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Items: 6

1.

Functional Analysis of the Ser149/Thr149 Variants of Human Aspartylglucosaminidase and Optimization of the Coding Sequence for Protein Production.

Banning A, König JF, Gray SJ, Tikkanen R.

Int J Mol Sci. 2017 Mar 26;18(4). pii: E706. doi: 10.3390/ijms18040706.

2.

Identification of Small Molecule Compounds for Pharmacological Chaperone Therapy of Aspartylglucosaminuria.

Banning A, Gülec C, Rouvinen J, Gray SJ, Tikkanen R.

Sci Rep. 2016 Nov 23;6:37583. doi: 10.1038/srep37583.

3.

Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulum.

Ikonen E, Julkunen I, Tollersrud OK, Kalkkinen N, Peltonen L.

EMBO J. 1993 Jan;12(1):295-302.

4.

Aspartylglucosaminuria in northern Norway: a molecular and genealogical study.

Tollersrud OK, Nilssen O, Tranebjaerg L, Borud O.

J Med Genet. 1994 May;31(5):360-3.

5.

Spectrum of mutations in aspartylglucosaminuria.

Ikonen E, Aula P, Grön K, Tollersrud O, Halila R, Manninen T, Syvänen AC, Peltonen L.

Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11222-6.

6.

Human aspartylglucosaminidase. A biochemical and immunocytochemical characterization of the enzyme in normal and aspartylglucosaminuria fibroblasts.

Enomaa N, Heiskanen T, Halila R, Sormunen R, Seppälä R, Vihinen M, Peltonen L.

Biochem J. 1992 Sep 1;286 ( Pt 2):613-8.

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