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Structure of the Aspergillus oryzae α-Amylase Complexed with the Inhibitor Acarbose at 2.0 Å Resolution ,

https://doi.org/10.1021/bi970539i
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Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1006/jmbi.1994.0106openalex-snapshot
Crystal Structure of Calcium-depletedBacillus licheniformisα-amylase at 2.2 Å Resolution
inferredcites →https://doi.org/10.1016/0003-9861(67)90118-xopenalex-snapshot
Multiple attack hypothesis of α-amylase action: Action of porcine pancreatic, human salivary, and Aspergillus oryzae α-amylases
inferredcites →https://doi.org/10.1016/0014-5793(94)01354-4openalex-snapshot
Refined structure for the complex of d ‐gluco‐dihydroacarbose with glucoamylase from Aspergillus awamori var. X100 to 2.2 Å resolution: dual conformations for extended inhibitors bound to the active site of glucoamylase
inferredcites →https://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
inferredcites →https://doi.org/10.1016/s0021-9258(17)40728-9openalex-snapshot
Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution.
inferredcites →https://doi.org/10.1016/s0022-2836(63)80023-6openalex-snapshot
Stereochemistry of polypeptide chain configurations
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/10.1021/cr00105a006openalex-snapshot
Catalytic mechanism of enzymic glycosyl transfer
inferredcites →https://doi.org/10.1042/bj2800309openalex-snapshot
A classification of glycosyl hydrolases based on amino acid sequence similarities
inferredcites →https://doi.org/10.1042/bj2930781openalex-snapshot
New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
inferredcites →https://doi.org/10.1042/bj3160695openalex-snapshot
Updating the sequence-based classification of glycosyl hydrolases
inferredcites →https://doi.org/10.1042/bj3210557openalex-snapshot
Nomenclature for sugar-binding subsites in glycosyl hydrolases
inferredcites →https://doi.org/10.1074/jbc.271.12.6889openalex-snapshot
Unequivocal Identification of Asp-214 as the Catalytic Nucleophile of Saccharomyces cerevisiae α-Glucosidase Using 5-Fluoro Glycosyl Fluorides
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a134659openalex-snapshot
Structure and Possible Catalytic Residues of Taka-Amylase A
inferredcites →https://doi.org/10.1107/s0021889891004399openalex-snapshot
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
inferredcites →https://doi.org/10.1107/s0021889892009944openalex-snapshot
PROCHECK: a program to check the stereochemical quality of protein structures
inferredcites →https://doi.org/10.1107/s0108767393007597openalex-snapshot
AMoRe: an automated package for molecular replacement
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/s0907444993000952openalex-snapshot
Crystallization of aHumicola lanuginosalipase–inhibitor complex with the use of polyethylene glycol monomethyl ether
inferredcites →https://doi.org/10.1107/s0907444996012255openalex-snapshot
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
inferredcites →https://doi.org/10.1111/j.1432-1033.1994.tb18739.xopenalex-snapshot
Domain B protruding at the third β strand of the α/β barrel in barley α‐amylase confers distinct isozyme‐specific properties
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/10.1111/j.1469-185x.1953.tb01386.xopenalex-snapshot
STEREOCHEMISTRY AND THE MECHANISM OF ENZYMATIC REACTIONS

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Structural rationale for the short branched substrate specificity of the glycogen debranching enzyme GlgX
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Deglycosylation induces extensive dynamics changes in α‐amylase revealed by hydrogen/deuterium exchange mass spectrometry
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Crystal structure of a catalytic-site mutant α-amylase from Bacillus subtilis complexed with maltopentaose
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Crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 Å resolution
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Sucrose-Utilizing Transglucosidases for Biocatalysis
