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Fig. 18 in Review of lignans from 2019 to 2021: Newly reported compounds, diverse activities, structure-activity relationships and clinical applications

Fig. 18. The "source-category-activities" network of lignans. (The green nodes represent the source (families), the red nodes indicate the category, and the purple nodes emblem the activities). (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 17 in Review of lignans from 2019 to 2021: Newly reported compounds, diverse activities, structure-activity relationships and clinical applications

Fig. 17. The potential structure-activity relationships of lignans in antitumor, anti-inflammatory and antioxidant effects.

Fig. 16 in Review of lignans from 2019 to 2021: Newly reported compounds, diverse activities, structure-activity relationships and clinical applications

Fig. 16. Structure based activity distribution. (A) The proportion of pharmacological activities; (B) distribution of bioactivities in different classification.

Fig. 15 in Review of lignans from 2019 to 2021: Newly reported compounds, diverse activities, structure-activity relationships and clinical applications

Fig. 15. Distribution of molecular resources analysis. (A) Main classifications of lignans; (B) distribution of lignan subclass structures; (C) distribution of lignans in top eight families.

Fig. 5 in Specialized compounds across ontogeny in the seagrass Posidonia oceanica

Fig. 5. Map of the sampling area showing where plant material was collected (Cala Xinxell and Cala Comtesa).

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Fig. 4. Compounds 1, 21 in Six C21 steroidal glycosides from Cynanchum wallichii Wight roots and their multidrug resistance reversal activities

Fig. 4. Compounds 1, 21, and 25 can reverse drug resistance by decreasing P-gp, NF-κB, and c-jun gene and protein expression. (A–C) MDR1, NFκB, and JUN gene expression in MCF-ADR and HepG2-ADM cells following co-treatment with 1, 21, and 25 and Doxorubicin. (D–E) MDR1, NFκB, and Jun protein expression in MCFADR and HepG2-ADM cells treated with 1, 21, and 25 in combination with DOX.

Fig. 4 in Specialized compounds across ontogeny in the seagrass Posidonia oceanica

Fig. 4. Principal Component Analysis. Arrows represent the loading of the variables (table S3). Dots represent the score of each replicate on PC1 and PC2. Number of replicates from all tissues analyzed were 6 for young leaves from non-reproductive plants (L1), old leaves from non-reproductive plants (L3), inflorescences (F), and old leaves from reproductive plants (RL3), 10 replicates for leaves from seedlings (SD); and 5 for young leaves from reproductive plants (RL1). Compounds labelled as 1 (chicoric acid), 2 (caffeoylferuloyltartaric acid), 3 (p-coumaroylcaffeoyltartaric acid), 4 (coutaric acid) and 5 (di-p-coumaroyltartaric acid).

Fig. 3 in Specialized compounds across ontogeny in the seagrass Posidonia oceanica

Fig. 3. Mean content of chemical traits in leaves of seedlings (SD), young leaves (L1), old leaves (L3), inflorescences (F), and rhizomes of reproductive (R) and nonreproductive (N) plants. Compounds in mg chicoric acid equivalents/g DW of plant labelled as 1 (chicoric ac.), 2 (caffeoylferuloyltartaric acid), 3 (p-coumaroylcaffeoyltartaric acid), 4 (coutaric acid) and 5 (di-p-coumaroyltartaric acid). Error bars indicate standard error. Dots represent the value of each replicate (for F, L1, L3 n = 6 for SD n = 10). Mean values and standard errors can be found in Table S1.

Fig. 2 in Specialized compounds across ontogeny in the seagrass Posidonia oceanica

Fig. 2. Representative total ion current (TIC) UPLC-MS chromatogram of extracts of Posidonia oceanica samples. Numbers indicate the compound in each peak, IS indicates internal standard.

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Fig. 2 in The GH3 amidosynthetases family and their role in metabolic crosstalk modulation of plant signaling compounds

Fig. 2. GH3 structure and mechanism of catalysis. A. Bi Uni Uni Bi Ping Pong mechanism of GH3 action. B. Structure of AtGH3.12 (active-site closed conformation) with attached salicylate and AMPCPP (nonhydrolysable ATP analogue). This monomeric protein consists of larger N-terminal domain (blue colour) and smaller Cterminal domain (green colour) which are linked by flexible hinge loop (red colour). C. AtGH3.12 active site. Salicylate (C atoms in cyan) is bound to the acyl acid site (C atoms in grey) with Tyr120, Arg 123, Ile 217, Phe 218 and Val 299 residues, as shown. AMPCPP is attached to the nucleotide site (C atoms in grey) with canonical loop (Lys104), β-turn-β motif (Tyr325, Glu329) and ribose interaction motif (Asp398), as shown. Lys104 and Glu329 coordinate a magnesium ion (green colour). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.) Note. Fig. 2B and C from "Determination of the GH3.12 protein conformation through HPLC-integrated SAXS measurements combined with X-ray crystallography," by A. Round, E. Brown, R. Marcellin, U. Kapp, C. S. Westfall, J.M. Jez, C. Zubieta, 2013, Acta Crystallogr. D Biol. Crystallogr, 69, p. 2073, 2076 (https://doi.org/10.1107/S0907444913019276). Copyright 2013 by Acta Crystallographica, Section D: Biological Crystallography. Reprinted with permission.

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Fig. 1 in The GH3 amidosynthetases family and their role in metabolic crosstalk modulation of plant signaling compounds

Fig. 1. Acyl acid substrates of GH3. This group includes jasmonic acid, natural and synthetic auxins, indole-derivative and benzoate-derivatives. Most AtGH3 enzymes are auxin specific. AtGH3.5, apart from auxins and indole-derivative, also conjugates benzoate-derivatives. AtGH3.12 strongly prefers isochorismate, precursor of SA, as a substrate. Jasmonic acid is conjugated to L-isoleucine during the reaction catalyzed by AtGH3.11/JAR1.

