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The Active Center of a Mammalian .alpha.-Amylase. Structure of the Complex of a Pancreatic .alpha.-Amylase with a Carbohydrate Inhibitor Refined to 2.2-.ANG. Resolution
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Outgoing claims: the papers this work cites, builds on, or argues with.
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Multiple Attack Mechanism in the Porcine Pancreatic α-Amylase Hydrolysis of Amylose and Amylopectin
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Structure and Molecular Model Refinement of Pig Pancreatic α-Amylase at 2·1 Å Resolution
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Protein-Oligosaccharide Interactions: Lysozyme, Phosphorylase, Amylases
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Multiple attack and polarity of action of porcine pancreatic α-amylase
inferredcites →https://doi.org/10.1016/0003-9861(85)90497-7openalex-snapshot
The effect of substrate modification on porcine pancreatic α-amylase subsite binding: Hydrolysis of substrates containing 2-deoxy-d-glucose and 2-amino-2-deoxy-d-glucose
inferredcites →https://doi.org/10.1016/0005-2795(67)90478-3openalex-snapshot
Isolation of two amylases in porcine pancreas
inferredcites →https://doi.org/10.1016/0006-291x(84)90441-8openalex-snapshot
Subsite profile of the active center of porcine pancreatic α-amylase. Kinetic studies using maltooligosaccharides as substrates
inferredcites →https://doi.org/10.1016/0006-3002(58)90228-2openalex-snapshot
Substrate cleavage points of α- and β-amylases
inferredcites →https://doi.org/10.1016/0008-6215(84)85072-7openalex-snapshot
The solution conformation of acarbose
inferredcites →https://doi.org/10.1016/0014-5793(73)80079-1openalex-snapshot
The metal specificity of mammalian α‐amylase as revealed by enzyme activity and structural probes
inferredcites →https://doi.org/10.1016/0014-5793(81)80624-2openalex-snapshot
Amino acid sequence of hog pancreatic α‐amylase isoenzyme I
inferredcites →https://doi.org/10.1016/0022-2836(91)90021-wopenalex-snapshot
Lysozyme revisited: Crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D
inferredcites →https://doi.org/10.1016/0022-5193(68)90141-0openalex-snapshot
A possible mechanism for amylase catalysis
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[27] Multiwire area X-ray diffractometers
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Complete amino acid sequence and location of the five disulfide bridges in porcine pancreatic α-amylase
inferredcites →https://doi.org/10.1016/0167-4838(89)90038-1openalex-snapshot
Detection of a covalent intermediate in the mechanism of action of porcine pancreatic α-amylase by using 13C nuclear magnetic resonance
inferredcites →https://doi.org/10.1016/0959-440x(91)90172-popenalex-snapshot
Atomic features of protein-carbohydrate interactions
inferredcites →https://doi.org/10.1016/s0008-6215(00)80118-4openalex-snapshot
The active site of porcine-pancreatic alpha-amylase: Factors contributing to catalysis
inferredcites →https://doi.org/10.1016/s0008-6215(00)90457-9openalex-snapshot
The effect of substrate modification on binding of porcine pancreatic alpha amylase: Hydrolysis of modified amylose containing d-allose residues
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/s0021-9258(18)69691-7openalex-snapshot
Metal Content of α-Amylases of Various Origins
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The three-dimensional structure of acarbose bound to glycogen phosphorylase.
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Conformation of Polypeptides and Proteins
inferredcites →https://doi.org/10.1016/s0300-9084(81)80149-6openalex-snapshot
Porcine pancreatic α-amylase I: Sequence between the 35 th and 410th amino acid
inferredcites →https://doi.org/10.1016/s1874-6047(08)60089-xopenalex-snapshot
6 Plant and Animal Amylases
inferredcites →https://doi.org/10.1021/bi00075a020openalex-snapshot
Substrate recognition at the binding site in mammalian pancreatic .alpha.-amylases
inferredcites →https://doi.org/10.1021/bi00077a015openalex-snapshot
Three histidine residues in the active center of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011: effects of the replacement on pH dependence and transition-state stabilization
inferredcites →https://doi.org/10.1021/bi00152a009openalex-snapshot
Catalytic center of cyclodextrin glycosyltransferase derived from x-ray structure analysis combined with site-directed mutagenesis
inferredcites →https://doi.org/10.1021/bi00303a031openalex-snapshot
Some aspects of the mechanism of complexation of red kidney bean .alpha.-amylase inhibitor and .alpha.-amylase
inferredcites →https://doi.org/10.1021/bi00319a019openalex-snapshot
Porcine pancreatic .alpha.-amylase hydrolysis of hydroxyethylated amylose and specificity of subsite binding
inferredcites →https://doi.org/10.1021/bi00482a025openalex-snapshot
Substrate-dependent shift of optimum pH in porcine pancreatic .alpha.-amylase-catalyzed reactions
inferredcites →https://doi.org/10.1038/scientificamerican1166-78openalex-snapshot
The Three-Dimensional Structure of an Enzyme Molecule
inferredcites →https://doi.org/10.1042/bj2590145openalex-snapshot
