The structural basis for deadenylation by the CCR4-NOT complex
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Drug Discovery,Biochemistry,Biotechnology
Link
http://link.springer.com/content/pdf/10.1007/s13238-010-0060-8.pdf
Reference60 articles.
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2. Albert, T.K., Hanzawa, H., Legtenberg, Y.I., de Ruwe, M.J., van den Heuvel, F.A., Collart, M.A., Boelens, R., and Timmers, H.T. (2002). Identification of a ubiquitin-protein ligase subunit within the CCR4-NOT transcription repressor complex. EMBO J 21, 355–364.
3. Andersen, K.R., Jonstrup, A.T., Van, L.B., and Brodersen, D.E. (2009). The activity and selectivity of fission yeast Pop2p are affected by a high affinity for Zn2+ and Mn2+ in the active site. RNA 15, 850–861.
4. Badarinarayana, V., Chiang, Y.C., and Denis, C.L. (2000). Functional interaction of CCR4-NOT proteins with TATAA-binding protein (TBP) and its associated factors in yeast. Genetics 155, 1045–1054.
5. Bai, Y., Salvadore, C., Chiang, Y.C., Collart, M.A., Liu, H.Y., and Denis, C.L. (1999). The CCR4 and CAF1 proteins of the CCR4-NOT complex are physically and functionally separated from NOT2, NOT4, and NOT5. Mol Cell Biol 19, 6642–6651.
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