Mutations in AID and UNG extend the function of AID
- 1 October 2003
- journal article
- Published by Springer Nature in Nature Immunology
- Vol. 4 (10) , 945-946
- https://doi.org/10.1038/ni1003-945
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Human uracil–DNA glycosylase deficiency associated with profoundly impaired immunoglobulin class-switch recombinationNature Immunology, 2003
- AID mutant analyses indicate requirement for class-switch-specific cofactorsNature Immunology, 2003
- C-Terminal Deletion of AID Uncouples Class Switch Recombination from Somatic Hypermutation and Gene ConversionMolecular Cell, 2003
- Processive AID-catalysed cytosine deamination on single-stranded DNA simulates somatic hypermutationNature, 2003
- H2AX Is Required for Recombination Between Immunoglobulin Switch Regions but Not for Intra-Switch Region Recombination or Somatic HypermutationThe Journal of Experimental Medicine, 2003
- Mlh1 Can Function in Antibody Class Switch Recombination Independently of Msh2The Journal of Experimental Medicine, 2003
- Transcription-targeted DNA deamination by the AID antibody diversification enzymeNature, 2003
- Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNaseProceedings of the National Academy of Sciences, 2003
- Immunoglobulin Isotype Switching Is Inhibited and Somatic Hypermutation Perturbed in UNG-Deficient MiceCurrent Biology, 2002
- Deficiency in Msh2 affects the efficiency and local sequence specificity of immunoglobulin class-switch recombination: parallels with somatic hypermutationThe EMBO Journal, 1999