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 Dana W. Aswad

University of California

1221 McGaugh Hall
University of California
Mail Code: 3900
Irvine, CA 92697-390

PHONE: (949) 824-6866
FAX: (949) 824-8551

E-MAIL: dwaswad@uci.edu

 

Dana W. Aswad
Professor, Molecular Biology and Biochemistry
School of Biological Sciences

PH.D., University of California, Berkeley, 1974, Biochemistry

Research Interests
Regulation of protein function and gene expresssion by post-translational modification. Biochemistry of protein damage, aging, and repair. Biochemical characterization of protein pharmaceuticals.

Faculty/lab web:
http://www.faculty.uci.edu/scripts/UCIFacultyProfiles/detailMBB.cfm?ID=2135
 
Graduate Programs:
Cell Biology Neurobiology Structural Biology and Molecular Biophysics Biotechnology
 
Professional Society American Society for Biochemistry and Molecular Biology
 
Abstract
Post-translational modification serves as an important mechanism for modulating the structure, activity and lifetime of many proteins. My laboratory is exploring the cellular function of protein L-isoaspartyl methyltransferase (PIMT), an enzyme that methylates damaged proteins that contain atypical isoaspartyl residues. Substantial evidence indicates that this enzyme serves to repair these atypical residues by converting the isopeptide bond to a normal peptide bond. Current research is focused on determining the physiological consequences of PIMT deficiency in a mouse model.

Patents: "Determination of Isoaspartate in Proteins" United States Patent No. 5,273,886; issued Dec. 28, 1993.


Other Experience
Updated: Last Updated: 07/11/2014

  Dimitrijevic A, Qin Z, Aswad DW. (2014) Isoaspartyl Formation in Creatine Kinase B Is Associated with Loss of Enzymatic Activity; Implications for the Linkage of Isoaspartate Accumulation and Neurological Dysfunction in the PIMT Knockout Mouse. PLoS One. 23: e100622. PMID:24955845

Qin Z, Yang J, Klassen HJ, and Aswad DW (2014) Isoaspartyl Protein Damage and Repair in Mouse Retina. Invest Ophthalmol Vis Sci. 55:1572-1579. PIMD:24550364

Qin Z, Kaufman RS, Khoury RN, Khoury MK, and Aswad DW (2013) Isoaspartate accumulation in mouse brain is associated with altered patterns of protein phosphorylation and acetylation, some of which are highly sex-dependent. PLoS One 8(11):e80758. PMID: 24224061

Doyle HA, Aswad DW, and Mamula MJ. (2013) Autoimmunity to isomerized histone H2B in systemic lupus erythematosus. Autoimmunity 46, 6-13.

Morrison GJ, Ganesan R, Qin Z, and Aswad DW. (2012) Considerations in the identification of endogenous substrates for protein L-isoaspartyl methyltransferase: the case of synuclein. PLoS One 7(8):e43288. PMID: 22905247.

Khoury MK, Parker I and Aswad DW (2010) Aquisition of chemiluminescent signals from immunoblots with a digital SLR camera. Analyt. Biochem. 397, 129-31.

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.

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