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α-Amylases from Archaea: Sequences, Structures and Evolution
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Biochemical properties of Glu-SH3 as a family 13 glycoside hydrolase with remarkable substrate specificity for trehalose: Implications to sequence-based classification of CAZymes
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Structure of a complex of Thermoactinomyces vulgaris R-47 α-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft
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Formation of covalent β-linked carbohydrate–enzyme intermediates during the reactions catalyzed by α-amylases
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inferred← citeshttps://doi.org/10.1016/s0014-5793(02)02362-1openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/s0167-4838(00)00041-8openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/s0167-4838(00)00233-8openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/s0969-2126(98)00066-5openalex-snapshot
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inferred← citeshttps://doi.org/10.1021/acs.jafc.1c05657openalex-snapshot
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inferred← citeshttps://doi.org/10.1021/acs.jafc.2c04487openalex-snapshot
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Met349 Mutations Enhance the Activity of 1,4-α-Glucan Branching Enzyme from Geobacillus thermoglucosidans STB02
inferred← citeshttps://doi.org/10.1021/acs.jafc.8b03080openalex-snapshot
Enhanced 2-O-α- d -Glucopyranosyl- l -ascorbic Acid Synthesis through Iterative Saturation Mutagenesis of Acceptor Subsite Residues in Bacillus stearothermophilus NO2 Cyclodextrin Glycosyltransferase
inferred← citeshttps://doi.org/10.1021/acs.joc.9b03152openalex-snapshot
Conformationally Controlled Reactivity of Carbasugars Uncovers the Choreography of Glycoside Hydrolase Catalysis
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/bi701160hopenalex-snapshot
Conversion of a Cyclodextrin Glucanotransferase into an α-Amylase: Assessment of Directed Evolution Strategies
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/jacs.0c13059openalex-snapshot
Activity-Based Protein Profiling of Retaining α-Amylases in Complex Biological Samples
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/10.1023/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/10.1038/ncomms11229openalex-snapshot
Crystal structure of glycogen debranching enzyme and insights into its catalysis and disease-causing mutations
inferred← citeshttps://doi.org/10.1038/s41467-025-61077-6openalex-snapshot
Molecular architecture and catalytic mechanism of human glycogen debranching enzyme
inferred← citeshttps://doi.org/10.1038/srep17144openalex-snapshot
Structure of Mycobacterium thermoresistibile GlgE defines novel conformational states that contribute to the catalytic mechanism
inferred← citeshttps://doi.org/10.1039/b205561aopenalex-snapshot
The C7N aminocyclitol family of natural products
inferred← citeshttps://doi.org/10.1039/c5dt04790kopenalex-snapshot
Interaction of europium and curium with alpha-amylase
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.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.1432-1033.2003.03733.xopenalex-snapshot
On the mechanism of 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/10.1073/pnas.1007531107openalex-snapshot
Crystal structure of a 117 kDa glucansucrase fragment provides insight into evolution and product specificity of GH70 enzymes
inferred← citeshttps://doi.org/10.1074/jbc.274.49.34868openalex-snapshot
The Cyclization Mechanism of Cyclodextrin Glycosyltransferase (CGTase) as Revealed by a γ-Cyclodextrin-CGTase Complex at 1.8-Å Resolution
inferred← citeshttps://doi.org/10.1074/jbc.m010998200openalex-snapshot
Amylosucrase, a Glucan-synthesizing Enzyme from the α-Amylase Family
inferred← citeshttps://doi.org/10.1074/jbc.m107533200openalex-snapshot
Hydrophobic Amino Acid Residues in the Acceptor Binding Site Are Main Determinants for Reaction Mechanism and Specificity of Cyclodextrin-glycosyltransferase