A super-secondary structure predicted to be common to several α-1,4- d -glucan-cleaving enzymes
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a134659openalex-snapshot
Structure and Possible Catalytic Residues of Taka-Amylase A
inferredcites →https://doi.org/10.1098/rspb.1967.0034openalex-snapshot
On the conformation of the hen egg-white lysozyme molecule
inferredcites →https://doi.org/10.1098/rspb.1967.0035openalex-snapshot
Crystallographic studies of the activity of hen egg-white lysozyme
inferredcites →https://doi.org/10.1107/s0108768191001908openalex-snapshot
Solution of the structure of Aspergillus niger acid α-amylase by combined molecular replacement and multiple isomorphous replacement methods
inferredcites →https://doi.org/10.1107/s0108768191001970openalex-snapshot
Structure and molecular model refinement of Aspergillus oryzae (TAKA) α-amylase: an application of the simulated-annealing method
inferredcites →https://doi.org/10.1107/s0567740880003378openalex-snapshot
The three-dimensional structure of α-amylase from porcine pancreas at 5 Å resolution – the active-site location
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/10.1126/science.235.4787.458openalex-snapshot
Crystallographic R Factor Refinement by Molecular Dynamics
inferredcites →https://doi.org/10.1126/science.35.899.458openalex-snapshot
The Accumulation of Oil and Gas in Sandstone
inferredcites →https://doi.org/10.1351/pac198961071293openalex-snapshot
Protein-carbohydrate interactions: basic molecular features
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Amylose chain behavior in an interacting context I. Influence of a nonchair ring on the maltose conformations
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Amylose chain behavior in an interacting context II. Molecular modeling of a maltopentaose fragment in the barley ?-amylase catalytic site
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Amylose chain behavior in an interacting context. III. Complete occupancy of the AMY2 barley ?-amylase cleft and comparison with biochemical data
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Cold‐Adapted Microorganisms: Adaptation Strategies and Biotechnological Potential
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X‐Ray Crystallography in Drug Discovery
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Alpha-amylase inhibitors selected from a combinatorial library of a cellulose binding domain scaffold
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Enzymes, 4. Non‐food Application
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Enzymolysis Modes Trigger Diversity in Inhibitor‐α‐Amylase Aggregating Behaviors and Activity Inhibition: A New Insight Into Enzyme Inhibition
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Characterization and application of grafted polypropylene and polystyrene treated with epichlorohydrin coupled with cellulose or starch for immobilization processes
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MOLECULAR CLONING OF SOLUBLE TREHALASE FROM Chironomus riparius LARVAE, ITS HETEROLOGOUS EXPRESSION IN Escherichia coli AND BIOINFORMATIC ANALYSIS
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Putative implication of α‐amylase loop 7 in the mechanism of substrate binding and reaction products release
inferred← citeshttps://doi.org/10.1002/bit.22083openalex-snapshot
Engineering of the α‐amylase from Geobacillus stearothermophilus US100 for detergent incorporation
inferred← citeshttps://doi.org/10.1002/cbic.201200272openalex-snapshot
Kinetics Studies on the Inhibition Mechanism of Pancreatic α‐Amylase by Glycoconjugated 1H‐1,2,3‐Triazoles: A New Class of Inhibitors with Hypoglycemiant Activity
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Towards Tuneable Retaining Glycosidase‐Inhibiting Peptides by Mimicry of a Plant Flavonol Warhead
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Structure‐based discovery of a new affinity ligand to pancreatic α‐amylase
inferred← citeshttps://doi.org/10.1002/pro.5560040414openalex-snapshot
Carbohydrate binding sites in a pancreatic α‐amylase‐substrate complex, derived from X‐ray structure analysis at 2.1 Å resolution
inferred← citeshttps://doi.org/10.1002/pro.5560040908openalex-snapshot
The structure of human pancreatic α -amylase at 1.8 Å resolution and comparisons with related enzymes
inferred← citeshttps://doi.org/10.1002/pro.5560061102openalex-snapshot
Structure of a pancreatic α‐amylase bound to a substrate analogue at 2.03 Å resolution
inferred← citeshttps://doi.org/10.1002/pro.5560070304openalex-snapshot
Crystal structures of the psychrophilic α‐amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor
inferred← citeshttps://doi.org/10.1002/prot.1044openalex-snapshot
Enzymatic circularization of a malto‐octaose linear chain studied by stochastic reaction path calculations on cyclodextrin glycosyltransferase
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The alteration of structural network upon transient association between proteins studied using graph theory
inferred← citeshttps://doi.org/10.1002/ptr.7480openalex-snapshot
Common bean ( Phaseolus vulgaris L.) α‐amylase inhibitors as safe nutraceutical strategy against diabetes and obesity: An update review
