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Noh, Kyung-Min, Maze, Ian, Zhao, Dan, Xiang, Bin, Wenderski, Wendy, Lewis, Peter W., Shen, Li, Li, Haitao, Allis, C. David (2015) ATRX tolerates activity-dependent histone H3 methyl/phos switching to maintain repetitive element silencing in neurons. Proceedings of the National Academy of Sciences, 112 (22) 6820-6827 doi:10.1073/pnas.1411258112

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Reference TypeJournal (article/letter/editorial)
TitleATRX tolerates activity-dependent histone H3 methyl/phos switching to maintain repetitive element silencing in neurons
JournalProceedings of the National Academy of Sciences
AuthorsNoh, Kyung-MinAuthor
Maze, IanAuthor
Zhao, DanAuthor
Xiang, BinAuthor
Wenderski, WendyAuthor
Lewis, Peter W.Author
Shen, LiAuthor
Li, HaitaoAuthor
Allis, C. DavidAuthor
Year2015 (June 2)Volume112
Issue22
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.1411258112Search in ResearchGate
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Mindat Ref. ID1837340Long-form Identifiermindat:1:5:1837340:0
GUID0
Full ReferenceNoh, Kyung-Min, Maze, Ian, Zhao, Dan, Xiang, Bin, Wenderski, Wendy, Lewis, Peter W., Shen, Li, Li, Haitao, Allis, C. David (2015) ATRX tolerates activity-dependent histone H3 methyl/phos switching to maintain repetitive element silencing in neurons. Proceedings of the National Academy of Sciences, 112 (22) 6820-6827 doi:10.1073/pnas.1411258112
Plain TextNoh, Kyung-Min, Maze, Ian, Zhao, Dan, Xiang, Bin, Wenderski, Wendy, Lewis, Peter W., Shen, Li, Li, Haitao, Allis, C. David (2015) ATRX tolerates activity-dependent histone H3 methyl/phos switching to maintain repetitive element silencing in neurons. Proceedings of the National Academy of Sciences, 112 (22) 6820-6827 doi:10.1073/pnas.1411258112
In(2015, June) Proceedings of the National Academy of Sciences Vol. 112 (22) Proceedings of the National Academy of Sciences

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(2018) Correction for Noh et al., ATRX tolerates activity-dependent histone H3 methyl/phos switching to maintain repetitive element silencing in neurons. Proceedings of the National Academy of Sciences, 115 (6) doi:10.1073/pnas.1800522115
Lewis, P. W., Elsaesser, S. J., Noh, K.-M., Stadler, S. C., Allis, C. D. (2010) Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. Proceedings of the National Academy of Sciences, 107 (32) 14075-14080 doi:10.1073/pnas.1008850107
Elsässer, Simon J., Noh, Kyung-Min, Diaz, Nichole, Allis, C. David, Banaszynski, Laura A. (2015) Histone H3.3 is required for endogenous retroviral element silencing in embryonic stem cells. Nature, 522 (7555). 240-244 doi:10.1038/nature14345
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Hake, S. B., Allis, C. D. (2006) Histone H3 variants and their potential role in indexing mammalian genomes: The "H3 barcode hypothesis". Proceedings of the National Academy of Sciences, 103 (17) 6428-6435 doi:10.1073/pnas.0600803103
Allis, C. D., Glover, C. V., Gorovsky, M. A. (1979) Micronuclei of Tetrahymena contain two types of histone H3. Proceedings of the National Academy of Sciences, 76 (10) 4857-4861 doi:10.1073/pnas.76.10.4857
Wang, Li, Greaves, Ian K., Groszmann, Michael, Wu, Li Min, Dennis, Elizabeth S., Peacock, W. James (2015) Hybrid mimics and hybrid vigor in Arabidopsis. Proceedings of the National Academy of Sciences, 112 (35) doi:10.1073/pnas.1514190112
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Bernardes, Natália Elisa, Fung, Ho Yee Joyce, Li, Yang, Chen, Zhe, Chook, Yuh Min (2022) Structure of IMPORTIN-4 bound to the H3–H4–ASF1 histone–histone chaperone complex. Proceedings of the National Academy of Sciences, 119 (38) doi:10.1073/pnas.2207177119
Lukasak, Bradley J., Mitchener, Michelle M., Kong, Lingchun, Dul, Barbara E., Lazarus, Cole D., Ramakrishnan, Aarthi, Ni, Jizhi, Shen, Li, Maze, Ian, Muir, Tom W. (2022) TGM2-mediated histone transglutamination is dictated by steric accessibility. Proceedings of the National Academy of Sciences, 119 (43) doi:10.1073/pnas.2208672119
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