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Cited by 897

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification

Petersen-Mahrt, Svend K., Harris, Reuben S., Neuberger, Michael S.·2002·Nature
DOI 10.1038/nature00862
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Research works printed but not linked: 28

  1. Muramatsu, M. et al. Specific expression of activation-induced cytidine deaminase (AID), a novel member of the RNA-editing deaminase family in germinal center B cells. J. Biol. Chem. 274, 18470–18476 (1999) · DOI · Paper page
  2. Muramatsu, M. et al. Class switch recombination and hypermutation require activation-induced cytidine deaminase (AID), a potential RNA editing enzyme. Cell 102, 553–563 (2000) · DOI · Paper page
  3. Revy, P. et al. Activation-induced cytidine deaminase (AID) deficiency causes the autosomal recessive form of the Hyper-IgM syndrome (HIGM2). Cell 102, 565–575 (2000) · DOI · Paper page
  4. Arakawa, H., Hauschild, J. & Buerstedde, J. M. Requirement of the Activation-Induced Deaminase (AID) gene for immunoglobulin gene conversion. Science 295, 1301–1306 (2002) · DOI · Paper page
  5. Harris, R. S., Sale, J. E., Petersen-Mahrt, S. K. & Neuberger, M. S. AID is essential for immunoglobulin V gene conversion in a cultured B cell line. Curr. Biol. 12, 435–438 (2002) · DOI
  6. Martin, A. et al. Activation-induced cytidine deaminase turns on somatic hypermutation in hybridomas. Nature 415, 802–806 (2002) · DOI · Paper page
  7. Okazaki, I., Kinoshita, K., Muramatsu, M., Yoshikawa, K. & Honjo, T. The AID enzyme induces class switch recombination in fibroblasts. Nature 416, 340–345 (2002) · DOI · Paper page
  8. Maizels, N. Somatic hypermutation: how many mechanisms diversify V region sequences? Cell 83, 9–12 (1995) · DOI
  9. Weill, J. C. & Reynaud, C. A. Rearrangement/hypermutation/gene conversion: when, where and why? Immunol. Today 17, 92–97 (1996) · DOI
  10. Sale, J. E., Calandrini, D. M., Takata, M., Takeda, S. & Neuberger, M. S. Ablation of XRCC2/3 transforms immunoglobulin V gene conversion into somatic hypermutation. Nature 412, 921–926 (2001) · DOI · Paper page
  11. Ehrenstein, M. R. & Neuberger, M. S. Deficiency in Msh2 affects the efficiency and local sequence specificity of immunoglobulin class-switch recombination: parallels with somatic hypermutation. EMBO J. 18, 3484–3490 (1999) · DOI · Paper page
  12. Rada, C., Ehrenstein, M. R., Neuberger, M. S. & Milstein, C. Hot spot focusing of somatic hypermutation in MSH2-deficient mice suggests two stages of mutational targeting. Immunity 9, 135–141 (1998) · DOI · Paper page
  13. Wiesendanger, M., Kneitz, B., Edelmann, W. & Scharff, M. D. Somatic hypermutation in MutS homologue (MSH)3-, MSH6-, and MSH3/MSH6-deficient mice reveals a role for the MSH2–MSH6 heterodimer in modulating the base substitution pattern. J. Exp. Med. 191, 579–584 (2000) · DOI
  14. Lindahl, T. Suppression of spontaneous mutagenesis in human cells by DNA base excision-repair. Mutat. Res. 462, 129–135 (2000) · DOI · Paper page
  15. Sale, J. E. & Neuberger, M. S. TdT-accessible breaks are scattered over the immunoglobulin V domain in a constitutively hypermutating B cell line. Immunity 9, 859–869 (1998) · DOI · Paper page
  16. Manis, J. P., Tian, M. & Alt, F. W. Mechanism and control of class-switch recombination. Trends Immunol. 23, 31–39 (2002) · DOI · Paper page
  17. Petersen, S. et al. AID is required to initiate Nbs1/γ-H2AX focus formation and mutations at sites of class switching. Nature 414, 660–665 (2001) · DOI · Paper page
  18. Chen, X., Kinoshita, K. & Honjo, T. Variable deletion and duplication at recombination junction ends: implication for staggered double-strand cleavage in class-switch recombination. Proc. Natl Acad. Sci. USA 98, 13860–13865 (2001) · DOI
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  23. Betz, A. G. et al. Elements regulating somatic hypermutation of an immunoglobulin kappa gene: critical role for the intron enhancer/matrix attachment region. Cell 77, 239–248 (1994) · DOI · Paper page
  24. Jarmuz, A. et al. An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. Genomics 79, 285–296 (2002) · DOI · Paper page
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  26. Navaratnam, N. et al. Escherichia coli cytidine deaminase provides a molecular model for ApoB RNA editing and a mechanism for RNA substrate recognition. J. Mol. Biol. 275, 695–714 (1998) · DOI
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Metadata

Authors
Petersen-Mahrt, S. K., Harris, R. S., & Neuberger, M. S.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2002-07
Volume
418
Issue
6893
Pages
99-104
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
DOI
10.1038/nature00862
OpenAlex
W2150010396
Cited by
897
References
2
FWCI
28.83
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)

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CoChat. (2026). Citation check: AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification. https://app.cochat.ai/papers/10.1038/nature00862
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Petersen-Mahrt, S. K., Harris, R. S., & Neuberger, M. S. (2002). AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification. Nature. https://doi.org/10.1038/nature00862

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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