ArticleThe Journal of biological chemistry2013
Specificity of Processing α-glucosidase I is guided by the substrate conformation: crystallographic and in silico studies.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 92 citations in OpenAlex.
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- TUSC3 serves as a rate-limiting gatekeeper of a glycan-mediated ER triage checkpoint for BMP4/Dpp.Cell reports · 2026Article
- Potent and selective α-glucosidase inhibition by coumarin-triazole conjugates: design,RSC advances · 2026Article
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- Exploring Small-Molecule Inhibitors of Glucosidase II: Advances, Challenges, and Therapeutic Potential in Cancer and Viral Infection.International journal of molecular sciences · 2025Review
- Identification of novel triazolopyrimidines as potent α-glucosidase inhibitor through design, synthesis, biological evaluations, and computational analysis.Scientific reports · 2025Article
- TUSC3 serves as a rate-limiting gatekeeper of a glycan-mediated ER Triage Checkpoint for BMP4/Dpp.bioRxiv : the preprint server for biology · 2025Article
- Chiral pyrimidinyl-piperazine carboxamide derivatives as potent yeast α-glucosidase inhibitors.Scientific reports · 2025Article
- Harnessing Phytochemicals to Regulate Catalytic Residues of Alpha-Amylase and Alpha-Glucosidase in Type 2 Diabetes.Cell biochemistry and biophysics · 2025Article
- Design, synthesis, and investigation of novel 5-arylpyrazole-glucose hybrids as α-glucosidase inhibitors.Scientific reports · 2025Article
- Design, synthesis, and evaluation of novel substituted imidazo[1,2-c]quinazoline derivatives as potential α-glucosidase inhibitors with bioactivity and molecular docking insights.Scientific reports · 2024Article
- Alpha-glucosidase inhibitory compounds from Vietnamese lichenRSC advances · 2024Article
- Expanding horizons of iminosugars as broad-spectrum anti-virals: mechanism, efficacy and novel developments.Natural products and bioprospecting · 2024Review
- Genetic and enzymatic characterization of Amy13E fromApplied and environmental microbiology · 2024Article
- Imidazo[1,2-c]quinazolines as a novel and potent scaffold of α-glucosidase inhibitors: design, synthesis, biological evaluations, and in silico studies.Scientific reports · 2023Article
- Synthesis and Molecular Docking Studies of Novel Biheterocyclic Propanamides as Antidiabetic Agents Having Mild Cytotoxicity.ACS omega · 2023Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundThe enzyme “GluI” is key to the synthesis of critical glycoproteins in the cell.
resultsWe have determined the structure of GluI, and modeled binding with its unique sugar substrate.
conclusionThe specificity of this interaction derives from a unique conformation of the substrate. SIGNIFICANCE: Understanding the mechanism of the enzyme is of basic importance and relevant to potential development of antiviral inhibitors. Processing α-glucosidase I (GluI) is a key member of the eukaryotic N-glycosylation processing pathway, selectively catalyzing the first glycoprotein trimming step in the endoplasmic reticulum. Inhibition of GluI activity impacts the infectivity of enveloped viruses; however, despite interest in this protein from a structural, enzymatic, and therapeutic standpoint, little is known about its structure and enzymatic mechanism in catalysis of the unique glycan substrate Glc3Man9GlcNAc2. The first structural model of eukaryotic GluI is here presented at 2-Å resolution. Two catalytic residues are proposed, mutations of which result in catalytically inactive, properly folded protein. Using Autodocking methods with the known substrate and inhibitors as ligands, including a novel inhibitor characterized in this work, the active site of GluI was mapped. From these results, a model of substrate binding has been formulated, which is most likely conserved in mammalian GluI.
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