Find research datasets worth reusing

opennotspecifiedJul 2021View details →

Fig. 2 in Screening of in vitro and in silico α-amylase, α-glucosidase, and lipase inhibitory activity of oxyprenylated natural compounds and semisynthetic derivatives

Fig. 2. In vitro inhibition activities.α-Amylase inhibition (A) andα-glucosidase inhibition (B) by acarbose and the pure active compounds. (C) Pancreatic lipase inhibition by orlistat and the pure active compounds. In each test, data are expressed as IC50 values in μM and values with the same letter (a–h) are not significantly different at p ≤ 0.05 level, according to a one-way analysis of variance (ANOVA).

Fig. 7 in Piperazine-2,5-dione derivatives and an α-pyrone polyketide from Penicillium griseofulvum and their immunosuppression activity

Fig. 7. DP4 probabilities of 13C NMR data for both diastereoisomers of 4; comparing of experimental and calculated ECD spectra of 4-A and 4-B.

Fig. 4. Linear correlation between the experimental and calculated 13C in Piperazine-2,5-dione derivatives and an α-pyrone polyketide from Penicillium griseofulvum and their immunosuppression activity

Fig. 4. Linear correlation between the experimental and calculated 13C NMR chemical shift of 1-A and 1-B and their compared 13C NMR data (Δδ δ – δ).

opennotspecifiedJul 2021View details →

Fig. 4 in Screening of in vitro and in silico α-amylase, α-glucosidase, and lipase inhibitory activity of oxyprenylated natural compounds and semisynthetic derivatives

Fig. 4. Docking of compounds 3, 9, 11, and 15 in human lipase enzyme. The original structure of the lipase enzyme (1LPB) contains the inhibitor methoxyundecylphosphinic acid (MUP, carbons coloured purple (A)). The docking results in lipase enzyme (B-E, green surface) with compounds 3 (pink, B), 9 (cyan, C), 11 (magenta, D), and 15 (green, E) are shown with their respective binding energies. The carbons of the residues lining the binding pocket are coloured in white, with the active site residues in yellow (S169, D193, and H280). Residues making hydrogen bonds with the ligands are indicated (B–E). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

opennotspecifiedJul 2021View details →

Fig. 3 in Screening of in vitro and in silico α-amylase, α-glucosidase, and lipase inhibitory activity of oxyprenylated natural compounds and semisynthetic derivatives

Fig. 3. Docking of compounds 3, 9, 11, and 15 in human α-amylase and α-glucosidase enzymes. The original structures of α-amylase (1XD0) and α-glucosidase (3TOP) enzymes contain the inhibitor acarbose (carbons coloured in orange and hexoses numbered in A and F, respectively). The docking results in α-amylase (B-E, light grey surface) and α-glucosidase (G-J, beige) enzymes with compounds 3 (pink, B and G), 9 (cyan, C and H), 11 (magenta, D and I), and 15 (green, E and J) are shown with their respective binding energies. The carbons of the residues lining the binding pocket are coloured in white, with the active site residues in yellow (R210, D212, E248, and R352 in α-amylase; D1420, E1423, and D1526 in α-glucosidase enzyme). Residues making hydrogen bonds with the ligands are indicated (B- E and G-J). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 7 in Xylarinaps A-E, five pairs of naphthalenone derivatives with neuroprotective activities from Xylaria nigripes

Fig. 7. Effects of compounds 1–5 on SOD in OGD-induced PC12 cells. The values represent mean ± SD (n = 6). *P <0.05, **P <0.01 vs. the control group; #P <0.05, ##P <0.01 vs. the model group.

Fig. 8 in Xylarinaps A-E, five pairs of naphthalenone derivatives with neuroprotective activities from Xylaria nigripes

Fig. 8. Effects of compounds 1–5 on MDA in OGD-induced PC12 cells. The values represent mean ± SD (n = 6). *P <0.05, **P <0.01 vs. the control group; #P <0.05, ##P <0.01 vs. the model group.

Fig. 10 in Xylarinaps A-E, five pairs of naphthalenone derivatives with neuroprotective activities from Xylaria nigripes

Fig. 10. Effects of compounds 1–5 on OGD-induced apoptosis of PC12 cells. (A) Apoptosis of PC12 cells detected by Hochest staining. (B) Apoptosis rate of PC12 cells for compounds 1–5. The values represent mean ± SD (n = 6). *P <0.05, **P <0.01 vs. the control group; #P <0.05, ##P <0.01 vs. the model group.

