Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif. (Q40306250)

19 September 2017

Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif. (English)

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19 September 2017

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Zuoxiang Xiao

1

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19 September 2017

Elana Ehrlich

2

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19 September 2017

Yunkai Yu

3

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19 September 2017

Kun Luo

4

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19 September 2017

Tao Wang

5

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19 September 2017

Chunjuan Tian

6

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19 September 2017

Xiao-Fang Yu

7

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19 September 2017

language of work or name

English

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publication date

13 March 2006

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19 September 2017

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19 September 2017

349

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19 September 2017

2

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19 September 2017

290-299

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Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM.

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Hypermutation of HIV-1 DNA in the Absence of the Vif Protein

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APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo

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Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase

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Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G.

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HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation

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Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation

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Recent insights into HIV-1 Vif.

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Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity

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G to A hypermutation of hepatitis B virus.

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Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family.

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Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/J.VIROL.2006.02.002

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19 September 2017

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