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Hybrid Pyrazole‐Tetrazole Derivatives with High α‐Amylase Inhibition Activity: Synthesis, Biological Evaluation and Docking Study
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Human α‐amylase and starch digestion: An interesting marriage
inferred← citeshttps://doi.org/10.1006/abbi.1999.1580openalex-snapshot
Slow-Binding Inhibition of Branching Enzyme by the Pseudooligosaccharide BAY e4609
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Localization of C-Terminal Domains Required for the Maximal Activity or for Determination of Substrate Preference of Maize Branching Enzymes
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The Mechanism of Salivary Amylase Hydrolysis: Role of Residues at Subsite S2′
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Crystal structure of a maltotetraose-formingexo-amylase from Pseudomonas stutzeri 1 1Edited by R. Huber
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Crystal structures of a mutant maltotetraose-forming exo-amylase cocrystallized with maltopentaose 1 1Edited by R. Huber
inferred← citeshttps://doi.org/10.1006/jmbi.1997.1599openalex-snapshot
Crystal structure of a catalytic-site mutant α-amylase from Bacillus subtilis complexed with maltopentaose
inferred← citeshttps://doi.org/10.1006/jmbi.1998.1667openalex-snapshot
Crystal structure of yellow meal worm α-amylase at 1.64 Å resolution
inferred← citeshttps://doi.org/10.1006/jmbi.1998.1683openalex-snapshot
Molecular structure of a barley α-amylase-inhibitor complex: implications for starch binding and catalysis
inferred← citeshttps://doi.org/10.1006/jmbi.1998.1992openalex-snapshot
Three-dimensional structure of Pseudomonas isoamylase at 2.2 Å resolution 1 1Edited by R. Huber
inferred← citeshttps://doi.org/10.1006/jmbi.1999.2647openalex-snapshot
Crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 Å resolution
inferred← citeshttps://doi.org/10.1006/jmbi.1999.3503openalex-snapshot
Crystal structure of amylomaltase from Thermus aquaticus, a glycosyltransferase catalysing the production of large cyclic glucans
inferred← citeshttps://doi.org/10.1006/jmbi.2000.3722openalex-snapshot
Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the ph optimum of a glycosidase 1 1Edited by M. F. Summers
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Crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus 1 1Edited by D. Rees
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The crystal structure of Thermotoga maritima maltosyltransferase and its implications for the molecular basis of the novel transfer specificity
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Structural and Functional Studies of Peptide–Carbohydrate Mimicry
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Macromolecular Motion at the Nanoscale of Enzymes Working on Polysaccharides
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Polysaccharide Degradation
inferred← citeshttps://doi.org/10.1007/978-3-642-56874-9_46openalex-snapshot
Biosynthesis and Degradation
inferred← citeshttps://doi.org/10.1007/978-3-662-03720-1_2openalex-snapshot
Three-dimensional Structural Variations and Functional Implications in α-Amylases
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Psychrophilic enzymes: insights into cold adaptation and catalysis from the first high resolution crystal structures
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Psychrophilic Enzymes: Cool Responses to Chilly Problems
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α-Amylase Inhibitor’s Performance in the Control of Diabetes Mellitus: An Application of Computational Biology
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Psychrophiles as the Source for Potential Industrial Psychrozymes
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Sequence of archaealMethanococcus jannaschii α-amylase contains features of families 13 and 57 of glycosyl hydrolases: A trace of their common ancestor?
inferred← citeshttps://doi.org/10.1007/pl00006236openalex-snapshot
Domain Evolution in the α-Amylase Family
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Molecular adaptations to cold in psychrophilic enzymes
inferred← citeshttps://doi.org/10.1007/s00018-013-1388-zopenalex-snapshot
α-Amylase: an enzyme specificity found in various families of glycoside hydrolases
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Psychrophilic enzymes: molecular basis of cold adaptation
inferred← citeshttps://doi.org/10.1007/s00253-003-1477-2openalex-snapshot
Biotechnology and molecular biology of the ?-glucosidase inhibitor acarbose
inferred← citeshttps://doi.org/10.1007/s00253-007-1287-zopenalex-snapshot
Characterisation of mutagenised acid-resistant alpha-amylase expressed in Bacillus subtilis WB600
inferred← citeshttps://doi.org/10.1007/s00253-008-1580-5openalex-snapshot
Acid stabilization of Bacillus licheniformis alpha amylase through introduction of mutations
inferred← citeshttps://doi.org/10.1007/s00253-019-10194-6openalex-snapshot
Importance of Trp139 in the product specificity of a maltooligosaccharide-forming amylase from Bacillus stearothermophilus STB04
inferred← citeshttps://doi.org/10.1007/s004250050195openalex-snapshot
Molecular characterization of a bean α-amylase inhibitor that inhibits the α-amylase of the Mexican bean weevil Zabrotes subfasciatus
