Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Phosphorylation of APOBEC3G by protein kinase A regulates its interaction with HIV-1 Vif.

Nature structural & molecular biology - 1 Nov 2008

Shirakawa Kotaro, Takaori-Kondo Akifumi, Yokoyama Masaru, Izumi Taisuke, Matsui Masashi, Io Katsuhiro, Sato Toshihiro, Sato Hironori, Uchiyama Takashi

Abstract excerpt

Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G (APOBEC3G, referred to here as A3G) is a potent antiretroviral host factor against human immunodeficiency virus type 1 (HIV-1). HIV-1 viral infectivity factor (Vif) counteracts A3G by promoting its degradation via the ubiquitin-proteasome pathway. Recent studies demonstrated that protein kinase A (PKA) phosphorylates activation-induced deaminase...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to APOBEC-3G Deaminase
Share to Arginine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cyclic AMP-Dependent Protein Kinases

Share to Cytidine Deaminase

Share to Gene Products, vif

Share to Recombinant Fusion Proteins

Share to Threonine

Share to Virion

Source

Identifiers

PMID: 18836454
DOI: 10.1038/nsmb.1497

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Phosphorylation of APOBEC3G by protein kinase A regulates its interaction with HIV-1 Vif.PMID 18836454Read ↗

Structural perspectives on HIV‐1 Vif and APOBEC3 restriction factor interactionsSemantic proximity Read ↗

Structural Features of Antiviral APOBEC3 Proteins are Linked to Their Functional ActivitiesSemantic proximity Read ↗

Various strategies for developing APOBEC3G protectors to circumvent human immunodeficiency virus type 1.Semantic proximity Read ↗

Functional and Structural Insights into a Vif/PPP2R5 Complex Elucidated Using Patient HIV-1 Isolates and Computational Modeling.Semantic proximity Read ↗

Human Immunodeficiency Virus Type 1 Replication and Regulation of APOBEC3G by Peptidyl Prolyl Isomerase Pin1Semantic proximity Read ↗

A Hepatitis C Virus NS5A Phosphorylation Site That Regulates RNA ReplicationSemantic proximity Read ↗

Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction.Semantic proximity Read ↗

Multifaceted HIV‐1 Vif interactions with human E3 ubiquitin ligase and APOBEC3sSemantic proximity Read ↗

GANP interacts with APOBEC3G and facilitates its encapsidation into the virions to reduce HIV-1 infectivity.Semantic proximity Read ↗

Identification of small molecule compounds targeting the interaction of HIV-1 Vif and human APOBEC3G by virtual screening and biological evaluationSemantic proximity Read ↗

Identification of specific determinants of human APOBEC3F, APOBEC3C, and APOBEC3DE and African green monkey APOBEC3F that interact with HIV-1 Vif.Semantic proximity Read ↗

FAM122A ensures cell cycle interphase progression and checkpoint control by inhibiting B55α/PP2A through helical motifsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.