inferred← citeshttps://doi.org/10.1074/jbc.m110.121707openalex-snapshot
Crystal Structure of Full-length Mycobacterium tuberculosis H37Rv Glycogen Branching Enzyme
inferred← citeshttps://doi.org/10.1074/jbc.m113.491449openalex-snapshot
Replacement of the Catalytic Nucleophile Aspartyl Residue of Dextran Glucosidase by Cysteine Sulfinate Enhances Transglycosylation Activity
inferred← citeshttps://doi.org/10.1074/jbc.m205746200openalex-snapshot
The X-ray Crystallographic Structure ofEscherichia coli Branching Enzyme
inferred← citeshttps://doi.org/10.1074/jbc.m207860200openalex-snapshot
Oligosaccharide and Sucrose Complexes of Amylosucrase
inferred← citeshttps://doi.org/10.1074/jbc.m302616200openalex-snapshot
Isomaltulose Synthase (PalI) of Klebsiella sp. LX3
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.m404311200openalex-snapshot
Complex Structures of Thermoactinomyces vulgaris R-47 α-Amylase 2 with Acarbose and Cyclodextrins Demonstrate the Multiple Substrate Recognition Mechanism
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.ra120.013595openalex-snapshot
Structure–function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17 exo-α-glucosidases
inferred← citeshttps://doi.org/10.1080/07388551.2017.1339664openalex-snapshot
Strategy in manipulating transglycosylation activity of glycosyl hydrolase for oligosaccharide production
inferred← citeshttps://doi.org/10.1080/10242420310001614333openalex-snapshot
Engineering of Hydrolysis Reaction Specificity in the Transglycosylase Cyclodextrin Glycosyltransferase
inferred← citeshttps://doi.org/10.1080/11263504.2022.2089760openalex-snapshot
Phenolic constituents, antioxidant and α-amylase inhibitory activities of Pulicaria vulgaris growing in Tunisia: an in vitro and in silico study
inferred← citeshttps://doi.org/10.1080/14756366.2023.2292482openalex-snapshot
Comparative metabolic study of the chloroform fraction of three Cystoseira species based on UPLC/ESI/MS analysis and biological activities
inferred← citeshttps://doi.org/10.1093/bbb/zbad177openalex-snapshot
Plant polysaccharide degradation-related enzymes in Aspergillus oryzae
inferred← citeshttps://doi.org/10.1093/bbb/zbae158openalex-snapshot
Structural insights into the inhibition mechanism of glucosidase inhibitors toward kojibiose hydrolase belonging to glycoside hydrolase family 65
inferred← citeshttps://doi.org/10.1093/glycob/cwr049openalex-snapshot
Crystal structure of the branching enzyme I (BEI) from Oryza sativa L with implications for catalysis and substrate binding
inferred← citeshttps://doi.org/10.1093/jpp/rgaa038openalex-snapshot
Steroidal saponins from Trillium govanianum as α-amylase, α-glucosidase, and dipeptidyl peptidase IV inhibitory agents
inferred← citeshttps://doi.org/10.1093/oxfordjournals.molbev.a003718openalex-snapshot
Evolution of α-Amylases: Architectural Features and Key Residues in the Stabilization of the (β/α)8 Scaffold
inferred← citeshttps://doi.org/10.1093/protein/15.1.21openalex-snapshot
Probing the catalytically essential residues of the α-l-arabinofuranosidase from Thermobacillus xylanilyticus
inferred← citeshttps://doi.org/10.1093/protein/gzl044openalex-snapshot
Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of -amylase-related proteins
inferred← citeshttps://doi.org/10.1093/protein/gzq051openalex-snapshot
A chemically modified α-amylase with a molten-globule state has entropically driven enhanced thermal stability†
inferred← citeshttps://doi.org/10.1107/s0907444904027118openalex-snapshot
Structure of aBacillus halmapalusfamily 13 α-amylase, BHA, in complex with an acarbose-derived nonasaccharide at 2.1 Å resolution
inferred← citeshttps://doi.org/10.1107/s0907444909040311openalex-snapshot
The apo structure of sucrose hydrolase fromXanthomonas campestrispv.campestrisshows an open active-site groove
inferred← citeshttps://doi.org/10.1107/s1744309106024729openalex-snapshot
Monoclinic crystal form ofAspergillus nigerα-amylase in complex with maltose at 1.8 Å resolution
inferred← citeshttps://doi.org/10.1107/s2053230x1801453xopenalex-snapshot
Crystal structure of glycosyltrehalose synthase fromSulfolobus shibataeDSM5389
