Compounds > aspartic acid
Page last updated: 2024-08-17

aspartic acid and Acid Alpha-Glucosidase Deficiency

aspartic acid has been researched along with Acid Alpha-Glucosidase Deficiency in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (50.00)18.2507
2000's2 (50.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Chen, CP; Hwu, WL; Lin, SP; Tsai, FJ; Tzen, CY; Wang, W1
Gellerich, FN; Hermans, MM; Kirschner, J; Korinthenberg, R; Kroos, MA; Reuser, AJ; Van Der Ploeg, AT1
Lin, CY; Shieh, JJ1
de Graaff, E; Hermans, MM; Kroos, MA; Oostra, BA; Reuser, AJ; Willemsen, R; Wisselaar, HA1

Other Studies

4 other study(ies) available for aspartic acid and Acid Alpha-Glucosidase Deficiency

ArticleYear
Detection of a homozygous D645E mutation of the acid alpha-glucosidase gene and glycogen deposition in tissues in a second-trimester fetus with infantile glycogen storage disease type II.
    Prenatal diagnosis, 2004, Volume: 24, Issue:3

    Topics: Adult; alpha-Glucosidases; Aspartic Acid; Female; Glutamic Acid; Glycogen; Glycogen Storage Disease Type II; Homozygote; Humans; Lysosomes; Mutation; Pregnancy; Pregnancy Trimester, Second

2004
A case of childhood Pompe disease demonstrating phenotypic variability of p.Asp645Asn.
    Neuromuscular disorders : NMD, 2004, Volume: 14, Issue:6

    Topics: alpha-Glucosidases; Amino Acid Substitution; Animals; Asparagine; Aspartic Acid; Blotting, Western; Chlorocebus aethiops; COS Cells; DNA Mutational Analysis; Echocardiography, Three-Dimensional; Fibroblasts; Glycogen Storage Disease Type II; Humans; Infant; Male; Muscles; Mutation; Phenotype; Transfection

2004
Identification of a de Novo point mutation resulting in infantile form of Pompe's disease.
    Biochemical and biophysical research communications, 1995, Aug-04, Volume: 213, Issue:1

    Topics: alpha-Glucosidases; Amino Acid Sequence; Aspartic Acid; Base Sequence; Codon; Glycogen Storage Disease Type II; Humans; Infant; Molecular Sequence Data; Point Mutation

1995
The conservative substitution Asp-645-->Glu in lysosomal alpha-glucosidase affects transport and phosphorylation of the enzyme in an adult patient with glycogen-storage disease type II.
    The Biochemical journal, 1993, Feb-01, Volume: 289 ( Pt 3)

    Topics: Adult; Alleles; alpha-Glucosidases; Aspartic Acid; Base Sequence; beta-N-Acetylhexosaminidases; Biological Transport; Black People; Cells, Cultured; Codon; DNA Mutational Analysis; Glutamates; Glutamic Acid; Glycogen; Glycogen Storage Disease Type II; Humans; Lysosomes; Microscopy, Immunoelectron; Molecular Sequence Data; Phenotype; Phosphorylation; Point Mutation; Polymerase Chain Reaction; Polymorphism, Genetic; Protein Processing, Post-Translational; Regulatory Sequences, Nucleic Acid; Sequence Analysis, DNA; Tunicamycin

1993