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glucan 1,4-alpha-glucosidase - metabolism (870) 870
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Journal Article
BMC genomics, ISSN 1471-2164, 12/2012, Volume 13, Issue 1, pp. 701 - 701
Background: Filamentous fungi such as Aspergillus niger are well known for their exceptionally high capacity for secretion of proteins, organic acids, and... 
unfolded protein response | secretion | Aspergillus niger | HacA | transcriptome | protein expression | endoplasmic reticulum | glucoamylase | Secretion | Transcriptome | Protein expression | Glucoamylase | Endoplasmic reticulum | Unfolded protein response | STRAINS | GENETIC-ANALYSIS | TRICHODERMA-REESEI | GENOMIC ANALYSIS | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | SECRETED PROTEINS | GENETICS & HEREDITY | ENDOPLASMIC-RETICULUM | STRESS | REVEALS | Gene Expression Regulation, Fungal | Aspergillus niger - growth & development | Glucan 1,4-alpha-Glucosidase - genetics | Glucan 1,4-alpha-Glucosidase - secretion | Maltose - metabolism | Culture Techniques | Aspergillus niger - enzymology | Gene Expression Profiling | Hydrolysis | Aspergillus niger - genetics | Glucan 1,4-alpha-Glucosidase - biosynthesis | Glucan 1,4-alpha-Glucosidase - metabolism | Aspergillus niger - metabolism | Biotechnology | RNA | Genes | Genomics | Genomes | Genetic transcription | Gene expression | Proteins | Aspergillus | Amylases | Analysis | Genetic research | Plant metabolites | Sugars | Enzymes | Microbiology | Glucose | Carbon | Manuscripts | Environmental conditions | Transcription factors | Growth rate | Transcription | Chemostats | Gene regulation | Traffic | Homeostasis | Glycosylation | organic acids | Fungi | Secondary metabolites | Vesicles | Overexpression | Protein folding | Glucan 1,4- alpha -glucosidase | Acetylation | Protein transport
Journal Article
Molecular Therapy, ISSN 1525-0016, 01/2005, Volume 11, Issue 1, pp. 48 - 56
Pompe disease (type II glycogen storage disease) is an autosomal recessive disorder caused by a deficiency of lysosomal acid α-glucosidase (GAA) leading to the... 
Pompe disease | autophagy | enzyme replacement therapy | acid α-glucosidase | tetracycline-controllable system | lysosomal storage disease | transgenic knockout | lysosomal trafficking | Transgenic knockout | Enzyme replacement therapy | Acid α-glucosidase | Lysosomal storage disease | Tetracycline-controllable system | Autophagy | Lysosomal trafficking | MEDICINE, RESEARCH & EXPERIMENTAL | LYSOSOMAL STORAGE DISEASES | MALTASE DEFICIENCY | KNOCKOUT MICE | MAMMALIAN-CELLS | acid alpha-glucosidase | SKELETAL-MUSCLE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | GENETICS & HEREDITY | REPLACEMENT THERAPY | EXPRESSION | MANNOSE 6-PHOSPHATE RECEPTORS | CLATHRIN | RABBIT MILK | Muscle Fibers, Fast-Twitch - cytology | Genetic Therapy | Muscle Fibers, Fast-Twitch - drug effects | Humans | Muscle Fibers, Fast-Twitch - metabolism | Muscle, Skeletal - metabolism | Glycogen Storage Disease Type II - therapy | Glycogen Storage Disease Type II - enzymology | Endocytosis | Glycogen - metabolism | Lysosomes - metabolism | Myocardium - metabolism | Glucan 1,4-alpha-Glucosidase - pharmacology | Glycogen - analysis | Recombinant Proteins - metabolism | Cell Line | Cricetinae | Glucan 1,4-alpha-Glucosidase - genetics | Glycogen Storage Disease Type II - genetics | Liver - metabolism | alpha-Glucosidases | Recombinant Proteins - genetics | Liver - secretion | Microscopy, Electron | Glucan 1,4-alpha-Glucosidase - deficiency | Animals | Glucan 1,4-alpha-Glucosidase - metabolism | Mice
Journal Article
Applied Microbiology and Biotechnology, ISSN 0175-7598, 3/2017, Volume 101, Issue 6, pp. 2415 - 2425
Journal Article
Biotechnology and bioengineering, ISSN 0006-3592, 2013, Volume 110, Issue 2, pp. 543 - 551
In filamentous fungi, most of the strategies used for the improvement of protein yields have been based on an increase in the transcript levels of a target... 
