ArticleBiochemical and biophysical research communications2006
APOBEC-1 and AID are nucleo-cytoplasmic trafficking proteins but APOBEC3G cannot traffic.
Article in Biochemical and biophysical research communications, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 30 citations in OpenAlex.
- Engineered deaminases as a key component of DNA and RNA editing tools.Molecular therapy. Nucleic acids · 2023Review
- Mechanism and regulation of secondary immunoglobulin diversification.Cell cycle (Georgetown, Tex.) · 2023Review
- Functions and consequences of AID/APOBEC-mediated DNA and RNA deamination.Nature reviews. Genetics · 2022Review
- Commentary on "Poor evidence for host-dependent regular RNA editing in the transcriptome of SARS-CoV-2".Journal of applied genetics · 2022Article
- MagnEdit-interacting factors that recruit DNA-editing enzymes to single base targets.Life science alliance · 2020Article
- Deciphering miRNAs' Action through miRNA Editing.International journal of molecular sciences · 2019Review
- Mouse APOBEC1 cytidine deaminase can induce somatic mutations in chromosomal DNA.BMC genomics · 2019Article
- A Rabbit Monoclonal Antibody against the Antiviral and Cancer Genomic DNA Mutating Enzyme APOBEC3B.Antibodies (Basel, Switzerland) · 2019Article
- Review
- Increased expression with differential subcellular location of cytidine deaminase APOBEC3G in human CD4(+) T-cell activation and dendritic cell maturation.Immunology and cell biology · 2016Article
- Consecutive interactions with HSP90 and eEF1A underlie a functional maturation and storage pathway of AID in the cytoplasm.The Journal of experimental medicine · 2015Article
- Sequence and structural determinants of human APOBEC3H deaminase and anti-HIV-1 activities.Retrovirology · 2015Article
- Endogenous APOBEC3A DNA cytosine deaminase is cytoplasmic and nongenotoxic.The Journal of biological chemistry · 2013Article
- Towards Inhibition of Vif-APOBEC3G Interaction: Which Protein to Target?Advances in virology · 2010Article
- AID upmutants isolated using a high-throughput screen highlight the immunity/cancer balance limiting DNA deaminase activity.Nature structural & molecular biology · 2009Article
- Two regions within the amino-terminal half of APOBEC3G cooperate to determine cytoplasmic localization.Journal of virology · 2008Article
- HIV-1 Vif, APOBEC, and intrinsic immunity.Retrovirology · 2008Review
- The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3G.Retrovirology · 2007Article
- T cells contain an RNase-insensitive inhibitor of APOBEC3G deaminase activity.PLoS pathogens · 2007Article
- C to U editing at position 32 of the anticodon loop precedes tRNA 5' leader removal in trypanosomatids.Nucleic acids research · 2007Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Human APOBEC3G (hA3G) is a member of the APOBEC-1 related protein (ARP) family of cytidine deaminases. hA3G functions as a natural defense against endogenous retrotransposons and a multitude of retroviruses, most notably human immunodeficiency virus type 1 (HIV-1). Nothing is known about the cellular function of hA3G, however, upon HIV-1 infection hA3G functions as an antiviral factor by mutating viral single-stranded DNA during reverse transcription. Whereas homologous deaminases such as APOBEC-1 and AID act on RNA and DNA, respectively, in the cell nucleus, hA3G mutagenic activity appears to be restricted to the cytoplasm. We demonstrate that hA3G is not a nucleo-cytoplasmic shuttling protein like APOBEC-1 and AID, but is strongly retained in the cytoplasm through a mechanism that involves both the N and C-terminal regions of the protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.