inferred← citeshttps://doi.org/10.1007/s10822-014-9754-yopenalex-snapshot
New insight in the structural features of haloadaptation in α-amylases from halophilic Archaea following homology modeling strategy: folded and stable conformation maintained through low hydrophobicity and highly negative charged surface
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Mechanistic Inhibition of α-Amylase by Corn Peptide: Site-Specific Binding Induces Conformational Destabilization and Enzymatic Activity Suppression
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Phytochemicals from Nigerian medicinal plants modulate therapeutically-relevant diabetes targets: insight from computational direction
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Psychrophilic Enzymes: Cool Responses to Chilly Problems
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Subsite mapping of porcine pancreatic alpha-amylase I and II using 4-nitrophenyl-α-maltooligosaccharides
inferred← citeshttps://doi.org/10.1016/0008-6215(95)00365-7openalex-snapshot
Elucidation of the subsite structure of bacterial saccharifying alpha-amylase and its mode of degradation of maltose
inferred← citeshttps://doi.org/10.1016/0014-5793(95)00291-gopenalex-snapshot
Isozyme hybrids within the protruding third loop domain of the barley α‐amylase (β/α)8‐barrel implication for BASI sensitivity and substrate affinity
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Structural consequences of neopullulanase mutations
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Mechanisms of enzymatic glycoside hydrolysis
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A cyclic phosphonamidate analogue of glucose as a selective inhibitor of inverting glycosidases
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Glycosyl Transferase Mechanisms
inferred← citeshttps://doi.org/10.1016/b978-0-12-374546-0.00011-0openalex-snapshot
Cytoplasmic carbohydrate molecules
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Enzymes and Their Action on Starch
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Interaction of starches and amylases—An in silico study
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Structure of cyclodextrin glucanotransferases
inferred← citeshttps://doi.org/10.1016/b978-012492543-4/50015-5openalex-snapshot
Transferring Groups by Displacement Reactions
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Amylase and Cellulase Structure and Function
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Structural studies of a Phe256Trp mutant of human salivary α-amylase: implications for the role of a conserved water molecule in enzyme activity
inferred← citeshttps://doi.org/10.1016/j.bbagen.2005.03.004openalex-snapshot
Differential scanning calorimetric studies of a Bacillus halodurans α-amylase
inferred← citeshttps://doi.org/10.1016/j.bbagen.2012.12.028openalex-snapshot
The surface structure of a complex substrate revealed by enzyme kinetics and Freundlich constants for α-amylase interaction with the surface of starch
inferred← citeshttps://doi.org/10.1016/j.bbapap.2003.10.012openalex-snapshot
Structural basis for the inhibition of mammalian and insect α-amylases by plant protein inhibitors
inferred← citeshttps://doi.org/10.1016/j.bbapap.2003.11.001openalex-snapshot
Porcine pancreatic α-amylase inhibition by the kidney bean (Phaseolus vulgaris) inhibitor (α-AI1) and structural changes in the α-amylase inhibitor complex
inferred← citeshttps://doi.org/10.1016/j.bbapap.2008.10.012openalex-snapshot
Evidence for pentagalloyl glucose binding to human salivary α-amylase through aromatic amino acid residues
inferred← citeshttps://doi.org/10.1016/j.bbapap.2012.05.005openalex-snapshot
Structural and functional characterization of recombinant medaka fish alpha-amylase expressed in yeast Pichia pastoris
inferred← citeshttps://doi.org/10.1016/j.bioorg.2019.02.040openalex-snapshot
Cucurbitane-type compounds from Momordica charantia: Isolation, in vitro antidiabetic, anti-inflammatory activities and in silico modeling approaches
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Dual α-amylase and α-glucosidase inhibitors: recent progress from natural and synthetic resources
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Syntheses of cellotriose and cellotetraose analogues as transition state mimics for mechanistic studies of cellulases
inferred← citeshttps://doi.org/10.1016/j.bmcl.2011.02.062openalex-snapshot
Selective α-glucosidase substrates and inhibitors containing short aromatic peptidyl moieties
inferred← citeshttps://doi.org/10.1016/j.carres.2006.10.028openalex-snapshot
Formation of covalent β-linked carbohydrate–enzyme intermediates during the reactions catalyzed by α-amylases
inferred← citeshttps://doi.org/10.1016/j.carres.2012.07.004openalex-snapshot
Studies of the effect of maltose on the direct binding of porcine pancreatic α-amylase to maize starch
inferred← citeshttps://doi.org/10.1016/j.carres.2021.108317openalex-snapshot
An overview of therapeutic potential of N-alkylated 1-deoxynojirimycin congeners
inferred← citeshttps://doi.org/10.1016/j.cbpa.2006.08.003openalex-snapshot
Cloning and characterization of α-amylase from Atlantic salmon (Salmo salar L.)
