Ankyrin for methylated lysines

Nature Structural and Molecular Biology

Volumn 15, Issue 3, 2008, Pages 221-222

  Brent, Michael M ^a   Marmorstein, Ronen ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID DERIVATIVE; ANKYRIN; CHAPERONE; CYTOSKELETON PROTEIN; DNA; GLUTAMIC ACID; HISTONE H3; LYSINE DERIVATIVE; METHYLAMMONIUM; METHYLTRANSFERASE; PEPTIDE; POLYPEPTIDE; TRYPTOPHAN; G9A HISTONE METHYLTRANSFERASE, MOUSE; HISTONE; HISTONE LYSINE METHYLTRANSFERASE; LYSINE; UNCLASSIFIED DRUG;

CHROMATIN; DISSOCIATION CONSTANT; DNA RECOMBINATION; DNA REPLICATION; DNA TRANSCRIPTION; FLUORESCENCE ANALYSIS; GENE MUTATION; METHYLATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; PROTEIN VARIANT; SHORT SURVEY; ANIMAL; CHEMISTRY; HUMAN; METABOLISM; MOUSE; NOTE;

ANIMALS; ANKYRIN REPEAT; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; LYSINE; METHYLATION; MICE;

EID: 40949126903     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb0308-221     Document Type: Short Survey

References (23)

1. Luger, K., Mader, A.W., Richmond, R.K., Sargent, D.F. & Richmond, T.J. Nature 389, 251-260 (1997).
2. De Koning, L., Corpet, A., Haber, J.E. & Almouzni, G. Nat. Struct. Mol. Biol. 14, 997-1007 (2007).
3. Wang, G.G., Allis, C.D. & Chi, P. Trends Mol. Med. 13, 373-380 (2007).
4. Bhaumik, S.R., Smith, E. & Shilatifard, A. Nat. Struct. Mol. Biol. 14, 1008-1016 (2007).
5. Taverna, S.D., Li, H., Ruthenburg, A.J., Allis, C.D. & Patel, D.J. Nat. Struct. Mol. Biol. 14, 1025-1040 (2007).
6. Dhalluin, C. et al. Nature 399, 491-496 (1999).
7. Collins, R.E. et al. Nat. Struct. Mol. Biol. 15, 245-250 (2008).
8. Sedgwick, S.G. & Smerdon, S.J. Trends Biochem. Sci. 24, 311-316 (1999).
9. Schultz, J., Milpetz, F., Bork, P. & Ponting, C.P. Proc. Natl. Acad. Sci. USA 95, 5857-5864 (1998).
10. Mosavi, L.K., Cammett, T.J., Desrosiers, D.C. & Peng, Z.Y. Protein Sci. 13, 1435-1448 (2004).
11. Kuo, M.H. et al. Nature 383, 269-272 (1996).
12. Owen, D.J. et al. EMBO J. 19, 6141-6149 (2000).
13. Maurer-Stroh, S. et al. Trends Biochem. Sci. 28, 69-74 (2003).
14. Couture, J.F., Collazo, E. & Trievel, R.C. Nat. Struct. Mol. Biol. 13, 698-703 (2006).
15. Ruthenburg, A.J. et al. Nat. Struct. Mol. Biol. 13, 704-712 (2006).
16. Schuetz, A. et al. EMBO J. 25, 4245-4252 (2006).
17. Lan, F. et al. Nature 448, 718-722 (2007).
18. Nielsen, P.R. et al. Nature 416, 103-107 (2002).
19. Jacobs, S.A. & Khorasanizadeh, S. Science 295, 2080-2083 (2002).
20. Li, H. et al. Nature 442, 1058-1061 (2006).
21. Botuyan, M.V. et al. Cell 127, 1361-1373 (2006).
22. Han, Z. et al. Mol. Cell 22, 137-144 (2006).
23. Wysocka, J. et al. Cell 121, 859-872 (2005).