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Fig. 6 in MAPKK2/4/5/7-MAPK3-JAZs modulate phenolic acid biosynthesis in Salvia miltiorrhiza

Fig. 6. Protein–protein interaction of SmMAPK3 with JA signaling members. Y2H (A) and LCI (B–C) assays to detect the interactions of SmMAPK3 with JAZs.

Fig. 5 in MAPKK2/4/5/7-MAPK3-JAZs modulate phenolic acid biosynthesis in Salvia miltiorrhiza

Fig. 5. Protein–protein interaction between SmMAPKKs and SmMAPK3. Y2H (A) and LCI (B–D) assays to detect upstream proteins of SmMAPK3.

Fig. 4 in MAPKK2/4/5/7-MAPK3-JAZs modulate phenolic acid biosynthesis in Salvia miltiorrhiza

Fig. 4. Overexpression of SmMAPK3 affects phenolic acid biosynthesis and the expression of biosynthetic genes in S. miltiorrhiza. (A) Relative quantitative analysis of SmMAPK3 expression in the transgenic lines and controls. *** indicates significant differences between OM and the control (P <0.001, Student's t-test). (B) Analysis of phenolic acid production from OE. (C–J) Relative expression levels of genes involved in phenolic acid biosynthesis in the OE lines.

Fig. 3 in MAPKK2/4/5/7-MAPK3-JAZs modulate phenolic acid biosynthesis in Salvia miltiorrhiza

Fig. 3. Tissue-specific expression analysis and elicitors-induced analysis of SmMAPK3 in S. miltiorrhiza. (A) Tissue-specific expression of SmMAPK3; the expression levels were normalized to values from roots. (B) SA-induced analysis of SmMAPK3. (C) MeJA-induced analysis of SmMAPK3.

Fig. 1 in MAPKK2/4/5/7-MAPK3-JAZs modulate phenolic acid biosynthesis in Salvia miltiorrhiza

Fig. 1. Identification and autophosphorylation of SmMAPK3 in S. miltiorrhiza. (A) Amplication of SmMAPK3 from S. miltiorrhiza. (B) Phylogenic tree analysis of SmMAPK3 with AtMAPKs. (C) The conserved domains of SmMAPK3. (D) Immunoblotting analysis of SmMAPK3 autophosphorylation in vitro with Phos-tag™ SDS–PAGE. Phosphorylated SmMAPK3 (pSmMAPK3) migrates more slowly in the gel.

Fig. 2. SmMAPK3 in MAPKK2/4/5/7-MAPK3-JAZs modulate phenolic acid biosynthesis in Salvia miltiorrhiza

Fig. 2. SmMAPK3 is associated with the biosynthesis of phenolic acids. (A) Expression patterns of phenolic acid biosynthetic genes in 18 samples. (B) Network built on correlations among kinases, structural genes and TFs. Pearson correlation coefficient (PCC) values were calculated for each pair of genes.

opennotspecifiedFeb 2022View details →

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.

opennotspecifiedFeb 2022View details →

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.

opennotspecifiedMay 2021View details →

Fig. 2 in Diterpenoids from Zhumeria majdae roots as potential heat shock protein 90 (HSP90) modulators

Fig. 2. Comparison of experimental and in silico calculated ECD spectra of compounds 1–3 and 19 in MeOH.

opennotspecifiedMay 2021View details →

Fig. 3 in Diterpenoids from Zhumeria majdae roots as potential heat shock protein 90 (HSP90) modulators

Fig. 3. Effect of 20 on HSP90α client protein levels in MCF7 cells after treatment with 20 (18 μM) for 48 h. Equal amounts (30 μg) of total protein lysate were separated on SDS-PAGE and client proteins were visualized by Western Blot analysis. α-tubulin and GAPDH were used as loading controls. The blots are representative of three different experiments with similar results. Numbers above each lane represent the densitometric values.

opennotspecifiedMay 2021View details →

Fig. 4. Binding mode between 20 and the C in Diterpenoids from Zhumeria majdae roots as potential heat shock protein 90 (HSP90) modulators

Fig. 4. Binding mode between 20 and the C-terminal domain of HSP90. The two chains of the protein are colored differently (blue and red). The hydrogen bond is represented with a blue dotted line, the salt bridge with a pink dotted line, and interacting hydrophobic residues are labeled in black with the corresponding chain explicated. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 9 in Modulation of cellular circadian clocks by triterpenoids

Fig. 9. Early responses of core clock genes in U2OS cells treated with celastrol, pristimerin, and cucurbitacin B.

Fig. 6 in Modulation of cellular circadian clocks by triterpenoids

Fig. 6. Response of PER2-luc reporter in U2OS cells to each compound administration; comparison with celastrol.

Fig. 4 in Modulation of cellular circadian clocks by triterpenoids

Fig. 4. Relationship between the structures of cucurbitacin B and its analogues and clock modulation.

Fig. 8 in Modulation of cellular circadian clocks by triterpenoids

Fig. 8. Celastrol increases the expression of Per2 and shortens the circadian period in NIH3T3 cells.

opennotspecifiedSep 2020View details →

Fig. 2 in Melatonin and calcium modulate the production of rosmarinic acid, luteolin, and apigenin in Dracocephalum kotschyi under salinity stress

Fig. 2. The effects of root pretreatment with Mel (100 μM) and CaCl2 (5 mM) individually or combined to 5 mM EGTA, 5 mM LaCl3 (La), 200 μM TFP and 100 μM p-CPA for 24 h on PAL (A) and RAS (B) genes expression levels in the leaves of D. kotschyi seedling under salt stress (75 mM NaCl). Bars represent the mean ± standard error (n = 3). Means accompanied by the same letter are not significantly different according to LSD at P ≤ 0.05.

opennotspecifiedSep 2020View details →

Fig. 1 in Melatonin and calcium modulate the production of rosmarinic acid, luteolin, and apigenin in Dracocephalum kotschyi under salinity stress

Fig. 1. The effects of root pretreatment with Mel (100 μM) and CaCl2 (5 mM) individually or combined to 5 mM EGTA, 5 mM LaCl3 (La), 200 μM TFP and 100 μM pCPA for 24 h on total phenolic content (TPC) (A), total flavonoid content (TFC) (B), rosmarinic acid (RA) (C), luteolin flavone (LF) (D) and apigenin flavone (AF) (E) and antioxidant capacity (F) in the leaves of D. kotschyi seedling under salt stress (75 mM NaCl). Bars represent the mean ± standard error (n = 3). Means accompanied by the same letter are not significantly different according to LSD at P ≤ 0.05.

opennotspecifiedSep 2020View details →

Fig. 3 in Melatonin and calcium modulate the production of rosmarinic acid, luteolin, and apigenin in Dracocephalum kotschyi under salinity stress

Fig. 3. The effects of root pretreatment with Mel (100 μM) and CaCl2 (5 mM) individually or combined to 5 mM EGTA, 5 mM LaCl3 (La), 200 μM TFP and 100 μM p-CPA for 24 h on PAL (A) and TAL (B) activities in the leaves of D. kotschyi seedling under salt stress (75 mM NaCl). Bars represent the mean ± standard error (n = 3). Means accompanied by the same letter are not significantly different according to LSD at P ≤ 0.05.

opencc-by-4.0Aug 2023View details →

Source data for Ordouie, E. et al. Differential phase-diversity electrooptic modulator for cancellation of fiber dispersion and laser noise.

<p>The experimental data and primary simulation results.</p>