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Subsite Mapping of the Human Pancreatic α-Amylase Active Site through Structural, Kinetic, and Mutagenesis Techniques,
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Isolation, Crystallization and Preliminary Diffraction Analyses of Human Pancreatic α-Amylase
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Refined Molecular Structure of Pig Pancreatic α-Amylase at 2·1 Å Resolution
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Satisfying Hydrogen Bonding Potential in Proteins
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Syntheses of 2-deoxy-2-fluoro mono- and oligo-saccharide glycosides from glycals and evaluation as glycosidase inhibitors
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Facile synthesis of acetylated glycosyl fluorides derived from di- and tri-saccharides
inferredcites →https://doi.org/10.1016/0008-6215(94)00317-9openalex-snapshot
Syntheses of 4′-deoxy-α-maltosyl fluoride and 4″-deoxy-α-maltotriosyl fluoride as probes of α-glucanotransferase mechanisms
inferredcites →https://doi.org/10.1016/0016-5085(88)90295-8openalex-snapshot
Fate and effects of the α-glucosidase inhibitor acarbose in humans
inferredcites →https://doi.org/10.1016/0167-4838(87)90331-1openalex-snapshot
The determination of subsite binding energies of porcine pancreatic α-amylase by comparing hydrolytic activity towards substrates
inferredcites →https://doi.org/10.1016/s0021-9258(18)62937-0openalex-snapshot
The Action Pattern of Porcine Pancreatic α-Amylase in Relationship to the Substrate Binding Site of the Enzyme
inferredcites →https://doi.org/10.1016/s0022-2836(77)80200-3openalex-snapshot
The protein data bank: A computer-based archival file for macromolecular structures
inferredcites →https://doi.org/10.1016/s0248-8663(89)80039-6openalex-snapshot
Inhibiteurs des alpha-glucosidases: une nouvelle approche thérapeutique du diabète et des hypoglycémies fonctionnelles
inferredcites →https://doi.org/10.1021/ja9627454openalex-snapshot
Design and Synthesis of 2‘-Deoxy-2‘-Fluorodisaccharides as Mechanism-Based Glycosidase Inhibitors That Exploit Aglycon Specificity
inferredcites →https://doi.org/10.1042/bj2800309openalex-snapshot
A classification of glycosyl hydrolases based on amino acid sequence similarities
inferredcites →https://doi.org/10.1074/jbc.271.39.23836openalex-snapshot
Structural and Functional Aspects of Chloride Binding to Alteromonas haloplanctis α-Amylase
inferredcites →https://doi.org/10.1107/s0108767393007597openalex-snapshot
AMoRe: an automated package for molecular replacement
inferredcites →https://doi.org/10.1111/j.1432-1033.1974.tb03257.xopenalex-snapshot
The Allosteric Activation of Mammalian α‐Amylase by Chloride
inferredcites →https://doi.org/10.1111/j.1432-1033.1996.0561z.xopenalex-snapshot
Crystal Structure of Pig Pancreatic α‐amylase Isoenzyme II, in Complex with the Carbohydrate Inhibitor Acarbose
inferredcites →https://doi.org/10.1128/mcb.8.3.1197openalex-snapshot
Concerted Evolution of Human Amylase Genes
inferredcites →https://doi.org/10.1177/10454411930040033501openalex-snapshot
The Remarkable Evolutionary History of the Human Amylase Genes
inferredcites →https://doi.org/10.2337/diacare.5.1.6openalex-snapshot
Constant Intravenous Insulin Infusion During Labor and Delivery in Diabetes Mellitus
inferredcites →https://doi.org/10.2337/diacare.5.2.92openalex-snapshot
