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opennotspecifiedJan 2022View details →

Fig. 2 in Lanostane triterpenoids from the fruiting bodies of Fomitopsis pinicola and their anti-inflammatory activities

Fig. 2. (a) Key 1H–1H COSY () and selected HMBC correlations (H→C) of 1; (b) Key NOESY correlations of 1.

opennotspecifiedOct 2022View details →

Fig. 6 in Meroterpenoids from the fungus Penicillium sclerotiorum GZU-XW03-2 and their anti-inflammatory activity

Fig. 6. Effect of compound 4 on LPS-stimulated protein iNOS expression in RAW264.7 cells. Data are presented as means ± SD (n = 3). ###p <0.001 versus the control group. *p <0.05, **p <0.01 versus the LPS group.

opennotspecifiedOct 2022View details →

Fig. 5 in Meroterpenoids from the fungus Penicillium sclerotiorum GZU-XW03-2 and their anti-inflammatory activity

Fig. 5. Effects of compound 4 on COX-2 (A), IL-6 (B) and IL-1β (C) release from LPS-stimulated RAW264.7 cells. Data are presented as means ± SD (n = 3). ###p <0.001 versus the control group. *p <0.05, **p <0.01 versus the LPS group.

Fig. 5 in On the free radical scavenging and metallic ion chelating activities of pyridoxal - Could the pro-oxidant risk be competitive?

Fig. 5. Optimized structures of the different Cu(I)/Cu(II)-neutral pyridoxal complexes calculated in water. Distances are in Å.

Fig. 3 in On the free radical scavenging and metallic ion chelating activities of pyridoxal - Could the pro-oxidant risk be competitive?

Fig. 3. Optimized structures of transition states (TSs) of RAF reactions at different sites between neutral pyridoxal and three radicals HOO●, NO ● and HO● in water. 2 Distances are in angstrom (Å) and angles are in degree (o).

Fig. 4 in Phenylpropanoids from Brachybotrys paridiformis Maxim. ex Oliv. and their anti-HBV activities

Fig. 4. Selected HMBC correlations (A B: proton A to carbon B; A B: proton A to carbon B and proton B to carbon A), COSY connectivities (bold lines in green) for compound 4. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 5 in Phenylpropanoids from Brachybotrys paridiformis Maxim. ex Oliv. and their anti-HBV activities

Fig. 5. Effect of compound 7 on cell viability (A) and inhibitory effect on HBsAg (B), HBeAg (C), and HBV DNA (D) in the supernatants of HepG2.2.15 cells. Lamivudine (3 TC) was used as the positive control in A–D. All values are expressed as means ± standard deviation (S.D.) from three separate experiments performed in triplicate. *p <0.05, **p <0.01 vs. the negative control.

Fig. 2 in Phenylpropanoids from Brachybotrys paridiformis Maxim. ex Oliv. and their anti-HBV activities

Fig. 2. Selected HMBC correlations (A B: proton A to carbon B; A B: proton A to carbon B and proton B to carbon A), COSY connectivities (bold lines in green) for compound 1. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 3 in Phenylpropanoids from Brachybotrys paridiformis Maxim. ex Oliv. and their anti-HBV activities

Fig. 3. Selected HMBC correlations (A B: proton A to carbon B; A B: proton A to carbon B and proton B to carbon A), COSY connectivities (bold lines in green) for compounds 2 and 3. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 2 in On the free radical scavenging and metallic ion chelating activities of pyridoxal - Could the pro-oxidant risk be competitive?

Fig. 2. Optimized structures of transition states (TSs) of FHT reactions of neutral pyridoxal with HOO● and NO ● at C9H, and with HO● at C6H to C9H and O12H 2 calculated in water. Optimized structure of FHT with HO● at O10H obtained in the gas phase. Distances are in angstrom (Å) and angles are in degree (o).

Fig. 4 in On the free radical scavenging and metallic ion chelating activities of pyridoxal - Could the pro-oxidant risk be competitive?

Fig. 4. Optimized structures of the different Fe(II)/Fe(III)-neutral pyridoxal complexes calculated in water. Distances are in Å.

Fig. 2. Key 1 H– 1 H in Pimarane, abietane, and labdane diterpenoids from Euphorbia pekinensis Rupr. and their anti-tumor activities

Fig. 2. Key 1 H– 1 H COSY (red bold lines) and HMBC (blue→) of compounds 5 (a1) and 16 (a2), NOSEY correlation (blue→) of compounds 5 (b1) and 16 (b2), The ORTEP drawing of compounds 5 (c1) and 16 (c2). (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 3. Key 1H–1H in Pimarane, abietane, and labdane diterpenoids from Euphorbia pekinensis Rupr. and their anti-tumor activities

Fig. 3. Key 1H–1H COSY (red bold lines) and HMBC (blue→) of compound 9 (a), NOSEY correlation (blue→) of compound 9 (b), The ORTEP drawing of compound 9 (c). (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 4. Key 1H–1H in Pimarane, abietane, and labdane diterpenoids from Euphorbia pekinensis Rupr. and their anti-tumor activities

Fig. 4. Key 1H–1H COSY (red bold lines) and HMBC (blue→) correlation of compounds 11 (a), 12 (b), 13 (c), and 15 (d). (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

opennotspecifiedFeb 2022View details →

Fig. 6 in Potential inhibitors of microglial activation from the roots of Vernicia montana Lour

Fig. 6. Anti-inflammatory activities of the isolated compounds 6, 7, 8, 13, 29, 30, and 33assayed on LPS-induced NO production in BV-2 microglial cells and their cell viability. (Each bar represents the mean ± SE of three independent experiments; ###p <0.001 compared with control group, *p <0.1, **p <0.01, ***p <0.001 compared with LPS group; Mino: minocycline).

Fig. 8 in PTP1B and α-glucosidase inhibitory activities of the chemical constituents from Hedera rhombea fruits: Kinetic analysis and molecular docking simulation

Fig. 8. Molecular docking related α-glucosidase inhibition by acarbose (green stick), BIP (red stick), 20 (cyan and yellow stick), and 26 (magenta stick) (a). 2D diagram of α-glucosidase inhibition by 20 [b (at the catalytic site) and c (at the allosteric site)] and 26 (d). The figure was generated using PyMOL and Discovery Studio Visualizer. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 7. Molecular docking related PTP1B in PTP1B and α-glucosidase inhibitory activities of the chemical constituents from Hedera rhombea fruits: Kinetic analysis and molecular docking simulation

Fig. 7. Molecular docking related PTP1B inhibition by compound C (magenta stick) and compound A (red stick), 20 (green stick), and 26 (yellow and blue stick) (a). 2D diagram of PTP1B inhibition by 20 (b) and 26 [c (at the catalytic site) and d (at the allosteric site)]. The figure was generated using PyMOL and Discovery Studio Visualizer. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 6 in PTP1B and α-glucosidase inhibitory activities of the chemical constituents from Hedera rhombea fruits: Kinetic analysis and molecular docking simulation

Fig. 6. Dixon plots (a and c), Lineweaver Burk plots (d and f), and secondary plots (b and e) for the α-glucosidase inhibition by 20 (a, b, d, and e) and 26 (c and f).

Fig. 5 in PTP1B and α-glucosidase inhibitory activities of the chemical constituents from Hedera rhombea fruits: Kinetic analysis and molecular docking simulation

Fig. 5. Lineweaver plots [a and b], Dixon plots [d and e], and secondary plots [c and f] for the inhibition of PTP1B enzyme by 20 (a and d) and 26 (b, c, e, and f), respectively.