|
SITE MENU FACULTY
MENU
1221 McGaugh HallI University of California Mail Code: 3900 Irvine, CA 92697-390
PHONE:
(949) 824-6866
|
|
Khoury MK, Parker I and Aswad DW (2009) Aquisition of chemiluminescent signals from immunoblots with a digital SLR camera. Analyt. Biochem., in press. Carter WG and Aswad DW (2008) Formation, localization, and repair of L-isoaspartyl sites in histones H2A and H2B in nucleosomes from rat liver and chicken erythrocytes. Biochemistry 47, 10757-64. Zhu, JX and Aswad, DW (2007) Selective cleavage of isoaspartyl peptide bonds by hydroxylamine after methyltransferase priming. Analyt. Biochem. 364, 1-7. Zhu JX, Doyle HA, Mamula MJ, Aswad DW. (2006) Protein repair in the brain: proteomic analysis of endogenous substrates for protein L-isoaspartyl methyltransferase in mouse brain. J Biol Chem. 281,33802-13. Reissner KJ, Paranandi MV, Luc TM, Doyle HA, Mamula MJ, Lowenson JD, and Aswad DW (2006) Synapsin I is a major endogenous substrate for protein L-isoaspartyl methyltransferase in mammalian brain. J. Biol. Chem. 281, 8389-98. Yang ML, Doyle HA, Gee RJ, Lowenson JD, Clarke S, Lawson BR, Aswad DW, Mamula MJ. (2006) Intracellular protein modification associated with altered T cell functions in autoimmunity. J Immunol. 177, 4541-9. Young, G.W, Hoofring, S.A., Mamula, M.J., Doyle, H.A., Bunick, G.J., Hu, Y. and Aswad, D.W (2005) Protein L-isoaspartyl methyltransferase catalyzes in vivo racemization of aspartate-25 in mammalian histone H2B. J. Biol. Chem. 280, 26094-98. Reissner, K. J. and Aswad, D.W. (2003) Deamidation and isoaspartate formation in proteins: unwanted alterations or surreptitious signals? Cell. Molec. Life Sci. 60, 1281-95. Li, H., Park, S., Kilburn, B., Jelinek, M. A., Henschen-Edman, A., Aswad, D. W., Stallcup, M. R. and Laird-Offringa, I. A. (2002) Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. J. Biol. Chem. 277, 44623-30. Young, A.L., Carter, W.G., Doyle, H.A., Mamula, M.J. and Aswad, D.W. (2001) Structural integrity of histone H2B in vivo requires the activity of protein L-isoaspartyl methyltransferase, a putative protein repair enzyme. J. Biol. Chem. 276, 37161-37165. Schurter, B.T., Koh, S.S., Chen, D., Bunick, G.J., Harp, J.M., Hanson, B.L., Henschen-Edman, A., Mackay, D. R., Stallcup, M. R., and Aswad, D.W. (2001) Methylation of histone H3 by coactivator-associated arginine methyltransferase 1. Biochemistry 40, 5747-5756. |
