ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2009
Post-translational regulation of activation-induced cytidine deaminase.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed.
- Activation-induced cytidine deaminase in tertiary lymphoid structures: dual roles and implications in cancer prognosis.Frontiers in oncology · 2025Review
- Diversity of Immunoglobulin (Ig) Isotypes and the Role of Activation-Induced Cytidine Deaminase (AID) in Fish.Molecular biotechnology · 2018Review
- Diversity in the Cow Ultralong CDR H3 Antibody Repertoire.Frontiers in immunology · 2018Review
- Cell Cycle Regulates Nuclear Stability of AID and Determines the Cellular Response to AID.PLoS genetics · 2015Article
- Article
- Functions and regulation of the APOBEC family of proteins.Seminars in cell & developmental biology · 2012Review
- APOBEC3 proteins and genomic stability: the high cost of a good defense.Cell cycle (Georgetown, Tex.) · 2012Article
- The current structural and functional understanding of APOBEC deaminases.Cellular and molecular life sciences : CMLS · 2009Review
- Regulation of activation-induced cytidine deaminase DNA deamination activity in B-cells by Ser38 phosphorylation.Biochemical Society transactions · 2009Article
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 assembled immunoglobulin genes in the B cells of mice and humans are altered by distinct processes known as class switch recombination (CSR) and somatic hypermutation, leading to diversification of the antibody repertoire. These two DNA modification processes are initiated by the B cell-specific protein factor activation-induced cytidine deaminase (AID). AID is post-translationally modified by phosphorylation at multiple sites, although functional significance during CSR has been implicated only for phosphorylation at serine-38 (S38). Although multiple laboratories have demonstrated that AID function is regulated via phosphorylation at S38, the precise biological role of S38 phosphorylation has been a topic of debate. Here, we discuss our interpretation of the significance of AID regulation via phosphorylation and also discuss how this form of AID regulation may have evolved in higher organisms.
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Registered trials
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