Effect of Acarbose on the 24-Hour Blood Glucose Profile and Pattern of Carbohydrate Absorption
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Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Examination of the active sites of human salivary α-amylase (HSA)
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Subsite mapping of human salivary α‐amylase and the mutant Y151M
inferred← citeshttps://doi.org/10.1016/s0022-2836(02)01326-8openalex-snapshot
Probing the Role of a Mobile Loop in Substrate Binding and Enzyme Activity of Human Salivary Amylase
inferred← citeshttps://doi.org/10.1016/s0022-2836(02)01384-0openalex-snapshot
Functional Sites in Protein Families Uncovered via an Objective and Automated Graph Theoretic Approach
inferred← citeshttps://doi.org/10.1016/s0076-6879(09)04619-9openalex-snapshot
Chapter 19 Enzymology of Aminoglycoside Biosynthesis—Deduction from Gene Clusters
inferred← citeshttps://doi.org/10.1021/acs.accounts.6c00510openalex-snapshot
Discovery, Design, and Evaluation of Nanomolar to Picomolar Inhibitors of Human Pancreatic α-Amylase for Control of Postprandial Blood Glucose Levels
inferred← citeshttps://doi.org/10.1021/acs.biochem.6b00992openalex-snapshot
Evaluation of the Significance of Starch Surface Binding Sites on Human Pancreatic α-Amylase
inferred← citeshttps://doi.org/10.1021/acs.biomac.5b00190openalex-snapshot
Investigating the Mechanisms of Amylolysis of Starch Granules by Solution-State NMR
inferred← citeshttps://doi.org/10.1021/acs.jafc.4c09006openalex-snapshot
Kinetic Analysis and Starch Digestion Product Composition Reveal the Subtle Relationship between the Anthocyanidin Structure and Inhibitory Activity on Pancreatic α-Amylase
inferred← citeshttps://doi.org/10.1021/acs.jafc.9b02293openalex-snapshot
Identification of Ellagitannins in the Unripe Fruit of Rubus Chingii Hu and Evaluation of its Potential Antidiabetic Activity
inferred← citeshttps://doi.org/10.1021/acs.jcim.2c00691openalex-snapshot
Role of Enzyme and Active Site Conformational Dynamics in the Catalysis by α-Amylase Explored with QM/MM Molecular Dynamics
inferred← citeshttps://doi.org/10.1021/acs.jcim.4c00475openalex-snapshot
Kinetic View of Enzyme Catalysis from Enhanced Sampling QM/MM Simulations
inferred← citeshttps://doi.org/10.1021/acs.jctc.5b00222openalex-snapshot
Establishing the Catalytic Mechanism of Human Pancreatic α-Amylase with QM/MM Methods
inferred← citeshttps://doi.org/10.1021/acs.jpcb.8b01321openalex-snapshot
Mechanistic Pathway on Human α-Glucosidase Maltase-Glucoamylase Unveiled by QM/MM Calculations
inferred← citeshttps://doi.org/10.1021/acsbiomaterials.0c01010openalex-snapshot
Machine Learning-Based Amino Acid Substitution of Short Peptides: Acquisition of Peptides with Enhanced Inhibitory Activities against α-Amylase and α-Glucosidase
inferred← citeshttps://doi.org/10.1021/acscatal.3c01473openalex-snapshot
How and When Does an Enzyme React? Unraveling α-Amylase Catalytic Activity with Enhanced Sampling Techniques
inferred← citeshttps://doi.org/10.1021/acscatal.5c02431openalex-snapshot
A Machine Learning-Driven, Probability-Based Approach to Enzyme Catalysis
inferred← citeshttps://doi.org/10.1021/acscatal.7b04400openalex-snapshot
A Buried Water Molecule Influences Reactivity in α-Amylase on a Subnanosecond Time Scale
inferred← citeshttps://doi.org/10.1021/acsomega.3c01819openalex-snapshot
