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Sci. Signal., 15 March 2011
Vol. 4, Issue 164, p. rs3
[DOI: 10.1126/scisignal.2001570]


Editor's Summary

Dynamics of the Stem Cell Phosphoproteome
Understanding the signaling events that control stem cell pluripotency and self-renewal and those governing differentiation should improve our ability to develop stem cell–based therapies. Rigbolt et al. performed global quantitative proteomic and phosphoproteomic analysis of human embryonic stem cells at five time points over 24 hours of nondirected (lineage-independent) differentiation initiated by two different paradigms. They identified a common core phosphoproteome associated with both differentiation protocols, discovered several temporal patterns of phosphorylation, and made predictions about changes in the activities of kinases during the differentiation period. DNA methyltransferases (DNMTs) exhibited dynamic changes in phosphorylation status that may influence their interaction with a promoter-bound protein complex, suggesting that the phosphorylation state of DNMTs may govern their recruitment to and thus silencing of target genes, such as those that promote pluripotency, during differentiation.

Citation: K. T. G. Rigbolt, T. A. Prokhorova, V. Akimov, J. Henningsen, P. T. Johansen, I. Kratchmarova, M. Kassem, M. Mann, J. V. Olsen, B. Blagoev, System-Wide Temporal Characterization of the Proteome and Phosphoproteome of Human Embryonic Stem Cell Differentiation. Sci. Signal. 4, rs3 (2011).

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   Abstract »    Full Text »    PDF »
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V. van Noort, J. Seebacher, S. Bader, S. Mohammed, I. Vonkova, M. J. Betts, S. Kuhner, R. Kumar, T. Maier, M. O'Flaherty, et al. (2014)
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P. Beltrao, P. Bork, N. J. Krogan, and V. van Noort (2014)
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   Abstract »    Full Text »    PDF »
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M. G. Fuzesi-Levi, G. Ben-Nissan, E. Bianchi, H. Zhou, M. J. Deery, K. S. Lilley, Y. Levin, and M. Sharon (2014)
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   Abstract »    Full Text »    PDF »
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W. Luu, E. J. Zerenturk, I. Kristiana, M. P. Bucknall, L. J. Sharpe, and A. J. Brown (2014)
J. Lipid Res. 55, 410-420
   Abstract »    Full Text »    PDF »
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M. Marcilla, A. Alpizar, M. Lombardia, A. Ramos-Fernandez, M. Ramos, and J. P. Albar (2014)
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   Abstract »    Full Text »    PDF »
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M. N. Melo-Braga, M. Schulz, Q. Liu, A. Swistowski, G. Palmisano, K. Engholm-Keller, L. Jakobsen, X. Zeng, and M. R. Larsen (2014)
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   Abstract »    Full Text »    PDF »
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Y. V. Miteva and I. M. Cristea (2014)
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   Abstract »    Full Text »    PDF »
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A. W. Schmid, B. Fauvet, M. Moniatte, and H. A. Lashuel (2013)
Mol. Cell. Proteomics 12, 3543-3558
   Abstract »    Full Text »    PDF »
Status of Large-scale Analysis of Post-translational Modifications by Mass Spectrometry.
J. V. Olsen and M. Mann (2013)
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   Abstract »    Full Text »    PDF »
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M. Ferron, C. Settembre, J. Shimazu, J. Lacombe, S. Kato, D. J. Rawlings, A. Ballabio, and G. Karsenty (2013)
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D. N. Simon, T. Domaradzki, W. A. Hofmann, and K. L. Wilson (2013)
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J. I. MacDonald and F. A. Dick (2013)
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S.-H. Chiou, B.-H. Jiang, Y.-L. Yu, S.-J. Chou, P.-H. Tsai, W.-C. Chang, L.-K. Chen, L.-H. Chen, Y. Chien, and G.-Y. Chiou (2013)
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C. Miller, I. Matic, K. C. Maier, B. Schwalb, S. Roether, K. Strasser, A. Tresch, M. Mann, and P. Cramer (2012)
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E. L. Rudashevskaya, J. Ye, O. N. Jensen, A. T. Fuglsang, and M. G. Palmgren (2012)
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