ArticleNAR cancer2020
The structure of APOBEC1 and insights into its RNA and DNA substrate selectivity.
Article in NAR cancer, 2020. 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.
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.
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Who cites it
21 citing papers in PubMed, 27 citations in OpenAlex.
- Deciphering APOBEC1 in Avians: unravelling loss events and functional insights.Immunogenetics · 2026Article
- High-precision cytosine base editors by evolving nucleic-acid-recognition hotspots in deaminase.Nature biotechnology · 2026Article
- Two codes of RNA editing by deamination in human diseases.Experimental & molecular medicine · 2026Review
- Systematic characterization of the composition and dynamics of processing body-associated mRNAs.Nature communications · 2025Article
- Decoding RNA-Protein Interactions: Methodological Advances and Emerging Challenges.Advanced genetics (Hoboken, N.J.) · 2025Review
- Programmed RNA editing with an evolved bacterial adenosine deaminase.Nature chemical biology · 2024Article
- High-sensitivity in situ capture of endogenous RNA-protein interactions in fixed cells and primary tissues.Nature communications · 2024Article
- APOBEC2 safeguards skeletal muscle cell fate through binding chromatin and regulating transcription of non-muscle genes during myoblast differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Identification of RBM46 as a novel APOBEC1 cofactor for C-to-U RNA-editing activity.Journal of molecular biology · 2023Article
- Loss of SYNCRIP unleashes APOBEC-driven mutagenesis, tumor heterogeneity, and AR-targeted therapy resistance in prostate cancer.Cancer cell · 2023Article
- The Design and Application of DNA-Editing Enzymes as Base Editors.Annual review of biochemistry · 2023Review
- Lactobacillus for ribosome peptide editing cancer.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2023Review
- The roles of APOBEC-mediated RNA editing in SARS-CoV-2 mutations, replication and fitness.Scientific reports · 2022Article
- Functions and consequences of AID/APOBEC-mediated DNA and RNA deamination.Nature reviews. Genetics · 2022Review
- Enzymatic Characterization of In Vitro Activity of RNA Methyltransferase PCIF1 on DNA.Biochemistry · 2022Article
- The Roles of APOBEC-mediated RNA Editing in SARS-CoV-2 Mutations, Replication and Fitness.Research square · 2022Article
- The Roles of APOBEC-mediated RNA Editing in SARS-CoV-2 Mutations, Replication and Fitness.bioRxiv : the preprint server for biology · 2022Article
- Prognostic value, immune signature and molecular mechanisms of the APOBEC family members APOBEC1, APOBEC3A, APOBEC3G and APOBEC3H in pancreatic adenocarcinoma.Frontiers in molecular biosciences · 2022Article
- Human MettL3-MettL14 RNA adenine methyltransferase complex is active on double-stranded DNA containing lesions.Nucleic acids research · 2021Article
- Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
APOBEC1 (APO1), a member of AID/APOBEC nucleic acid cytosine deaminase family, can edit apolipoprotein B mRNA to regulate cholesterol metabolism. This APO1 RNA editing activity requires a cellular cofactor to achieve tight regulation. However, no cofactors are required for deamination on DNA by APO1 and other AID/APOBEC members, and aberrant deamination on genomic DNA by AID/APOBEC deaminases has been linked to cancer. Here, we present the crystal structure of APO1, which reveals a typical APOBEC deaminase core structure, plus a unique well-folded C-terminal domain that is highly hydrophobic. This APO1 C-terminal hydrophobic domain (A1HD) interacts to form a stable dimer mainly through hydrophobic interactions within the dimer interface to create a four-stranded β-sheet positively charged surface. Structure-guided mutagenesis within this and other regions of APO1 clarified the importance of the A1HD in directing RNA and cofactor interactions, providing insights into the structural basis of selectivity on DNA or RNA substrates.
Identifiers
What Socratic 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 Socratic graph.