ArticleFrontiers in microbiology2012
Antiviral Mechanism and Biochemical Basis of the Human APOBEC3 Family.
Article in Frontiers in microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed.
- Review
- Modeling Human Protein Physical Interactions Involved in HIV Attachment In Silico.International journal of molecular sciences · 2025Article
- Host response to Aplysia Abyssovirus 1 in nervous system and gill.Developmental and comparative immunology · 2024Article
- The role of RNA-modifying proteins in renal cell carcinoma.Cell death & disease · 2024Review
- The Drivers, Mechanisms, and Consequences of Genome Instability in HPV-Driven Cancers.Cancers · 2022Review
- Viruses with U-DNA: New Avenues for Biotechnology.Viruses · 2021Review
- The Essential Co-Option of Uracil-DNA Glycosylases by Herpesviruses Invites Novel Antiviral Design.Microorganisms · 2020Review
- Enterovirus 71 antagonizes the inhibition of the host intrinsic antiviral factor A3G.Nucleic acids research · 2018Article
- Molecular Interactions of a DNA Modifying Enzyme APOBEC3F Catalytic Domain with a Single-Stranded DNA.Journal of molecular biology · 2018Article
- APOBEC3G Regulation of the Evolutionary Race Between Adaptive Immunity and Viral Immune Escape Is Deeply Imprinted in the HIV Genome.Frontiers in immunology · 2018Article
- Nanoscale Characterization of Interaction of APOBEC3G with RNA.Biochemistry · 2017Article
- Nuclear Magnetic Resonance Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity.Biochemistry · 2016Article
- Inhibition of APOBEC3G activity impedes double-stranded DNA repair.The FEBS journal · 2016Article
- APOBEC3G Interacts with ssDNA by Two Modes: AFM Studies.Scientific reports · 2015Article
- APOBECs and virus restriction.Virology · 2015Review
- Sequence and structural determinants of human APOBEC3H deaminase and anti-HIV-1 activities.Retrovirology · 2015Article
- Endogenous CCL2 neutralization restricts HIV-1 replication in primary human macrophages by inhibiting viral DNA accumulation.Retrovirology · 2015Article
- APOBEC3G inhibits HIV-1 RNA elongation by inactivating the viral trans-activation response element.Journal of molecular biology · 2014Article
- Article
- Insight into the HIV-1 Vif SOCS-box-ElonginBC interaction.Open biology · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human APOBEC3 (A3) family (A, B, C, DE, F, G, and H) comprises host defense factors that potently inhibit the replication of diverse retroviruses, retrotransposons, and the other viral pathogens. HIV-1 has a counterstrategy that includes expressing the Vif protein to abrogate A3 antiviral function. Without Vif, A3 proteins, particularly APOBEC3G (A3G) and APOBEC3F (A3F), inhibit HIV-1 replication by blocking reverse transcription and/or integration and hypermutating nascent viral cDNA. The molecular mechanisms of this antiviral activity have been primarily attributed to two biochemical characteristics common to A3 proteins: catalyzing cytidine deamination in single-stranded DNA (ssDNA) and a nucleic acid-binding capability that is specific to ssDNA or ssRNA. Recent advances suggest that unique property of A3G dimer/oligomer formations, is also important for the modification of antiviral activity. In this review article we summarize how A3 proteins, particularly A3G, inhibit viral replication based on the biochemical and structural characteristics of the A3G protein.
Indexed as
Identifiers
What OpenQuestion holds
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.