inferred← citeshttps://doi.org/10.1016/j.chembiol.2005.10.005openalex-snapshot
De Novo Design of α-Amylase Inhibitor: A Small Linear Mimetic of Macromolecular Proteinaceous Ligands
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2006.03.022openalex-snapshot
Oxidatively stable maltopentaose-producing α-amylase from a deep-sea Bacillus isolate, and mechanism of its oxidative stability validated by site-directed mutagenesis
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2008.05.006openalex-snapshot
Purification and characterization of five alkaline, thermotolerant, and maltotetraose-producing α-amylases from Bacillus halodurans MS-2-5, and production of recombinant enzymes in Escherichia coli
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Inhibition of enzymes associated with obesity by the polyphenol-rich extracts of Hibiscus sabdariffa
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Effect of starch-catechin interaction on regulation of starch digestibility during hot-extrusion 3D printing: Structural analysis and simulation study
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2022.108005openalex-snapshot
Effects of chickpea protein fractions on α-amylase activity in digestion
inferred← citeshttps://doi.org/10.1016/j.ibmb.2024.104097openalex-snapshot
Structural and functional comparisons of salivary α-glucosidases from the mosquito vectors Aedes aegypti, Anopheles gambiae, and Culex quinquefasciatus
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2019.11.006openalex-snapshot
Structure of maltotetraose-forming amylase from Pseudomonas saccharophila STB07 provides insights into its product specificity
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2020.07.125openalex-snapshot
Chain conformation of an acidic polysaccharide from green tea and related mechanism of α-amylase inhibitory activity
inferred← citeshttps://doi.org/10.1016/j.jbiotec.2012.12.007openalex-snapshot
Structure-based engineering of histidine residues in the catalytic domain of α-amylase from Bacillus subtilis for improved protein stability and catalytic efficiency under acidic conditions
inferred← citeshttps://doi.org/10.1016/j.jksus.2024.103521openalex-snapshot
Purification, characterization and molecular docking studies of analogous alpha amylase inhibitor compounds
inferred← citeshttps://doi.org/10.1016/j.jmb.2003.07.014openalex-snapshot
Temperature Adaptation of Proteins: Engineering Mesophilic-like Activity and Stability in a Cold-adapted α-Amylase
inferred← citeshttps://doi.org/10.1016/j.jmb.2003.09.056openalex-snapshot
The Structural Bases of the Processive Degradation of ι-Carrageenan, a Main Cell Wall Polysaccharide of Red Algae
inferred← citeshttps://doi.org/10.1016/j.jmb.2004.03.062openalex-snapshot
Crystal Structure of α-Galactosidase from Trichoderma reesei and Its Complex with Galactose: Implications for Catalytic Mechanism
inferred← citeshttps://doi.org/10.1016/j.jmb.2005.02.011openalex-snapshot
Crystal Structure of Maltooligosyltrehalose Trehalohydrolase from Deinococcus radiodurans in Complex with Disaccharides
inferred← citeshttps://doi.org/10.1016/j.jmb.2006.03.004openalex-snapshot
Kinetics and Energetics of Ligand Binding Determined by Microcalorimetry: Insights into Active Site Mobility in a Psychrophilic α-Amylase
inferred← citeshttps://doi.org/10.1016/j.jmb.2008.03.016openalex-snapshot
Substrate Recognition Mechanism of α-1,6-Glucosidic Linkage Hydrolyzing Enzyme, Dextran Glucosidase from Streptococcus mutans
inferred← citeshttps://doi.org/10.1016/j.jmb.2008.09.089openalex-snapshot
Probing the Role of Aromatic Residues at the Secondary Saccharide-Binding Sites of Human Salivary α-Amylase in Substrate Hydrolysis and Bacterial Binding
inferred← citeshttps://doi.org/10.1016/j.molstruc.2021.131807openalex-snapshot
Synthesis and molecular docking studies of 5-acetyl-2-(arylidenehydrazin-1-yl)-4-methyl-1,3-thiazoles as α-amylase inhibitors
inferred← citeshttps://doi.org/10.1016/j.molstruc.2022.132398openalex-snapshot
New spiropyrrolothiazole derivatives bearing an oxazolone moiety as potential antidiabetic agent: Design, synthesis, crystal structure, Hirshfeld surface analysis, ADME and molecular docking studies
inferred← citeshttps://doi.org/10.1016/j.molstruc.2024.139482openalex-snapshot
Anti-diabetic, anti-bacterial and anti-oxidant potential of new biologically active thiazole-derivatives: Experimental and molecular docking studies
inferred← citeshttps://doi.org/10.1016/j.prmcm.2026.100786openalex-snapshot
Phytochemical profiling of Ocimum sanctum L. varieties and prediction of rosmarinic acid as a chemical marker for dermatological applications via in silico approaches
