PubMed_ArguminSci  

PubMed:29194348 JSONTXT 6 Projects

Annnotations TAB TSV DIC JSON TextAE

Id Subject Object Predicate Lexical cue
T1 136-257 DRI_Background denotes Sargassum serratifolium C. Agardh (Phaeophyceae, Fucales) is a marine brown alga that belongs to the family Sargassaceae.
T2 258-327 DRI_Background denotes It is widely distributed throughout coastal areas of Korea and Japan.
T3 328-502 DRI_Background denotes S. serratifolium has been found to contain high concentrations of plastoquinones, which have strong anti-cancer, anti-inflammatory, antioxidant, and neuroprotective activity.
T4 503-723 DRI_Background denotes This study aims to investigate the anti-diabetic activity of S. serratifolium and its major constituents through inhibition of protein tyrosine phosphatase 1B (PTP1B), α-glucosidase, and ONOO--mediated albumin nitration.
T5 724-726 DRI_Background denotes S.
T6 751-853 DRI_Background denotes extract and fractions exhibited broad PTP1B and α-glucosidase inhibitory activity (IC50, 1.83~7.04 and
T7 871-914 DRI_Background denotes for PTP1B and α-glucosidase, respectively).
T8 915-1114 DRI_Background denotes In an attempt to identify bioactive compounds, three plastoquinones (sargahydroquinoic acid, sargachromenol and sargaquinoic acid) were isolated from the active n-hexane fraction of S. serratifolium.
T9 1115-1219 DRI_Outcome denotes All three plastoquinones exhibited dose-dependent inhibitory activity against PTP1B in the IC50 range of
T10 1233-1396 DRI_Outcome denotes , while sargachromenol and sargaquinoic acid showed dose-dependent inhibitory activity against α-glucosidase (IC50 42.41 ± 3.09 and 96.17 ± 3.48 µM, respectively).
T11 1397-1585 DRI_Background denotes In the kinetic study of PTP1B enzyme inhibition, sargahydroquinoic acid and sargaquinoic acid led to mixed-type inhibition, whereas sargachromenol displayed noncompetitive-type inhibition.
T12 1672-1959 DRI_Approach denotes Docking simulations of these plastoquinones demonstrated negative binding energies and close proximity to residues in the binding pocket of PTP1B and α-glucosidase, indicating that these plastoquinones have high affinity and tight binding capacity towards the active site of the enzymes.
T13 1960-2143 DRI_Background denotes These results demonstrate that S. serratifolium and its major plastoquinones may have the potential as functional food ingredients for the prevention and treatment of type 2 diabetes.