ArticleNature communications2016
Crystal structure of glycogen debranching enzyme and insights into its catalysis and disease-causing mutations.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 49 citations in OpenAlex.
- Off-Target Binding of Miglustat to Glycogen Debranching Enzyme.International journal of molecular sciences · 2026Article
- Molecular architecture and catalytic mechanism of human glycogen debranching enzyme.Nature communications · 2025Article
- Atg45 is an autophagy receptor for glycogen, a non-preferred cargo of bulk autophagy in yeast.iScience · 2024Article
- Targeting intracellular nontuberculous mycobacteria andMicrobiology spectrum · 2024Article
- Identification of candidate genes and residues for improving nitrogen use efficiency in the N-sensitive medicinal plant Panax notoginseng.BMC plant biology · 2024Article
- A functional mini-GDE transgene corrects impairment in models of glycogen storage disease type III.The Journal of clinical investigation · 2024Article
- A Functional Human Glycogen Debranching Enzyme Encoded by a Synthetic Gene: Its Implications for Glycogen Storage Disease Type III Management.Protein and peptide letters · 2024Article
- Glycogen storage diseases.Nature reviews. Disease primers · 2023Review
- Glycogen debranching pathway deduced from substrate specificity of glycogen debranching enzyme.Glycoconjugate journal · 2022Article
- Crystal structures of glycogen-debranching enzyme mutants in complex with oligosaccharides.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Hepatic glycogen storage diseases: pathogenesis, clinical symptoms and therapeutic management.Archives of medical science : AMS · 2021Article
- Characterization of Glycoside Hydrolase Families 13 and 31 Reveals Expansion and Diversification of α-Amylase Genes in the PhlebotomineFrontiers in physiology · 2021Article
- New approach to prepare fluorogenic branched dextrins for assaying glycogen debranching enzyme.Glycoconjugate journal · 2020Article
- Role of Metabolism in Bone Development and Homeostasis.International journal of molecular sciences · 2020Review
- A Novel Gene Therapy Approach for GSD III Using an AAV Vector Encoding a Bacterial Glycogen Debranching Enzyme.Molecular therapy. Methods & clinical development · 2020Article
- Article
- Genomes and secretomes of Ascomycota fungi reveal diverse functions in plant biomass decomposition and pathogenesis.BMC genomics · 2019Article
- Glucose and glycogen in the diabetic kidney: Heroes or villains?EBioMedicine · 2019Review
- Brain Glycogen Structure and Its Associated Proteins: Past, Present and Future.Advances in neurobiology · 2019Review
- A new interpretation of sulfate activation of rabbit muscle glycogen phosphorylase.Glycoconjugate journal · 2018Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycogen is a branched glucose polymer and serves as an important energy store. Its debranching is a critical step in its mobilization. In animals and fungi, the 170 kDa glycogen debranching enzyme (GDE) catalyses this reaction. GDE deficiencies in humans are associated with severe diseases collectively termed glycogen storage disease type III (GSDIII). We report crystal structures of GDE and its complex with oligosaccharides, and structure-guided mutagenesis and biochemical studies to assess the structural observations. These studies reveal that distinct domains in GDE catalyse sequential reactions in glycogen debranching, the mechanism of their catalysis and highly specific substrate recognition. The unique tertiary structure of GDE provides additional contacts to glycogen besides its active sites, and our biochemical experiments indicate that they mediate its recruitment to glycogen and regulate its activity. Combining the understanding of the GDE catalysis and functional characterizations of its disease-causing mutations provides molecular insights into GSDIII.
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