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https://doi.org/10.2139/ssrn.4674192
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Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/cbdv.201100451openalex-extracted
Two Novel Potent α‐Amylase Inhibitors from the Family of Acarviostatins Isolated from the Culture of Streptomyces coelicoflavus ZG0656
inferredcites →https://doi.org/10.1006/abbi.1999.1423openalex-extracted
Comparative Study of the Inhibition of α-Glucosidase, α-Amylase, and Cyclomaltodextrin Glucanosyltransferase by Acarbose, Isoacarbose, and Acarviosine–Glucose
inferredcites →https://doi.org/10.1007/bf01300287openalex-extracted
Effects of acarbose on starch hydrolysis
inferredcites →https://doi.org/10.1007/bf01851228openalex-extracted
Inhibition of human intestinalα-glucosidehydrolases by a new complex oligosaccharide
inferredcites →https://doi.org/10.1007/bf01851236openalex-extracted
The effects of theα-glucosidase inhibitor BAY g 5421 (Acarbose) on meal-stimulated elevations of circulating glucose, insulin, and triglyceride levels in man
inferredcites →https://doi.org/10.1007/bf01851237openalex-extracted
The effects of theα-glucosidase inhibitor BAY g 5421 (Acarbose) on postprandial blood glucose, serum insulin, and triglyceride levels: Dose-time-response relationships in man
inferredcites →https://doi.org/10.1007/s00253-003-1477-2openalex-extracted
Biotechnology and molecular biology of the ?-glucosidase inhibitor acarbose
inferredcites →https://doi.org/10.1007/s00253-008-1582-3openalex-extracted
Three trehalose synthetic pathways in the acarbose-producing Actinoplanes sp. SN223/29 and evidence for the TreY role in biosynthesis of component C
inferredcites →https://doi.org/10.1007/s13300-017-0226-yopenalex-extracted
Effects of Acarbose on the Gut Microbiota of Prediabetic Patients: A Randomized, Double-blind, Controlled Crossover Trial
inferredcites →https://doi.org/10.1016/0008-6215(89)85022-0openalex-extracted
Synthesis of “dihydroacarbose”, an α-d-glucosidase inhibitor having a pseudo-tetrasaccharide structure
inferredcites →https://doi.org/10.1016/0008-6215(92)84132-copenalex-extracted
Chemical modification of the sugar part of methyl acarviosin: synthesis and inhibitory activities of nine analogues
inferredcites →https://doi.org/10.1016/j.carres.2007.11.012openalex-extracted
Two novel aminooligosaccharides isolated from the culture of Streptomyces coelicoflavus ZG0656 as potent inhibitors of α-amylase
inferredcites →https://doi.org/10.1016/j.carres.2008.01.020openalex-extracted
Four acarviosin-containing oligosaccharides identified from Streptomyces coelicoflavus ZG0656 are potent inhibitors of α-amylase
inferredcites →https://doi.org/10.1016/j.synbio.2017.11.005openalex-extracted
Improving acarbose production and eliminating the by-product component C with an efficient genetic manipulation system of Actinoplanes sp. SE50/110
inferredcites →https://doi.org/10.1016/s0008-6215(01)00016-7openalex-extracted
Inhibition of β-glycosidases by acarbose analogues containing cellobiose and lactose structures
inferredcites →https://doi.org/10.1016/s0008-6215(02)00018-6openalex-extracted
Addition of maltodextrins to the nonreducing-end of acarbose by reaction of acarbose with cyclomaltohexaose and cyclomaltodextrin glucanyltransferase
inferredcites →https://doi.org/10.1016/s0008-6215(02)00350-6openalex-extracted
Synthesis of acarbose analogues by transglycosylation reactions of Leuconostoc mesenteroides B-512FMC and B-742CB dextransucrases
inferredcites →https://doi.org/10.1016/s0008-6215(03)00293-3openalex-extracted
Study of the inhibition of four alpha amylases by acarbose and its 4IV-α-maltohexaosyl and 4IV-α-maltododecaosyl analogues
