Associated Papers
Insights on SNPs of Human Activation-Induced Cytidine Deaminase AID.
Koveshnikova EA et al.
International Journal of Molecular Sciences, 2025
Clinical implications of experimental analyses of AID function on predictive computational tools: Challenge of missense variants.
Abolhassani H et al.
Clinical Genetics, 2020
AID and Apobec3G haphazard deamination and mutational diversity.
Jaszczur M et al.
Cellular and Molecular Life Sciences : Cmls, 2013
A structural basis for the biochemical behavior of activation-induced deoxycytidine deaminase class-switch recombination-defective hyper-IgM-2 mutants.
Mu Y et al.
The Journal of Biological Chemistry, 2012
Novel mutation of the activation-induced cytidine deaminase gene in a Tajik family: special review on hyper-immunoglobulin M syndrome.
Mahdaviani SA et al.
Expert Review of Clinical Immunology, 2012
Inherited defects of immunoglobulin class switch recombination.
Kracker S et al.
Advances in Experimental Medicine and Biology, 2010
Genome-wide analysis to predict protein sequence variations that change phosphorylation sites or their corresponding kinases.
Ryu GM et al.
Nucleic Acids Research, 2009
19139070 (PubMed )
Supplement: gkn1008_nar-01723-s-2008-File009.xls › TypeII_
Activation-induced cytidine deaminase: structure-function relationship as based on the study of mutants.
Durandy A et al.
Human Mutation, 2006
AID mutant analyses indicate requirement for class-switch-specific cofactors.
Ta VT et al.
Nature Immunology, 2003
Activation-induced cytidine deaminase (AID) deficiency causes the autosomal recessive form of the Hyper-IgM syndrome (HIGM2).
Revy P et al.
Cell, 2000
Select a paper to view details