Fig. 5 in Structural characterization of prenylated compounds from Broussonetia kazinoki and their antiosteoclastogenic activity

Fig. 5. Effects of 2 (A), 3 (B), and 6 (C) on RANKL-induced osteoclastogenesis in BMMs. These compounds inhibit RANKL-induced differentiation of BMMs into osteoclast. Mouse BMMs were seeded into 96 well-plates in the presence of M-CSF (30 ng/mL) and RANKL (100 ng/mL) with or without different concentrations (0, 3, 10, 30 μM) of 2, 3, and 6 for 6 days, and then cells were stained for TRAP. The quantities of TRAP-positive multinucleated (>5 nuclei) osteoclasts were determined following image capture (magnification, ×40). Data were presented as the mean ±SE (P <0.05).

Fig. 3 in Structural characterization of prenylated compounds from Broussonetia kazinoki and their antiosteoclastogenic activity

Fig. 3. Calculated and experimental ECD spectra of 1 (left) and experimental ECD spectrum of 2–7 (right) in MeOH.

Fig. 2 in Structural characterization of prenylated compounds from Broussonetia kazinoki and their antiosteoclastogenic activity

Fig. 2. Key HMBC (blue arrows) and COSY (black bold) correlations for compounds 1–3 and 5–8. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 6. Compound 6 in Structural characterization of prenylated compounds from Broussonetia kazinoki and their antiosteoclastogenic activity

Fig. 6. Compound 6 suppresses resorption pits in BMMs. BMMs were incubated with M-CSF (30 ng/mL) and RANKL (100 ng/mL) on Corning OsteoAssay Surface 24 well-plates and treated with indicated concentrations of compound 6 for seven days. The cells were washed, and the pit area was determined by using Image J software. Data are presented as the mean ±SE (P <0.05).

Fig. 4 in Structural characterization of prenylated compounds from Broussonetia kazinoki and their antiosteoclastogenic activity

Fig. 4. Antiosteoclastogenic effect from isolated compounds. (A) RAW264.7 cells were cultured into 96 well-plates under stimulation of RANKL (100 ng/mL) with or without indicated compounds (10 μM) for four days, then the cells were stained for TRAP. The quantities of TRAP-positive multinucleated (>5 nuclei) osteoclasts were presented as the mean ±SE (P <0.01, versus vehicle-treated control; n =3). (B) RAW264.7 cells were plated in 96 well-plates and incubated with M-CSF (30 ng/mL) in the presence of indicated concentrations of isolated compounds for 48 h. Cell viability was measured by MTT assay. Data were presented as the mean ±SE (P <0.01, versus vehicle-treated control; n =3).

Fig. 5 in Unique localization of jasmonic acid-related compounds in developing Phaseolus vulgaris L. (common bean) seeds revealed through desorption electrospray ionization-mass spectrometry imaging

Fig. 5. DESI-MS/MSI of OPDA and OPC-8 in the developing Phaseolus vulgaris seeds. (a) Optical image of the seed section for OPDA analysis. (b) MS/MS spectrum of precursor ion at m/z 291.1966 ± 1 Da obtained at the target enhanced mode for m/z 165.1. (c) Ion image at m/z 165.1300. (d) Optical image of the seed section for OPC-8:0 analysis. (e) MS/MS spectrum of precursor ion at m/z 293.2122 ± 1 Da obtained at the target enhanced mode for m/z 225.1. Ion images at m/z (f) 223.1400 and (g) 231.2142. Scale bar = 2 mm. Compound names are defined in Table 1.

Fig. 4 in Unique localization of jasmonic acid-related compounds in developing Phaseolus vulgaris L. (common bean) seeds revealed through desorption electrospray ionization-mass spectrometry imaging

Fig. 4. LC-ESI-MS/MS analysis of JA-related compounds in the extracts from the radicle and seed coat of developing Phaseolus vulgaris seeds. MS/MS spectra of peaks at (a) 5.3 min in Fig. 3c, (b) 5.3 min in Fig. 3d, (c) 6.5 min in Fig. 3c and (d) 6.5 min in Fig. 3d and (e) 6.3 min in Fig. 3e and (f) 6.3 min in Fig. 3f and (g) 6.4 min in Fig. 3e, (h) 6.4 min in Fig. 3f, (i) 6.7 min in Fig. 3e, and (j) 6.7 min in Fig. 3f. Compound names are defined in Table 1.

Fig. 2 in Unique localization of jasmonic acid-related compounds in developing Phaseolus vulgaris L. (common bean) seeds revealed through desorption electrospray ionization-mass spectrometry imaging

Fig. 2. LC-ESI-MS/MS analysis of JA-related compound standards. Spectra of (a) OPDA, (b) OPC-8:0, and (c) JA standards. Compound names are defined in Table 1.

Fig. 1 in Unique localization of jasmonic acid-related compounds in developing Phaseolus vulgaris L. (common bean) seeds revealed through desorption electrospray ionization-mass spectrometry imaging

Fig. 1. DESI-MSI analysis of JA-related compounds in the developing Phaseolus vulgaris seeds. (a) Optical image of the section. (b) Mass spectrum obtained from the section. Ion images of m/z (c) 277.2172, (d) 291.1953, and (e) 293.2117. Three different developing seeds were analyzed, and the results from one are shown as representative data. Scale bar = 2 mm. Compound names are defined in Table 1.