inferred← citeshttps://doi.org/10.1016/j.procbio.2017.04.040openalex-snapshot
Improvement of the acid stability of Bacillus licheniformis alpha amylase by site-directed mutagenesis
inferred← citeshttps://doi.org/10.1016/j.saa.2018.08.057openalex-snapshot
Inhibition of α-amylase by flavonoids: Structure activity relationship (SAR)
inferred← citeshttps://doi.org/10.1016/j.synbio.2024.03.006openalex-snapshot
Acarbose glycosylation by AcbE for the production of acarstatins with enhanced α-amylase inhibitory activity
inferred← citeshttps://doi.org/10.1016/j.tet.2011.08.012openalex-snapshot
Synthesis and α-amylase inhibitory activity of glucose–deoxynojirimycin conjugates
inferred← citeshttps://doi.org/10.1016/j.tetlet.2016.02.053openalex-snapshot
Synthesis and study of the pancreatic α-amylase inhibitory activity of methyl acarviosin and its derivatives
inferred← citeshttps://doi.org/10.1016/s0003-9969(98)00112-5openalex-snapshot
The roles of histidine residues at the starch-binding site in streptococcal-binding activities of human salivary amylase
inferred← citeshttps://doi.org/10.1016/s0008-6215(03)00293-3openalex-snapshot
Study of the inhibition of four alpha amylases by acarbose and its 4IV-α-maltohexaosyl and 4IV-α-maltododecaosyl analogues
inferred← citeshttps://doi.org/10.1016/s0008-6215(96)00310-2openalex-snapshot
Action pattern of porcine pancreatic alpha-amylase on three different series of β-maltooligosaccharide glycosides
inferred← citeshttps://doi.org/10.1016/s0008-6215(96)00320-5openalex-snapshot
d-Glyconhydroximolactams strongly inhibit α-glycosidases
inferred← citeshttps://doi.org/10.1016/s0008-6215(97)00150-xopenalex-snapshot
Study of the action of human salivary alpha-amylase on 2-chloro-4-nitrophenyl α-maltotrioside in the presence of potassium thiocyanate
inferred← citeshttps://doi.org/10.1016/s0008-6215(98)00029-9openalex-snapshot
New enzymatic synthesis of 63-modified maltooligosaccharides and their inhibitory activities for human α-amylases
inferred← citeshttps://doi.org/10.1016/s0014-5793(03)00286-2openalex-snapshot
The fully conserved Asp residue in conserved sequence region I of the α‐amylase family is crucial for the catalytic site architecture and activity
inferred← citeshttps://doi.org/10.1016/s0014-5793(96)01131-3openalex-snapshot
RBI, a one‐domain α‐amylase/trypsin inhibitor with completely independent binding sites
inferred← citeshttps://doi.org/10.1016/s0022-2836(02)00570-3openalex-snapshot
Crystal Structure of Thermotoga maritima 4-α-Glucanotransferase and its Acarbose Complex: Implications for Substrate Specificity and Catalysis
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/s0065-2318(00)55007-0openalex-snapshot
A fresh understanding of the stereochemical behavior of glycosylases: Structural distinction of “inverting” (2-MCO-type) versus “retaining” (1-MCO-type) enzymes
inferred← citeshttps://doi.org/10.1016/s0079-6107(97)00015-1openalex-snapshot
α-amylase family: Molecular biology and evolution
inferred← citeshttps://doi.org/10.1016/s0092-8674(00)81852-8openalex-snapshot
Secreted Fringe-like Signaling Molecules May Be Glycosyltransferases
inferred← citeshttps://doi.org/10.1016/s0141-0229(01)00498-7openalex-snapshot
Catalytic mechanism and product specificity of cyclodextrin glycosyltransferase, a prototypical transglycosylase from the α-amylase family
inferred← citeshttps://doi.org/10.1016/s0141-8130(97)00047-0openalex-snapshot
Inhibition of reduced DP18-maltodextrin and amylose hydrolysis by acarbose: kinetic studies
inferred← citeshttps://doi.org/10.1016/s0167-4838(00)00210-7openalex-snapshot
Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility
inferred← citeshttps://doi.org/10.1016/s0167-4838(00)00233-8openalex-snapshot
Engineering of cyclodextrin glycosyltransferase reaction and product specificity
inferred← citeshttps://doi.org/10.1016/s0167-4838(00)00240-5openalex-snapshot
Protein engineering of bacterial α-amylases
inferred← citeshttps://doi.org/10.1016/s0167-4838(00)00302-2openalex-snapshot
Relationship of sequence and structure to specificity in the α-amylase family of enzymes
inferred← citeshttps://doi.org/10.1016/s0167-4838(97)00118-0openalex-snapshot
Effect of pressure on the mechanism of hydrolysis of maltotetraose, maltopentaose, and maltohexose catalyzed by porcine pancreatic α-amylase
inferred← citeshttps://doi.org/10.1016/s0167-4838(99)00011-4openalex-snapshot
Molecular cloning and primary structure analysis of porcine pancreatic α-amylase
inferred← citeshttps://doi.org/10.1016/s0167-7306(08)60586-4openalex-snapshot