Phytochemical Composition, In Vitro Antimicrobial, Antioxidant, and Enzyme Inhibition Activities, and In Silico Molecular Docking and Dynamics Simulations of Centaurea lycaonica : A Computational and Experimental Approach
inferred← citeshttps://doi.org/10.1021/acssuschemeng.3c02292openalex-snapshot
Real-Time Monitoring of Glycemic Starch Using Biosynthesized Gold Nanoparticle–Amylase Composites
inferred← citeshttps://doi.org/10.1021/ar400132gopenalex-snapshot
Naturally Occurring Sulfonium-Ion Glucosidase Inhibitors and Their Derivatives: A Promising Class of Potential Antidiabetic Agents
inferred← citeshttps://doi.org/10.1021/bi049015qopenalex-snapshot
Single Amino Acid Mutations Interchange the Reaction Specificities of Cyclodextrin Glycosyltransferase and the Acarbose-Modifying Enzyme Acarviosyl Transferase
inferred← citeshttps://doi.org/10.1021/bi602408jopenalex-snapshot
Identification of Acceptor Substrate Binding Subsites +2 and +3 in the Amylomaltase fromThermus thermophilusHB8
inferred← citeshttps://doi.org/10.1021/bi701652topenalex-snapshot
Alternative Catalytic Anions Differentially Modulate Human α-Amylase Activity and Specificity,
inferred← citeshttps://doi.org/10.1021/bi800852aopenalex-snapshot
Structural Basis of UDP-galactose Binding by α-1,3-Galactosyltransferase (α3GT): Role of Negative Charge on Aspartic Acid 316 in Structure and Activity
inferred← citeshttps://doi.org/10.1021/bi901400popenalex-snapshot
Directed “in Situ” Inhibitor Elongation as a Strategy To Structurally Characterize the Covalent Glycosyl-Enzyme Intermediate of Human Pancreatic α-Amylase,
inferred← citeshttps://doi.org/10.1021/ct700116nopenalex-snapshot
Stability of the Free and Bound Microstates of a Mobile Loop of α-Amylase Obtained from the Absolute Entropy and Free Energy
inferred← citeshttps://doi.org/10.1021/jf502667zopenalex-snapshot
α-Amylase Inhibitory Triterpene from Abrus precatorius Leaves
inferred← citeshttps://doi.org/10.1021/jf5032907openalex-snapshot
Effects of Oolong Tea Polyphenols, EGCG, and EGCG3″Me on Pancreatic α-Amylase Activity in Vitro
inferred← citeshttps://doi.org/10.1021/jf703655kopenalex-snapshot
Enzymatic Synthesis of a Selective Inhibitor for α-Glucosidases: α-Acarviosinyl-(1→9)-3-α- d -glucopyranosylpropen
inferred← citeshttps://doi.org/10.1021/jm301273uopenalex-snapshot
Order and Disorder: Differential Structural Impacts of Myricetin and Ethyl Caffeate on Human Amylase, an Antidiabetic Target
inferred← citeshttps://doi.org/10.1021/jm800115xopenalex-snapshot
Flavonoids for Controlling Starch Digestion: Structural Requirements for Inhibiting Human α-Amylase
inferred← citeshttps://doi.org/10.1021/jo702565qopenalex-snapshot
Synthesis and Testing of 2-Deoxy-2,2-Dihaloglycosides as Mechanism-Based Inhibitors of α-Glycosidases
inferred← citeshttps://doi.org/10.1021/jp801827fopenalex-snapshot
Entropy and Free Energy of a Mobile Protein Loop in Explicit Water
inferred← citeshttps://doi.org/10.1023/a:1025072520607openalex-snapshot
Crystal Structure of the Pig Pancreatic α-Amylase Complexed with Malto-Oligosaccharides
inferred← citeshttps://doi.org/10.1023/b:jopc.0000039552.94529.95openalex-snapshot
Crystal Structure of the Pig Pancreatic α-Amylase Complexed with ρ-Nitrophenyl-α-D-Maltoside-Flexibility in the Active Site
inferred← citeshttps://doi.org/10.1038/84168openalex-snapshot
Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs.