inferred← citeshttps://doi.org/10.1107/s2059798318014900openalex-snapshot
The structure of the AliC GH13 α-amylase from Alicyclobacillus sp. reveals the accommodation of starch branching points in the α-amylase family
inferred← citeshttps://doi.org/10.1107/s205979832100677xopenalex-snapshot
A GH13 α-glucosidase from Weissella cibaria uncommonly acts on short-chain maltooligosaccharides
inferred← citeshttps://doi.org/10.1110/ps.0202602openalex-snapshot
Structural basis of α‐amylase activation by chloride
inferred← citeshttps://doi.org/10.1110/ps.041079305openalex-snapshot
Structural and mechanistic studies of chloride induced activation of human pancreatic α‐amylase
inferred← citeshttps://doi.org/10.1110/ps.8.3.635openalex-snapshot
Cloning, mutagenesis, and structural analysis of human pancreatic α‐amylase expressed in pichia pastoris
inferred← citeshttps://doi.org/10.1111/1744-7917.12401openalex-snapshot
Effects and mechanisms of Bacillus thuringiensis crystal toxins for mosquito larvae
inferred← citeshttps://doi.org/10.1111/febs.70684openalex-snapshot
Structure–function relationships of CldA : a unique functional intermediate between starch hydrolases and cyclomaltodextrin glucanotransferases
inferred← citeshttps://doi.org/10.1111/ijfs.14816openalex-snapshot
Biological activity of rice extract and the inhibition potential of rice extract, rice volatile compounds and their combination against α‐glucosidase, α‐amylase and tyrosinase
inferred← citeshttps://doi.org/10.1111/j.1432-1033.2004.04182.xopenalex-snapshot
Human salivary α‐amylase Trp58 situated at subsite −2 is critical for enzyme activity
inferred← citeshttps://doi.org/10.1111/j.1432-1033.2004.04183.xopenalex-snapshot
The crystal structure of Thermoactinomyces vulgaris R‐47 α‐amylase II (TVA II) complexed with transglycosylated product
inferred← citeshttps://doi.org/10.1111/j.1742-4658.2005.05013.xopenalex-snapshot
Complexes of Thermoactinomyces vulgaris R‐47 α‐amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with α‐(1,6) glycosidic linkages
inferred← citeshttps://doi.org/10.1111/j.1747-0285.2012.01426.xopenalex-snapshot
An Isoquinoline Alkaloid, Berberine, Can Inhibit Fungal Alpha Amylase: Enzyme Kinetic and Molecular Modeling Studies
inferred← citeshttps://doi.org/10.1128/aem.00121-08openalex-snapshot
Enhancement of the Alcoholytic Activity of α-Amylase AmyA fromThermotoga maritimaMSB8 (DSM 3109) by Site-Directed Mutagenesis
inferred← citeshttps://doi.org/10.1128/aem.00449-17openalex-snapshot
Rational Engineering of a Cold-Adapted α-Amylase from the Antarctic Ciliate Euplotes focardii for Simultaneous Improvement of Thermostability and Catalytic Activity
inferred← citeshttps://doi.org/10.1128/aem.65.4.1644-1651.1999openalex-snapshot
Modes of Action of Acarbose Hydrolysis and Transglycosylation Catalyzed by a Thermostable Maltogenic Amylase, the Gene for Which Was Cloned from a Thermus Strain
inferred← citeshttps://doi.org/10.1128/jb.185.23.6981-6984.2003openalex-snapshot
Crystal Structure of Bacillus subtilis α-Amylase in Complex with Acarbose
inferred← citeshttps://doi.org/10.1271/bbb.120473openalex-snapshot
Amino Acids in Conserved Region II Are Crucial to Substrate Specificity, Reaction Velocity, and Regioselectivity in the Transglucosylation of Honeybee GH-13 α-Glucosidases
inferred← citeshttps://doi.org/10.1271/bbb.64.2692openalex-snapshot
Analysis of Catalytic Residues ofThermoactinomyces vulgarisR-47 α-Amylase II (TVA II) by Site-directed Mutagenesis
inferred← citeshttps://doi.org/10.1271/bbb.65.619openalex-snapshot
Structures of Thermoactinomyces vulgaris R-47 α-Amylase II Complexed with Substrate Analogues
inferred← citeshttps://doi.org/10.1271/bbb.80325openalex-snapshot
Biochemical and Crystallographic Characterization of the Starch Branching Enzyme I (BEI) from Oryza sativa L
inferred← citeshttps://doi.org/10.1371/journal.pone.0057432openalex-snapshot
Effect of Heavy Atoms on the Thermal Stability of α-Amylase from Aspergillus oryzae
inferred← citeshttps://doi.org/10.1371/journal.pone.0125507openalex-snapshot
The Characterization of Modified Starch Branching Enzymes: Toward the Control of Starch Chain-Length Distributions
