HIV-1 Vif-mediated ubiquitination/degradation of APOBEC3G involves four critical lysine residues in its C-terminal domain.
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HIV-1 Vif versus the APOBEC3 cytidine deaminases: an intracellular duel between pathogen and host restriction factorsHIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchStructural Insights into HIV-1 Vif-APOBEC3F InteractionLentiviral Vif degrades the APOBEC3Z3/APOBEC3H protein of its mammalian host and is capable of cross-species activity.HIV-1 Vpr redirects host ubiquitination pathway.HIV-1 Vpr loads uracil DNA glycosylase-2 onto DCAF1, a substrate recognition subunit of a cullin 4A-ring E3 ubiquitin ligase for proteasome-dependent degradation.N-terminal hemagglutinin tag renders lysine-deficient APOBEC3G resistant to HIV-1 Vif-induced degradation by reduced polyubiquitination.Random mutagenesis MAPPIT analysis identifies binding sites for Vif and Gag in both cytidine deaminase domains of Apobec3G.Role of HIV-1 nucleocapsid protein in HIV-1 reverse transcription.Multifaceted counter-APOBEC3G mechanisms employed by HIV-1 Vif.The role of amino-terminal sequences in cellular localization and antiviral activity of APOBEC3B.Structural Features of Antiviral APOBEC3 Proteins are Linked to Their Functional Activities.Genetic and functional characterization of HIV-1 Vif on APOBEC3G degradation: First report of emergence of B/C recombinants from North India.Identification of the HIV-1 Vif and Human APOBEC3G Protein Interface.HIV-1 Adapts To Replicate in Cells Expressing Common Marmoset APOBEC3G and BST2Host restriction factors in retroviral infection: promises in virus-host interaction.HIV-1 viral infectivity factor (Vif) alters processive single-stranded DNA scanning of the retroviral restriction factor APOBEC3GDispersed sites of HIV Vif-dependent polyubiquitination in the DNA deaminase APOBEC3F.Vif proteins from diverse primate lentiviral lineages use the same binding site in APOBEC3GViral takeover of the host ubiquitin system.HIV-1, ubiquitin and ubiquitin-like proteins: the dialectic interactions of a virus with a sophisticated network of post-translational modifications.A Comparison of Two Single-Stranded DNA Binding Models by Mutational Analysis of APOBEC3G.HIV-1 Vif: a guardian of the virus that opens up a new era in the research field of restriction factorsDifferential Contributions of Ubiquitin-Modified APOBEC3G Lysine Residues to HIV-1 Vif-Induced DegradationPolyubiquitination of APOBEC3G is essential for its degradation by HIV-1 Vif.Towards Inhibition of Vif-APOBEC3G Interaction: Which Protein to Target?Importance of the proline-rich multimerization domain on the oligomerization and nucleic acid binding properties of HIV-1 VifMoloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G through interference with the Vif-mediated ubiquitin-proteasome pathway.Multiple Inhibitory Factors Act in the Late Phase of HIV-1 Replication: a Systematic Review of the Literature.Viral subversion of APOBEC3s: Lessons for anti-tumor immunity and tumor immunotherapy.
P2860
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P2860
HIV-1 Vif-mediated ubiquitination/degradation of APOBEC3G involves four critical lysine residues in its C-terminal domain.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
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2009年學術文章
@zh-hant
name
HIV-1 Vif-mediated ubiquitinat ...... dues in its C-terminal domain.
@en
HIV-1 Vif-mediated ubiquitinat ...... dues in its C-terminal domain.
@nl
type
label
HIV-1 Vif-mediated ubiquitinat ...... dues in its C-terminal domain.
@en
HIV-1 Vif-mediated ubiquitinat ...... dues in its C-terminal domain.
@nl
prefLabel
HIV-1 Vif-mediated ubiquitinat ...... dues in its C-terminal domain.
@en
HIV-1 Vif-mediated ubiquitinat ...... dues in its C-terminal domain.
@nl
P2093
P2860
P356
P1476
HIV-1 Vif-mediated ubiquitinat ...... dues in its C-terminal domain.
@en
P2093
Denise S B Chan
Hiroaki Yoshii
Judith G Levin
Junko Shibata
Naoki Yamamoto
Wataru Sugiura
P2860
P304
19539-19544
P356
10.1073/PNAS.0906652106
P407
P577
2009-11-03T00:00:00Z