Associated Papers
A new horizon in the phosphorylated sites of AGA: the structural impact of C163S mutation in aspartylglucosaminuria through molecular dynamics simulation.
Balasundaram A et al.
Journal of Biomolecular Structure & Dynamics, 2024
Validation of Aspartylglucosaminidase Activity Assay for Human Serum Samples: Establishment of a Biomarker for Diagnostics and Clinical Studies.
Banning A et al.
International Journal of Molecular Sciences, 2023
A cross-sectional natural history study of aspartylglucosaminuria.
Goodspeed K et al.
Jimd Reports, 2022
Towards Splicing Therapy for Lysosomal Storage Disorders: Methylxanthines and Luteolin Ameliorate Splicing Defects in Aspartylglucosaminuria and Classic Late Infantile Neuronal Ceroid Lipofuscinosis.
Banning A et al.
Cells, 2021
Aspartylglucosaminuria: Clinical Presentation and Potential Therapies.
Goodspeed K et al.
Journal of Child Neurology, 2021
The T99K variant of glycosylasparaginase shows a new structural mechanism of the genetic disease aspartylglucosaminuria.
Pande S et al.
Protein Science : a Publication of the Protein Society, 2019
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
Aspartylglycosaminuria: a review.
Arvio M et al.
Orphanet Journal of Rare Diseases, 2016
Identification of Small Molecule Compounds for Pharmacological Chaperone Therapy of Aspartylglucosaminuria.
Banning A et al.
Scientific Reports, 2016
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
Molecular genetics of the Finnish disease heritage.
Peltonen L et al.
Human Molecular Genetics, 1999
Primary folding of aspartylglucosaminidase. Significance of disulfide bridges and evidence of early multimerization.
Riikonen A et al.
The Journal of Biological Chemistry, 1996
Immediate interaction between the nascent subunits and two conserved amino acids Trp34 and Thr206 are needed for the catalytic activity of aspartylglucosaminidase.
Riikonen A et al.
The Journal of Biological Chemistry, 1995
[Aspartylglucosaminuria: a point mutation as a cause of mental defect].
Ikonen E et al.
Duodecim; Laaketieteellinen Aikakauskirja, 1994
Aspartylglycosaminuria: protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation.
Mononen I et al.
Faseb Journal : Official Publication of the Federation of American Societies for Experimental Biology, 1993
Aspartylglycosaminuria in a non-Finnish patient caused by a donor splice mutation in the glycoasparaginase gene.
Mononen I et al.
The Journal of Biological Chemistry, 1992
Mutations causing aspartylglucosaminuria (AGU): a lysosomal accumulation disease.
Ikonen E et al.
Human Mutation, 1992