9 is influenced by the specific location and extent of chemically modified capsid residues
Important roles of C-terminal residues in degradation of capsid protein of classical swine fever virus
Non‐Immunosuppressive Cyclophilin Inhibitors