inferred← citeshttps://doi.org/10.1038/nchembio.1865openalex-snapshot
The amylase inhibitor montbretin A reveals a new glycosidase inhibition motif
inferred← citeshttps://doi.org/10.1038/s41467-020-16341-2openalex-snapshot
Computer simulations explain the anomalous temperature optimum in a cold-adapted enzyme
inferred← citeshttps://doi.org/10.1038/s41598-018-23736-1openalex-snapshot
Acute metabolic actions of the major polyphenols in chamomile: an in vitro mechanistic study on their potential to attenuate postprandial hyperglycaemia
inferred← citeshttps://doi.org/10.1039/b411473fopenalex-snapshot
New aminocyclitols as modulators of glucosylceramide metabolism
inferred← citeshttps://doi.org/10.1039/b926600copenalex-snapshot
Casuarine-6-O-α-d-glucoside and its analogues are tight binding inhibitors of insect and bacterial trehalases
inferred← citeshttps://doi.org/10.1039/c004698copenalex-snapshot
The biological potential of flavones
inferred← citeshttps://doi.org/10.1039/c1mb05008gopenalex-snapshot
Interaction of natural polyphenols with α-amylase in vitro : molecular property–affinity relationship aspect
inferred← citeshttps://doi.org/10.1039/c2ib00152gopenalex-snapshot
CdTe/CdSe quantum dots improve the binding affinities between α-amylase and polyphenols
inferred← citeshttps://doi.org/10.1039/c9sc02610jopenalex-snapshot
Synthesis of montbretin A analogues yields potent competitive inhibitors of human pancreatic α-amylase
inferred← citeshttps://doi.org/10.1039/d0ra01553aopenalex-snapshot
Cu/TEMPO catalyzed dehydrogenative 1,3-dipolar cycloaddition in the synthesis of spirooxindoles as potential antidiabetic agents
inferred← citeshttps://doi.org/10.1039/d1fo02995aopenalex-snapshot
Inhibitory activity of flavonoids against human sucrase-isomaltase (α-glucosidase) activity in a Caco-2/TC7 cellular model
inferred← citeshttps://doi.org/10.1039/d4fo00414kopenalex-snapshot
Inhibitory effect of extracts from edible parts of nuts on α-amylase activity: a systematic review
inferred← citeshttps://doi.org/10.1039/d6sc02180hopenalex-snapshot
Methods for the establishment of enzymatic mechanisms – from QM to ML
inferred← citeshttps://doi.org/10.1046/j.1432-1033.2002.03185.xopenalex-snapshot
Barley α‐amylase Met53 situated at the high‐affinity subsite −2 belongs to a substrate binding motif in the β→α loop 2 of the catalytic (β/α)8‐barrel and is critical for activity and substrate specificity
inferred← citeshttps://doi.org/10.1046/j.1432-1033.2002.03212.xopenalex-snapshot
Subsite mapping of the binding region of α‐amylases with a computer program
inferred← citeshttps://doi.org/10.1046/j.1432-1033.2003.03733.xopenalex-snapshot
On the mechanism of α‐amylase
inferred← citeshttps://doi.org/10.1046/j.1523-1755.62.s81.5.xopenalex-snapshot
Pharmacokinetics of icodextrin in peritoneal dialysis patients
inferred← citeshttps://doi.org/10.1073/pnas.2416621121openalex-snapshot
Correlating enzymatic reactivity for different substrates using transferable data-driven collective variables
inferred← citeshttps://doi.org/10.1074/jbc.m009257200openalex-snapshot
On the Role of Conserved Histidine 106 in 10-Formyltetrahydrofolate Dehydrogenase Catalysis
inferred← citeshttps://doi.org/10.1074/jbc.m111.314658openalex-snapshot
Functional Regulation of Sugar Assimilation by N-Glycan-specific Interaction of Pancreatic α-Amylase with Glycoproteins of Duodenal Brush Border Membrane
inferred← citeshttps://doi.org/10.1074/jbc.m112.351858openalex-snapshot
Modulation of Starch Digestion for Slow Glucose Release through “Toggling” of Activities of Mucosal α-Glucosidases
inferred← citeshttps://doi.org/10.1074/jbc.m211339200openalex-snapshot
Differential Regulation of a Hyperthermophilic α-Amylase with a Novel (Ca,Zn) Two-metal Center by Zinc
inferred← citeshttps://doi.org/10.1074/jbc.m312825200openalex-snapshot
Tyrosine 105 and Threonine 212 at Outermost Substrate Binding Subsites –6 and +4 Control Substrate Specificity, Oligosaccharide Cleavage Patterns, and Multiple Binding Modes of Barley α-Amylase 1
