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References from Biochemical analysis of APOBEC3A-induced mutational signatures and clustered mutagenesis. Local targets link to admitted publications; unresolved targets remain external evidence.
APOBEC-Induced Mutagenesis in Cancer
10.1146/annurev-genet-072920-035840 · 2022 · External reference
Functions and consequences of AID/APOBEC-mediated DNA and RNA deamination
10.1038/s41576-022-00459-8 · 2022 · External reference
Mutational processes molding the genomes of 21 breast cancers
10.1016/j.cell.2012.04.024 · 2012 · External reference
Signatures of mutational processes in human cancer
10.1038/nature12477 · 2013 · External reference
An APOBEC cytidine deaminase mutagenesis pattern is widespread in human cancers
10.1038/ng.2702 · 2013 · External reference
Mechanisms of APOBEC3 mutagenesis in human cancer cells
10.1038/s41586-022-04972-y · 2022 · External reference
Mutational impact of APOBEC3A and APOBEC3B in a human cell line and comparisons to breast cancer
10.1371/journal.pgen.1011043 · 2023 · External reference
An APOBEC3A hypermutation signature is distinguishable from the signature of background mutagenesis by APOBEC3B in human cancers
10.1038/ng.3378 · 2015 · External reference
APOBEC3A and APOBEC3B Preferentially Deaminate the Lagging Strand Template during DNA Replication
10.1016/j.celrep.2016.01.021 · 2016 · External reference
APOBEC3A catalyzes mutation and drives carcinogenesis in vivo
10.1084/jem.20200261 · 2020 · External reference
Prospectively defined patterns of APOBEC3A mutagenesis are prevalent in human cancers
10.1016/j.celrep.2022.110555 · 2022 · External reference
Distinguishing preferences of human APOBEC3A and APOBEC3B for cytosines in hairpin loops, and reflection of these preferences in APOBEC-signature cancer genome mutations
10.1038/s41467-024-46231-w · 2024 · External reference
DNA deaminases induce break-associated mutation showers with implication of APOBEC3B and 3A in breast cancer kataegis
10.7554/elife.00534 · 2013 · External reference
Mutational Strand Asymmetries in Cancer Genomes Reveal Mechanisms of DNA Damage and Repair
10.1016/j.cell.2015.12.050 · 2016 · External reference
Strand-biased cytosine deamination at the replication fork causes cytosine to thymine mutations in Escherichia coli
10.1073/pnas.1522325113 · 2016 · External reference
APOBEC-induced mutations in human cancers are strongly enriched on the lagging DNA strand during replication
10.1101/gr.197046.115 · 2016 · External reference
Passenger hotspot mutations in cancer driven by APOBEC3A and mesoscale genomic features
10.1126/science.aaw2872 · 2019 · External reference
An extended APOBEC3A mutation signature in cancer
10.1038/s41467-021-21891-0 · 2021 · External reference
Structure-guided inhibition of the cancer DNA-mutating enzyme APOBEC3A
10.1038/s41467-023-42174-w · 2023 · External reference
APOBEC3A deaminates CTG hairpin loops to promote fragility and instability of expanded CAG/CTG repeats
10.1073/pnas.2408179122 · 2025 · External reference
Family-Wide Comparative Analysis of Cytidine and Methylcytidine Deamination by Eleven Human APOBEC Proteins
10.1016/j.jmb.2017.04.021 · 2017 · External reference
A DNA sequence recognition loop on APOBEC3A controls substrate specificity
10.1371/journal.pone.0097062 · 2014 · External reference
Biochemical reconstitution of UV-induced mutational processes
10.1093/nar/gkz335 · 2019 · External reference
Efficient base editing in methylated regions with a human APOBEC3A-Cas9 fusion
10.1038/nbt.4198 · 2018 · External reference
PCNA is efficiently loaded on the DNA recombination intermediate to modulate polymerase delta, eta, and zeta activities
10.1073/pnas.1222241110 · 2013 · External reference
NGS-based analysis of base-substitution signatures created by yeast DNA polymerase eta and zeta on undamaged and abasic DNA templates in vitro
10.1016/j.dnarep.2017.08.011 · 2017 · External reference
Biochemical analysis of H(2)O(2)-induced mutation spectra revealed that multiple damages were involved in the mutational process
2023 · External reference
Biochemical and photochemical mechanisms that produce different UV-induced mutation spectra
2021 · External reference
Unresolved reference
External reference
WebLogo: a sequence logo generator
10.1101/gr.849004 · 2004 · External reference
Deamination hotspots among APOBEC3 family members are defined by both target site sequence context and ssDNA secondary structure
10.1093/nar/gkz1164 · 2020 · External reference
Deoxycytidyl transferase activity of yeast REV1 protein
10.1038/382729a0 · 1996 · External reference
The human REV1 gene codes for a DNA template-dependent dCMP transferase
10.1093/nar/27.22.4468 · 1999 · External reference
Yeast Rev1 protein is a G template-specific DNA polymerase
10.1074/jbc.m112146200 · 2002 · External reference
Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions
10.1038/35023030 · 2000 · External reference
The choice of nucleotide inserted opposite abasic sites formed within chromosomal DNA reveals the polymerase activities participating in translesion DNA synthesis
10.1016/j.dnarep.2013.07.008 · 2013 · External reference
Distinct repair processes produce APOBEC-induced deletions, tandem substitutions, and complex mutations in yeast and human cells
10.1073/pnas.2609794123 · 2026 · External reference
APOBEC3G DNA deaminase acts processively 3′ --> 5′ on single-stranded DNA
10.1038/nsmb1086 · 2006 · External reference
Stochastic properties of processive cytidine DNA deaminases AID and APOBEC3G
10.1098/rstb.2008.0195 · 2009 · External reference
Molecular mechanism for regulating APOBEC3G DNA editing function by the non-catalytic domain
10.1038/s41467-024-52671-1 · 2024 · External reference
Hypermutation by intersegmental transfer of APOBEC3G cytidine deaminase
10.1038/nsmb.1495 · 2008 · External reference
AID and Apobec3G haphazard deamination and mutational diversity
10.1007/s00018-012-1212-1 · 2013 · External reference
Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G
10.1074/jbc.m110.107987 · 2010 · External reference
Single-Molecule Force Spectroscopy Studies of APOBEC3A-Single-Stranded DNA Complexes
10.1021/acs.biochem.6b00214 · 2016 · External reference
Replication protein A (RPA) hampers the processive action of APOBEC3G cytosine deaminase on single-stranded DNA
10.1371/journal.pone.0024848 · 2011 · External reference
Visualization of uracils created by APOBEC3A using UdgX shows colocalization with RPA at stalled replication forks
10.1093/nar/gkaa845 · 2020 · External reference