3 research outputs found

    Additional file 1: Table S1. of RNA-seq-based evaluation of bicolor tepal pigmentation in Asiatic hybrid lilies (Lilium spp.)

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    Summary of assembled sequences from the tepal parts of the Asiatic hybrid lily Lollypop. Table S3. Primers used for quantitative RT-PCR (qRT-PCR) analysis. Figure S1. Phenylpropanoid, anthocyanin, and cinnamic acid derivative biosynthesis pathways in lily tepals. Enzymes whose genes are up-regulated in upper tepals (estimated by qRT-PCR) are shown in blue. 3GT, anthocyanidin 3-O-glucosyltransferase; 3RT, anthocyanidin-3-glucoside rhamnosyltransferase; 4CL, 4-coumaroyl: CoA-ligase; 7GT, anthocyanidin-3-rutinoside 7-glucosyltransferase; ANS, anthocyanidin synthase; CHI, chalcone isomerase; CHS, chalcone synthase; C3H, p-coumarate 3-hydroxylase; C4H, cinnamate 4-hydroxylase; DFR, dihydroflavonol 4-reductase; F3H, flavanone 3-hydroxylase; F3′H, flavonoid 3′-hydroxylase; FLS, flavonol synthase; GST, glutathione S-transferase; HCT, shikimate O-hydroxycinnamoyl transferase; MATE, multidrug and toxic compound extrusion transporter; PAL, phenylalanine ammonia-lyase. Figure S2. HPLC analysis of anthocyanins and CADs in upper tepals (upper) and tepal bases (basal) of lily cultivars. A: Absorbance at 525 nm (anthocyanins) of the tepal extracts in Lollypop, and cyanidin 3-O-glycoside (Cy3G) and cyanidin 3-O-rutinoside (Cy3R) standards. B: Absorbance at 340 nm (CADs) of the tepal extracts in six cultivars. Figure S3. Alignment of predicted amino acid sequences of isoforms annotated as LhPAL1, LhPAL2, and LhPAL3 (A), and LhCHSa and LhCHSb (B). Letters on black and grey backgrounds indicate identical and similar amino acids, respectively. Asterisks indicate stop codons. Figure S4. Relative expression levels of c30288_g1 (HCT), c10735_g1 (MYB3), c25442_g1 (MYB8), c25442_g2, c24227_g1 (R3-MYB), c24227_g2 (R3-MYB), c18278_g2 (R3-MYB), c36339_g1 (SPL9), and c16635-g1 (RCP1) in upper tepals and tepal bases of Lollypop during floral development (St 1–5). ACTIN was used to normalize the expression of target genes. Values and vertical bars indicate the mean ± standard error (n = 3). The same letters above the columns indicate that the values are not statistically significant (p <0.05) by Tukey’s HSD. Figure S5. Relative expression levels of LhMYB12 in Sugar Love and WD40 in Sugar Love and Montreux in upper tepals and tepal bases during floral development (St 1–5, A) and flowers of the cultivars Montreux and Sugar Love (B). ACTIN was used to normalize the expression of target genes. Values and vertical bars indicate the means ± standard error (n = 3). The same letters above the columns indicate that the values are not statistically significant (p <0.05) by Tukey’s HSD. Figure S6. Putative miR828 and pri-miR828 sequences in Lollypop. A: Putative miR828 and its target site appeared in c22900_g1 (MYB12). B: Sequence alignment of c13793_g1 and pri-miR828 in Glycine max [GmPri-miR828a (NR_126648) and GmPri-miR828b (NR_126651)], Vitis vinifera [VvPri-miR828a (NR_127861) and VvPri-miR828b (LM611741)], and Malus domestica [MdPri-miR828b (NR_120979) and MdPri-miR828a (NR_120978)]. (PDF 1261 kb

    Design, Synthesis, and Biological Evaluation of 3‑(1-Aryl‑1<i>H</i>‑indol-5-yl)propanoic Acids as New Indole-Based Cytosolic Phospholipase A<sub>2</sub>α Inhibitors

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    This article describes the design, synthesis, and biological evaluation of new indole-based cytosolic phospholipase A<sub>2</sub>α (cPLA<sub>2</sub>α, a group IVA phospholipase A<sub>2</sub>) inhibitors. A screening-hit compound from our library, (<i>E</i>)-3-{4-[(4-chlorophenyl)­thio]-3-nitrophenyl}­acrylic acid (<b>5</b>), was used to design a class of 3-(1-aryl-1<i>H</i>-indol-5-yl)­propanoic acids as new small molecule inhibitors. The resultant structure–activity relationships studied using the isolated enzyme and by cell-based assays revealed that the 1-(<i>p</i>-<i>O</i>-substituted)­phenyl, 3-phenylethyl, and 5-propanoic acid groups on the indole core are essential for good inhibitory activity against cPLA<sub>2</sub>α. Optimization of the <i>p</i>-substituents on the N1 phenyl group led to the discovery of <b>56n</b> (ASB14780), which was shown to be a potent inhibitor of cPLA<sub>2</sub>α via enzyme assay, cell-based assay, and guinea pig and human whole-blood assays. It displayed oral efficacy toward mice tetradecanoyl phorbol acetate-induced ear edema and guinea pig ovalbumin-induced asthma models
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