|
Aspartylglucosaminuria
|
1.000 |
GeneticVariation
|
phenotype |
BEFREE |
The T99K variant of glycosylasparaginase shows a new structural mechanism of the genetic disease aspartylglucosaminuria.
|
30901125 |
2019 |
|
Aspartylglucosaminuria
|
1.000 |
GeneticVariation
|
phenotype |
CLINVAR |
The Spectrum of Movement Disorders in Childhood-Onset Lysosomal Storage Diseases.
|
29930972 |
2019 |
|
Aspartylglucosaminuria
|
1.000 |
GeneticVariation
|
phenotype |
BEFREE |
Betaine, which can partially rescue the AGA activity in AGU patients carrying certain missense mutations, turned out to be ineffective in the case of Ser72Pro substitution.
|
29247835 |
2018 |
|
Aspartylglucosaminuria
|
1.000 |
Biomarker
|
phenotype |
BEFREE |
Aspartylglucosaminidase (AGA) is a low-abundance intracellular enzyme that plays a key role in the last stage of glycoproteins degradation, and whose deficiency leads to human aspartylglucosaminuria, a lysosomal storage disease.
|
28742131 |
2017 |
|
Aspartylglucosaminuria
|
1.000 |
Biomarker
|
phenotype |
BEFREE |
Aspartylglucosaminuria (AGU) is an autosomal recessive lysosomal storage disorder caused by a deficiency of the lysosomal enzyme, aspartylglucosaminidase (AGA).
|
28063748 |
2017 |
|
Aspartylglucosaminuria
|
1.000 |
AlteredExpression
|
phenotype |
BEFREE |
Treatment of patient fibroblasts with these compounds results in increased AGA activity and processing, implicating that these substances may be suitable for chaperone mediated therapy for AGU.
|
27876883 |
2016 |
|
Aspartylglucosaminuria
|
1.000 |
Biomarker
|
phenotype |
GENOMICS_ENGLAND |
Advantages and pitfalls of an extended gene panel for investigating complex neurometabolic phenotypes.
|
27604308 |
2016 |
|
Aspartylglucosaminuria
|
1.000 |
Biomarker
|
phenotype |
BEFREE |
Treatment of AGU mice with recombinant AGA resulted in rapid correction of the pathophysiologic characteristics of AGU in non-neuronal tissues of the animals.
|
27906067 |
2016 |
|
Aspartylglucosaminuria
|
1.000 |
GeneticVariation
|
phenotype |
CLINVAR |
Structural basis of a point mutation that causes the genetic disease aspartylglucosaminuria.
|
25456816 |
2014 |
|
Aspartylglucosaminuria
|
1.000 |
GeneticVariation
|
phenotype |
BEFREE |
Aspartylglucosaminuria: unusual neonatal presentation in Qatari twins with a novel aspartylglucosaminidase gene mutation and 3 new cases in a Turkish family.
|
23271757 |
2014 |
|
Aspartylglucosaminuria
|
1.000 |
Biomarker
|
phenotype |
BEFREE |
The specific enzyme linked to AGU is a lysosomal hydrolase called glycosylasparaginase.
|
25456816 |
2014 |
|
Aspartylglucosaminuria
|
1.000 |
Biomarker
|
phenotype |
BEFREE |
In the current work, ERT of AGU mice was initiated at the age of 1 week with three different dosage schedules of recombinant glycosylasparaginase.
|
20607610 |
2010 |
|
Aspartylglucosaminuria
|
1.000 |
GeneticVariation
|
phenotype |
CLINVAR |
Structural basis of aspartylglucosaminuria.
|
18992224 |
2008 |
|
Aspartylglucosaminuria
|
1.000 |
GeneticVariation
|
phenotype |
BEFREE |
To elucidate the basis of aspartylglucosaminuria (AGU) from the viewpoint of enzyme structure, we constructed structural models of mutant aspartylglucosaminidase (AGA) proteins using molecular modeling software, TINKER.
|
18992224 |
2008 |
|
Aspartylglucosaminuria
|
1.000 |
Biomarker
|
phenotype |
BEFREE |
Aspartylglucosaminuria (AGU) is a lysosomal storage disease with severe neurodegenerative clinical features resulting from the deficiency of lysosomal aspartylglucosaminidase (AGA).
|
16518877 |
2006 |
|
Aspartylglucosaminuria
|
1.000 |
Biomarker
|
phenotype |
BEFREE |
The disease mechanism of AGU and the biochemistry and cell biology of the lysosomal aspartylglucosaminidase (AGA) enzyme are well characterized.
|
15365992 |
2004 |
|
Aspartylglucosaminuria
|
1.000 |
GeneticVariation
|
phenotype |
BEFREE |
Here we use the three-dimensional structure of AGA to predict structural consequences of AGU mutations, including six novel mutations, and make an effort to characterize every known disease mutation by dissecting the effect of mutations on intracellular stability, maturation, transport and the activity of AGA.
|
11309371 |
2001 |
|
Aspartylglucosaminuria
|
1.000 |
GeneticVariation
|
phenotype |
CLINVAR |
Here we use the three-dimensional structure of AGA to predict structural consequences of AGU mutations, including six novel mutations, and make an effort to characterize every known disease mutation by dissecting the effect of mutations on intracellular stability, maturation, transport and the activity of AGA.
|
11309371 |
2001 |
|
Aspartylglucosaminuria
|
1.000 |
CausalMutation
|
phenotype |
CLINVAR |
Here we use the three-dimensional structure of AGA to predict structural consequences of AGU mutations, including six novel mutations, and make an effort to characterize every known disease mutation by dissecting the effect of mutations on intracellular stability, maturation, transport and the activity of AGA.
|
11309371 |
2001 |
|
Aspartylglucosaminuria
|
1.000 |
GermlineCausalMutation
|
phenotype |
ORPHANET |
Here we use the three-dimensional structure of AGA to predict structural consequences of AGU mutations, including six novel mutations, and make an effort to characterize every known disease mutation by dissecting the effect of mutations on intracellular stability, maturation, transport and the activity of AGA.
|
11309371 |
2001 |
|
Aspartylglucosaminuria
|
1.000 |
GeneticVariation
|
phenotype |
UNIPROT |
Here we use the three-dimensional structure of AGA to predict structural consequences of AGU mutations, including six novel mutations, and make an effort to characterize every known disease mutation by dissecting the effect of mutations on intracellular stability, maturation, transport and the activity of AGA.
|
11309371 |
2001 |
|
Aspartylglucosaminuria
|
1.000 |
Biomarker
|
phenotype |
BEFREE |
The combined evidence indicates that cell-to-cell transfer of GA plays a main role in enzyme replacement therapy of AGU by normal lymphocytes.
|
11418116 |
2001 |
|
Aspartylglucosaminuria
|
1.000 |
Biomarker
|
phenotype |
MGD |
Enzyme replacement therapy in a mouse model of aspartylglycosaminuria.
|
10657992 |
2000 |
|
Aspartylglucosaminuria
|
1.000 |
AlteredExpression
|
phenotype |
BEFREE |
Thus, the high frequency of mucosal overgrowth in AGU patients does not appear to be directly associated with lysosomal storage or with alterations in the level of AGA expression.
|
10353787 |
1999 |
|
Aspartylglucosaminuria
|
1.000 |
GeneticVariation
|
phenotype |
CLINVAR |
A novel exonic mutation in the aspartylglucosaminidase gene causes exon skipping.
|
10399108 |
1999 |