inferredcites →https://doi.org/10.1016/s0008-6215(98)00276-6openalex-extracted
Transglycosylation reactions of Bacillus stearothermophilus maltogenic amylase with acarbose and various acceptors
inferredcites →https://doi.org/10.1021/acschembio.2c00795openalex-extracted
Acarbose May Function as a Competitive Exclusion Agent for the Producing Bacteria
inferredcites →https://doi.org/10.1021/acschembio.8b00309openalex-extracted
Nonmicrobicidal Small Molecule Inhibition of Polysaccharide Metabolism in Human Gut Microbes: A Potential Therapeutic Avenue
inferredcites →https://doi.org/10.1021/bi00186a031openalex-extracted
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
inferredcites →https://doi.org/10.1021/bi048334eopenalex-extracted
Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic α-Amylase in Complex with Analogues and Their Elongated Counterparts ,
inferredcites →https://doi.org/10.1021/bi9921182openalex-extracted
Subsite Mapping of the Human Pancreatic α-Amylase Active Site through Structural, Kinetic, and Mutagenesis Techniques,
inferredcites →https://doi.org/10.1038/s41467-017-01682-2openalex-extracted
Analyses of gut microbiota and plasma bile acids enable stratification of patients for antidiabetic treatment
inferredcites →https://doi.org/10.1038/s41586-021-04091-0openalex-extracted
The human microbiome encodes resistance to the antidiabetic drug acarbose
inferredcites →https://doi.org/10.1038/s42255-023-00796-wopenalex-extracted
Inactivation of the antidiabetic drug acarbose by human intestinal microbial-mediated degradation
inferredcites →https://doi.org/10.1042/etls20180010openalex-extracted
Biosynthesis and metabolic engineering of pseudo-oligosaccharides
inferredcites →https://doi.org/10.1046/j.1432-1327.1998.2530251.xopenalex-extracted
Molecular and enzymatic characterization of a maltogenic amylase that hydrolyzes and transglycosylates acarbose
inferredcites →https://doi.org/10.1111/1753-0407.12232openalex-extracted
Acarbose treatment affects the serum levels of inflammatory cytokines and the gut content of bifidobacteria in C hinese patients with type 2 diabetes mellitus
inferredcites →https://doi.org/10.1126/science.aao5774openalex-extracted
Gut bacteria selectively promoted by dietary fibers alleviate type 2 diabetes
inferredcites →https://doi.org/10.1128/jb.183.15.4484-4492.2001openalex-extracted
Identification, Cloning, Expression, and Characterization of the Extracellular Acarbose-Modifying Glycosyltransferase, AcbD, fromActinoplanessp. Strain SE50
inferredcites →https://doi.org/10.1136/bmj.1.6158.220openalex-extracted
Improved metabolic profiles in insulin-treated diabetic patients given an alpha-glucosidehydrolase inhibitor.
inferredcites →https://doi.org/10.1271/bbb1961.39.2271openalex-extracted
New amylase inhibitor (S-AI) from Streptomyces diastaticus var. amylostaticus No. 2476.
inferredcites →https://doi.org/10.13345/j.cjb.210248openalex-extracted
[Biosynthesis and regulatory mechanism of acarbose and its structural analogs: a review].
inferredcites →https://doi.org/10.7164/antibiotics.34.1424openalex-extracted
Oligostatins, new antibiotics with amylase inhibitory activity. I. Production, isolation and characterization.
inferredcites →https://doi.org/10.7164/antibiotics.36.1157openalex-extracted
New .ALPHA.-amylase inhibitor, trestatins. I. isolation, characterization and biological activites of trestatins A, B and C.
inferredcites →https://doi.org/10.7164/antibiotics.36.1166openalex-extracted
New .ALPHA.-amylase inhibitor, trestatins. II. structure determination of trestatins A, B and C.
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