Chapter 3 3D Structure 1. The Structural Features of Protein-Carbohydrate Interactions Revealed by X-Ray Crystallography
inferred← citeshttps://doi.org/10.1016/s0378-1119(00)00229-8openalex-snapshot
Structural similarities and evolutionary relationships in chloride-dependent α-amylases
inferred← citeshttps://doi.org/10.1016/s0921-0423(06)80099-7openalex-snapshot
Mutational analysis of catalytic mechanism and specificity in amylolytic enzymes
inferred← citeshttps://doi.org/10.1016/s0921-0423(06)80101-2openalex-snapshot
Protein engineering of cyclodextrin glycosyltransferase from Bacillus circulans strain 251
inferred← citeshttps://doi.org/10.1016/s0921-0423(96)80364-9openalex-snapshot
Structure and activity of some starch-metabolising enzymes
inferred← citeshttps://doi.org/10.1016/s0921-0423(98)80051-8openalex-snapshot
Effect of temperature and Ca2+ on the degree of multiple attack exhibited by mesophilic and thermophilic α-amylases
inferred← citeshttps://doi.org/10.1016/s0922-338x(98)80088-3openalex-snapshot
Bacillus animal type α-amylase: Cloning and sequencing of the gene, and comparison of the deduced amino acid sequence with that of other amylases
inferred← citeshttps://doi.org/10.1016/s0960-894x(99)00175-4openalex-snapshot
Isotope edited NMR studies of glycosidases: design and synthesis of a novel glycosidase inhibitor
inferred← citeshttps://doi.org/10.1016/s0965-1748(00)00071-0openalex-snapshot
cDNA cloning, biochemical characterization and inhibition by plant inhibitors of the α-amylases of the Western corn rootworm, Diabrotica virgifera virgifera
inferred← citeshttps://doi.org/10.1016/s0969-2126(01)00230-1openalex-snapshot
The three-dimensional structure of 6-phospho-β-galactosidase from Lactococcus lactis
inferred← citeshttps://doi.org/10.1016/s0969-2126(94)00120-0openalex-snapshot
Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor
inferred← citeshttps://doi.org/10.1016/s0969-2126(96)00075-5openalex-snapshot
Crystal structures of guinea-pig, goat and bovine α-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase
inferred← citeshttps://doi.org/10.1016/s0969-2126(96)00151-7openalex-snapshot
Substrate mimicry in the active center of a mammalian α amylase: structural analysis of an enzyme–inhibitor complex
inferred← citeshttps://doi.org/10.1016/s0969-2126(98)00032-xopenalex-snapshot
Activation of Bacillus licheniformis α-amylase through a disorder→order transition of the substrate-binding site mediated by a calcium–sodium–calcium metal triad
inferred← citeshttps://doi.org/10.1016/s0969-2126(98)00092-6openalex-snapshot
A novel strategy for inhibition of α-amylases: yellow meal worm α-amylase in complex with the Ragi bifunctional inhibitor at 2.5 å resolution
inferred← citeshttps://doi.org/10.1016/s0969-2126(98)00149-xopenalex-snapshot
Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular level
inferred← citeshttps://doi.org/10.1016/s0981-9428(00)01171-2openalex-snapshot
Molecular basis for the specific binding of different α-amylase inhibitors from Phaseolus vulgaris seeds to the active site of α-amylase
inferred← citeshttps://doi.org/10.1016/s1093-3263(97)00012-0openalex-snapshot
Applications of nuclear magnetic resonance spectroscopy and molecular modeling to the study of protein-carbohydrate interactions
inferred← citeshttps://doi.org/10.1016/s1389-1723(03)80191-3openalex-snapshot
Secondary calcium-binding parameter of Bacillus amyloliquefaciens α-amylase obtained from inhibition kinetics
inferred← citeshttps://doi.org/10.1016/s1568-1254(01)80005-xopenalex-snapshot
Chapter 3 Cold-adapted enzymes: An unachieved symphony
inferred← citeshttps://doi.org/10.1021/acs.biochem.5b00228openalex-snapshot
Crystal Structures of Escherichia coli Branching Enzyme in Complex with Linear Oligosaccharides
inferred← citeshttps://doi.org/10.1021/bi00251a005openalex-snapshot
Crystal Structure of Endo-.beta.-N-acetylglucosaminidase F1, an .alpha./.beta.-Barrel Enzyme Adapted for a Complex Substrate
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/bi701160hopenalex-snapshot
Conversion of a Cyclodextrin Glucanotransferase into an α-Amylase: Assessment of Directed Evolution Strategies
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/bi902183wopenalex-snapshot
X-ray Crystallographic Analyses of Pig Pancreatic α-Amylase with Limit Dextrin, Oligosaccharide, and α-Cyclodextrin,
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/ja500172dopenalex-snapshot
Metal-Dependent Conformational Activation Explains Highly Promutagenic Replication across O6-Methylguanine by Human DNA Polymerase β
inferred← citeshttps://doi.org/10.1021/jp801827fopenalex-snapshot
