Associated Papers
A cross-sectional natural history study of aspartylglucosaminuria.
Goodspeed K et al.
Jimd Reports, 2022
Aspartylglucosaminuria: Clinical Presentation and Potential Therapies.
Goodspeed K et al.
Journal of Child Neurology, 2021
Clinical experience with carrier screening in a general population: support for a comprehensive pan-ethnic approach.
Westemeyer M et al.
Genetics in Medicine : Official Journal of the American College of Medical Genetics, 2020
Amlexanox provides a potential therapy for nonsense mutations in the lysosomal storage disorder Aspartylglucosaminuria.
Banning A et al.
Biochimica Et Biophysica Acta. Molecular Basis of Disease, 2018
Functional Analysis of the Ser149/Thr149 Variants of Human Aspartylglucosaminidase and Optimization of the Coding Sequence for Protein Production.
Banning A et al.
International Journal of Molecular Sciences, 2017
Nicotine and oxidative stress induced exomic variations are concordant and overrepresented in cancer-associated genes.
Bavarva JH et al.
Oncotarget, 2014
Structural basis of aspartylglucosaminuria.
Saito S et al.
Biochemical and Biophysical Research Communications, 2008
Autoproteolytic activation of human aspartylglucosaminidase.
Saarela J et al.
The Biochemical Journal, 2004
Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations.
Saarela J et al.
Human Molecular Genetics, 2001
Aspartylglycosaminuria: biochemistry and molecular biology.
Aronson NN
Biochimica Et Biophysica Acta, 1999
Activation and oligomerization of aspartylglucosaminidase.
Saarela J et al.
The Journal of Biological Chemistry, 1998
Mice with an aspartylglucosaminuria mutation similar to humans replicate the pathophysiology in patients.
Jalanko A et al.
Human Molecular Genetics, 1998
Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: implications for catalytic mechanism and autocatalytic activation.
Tikkanen R et al.
The Embo Journal, 1996
Ser72Pro active-site disease mutation in human lysosomal aspartylglucosaminidase: abnormal intracellular processing and evidence for extracellular activation.
Peltola M et al.
Human Molecular Genetics, 1996