Arginine methylation at a glance-Reference-Cited by-同舟云学术

Arginine methylation at a glance

Published:2007-12-15 Issue:24 Volume:120 Page:4243-4246
ISSN:1477-9137
Container-title:Journal of Cell Science
language:en
Short-container-title:

Author:

Bedford Mark T.¹

Affiliation:

1. Department of Carcinogenesis, The University of Texas M. D. Anderson Cancer Center, Smithville, TX 78957, USA

Publisher

The Company of Biologists

Subject

Cell Biology

Link

http://journals.biologists.com/jcs/article-pdf/120/24/4243/1371310/4243.pdf

Reference62 articles.

1. Bachand, F. and Silver, P. A. (2004). PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits. EMBO J.23, 2641-2650.

2. Bedford, M. T. (2006). The family of protein arginine methyltransferases. In The Enzymes (ed. S. G. Clarke and F. Tamanoi), pp. 31-50. Amsterdam: Academic Press.

3. Bedford, M. T. and Richard, S. (2005). Arginine methylation an emerging regulator of protein function. Mol. Cell18, 263-272.

4. Bedford, M. T., Reed, R. and Leder, P. (1998). WW domain-mediated interactions reveal a spliceosome-associated protein that binds a third class of proline-rich motif: the proline glycine and methionine-rich motif. Proc. Natl. Acad. Sci. USA95, 10602-10607.

5. Bedford, M. T., Frankel, A., Yaffe, M. B., Clarke, S., Leder, P. and Richard, S. (2000). Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains. J. Biol. Chem.275, 16030-16036.

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