Entropy and Free Energy of a Mobile Protein Loop in Explicit Water
inferred← citeshttps://doi.org/10.1021/jp900790nopenalex-snapshot
Dynamic Properties of a Psychrophilic α-Amylase in Comparison with a Mesophilic Homologue
inferred← citeshttps://doi.org/10.1023/a:1005925819741openalex-snapshot
Plant α-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin
inferred← citeshttps://doi.org/10.1023/a:1023024012657openalex-snapshot
Molecular Cloning of α-Amylases from Cotton Boll Weevil, Anthonomus grandis and Structural Relations to Plant Inhibitors: An Approach to Insect Resistance
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/nsb0597-405openalex-snapshot
Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase
inferred← citeshttps://doi.org/10.1038/s41467-022-34123-wopenalex-snapshot
Oxygen mediated oxidative couplings of flavones in alkaline water
inferred← citeshttps://doi.org/10.1038/s41598-021-92554-9openalex-snapshot
Stereoselective synthesis of a 4-⍺-glucoside of valienamine and its X-ray structure in complex with Streptomyces coelicolor GlgE1-V279S
inferred← citeshttps://doi.org/10.1038/srep23126openalex-snapshot
Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass
inferred← citeshttps://doi.org/10.1039/b205561aopenalex-snapshot
The C7N aminocyclitol family of natural products
inferred← citeshttps://doi.org/10.1039/c4ra16825aopenalex-snapshot
Biocatalytic one-pot three-component synthesis of 3,3′-disubstituted oxindoles and spirooxindole pyrans using α-amylase from hog pancreas
inferred← citeshttps://doi.org/10.1039/d4qo00886copenalex-snapshot
Chemoselective reaction of methoxyaminomethyl BODIPYs with unprotected carbohydrates: a powerful tool for accessing BODIPY neoglycosides
inferred← citeshttps://doi.org/10.1039/d5ob01795eopenalex-snapshot
C(3)–H alkenylation of quinoxalin-2(1 H )-ones with Hantzsch esters and in silico studies
inferred← citeshttps://doi.org/10.1039/d6ra00931jopenalex-snapshot
Novel piperazine–triazole hybrids as PTP1B and alpha-amylase inhibitors: synthesis, biological evaluation and computational validation through network pharmacology, molecular docking, MD simulations, DFT and MMPBSA analysis
inferred← citeshttps://doi.org/10.1042/bj3290065openalex-snapshot
Expression of the Schwanniomyces occidentalis SWA2 amylase in Saccharomyces cerevisiae: role of N-glycosylation on activity, stability and secretion
inferred← citeshttps://doi.org/10.1042/ebc20220193openalex-snapshot
Psychrophilic enzymes: strategies for cold-adaptation
inferred← citeshttps://doi.org/10.1046/j.0014-2956.2001.02609.xopenalex-snapshot
Modulation of activity and substrate binding modes by mutation of single and double subsites +1/+2 and −5/−6 of barley α‐amylase 1
inferred← citeshttps://doi.org/10.1046/j.0014-2956.2001.02714.xopenalex-snapshot
Substrate recognition by three family 13 yeast α‐glucosidases
inferred← citeshttps://doi.org/10.1046/j.1365-2583.2003.00423.xopenalex-snapshot
Expression of functional Anopheles merus α‐amylase in the baculovirus/ Spodoptera frugiperda system
inferred← citeshttps://doi.org/10.1046/j.1432-1033.2000.01790.xopenalex-snapshot
X‐ray structure of acarbose bound to amylomaltase from Thermus aquaticus
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.1432-1033.2003.03376.xopenalex-snapshot
Thermoanaerobacterium thermosulfurigenes cyclodextrin glycosyltransferase
inferred← citeshttps://doi.org/10.1046/j.1432-1327.1999.00611.xopenalex-snapshot
Mechanism of porcine pancreatic α‐amylase
inferred← citeshttps://doi.org/10.1046/j.1432-1327.1999.00664.xopenalex-snapshot
Electrostatics in the active site of an α‐amylase
inferred← citeshttps://doi.org/10.1046/j.1432-1327.2000.01448.xopenalex-snapshot
Involvement of Gln937 of Streptococcus downei GTF‐I glucansucrase in transition‐state stabilization
inferred← citeshttps://doi.org/10.1074/jbc.270.49.29256openalex-snapshot
Crystallographic Studies of the Interaction of Cyclodextrin Glycosyltransferase from Bacillus circulans Strain 251 with Natural Substrates and Products
inferred← citeshttps://doi.org/10.1074/jbc.271.39.23836openalex-snapshot
Structural and Functional Aspects of Chloride Binding to Alteromonas haloplanctis α-Amylase
inferred← citeshttps://doi.org/10.1074/jbc.272.25.15729openalex-snapshot
Cyclodextrins Are Not the Major Cyclic α-1,4-Glucans Produced by the Initial Action of Cyclodextrin Glucanotransferase on Amylose
inferred← citeshttps://doi.org/10.1074/jbc.272.3.1601openalex-snapshot
Altering Substrate Specificity of Bacillus sp. SAM1606 α-Glucosidase by Comparative Site-specific Mutagenesis
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