inferred← citeshttps://doi.org/10.1371/journal.pone.0153868openalex-snapshot
Aspergillus Oryzae S2 α-Amylase Domain C Involvement in Activity and Specificity: In Vivo Proteolysis, Molecular and Docking Studies
inferred← citeshttps://doi.org/10.1371/journal.pone.0231513openalex-snapshot
Crystal structure of β-L-arabinobiosidase belonging to glycoside hydrolase family 121
inferred← citeshttps://doi.org/10.1371/journal.pone.0275765openalex-snapshot
Identification of potential human pancreatic α-amylase inhibitors from natural products by molecular docking, MM/GBSA calculations, MD simulations, and ADMET analysis
inferred← citeshttps://doi.org/10.1371/journal.ppat.1006998openalex-snapshot
PgaB orthologues contain a glycoside hydrolase domain that cleaves deacetylated poly-β(1,6)-N-acetylglucosamine and can disrupt bacterial biofilms
inferred← citeshttps://doi.org/10.14233/ajchem.2026.35064openalex-snapshot
Therapeutic Potential of Disubstituted [{[5-(2-Chloro phenyl)-1,3,4-thiadiazole-2-yl]imino}-methyl]phenyl Derivatives as α-Amylase Antagonists: Synthesis, In silico and In vitro Screening
inferred← citeshttps://doi.org/10.18174/121664openalex-snapshot
Galactosyl hydrolases from Bifidobacterium adolescentis and Bifidobacterium longum
inferred← citeshttps://doi.org/10.2174/0115680266311132240807065631openalex-snapshot
Advancements in Computational Approaches for Antidiabetic Drug Discovery: A Review
inferred← citeshttps://doi.org/10.2174/1573407219666230607154721openalex-snapshot
Phytochemistry and Biological Assessment of Thuja articulata Trunk Barks: HPLC-PDA-ESI-MS Analysis, Bioevaluation, and Molecular Docking
inferred← citeshttps://doi.org/10.2183/pjab.100.027openalex-snapshot
Crystals of taka-amylase A, a cornerstone of protein chemistry in Japan
inferred← citeshttps://doi.org/10.2210/pdb6gxv/pdbopenalex-snapshot
Amylase in complex with acarbose
inferred← citeshttps://doi.org/10.2210/pdb6sau/pdbopenalex-snapshot
Structural and Functional Characterization of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance
inferred← citeshttps://doi.org/10.2478/s11756-008-0170-4openalex-snapshot
Role of the phenylalanine 260 residue in defining product profile and alcoholytic activity of the α-amylase AmyA from Thermotoga maritima
inferred← citeshttps://doi.org/10.3109/10242422.2012.674720openalex-snapshot
Probing enzyme–substrate interactions at the catalytic subsite ofLeuconostoc mesenteroidessucrose phosphorylase with site-directed mutagenesis: the roles of Asp49and Arg395
inferred← citeshttps://doi.org/10.31274/etd-180810-3473openalex-snapshot
Studies on mechanisms of resistant starch analytical methods
inferred← citeshttps://doi.org/10.3389/fmicb.2016.01129openalex-snapshot
Bacterial and Archaeal α-Amylases: Diversity and Amelioration of the Desirable Characteristics for Industrial Applications
inferred← citeshttps://doi.org/10.3390/jof7100816openalex-snapshot
Structural Insight into a Yeast Maltase—The BaAG2 from Blastobotrys adeninivorans with Transglycosylating Activity
inferred← citeshttps://doi.org/10.3390/jox13010009openalex-snapshot
Inhibition Kinetics and Theoretical Studies on Zanthoxylum chalybeum Engl. Dual Inhibitors of α-Glucosidase and α-Amylase
inferred← citeshttps://doi.org/10.3390/molecules26175214openalex-snapshot
Trifluoromethylated Flavonoid-Based Isoxazoles as Antidiabetic and Anti-Obesity Agents: Synthesis, In Vitro α-Amylase Inhibitory Activity, Molecular Docking and Structure–Activity Relationship Analysis
inferred← citeshttps://doi.org/10.3390/molecules28145327openalex-snapshot
Structural and Functional Characterization of Drosophila melanogaster α-Amylase
inferred← citeshttps://doi.org/10.3390/molecules29163893openalex-snapshot
Phytochemical Analysis, Biological Activities, and Docking of Phenolics from Shoot Cultures of Hypericum perforatum L. Transformed by Agrobacterium rhizogenes
inferred← citeshttps://doi.org/10.3390/pr10040780openalex-snapshot
Evaluation of Porcine and Aspergillus oryzae α-Amylases as Possible Model for the Human Enzyme
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