ArticleNature communications2013
NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity.
Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 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
103 citing papers in PubMed, 135 citations in OpenAlex.
- Chemiluminescent Deoxyribozyme Sensors for DNA-Editing Enzymes.ACS chemical biology · 2026Article
- Two codes of RNA editing by deamination in human diseases.Experimental & molecular medicine · 2026Review
- Article
- Review
- Direct inhibition of human APOBEC3 deaminases by HIV-1 Vif independent of the proteolysis pathway.Biophysical journal · 2024Article
- Structure-guided inhibition of the cancer DNA-mutating enzyme APOBEC3A.Nature communications · 2023Article
- Dynamics of single-base editing: Theoretical analysis.The Journal of chemical physics · 2023Article
- APOBEC3A Catalytic Inactivity Mutation Induces Tertiary Structure Destabilization.ACS medicinal chemistry letters · 2023Article
- Ancestral reconstruction reveals catalytic inactivation of activation-induced cytidine deaminase concomitant with cold water adaption in the Gadiformes bony fish.BMC biology · 2022Article
- Structure-Guided Design of a Potent and Specific Inhibitor against the Genomic Mutator APOBEC3A.ACS chemical biology · 2022Article
- APOBEC3A regulates transcription from interferon-stimulated response elements.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The current toolbox for APOBEC drug discovery.Trends in pharmacological sciences · 2022Review
- Two different kinds of interaction modes of deaminase APOBEC3A with single-stranded DNA in solution detected by nuclear magnetic resonance.Protein science : a publication of the Protein Society · 2022Article
- The role of structural dynamics in the thermal adaptation of hyperthermophilic enzymes.Frontiers in molecular biosciences · 2022Article
- Meet the IUPAB councilor - Angela M. Gronenborn.Biophysical reviews · 2021Article
- A general theoretical framework to design base editors with reduced bystander effects.Nature communications · 2021Article
- Interaction with the CCT chaperonin complex limits APOBEC3A cytidine deaminase cytotoxicity.EMBO reports · 2021Article
- Structure-Based Design of First-Generation Small Molecule Inhibitors Targeting the Catalytic Pockets of AID, APOBEC3A, and APOBEC3B.ACS pharmacology & translational science · 2021Article
- Interactions of APOBEC3s with DNA and RNA.Current opinion in structural biology · 2021Review
- Review
43 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Human APOBEC3A is a single-stranded DNA cytidine deaminase that restricts viral pathogens and endogenous retrotransposons, and has a role in the innate immune response. Furthermore, its potential to act as a genomic DNA mutator has implications for a role in carcinogenesis. A deeper understanding of APOBEC3A's deaminase and nucleic acid-binding properties, which is central to its biological activities, has been limited by the lack of structural information. Here we report the nuclear magnetic resonance solution structure of APOBEC3A and show that the critical interface for interaction with single-stranded DNA substrates includes residues extending beyond the catalytic centre. Importantly, by monitoring deaminase activity in real time, we find that A3A displays similar catalytic activity on APOBEC3A-specific TTCA- or A3G-specific CCCA-containing substrates, involving key determinants immediately 5' of the reactive C. Our results afford novel mechanistic insights into APOBEC3A-mediated deamination and provide the structural basis for further molecular studies.
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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.