nidulans | oryzae | gene | 5'-untranslated region | translation | promoter | transformation | protein expression | cloning | Aspergillus niger | mRNA 5′UTR | multicopper oxidase | high‐throughput screening | High-throughput screening | Multicopper oxidase | MRNA 5′UTR | TRANSFORMATION | mRNA 5'UTR | high-throughput screening | TRANSLATION | 5'-UNTRANSLATED REGION | GENE | ORYZAE | CLONING | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PROTEIN EXPRESSION | NIDULANS | PROMOTER | Fungal Proteins - chemistry | Oxidoreductases - analysis | Glucan 1,4-alpha-Glucosidase - genetics | Protein Biosynthesis | Oxidoreductases - metabolism | Oxidoreductases - genetics | RNA, Messenger - genetics | Aspergillus niger - enzymology | Fungal Proteins - genetics | Recombinant Fusion Proteins - chemistry | RNA, Messenger - metabolism | Oxidoreductases - chemistry | Recombinant Fusion Proteins - metabolism | High-Throughput Screening Assays | 5' Untranslated Regions | Aspergillus niger - genetics | Escherichia coli - genetics | Glucan 1,4-alpha-Glucosidase - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Glucan 1,4-alpha-Glucosidase - biosynthesis | Glucan 1,4-alpha-Glucosidase - metabolism | Recombinant Fusion Proteins - genetics | Fungal Proteins - metabolism | Oxidases | Amylases | Messenger RNA | Recombinant proteins | Analysis | Genes
Journal Article
PloS one, ISSN 1932-6203, 2014, Volume 9, Issue 7, p. e102092
Pompe disease is an inherited lysosomal storage disorder that results from a deficiency in acid a-glucosidase (GAA) activity due to mutations in the GAA gene.... 
LONG-TERM | ALGLUCOSIDASE ALPHA | MULTIDISCIPLINARY SCIENCES | MUTATION | MICE | FABRY-DISEASE | INFANTILE | ENZYME REPLACEMENT THERAPY | BETA-GLUCOSIDASE | FIBROBLASTS | CHILDREN | 1-Deoxynojirimycin - pharmacokinetics | Humans | Cercopithecus aethiops | Endoplasmic Reticulum - metabolism | Biological Availability | Protein Transport - drug effects | Enzyme Stability - drug effects | Glycogen Storage Disease Type II - pathology | Glycogen Storage Disease Type II - enzymology | Proteolysis - drug effects | Glycogen - metabolism | Lysosomes - metabolism | Biocatalysis - drug effects | Isoenzymes - metabolism | Endoplasmic Reticulum - drug effects | Glucan 1,4-alpha-Glucosidase - biosynthesis | 1-Deoxynojirimycin - administration & dosage | Disease Models, Animal | Lysosomes - drug effects | Glucan 1,4-alpha-Glucosidase - genetics | Administration, Oral | Isoenzymes - genetics | Mutant Proteins - genetics | Mice, Transgenic | Mutant Proteins - metabolism | Gene Knockout Techniques | Mutant Proteins - biosynthesis | 1-Deoxynojirimycin - pharmacology | Animals | Glucan 1,4-alpha-Glucosidase - metabolism | Glycogen Storage Disease Type II - metabolism | Mice | Mutation | Isoenzymes - biosynthesis | COS Cells | Muscles | Glycogen | Amylases | Enzymes | Stability | Incubation | Medical treatment | Oral administration | Transgenic mice | Lysosomes | Glucosidase | Pharmacology | Tissues | Substrates | Skeletal muscle | Musculoskeletal system | Reduction | Acids | Protein folding | Proteolysis | Rodents | Isoforms | Fibroblasts | Endoplasmic reticulum
Journal Article