inferred← citeshttps://doi.org/10.1074/jbc.m406804200openalex-snapshot
In Situ Extension as an Approach for Identifying Novel α-Amylase Inhibitors
inferred← citeshttps://doi.org/10.1074/jbc.m505515200openalex-snapshot
Oligosaccharide Binding to Barley α-Amylase 1
inferred← citeshttps://doi.org/10.1074/jbc.m703138200openalex-snapshot
Clostridium difficile Glucosyltransferase Toxin B-essential Amino Acids for Substrate Binding
inferred← citeshttps://doi.org/10.1080/07328300008544151openalex-snapshot
Acarbose Binding Specificity with Oral Bacterial Glucosyltransferase
inferred← citeshttps://doi.org/10.1080/07391102.2020.1801507openalex-snapshot
Molecular dynamics simulation for screening phytochemicals as α-amylase inhibitors from medicinal plants
inferred← citeshttps://doi.org/10.1080/07391102.2023.2175372openalex-snapshot
Synthesis, in silico , in vitro and in vivo studies of novel natural-based arylidenes curcumin as potential glycohydrolase digestive enzymes inhibitors
inferred← citeshttps://doi.org/10.1080/07391102.2023.2227721openalex-snapshot
Targeting α-amylase enzyme through multi-fold structure-based virtual screening and molecular dynamic simulation
inferred← citeshttps://doi.org/10.1080/07391102.2023.2248265openalex-snapshot
Phytochemical profiling and evaluation of the antidiabetic potential of Ichnocarpus frutescens (Krishna Sariva): kinetic study, molecular modelling, and free energy approach
inferred← citeshttps://doi.org/10.1080/0972060x.2025.2471856openalex-snapshot
Assessing antioxidant potential and α-amylase inhibitory activity of essential oil from Neolitsea bidoupensis leaves
inferred← citeshttps://doi.org/10.1080/0972060x.2026.2652894openalex-snapshot
GC-MS profiling, antioxidant and enzyme inhibitory activities of Enydra fluctuans essential oil
inferred← citeshttps://doi.org/10.1080/0972060x.2026.2724308openalex-snapshot
Unraveling chemical composition and bioactivities of Buddleja asiatica aerial part essential oil
inferred← citeshttps://doi.org/10.1080/10408390903372466openalex-snapshot
Slowly Digestible Starch: Concept, Mechanism, and Proposed Extended Glycemic Index
inferred← citeshttps://doi.org/10.1080/10408398.2010.548108openalex-snapshot
A Review on Structure–Activity Relationship of Dietary Polyphenols Inhibiting α-Amylase
inferred← citeshttps://doi.org/10.1080/10408398.2014.922043openalex-snapshot
Mechanisms of starch digestion by α -amylase—Structural basis for kinetic properties
inferred← citeshttps://doi.org/10.1080/10408398.2020.1862755openalex-snapshot
Flavonoids as potential agents in the management of type 2 diabetes through the modulation of α-amylase and α-glucosidase activity: a review
inferred← citeshttps://doi.org/10.1080/10799893.2020.1800734openalex-snapshot
In silico assessment of potential leads identified from Bauhinia rufescens Lam. as α-glucosidase and α-amylase inhibitors
inferred← citeshttps://doi.org/10.1080/10942912.2024.2387435openalex-snapshot
Integrated assessment of phytochemicals, Antilipase, hemoglobin antiglycation, antihyperglycemic, antifungal and antibacterial properties of vetiveria zizanioides (L.) Nash
inferred← citeshttps://doi.org/10.1080/14756366.2018.1558221openalex-snapshot
Evaluation of a flavonoids library for inhibition of pancreatic α-amylase towards a structure–activity relationship
inferred← citeshttps://doi.org/10.1080/714040434openalex-snapshot
Open Pore Block of Connexin26 and Connexin32 Hemichannels by Neutral, Acidic and Basic Glycoconjugates
inferred← citeshttps://doi.org/10.1093/glycob/cwt044openalex-snapshot
The structure of the Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding mode
inferred← citeshttps://doi.org/10.1093/jn/137.7.1725openalex-snapshot
Contribution of Mucosal Maltase-Glucoamylase Activities to Mouse Small Intestinal Starch α-Glucogenesis3
inferred← citeshttps://doi.org/10.1093/jn/138.4.685openalex-snapshot
Luminal Starch Substrate “Brake” on Maltase-Glucoamylase Activity Is Located within the Glucoamylase Subunit3
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