catechin has been researched along with acarbose in 6 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 2 (33.33) | 29.6817 |
2010's | 3 (50.00) | 24.3611 |
2020's | 1 (16.67) | 2.80 |
Authors | Studies |
---|---|
Chou, CJ; Frei, N; Grigorov, M; Lo Piparo, E; Scheib, H; Williamson, G | 1 |
Barnes, JC; Bradley, P; Day, NC; Fourches, D; Reed, JZ; Tropsha, A | 1 |
Campkin, D; Houston, TA; Kiefel, MJ; Simone, MI; Wood, A | 1 |
Curtis-Long, MJ; Kang, JE; Kim, JH; Lee, HS; Park, KH; Ryu, HW; Seo, WD; Yang, MS | 1 |
Cuong, NX; Jo, SH; Kim, YH; Kwon, YI; Luyen, BT; Minh, CV; Nam, NH; Tai, BH; Thao, NP; Yang, SY | 1 |
Choi, HJ; Eom, SH; Kim, T; Kim, TH; Lee, J | 1 |
1 review(s) available for catechin and acarbose
Article | Year |
---|---|
Recent results from non-basic glycosidase inhibitors: How structural diversity can inform general strategies for improving inhibition potency.
Topics: Enzyme Inhibitors; Glycoside Hydrolases; Imino Sugars | 2022 |
5 other study(ies) available for catechin and acarbose
Article | Year |
---|---|
Flavonoids for controlling starch digestion: structural requirements for inhibiting human alpha-amylase.
Topics: alpha-Amylases; Catalytic Domain; Digestion; Flavones; Flavonols; Humans; Hydrogen Bonding; Ligands; Models, Molecular; Protein Conformation; Saliva; Starch; Structure-Activity Relationship | 2008 |
Cheminformatics analysis of assertions mined from literature that describe drug-induced liver injury in different species.
Topics: Animals; Chemical and Drug Induced Liver Injury; Cluster Analysis; Databases, Factual; Humans; MEDLINE; Mice; Models, Chemical; Molecular Conformation; Quantitative Structure-Activity Relationship | 2010 |
Sulfonamide chalcone as a new class of alpha-glucosidase inhibitors.
Topics: alpha-Amylases; beta-Amylase; Chalcones; Enzyme Inhibitors; Glycoside Hydrolase Inhibitors; Kinetics; Models, Molecular; Structure-Activity Relationship; Sulfonamides | 2005 |
Rat intestinal sucrase inhibition of constituents from the roots of Rosa rugosa Thunb.
Topics: Animals; Dose-Response Relationship, Drug; Enzyme Inhibitors; Intestine, Small; Molecular Conformation; Plant Roots; Rats; Rosa; Structure-Activity Relationship; Sucrase; Triterpenes | 2014 |
Potential α-glucosidase inhibitors from thermal transformation of (+)-catechin.
Topics: alpha-Glucosidases; Catechin; Dimerization; Enzyme Inhibitors; Glycoside Hydrolase Inhibitors; Kinetics; Magnetic Resonance Spectroscopy; Molecular Conformation; Protein Binding; Stereoisomerism; Temperature | 2014 |