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Longerich, S., Basu, U., Alt, F. & Storb, U. AID in somatic hypermutation and class switch recombination. Curr Opin Immunol 18, 164–74 (2006).
Rogerson, B. Mapping the upstream boundary of somatic mutations in rearranged immunoglobulin transgenes and endogenous genes. Mol. Immunol. 31, 83–98 (1994).
Wu, P. & Claflin, L. Promoter-associated displacement of hypermutations. Internatl. Immunol. 10, 1131–1138 (1998).
Motoyama, N., Miwa, T., Suzuki, Y., Okada, H. & Azuma, T. Comparison of somatic mutation frequency among immunoglobulin genes. J. Exp. Med. 179, 395–403 (1994).
Lebecque, S. & Gearhart, P. Boundaries of somatic mutation in rearranged immunoglobulin genes: 5’ boundary is near the promoter, and 3’ boundary is ~ 1kb from V(D)J gene. J. Exp. Med. 172, 1717–1727 (1990).
Rada, C., Gonzalez-Fernandez, A., Jarvis, J. M. & Milstein, C. The 5’ boundary of somatic hypermutation in a Vk gene is in the leader intron. Eur. J. immunol. 24, 1453–1457 (1994).
Longerich, S., Tanaka, A., Bozek, G. & Storb, U. The very 5’ end and the constant region of Ig genes are spared from somatic mutation because AID does not access these regions. J. Exp. Med. 202, 1443–1454 (2005).
Chaudhuri, J., Khuong, C. & Alt, F. W. Replication protein A interacts with AID to promote deamination of somatic hypermutation targets. Nature 430, 992–998 (2004).
Peters, A. & Storb, U. Somatic hypermutation of immunoglobulin genes is linked to transcription initiation. Immunity 4, 57–65 (1996).
Rada, C. & Milstein, C. The intrinsic hypermutability of antibody heavy and light chain genes decays exponentially. EMBO J. 20, 4570–4576 (2001).
Motoyama, N., Okada, H. & Azuma, T. Somatic mutation in constant region of mouse 1 light chains. Proc. Natl. Acad. Sci. USA 88, 7933–7937 (1991).
Storb, U. et al. Physical linkage of mouse λ genes by pulsed -field gel electrophoresis suggests that the rearrangement process favors proximate target sequences. Mol.Cell.Biol. 9, 711–718 (1989).
Bransteitter, R., Pham, P., Scharff, M. & Goodman, M. Activation-induced cytidine deminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase. Proc. Natl. Acad. Sci. USA 100, 4102–4107 (2003).
Dickerson, S., Market, E., Besmer, E. & Papavasiliou, F. N. AID mediates hypermutation by deaminating single stranded DNA. J. Exp. Med. 197, 1291–1296 (2003).
Pham, P., Bransteitter, R., Petruska, J. & Goodman, M. Processive AID-catalysed cytosine deamination on single-stranded DNA simulates somatic hypermutation. Nature 424, 103–107 (2003).
Bransteitter, R., Pham, P., Calabrese, P. & Goodman, M. F. Biochemical analysis of hypermutational targeting by wild type and mutant activation-induced cytidine deaminase. J. Biol. Chem. 279, 51612–51621 (2004).
Chaudhuri, J. et al. Transcription-targeted DNA deamination by the AID antibody diversification enzyme. Nature 421, 726–730 (2003).
Sohail, A., Klapacz, J., Samaranayake, M., Ullah, A. & Bhagwat, A. Human activation-induced cytidine deaminase causes transcription-dependent, strand-biased C to U deaminations. Nuc. Acids Res. 31, 2990–2994 (2003).
Shen, H. & Storb, U. Activation-induced cytidine deaminase (AID) can target both DNA strands when the DNA is supercoiled. Proc. Natl. Acad. Sci. 101, 12997–13002 (2004).
Shen, H., S., R. & U., S. Targeting of the activation-induced cytosine deaminase is strongly influenced by the sequence and structure of the targeted DNA. Mol. Cell. Biol. 25, 10815–10821 (2005).
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Storb, U. et al. (2007). Targeting of AID to Immunoglobulin Genes. In: Gupta, S., Alt, F., Cooper, M., Melchers, F., Rajewsky, K. (eds) Mechanisms of Lymphocyte Activation and Immune Regulation XI. Advances in Experimental Medicine and Biology, vol 596. Springer, Boston, MA. https://doi.org/10.1007/0-387-46530-8_8
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DOI: https://doi.org/10.1007/0-387-46530-8_8
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