References:

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2. Tikkanen ,R., Riikonen, A., Oinonen, C., Rouvinen, R., and Peltonen, L. Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: implications for catalytic mechanism and autocatalytic activation. (1996) EMBO J. 12,2954-60.

3. Riikonen, A., Rouvinen, J., Tikkanen, R., Julkunen, Il, Peltonen, L., and Jalanko, A. Primary Folding of Aspartylglucosaminidase (1996) J. Biol. Chem. 271, 21340-21344

4. Ikonen, E., Tollersrud, O.-K., Kalkkinen, N. and Peltonen, L. Lysosomal aspartylglucosaminidase is processed to the acive subunit in the endoplasmic reticulum. (1993) EMBO J. 13, 295-302.

5. Riikonen, A., Tikkanen, R., Jalanko, A., Peltonen, L. Immediate interaction between the nascent subunits and two conserved amino acids Trp34 and Thr206 are needed for the catalytic activity of aspartylglucosaminidase. (1995) J. Biol. Chem. 270:4903-4907

6. Oinonen, C., Tikkanen, R., Rouvinen, J., and Peltonen, L. Three-dimensional structure of human lysosomal aspartylglucosaminidase (1995) Nat. Struct. Biol. 2, 1102-1108

7. OMIM http://www.3.ncbi.nim.nih.gov:80/htbin-post/Omim/dispmim?208400 Aspartylglucosaminuria