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Hasler, J., Rada, C., Neuberger, M. S. (2011) Cytoplasmic activation-induced cytidine deaminase (AID) exists in stoichiometric complex with translation elongation factor 1  (eEF1A) Proceedings of the National Academy of Sciences, 108 (45) 18366-18371 doi:10.1073/pnas.1106729108

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Reference TypeJournal (article/letter/editorial)
TitleCytoplasmic activation-induced cytidine deaminase (AID) exists in stoichiometric complex with translation elongation factor 1  (eEF1A)
JournalProceedings of the National Academy of Sciences
AuthorsHasler, J.Author
Rada, C.Author
Neuberger, M. S.Author
Year2011 (November 8)Volume108
Issue45
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.1106729108Search in ResearchGate
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Mindat Ref. ID1796667Long-form Identifiermindat:1:5:1796667:4
GUID0
Full ReferenceHasler, J., Rada, C., Neuberger, M. S. (2011) Cytoplasmic activation-induced cytidine deaminase (AID) exists in stoichiometric complex with translation elongation factor 1  (eEF1A) Proceedings of the National Academy of Sciences, 108 (45) 18366-18371 doi:10.1073/pnas.1106729108
Plain TextHasler, J., Rada, C., Neuberger, M. S. (2011) Cytoplasmic activation-induced cytidine deaminase (AID) exists in stoichiometric complex with translation elongation factor 1  (eEF1A) Proceedings of the National Academy of Sciences, 108 (45) 18366-18371 doi:10.1073/pnas.1106729108
In(2011, November) Proceedings of the National Academy of Sciences Vol. 108 (45) Proceedings of the National Academy of Sciences

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Han, L., Masani, S., Yu, K. (2011) Overlapping activation-induced cytidine deaminase hotspot motifs in Ig class-switch recombination. Proceedings of the National Academy of Sciences, 108 (28) 11584-11589 doi:10.1073/pnas.1018726108
Kobayashi, M., Sabouri, Z., Sabouri, S., Kitawaki, Y., Pommier, Y., Abe, T., Kiyonari, H., Honjo, T. (2011) Decrease in topoisomerase I is responsible for activation-induced cytidine deaminase (AID)-dependent somatic hypermutation. Proceedings of the National Academy of Sciences, 108 (48) 19305-19310 doi:10.1073/pnas.1114522108
Shen, H. M., Storb, U. (2004) Activation-induced cytidine deaminase (AID) can target both DNA strands when the DNA is supercoiled. Proceedings of the National Academy of Sciences, 101 (35) 12997-13002 doi:10.1073/pnas.0404974101
Meyers, G., Ng, Y.-S., Bannock, J. M., Lavoie, A., Walter, J. E., Notarangelo, L. D., Kilic, S. S., Aksu, G., Debre, M., Rieux-Laucat, F., Conley, M. E., Cunningham-Rundles, C., Durandy, A., Meffre, E. (2011) Activation-induced cytidine deaminase (AID) is required for B-cell tolerance in humans. Proceedings of the National Academy of Sciences, 108 (28) 11554-11559 doi:10.1073/pnas.1102600108
Kuraoka, M., Holl, T. M., Liao, D., Womble, M., Cain, D. W., Reynolds, A. E., Kelsoe, G. (2011) Activation-induced cytidine deaminase mediates central tolerance in B cells. Proceedings of the National Academy of Sciences, 108 (28) 11560-11565 doi:10.1073/pnas.1102571108
Gomez-Gonzalez, B., Aguilera, A. (2007) Activation-induced cytidine deaminase action is strongly stimulated by mutations of the THO complex. Proceedings of the National Academy of Sciences, 104 (20) 8409-8414 doi:10.1073/pnas.0702836104
Munoz, D. P., Lee, E. L., Takayama, S., Coppe, J.-P., Heo, S.-J., Boffelli, D., Di Noia, J. M., Martin, D. I. K. (2013) Activation-induced cytidine deaminase (AID) is necessary for the epithelial-mesenchymal transition in mammary epithelial cells. Proceedings of the National Academy of Sciences, 110 (32) doi:10.1073/pnas.1301021110
Kato, L., Begum, N. A., Burroughs, A. M., Doi, T., Kawai, J., Daub, C. O., Kawaguchi, T., Matsuda, F., Hayashizaki, Y., Honjo, T. (2012) Nonimmunoglobulin target loci of activation-induced cytidine deaminase (AID) share unique features with immunoglobulin genes. Proceedings of the National Academy of Sciences, 109 (7) 2479-2484 doi:10.1073/pnas.1120791109
Kotani, A., Kakazu, N., Tsuruyama, T., Okazaki, I.-m., Muramatsu, M., Kinoshita, K., Nagaoka, H., Yabe, D., Honjo, T. (2007) Activation-induced cytidine deaminase (AID) promotes B cell lymphomagenesis in Emu-cmyc transgenic mice. Proceedings of the National Academy of Sciences, 104 (5) 1616-1620 doi:10.1073/pnas.0610732104
Schrader, J. M., Chapman, S. J., Uhlenbeck, O. C. (2011) Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding. Proceedings of the National Academy of Sciences, 108 (13) 5215-5220 doi:10.1073/pnas.1102128108
Muto, T., Okazaki, I.-m., Yamada, S., Tanaka, Y., Kinoshita, K., Muramatsu, M., Nagaoka, H., Honjo, T. (2006) Negative regulation of activation-induced cytidine deaminase in B cells. Proceedings of the National Academy of Sciences, 103 (8) 2752-2757 doi:10.1073/pnas.0510970103
 
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