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
The Role of Hematopoietic Cell Transplant in the Glycoprotein Diseases.
Naumchik BM et al.
Cells, 2020
Reinterpretation of common pathogenic variants in ClinVar revealed a high proportion of downgrades.
Xiang J et al.
Scientific Reports, 2020
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
Optical coherence tomography features in brothers with aspartylglucosaminuria.
Goodspeed K et al.
Annals of Clinical and Translational Neurology, 2018
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
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
Aspartylglucosaminuria: unusual neonatal presentation in Qatari twins with a novel aspartylglucosaminidase gene mutation and 3 new cases in a Turkish family.
Opladen T et al.
Journal of Child Neurology, 2014
Improving the prediction of disease-related variants using protein three-dimensional structure.
Capriotti E et al.
Bmc Bioinformatics, 2011
Loss of protein structure stability as a major causative factor in monogenic disease.
Yue P et al.
Journal of Molecular Biology, 2005
Carriers of the aspartylglucosaminuria genetic mutation and chronic arthritis.
Arvio M et al.
Annals of the Rheumatic Diseases, 2002
Human leukocyte glycosylasparaginase: cell-to-cell transfer and properties in correction of aspartylglycosaminuria.
Dunder U et al.
Febs Letters, 2001
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
Overgrowth of oral mucosa and facial skin, a novel feature of aspartylglucosaminuria.
Arvio P et al.
Journal of Medical Genetics, 1999
Molecular genetics of the Finnish disease heritage.
Peltonen L et al.
Human Molecular Genetics, 1999
Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post bone marrow transplantation.
Laitinen A et al.
Clinical Genetics, 1997
Primary folding of aspartylglucosaminidase. Significance of disulfide bridges and evidence of early multimerization.
Riikonen A et al.
The Journal of Biological Chemistry, 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
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
Identification of a novel mutation causing aspartylglucosaminuria reveals a mutation hotspot region in the aspartylglucosaminidase gene.
Isoniemi A et al.
Human Mutation, 1995
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