Fig. 9 in Xylarinaps A-E, five pairs of naphthalenone derivatives with neuroprotective activities from Xylaria nigripes

Fig. 9. Effects of compounds 1–5 on GSH-Px in OGD-induced PC12 cells. The values represent mean ± SD (n =6). *P <0.05, **P <0.01 vs. the control group; #P <0.05, ##P <0.01 vs. the model group.

Fig. 6 in Xylarinaps A-E, five pairs of naphthalenone derivatives with neuroprotective activities from Xylaria nigripes

Fig. 6. Effects of compounds 1–5 on cell viability in OGD-induced PC12 cells. The values represent mean ± SD (n = 6). *P <0.05, **P <0.01 vs. the control group; #P <0.05, ##P <0.01 vs. the model group.

opennotspecifiedNov 2021View details →

Fig. 3 in Benzofuran ε-caprolactam glucosides, amides and phenylpropanoid derivatives with anti-inflammatory activity from Oxybaphus himalaicus

Fig. 3. Calculated and experimental ECD spectra (a) and chiral analysis chromatogram (b) of 1a and 1b.

opennotspecifiedNov 2021View details →

Fig. 2. Key HMBC, 1 H– 1 H in Benzofuran ε-caprolactam glucosides, amides and phenylpropanoid derivatives with anti-inflammatory activity from Oxybaphus himalaicus

Fig. 2. Key HMBC, 1 H– 1 H COSY and NOESY correlations of compounds (1 3) and X-ray ORTEP drawing of 1.

Fig. 4 in Condensation derivatives of 4-isopropylbenzaldehyde with acetophenone from the red alga Laurencia tristicha

Fig. 4. Absolute configurations determination of compounds 2a/2b, 3a/3b, and 4a/4b by comparison of the experimental ECD curves (measured at about 1 mg/mL in methanol) with calculated curves.

Fig. 9 in Chemical epigenetic manipulation triggers the production of sesquiterpenes from the deep-sea derived Eutypella fungus

Fig. 9. Experimental ECD spectrum of 7c in MeOH. The arrow indicated the electric transition dipole of the chromophores.

Fig. 1 in Emodin - A natural anthraquinone derivative with diverse pharmacological activities

Fig. 1. Chemical structures of emodin and its analogues [Emodin (R1 = OH; R2 = CH3); Rhein (R1 = H; R2 = COOH); Chrysophanol (R1 = H; R2 = CH3); Aloeemodin (R1 = H; R2 = CH2OH); Physcion (R1 = OCH3; R2 = CH3)].

Fig. 1 in Design, synthesis and screening of a drug discovery library based on an Eremophila-derived serrulatane scaffold

Fig. 1. Chemical structures of the targeted NP diterpenoid scaffolds (1–2), methylated products (3–4) and the amide library (5–16).

Fig. 4 in Design, synthesis and screening of a drug discovery library based on an Eremophila-derived serrulatane scaffold

Fig. 4. Representative flow cytometry examples of GFP expression (i.e., HIV production) in J-Lat 10.6 cells in the absence of stimulation (A), treatment with 50 nM PMA (B) and PMA plus 100 μM compound 2 (C). Dose response profiles (D) of compounds on GFP expression induced by 50 nM PMA in J-Lat 10.6 cells. Data denote mean ± s.d. from three independent experiments.

Fig. 3 in Design, synthesis and screening of a drug discovery library based on an Eremophila-derived serrulatane scaffold

Fig. 3. Microscopic images of the skinny (Skn) phenotype in L4s induced by compound 3 compared with the wild-type (WT) phenotype control (cultured in culture medium + 0.25% DMSO); the bottom panels enlarged from the dashed/ boxed areas in the upper panels.

Fig. 5 in Hygroline derivatives from Schizanthus tricolor and their anti-trypanosomatid and antiplasmodial activities

Fig. 5. Key HMBC (blue arrows), ROESY (green arrows) correlations and selected coupling constants (red dashed arrow) of compound 19. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 4 in Hygroline derivatives from Schizanthus tricolor and their anti-trypanosomatid and antiplasmodial activities

Fig. 4. Key HMBC (blue arrows), ROESY (green arrows) correlations and selected coupling constants (red dashed arrow) of compounds 1 and 3. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)