Mechanistic Pathway on Human α-Glucosidase Maltase-Glucoamylase Unveiled by QM/MM Calculations
Author:
Affiliation:
1. REQUIMTE/UCIBIO, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre s/n, 4169-007 Porto, Portugal
Funder
European Regional Development Fund
Funda??o para a Ci?ncia e a Tecnologia
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.8b01321
Reference53 articles.
1. Probing the Binding of Syzygium-Derived α-Glucosidase Inhibitors with N- and C-Terminal Human Maltase Glucoamylase by Docking and Molecular Dynamics Simulation
2. Luminal Starch Substrate “Brake” on Maltase-Glucoamylase Activity Is Located within the Glucoamylase Subunit
3. Modeling of cooked starch digestion process using recombinant human pancreatic α-amylase and maltase-glucoamylase for in vitro evaluation of α-glucosidase inhibitors
4. Subsite Mapping of the Human Pancreatic α-Amylase Active Site through Structural, Kinetic, and Mutagenesis Techniques,
5. Branch pattern of starch internal structure influences the glucogenesis by mucosal Nt-maltase-glucoamylase
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