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Fig. 7 in Triterpenic and phenolic acids production changed in Salvia officinalis via in vitro and in vivo polyploidization: A consequence of altered genes expression

Fig. 7. Relative expression of six genes related to the biosynthesis of TAs, including farnesyl diphosphate synthase (FDS), squalene synthase (SQS), squalene epoxidases (SQE), lupeol synthase (LUS), β-amyrin synthase (BAS), and mixed function amyrin synthase (MFAS) genes in the different ploidy levels of in vitro and in vivo conditions of S. officinalis. Error bars are shown as standard deviation (n = 3).

Fig. 6 in Triterpenic and phenolic acids production changed in Salvia officinalis via in vitro and in vivo polyploidization: A consequence of altered genes expression

Fig. 6. The observation of stomata characteristics in vivo plants of diploid (A1,2) and mixoploid (B1,2) of S. officinalis. Bars = 50 and 10 μm.

Fig. 5 in Triterpenic and phenolic acids production changed in Salvia officinalis via in vitro and in vivo polyploidization: A consequence of altered genes expression

Fig. 5. The observation of stomata characteristics in vitro plants of diploid (A1,2), tetraploid (B1,2), and mixoploid (C1,2) of S. officinalis. Bars = 50 and 10 μm.

Fig. 2 in Triterpenic and phenolic acids production changed in Salvia officinalis via in vitro and in vivo polyploidization: A consequence of altered genes expression

Fig. 2. Chromosome numbers of root tip cells from diploid plants 2n = 2x = 14 (A); and tetraploid plants 2n = 4x = 28 (B) of S. officinalis.

Fig. 1 in Triterpenic and phenolic acids production changed in Salvia officinalis via in vitro and in vivo polyploidization: A consequence of altered genes expression

Fig. 1. Histograms of flow cytometric analysis of diploid (A), tetraploid (B) and mixoploid (C) plants of S. officinalis.

Fig. 4 in Triterpenic and phenolic acids production changed in Salvia officinalis via in vitro and in vivo polyploidization: A consequence of altered genes expression

Fig. 4. The morphological characteristics of in vivo plants of diploid (A), and mixoploid (B) of S. officinalis.

Fig. 8 in Triterpenic and phenolic acids production changed in Salvia officinalis via in vitro and in vivo polyploidization: A consequence of altered genes expression

Fig. 8. Pearson correlation and the relationship between TAs contents of betulinic acid (BA), ursolic acid (UA), and oleanolic acid (OA) and gene expression related to triterpenic acids biosynthesis pathway including farnesyl diphosphate synthase (FDS), squalene synthase (SQS), squalene epoxidases (SQE), lupeol synthase (LUS), β-amyrin synthase (BAS), and mixed function amyrin synthase (MFAS) genes in different ploidy levels of in vitro and in vivo conditions of S. officinalis.

Fig. 3 in 21-Hydroxypregnane 21-O-malonylation, a crucial step in cardenolide biosynthesis, can be achieved by substrate-promiscuous BAHD-type phenolic glucoside malonyltransferases from Arabidopsis thaliana and homolog proteins from Digitalis lanata

Fig. 3. Size exclusion chromatography (SEC) and indication of relative 21MaT activity investigation pools III (A) and IV (B) of the ammonium sulfate precipitation.

Fig. 4 in 21-Hydroxypregnane 21-O-malonylation, a crucial step in cardenolide biosynthesis, can be achieved by substrate-promiscuous BAHD-type phenolic glucoside malonyltransferases from Arabidopsis thaliana and homolog proteins from Digitalis lanata

Fig. 4. Docking of modeled AtPMaT1 (ribbon diagram) with an overlay of the potential pregnane substrates (Sub) (shown in grey). The catalytic histidine (His) and the cosubstrate (CoS) are also shown.

Fig. 1 in 21-Hydroxypregnane 21-O-malonylation, a crucial step in cardenolide biosynthesis, can be achieved by substrate-promiscuous BAHD-type phenolic glucoside malonyltransferases from Arabidopsis thaliana and homolog proteins from Digitalis lanata

Fig. 1. Postulated biosynthetic pathway of cardenolide formation in Digitalis. The malonylation step [8] is marked by a rectangle. 1 Putative side chain cleaving enzyme (SCCE), 2 NAD:3β-hydroxysteroid dehydrogenase (3βHSD), 3 Δ4,5-3-ketosteroid-isomerase (3KSI), 4 progesterone-5β-reductase (P5βR), 5 NAD:3β-hydroxysteroid dehydrogenase (3βHSD), 6 putative pregnane 14β-hydroxylase, 7 putative pregnane 21β-hydroxylase, 8 malonyl coenzyme A:21- hydroxypregnane 21-O-malonyltransferase (21MaT).

Fig. 6 in 21-Hydroxypregnane 21-O-malonylation, a crucial step in cardenolide biosynthesis, can be achieved by substrate-promiscuous BAHD-type phenolic glucoside malonyltransferases from Arabidopsis thaliana and homolog proteins from Digitalis lanata

Fig. 6. Docking of homology modeled malonyltransferases with 3-O-acetylketol (displayed in grey) showing the distances between the catalytic histidine (His), the hydroxy group to be malonylated (Sub) and the malonyl residue presented by the co-substrate (CoA). A AtPMaT1 B AtPMaT2 C DlMaT1.

Fig. 5 in 21-Hydroxypregnane 21-O-malonylation, a crucial step in cardenolide biosynthesis, can be achieved by substrate-promiscuous BAHD-type phenolic glucoside malonyltransferases from Arabidopsis thaliana and homolog proteins from Digitalis lanata

Fig. 5. Expression of Dlmat1, Dlmat2, Dlmat3, and Dlmat4 in different plant tissues measured by real-time quantitative PCR (qPCR). Expression rates are standardized to the values of the actin transcript in each tissue and were displayed in relation to the expression in young leaves (set to equal 1) for each Dlmat gene.

Fig. 5 in Determination of phenolic profiles of Herniaria polygama and Herniaria incana fractions and their in vitro antioxidant and anti-inflammatory effects

Fig. 5. Antioxidant activity of the examined fractions isolated from Herniaria incana (HIhfr) and Herniaria polygama (HPfr) in blood plasma under the ONOO - induced oxidative stress in vitro. Protective effects of the examined Herniaria fractions were evaluated based on measurements of protein thiol groups (panel A), 3- nitrotyrosine (panel B), and the ferric reducing ability of plasma (panel C); n = 7, 8, and 9 for –SH groups, 3-nitrotyrosine, and FRAP assay, respectively.

Fig. 4 in Determination of phenolic profiles of Herniaria polygama and Herniaria incana fractions and their in vitro antioxidant and anti-inflammatory effects

Fig. 4. UHPLC – diode array detector (DAD) and charged aerosol detector (CAD) profiles of the Herniaria incana herb phenolic fraction.

Fig. 3 in Determination of phenolic profiles of Herniaria polygama and Herniaria incana fractions and their in vitro antioxidant and anti-inflammatory effects

Fig. 3. The chemical structures of isolated compounds (46, 52, 54, 55, and 56) from Herniaria incanaherb.

Fig. 2 in Determination of phenolic profiles of Herniaria polygama and Herniaria incana fractions and their in vitro antioxidant and anti-inflammatory effects

Fig. 2. UHPLC – diode array detector (DAD) and charged aerosol detector (CAD) profiles of the Herniaria polygama phenolic fraction.

Fig. 6 in Determination of phenolic profiles of Herniaria polygama and Herniaria incana fractions and their in vitro antioxidant and anti-inflammatory effects

Fig. 6. Evaluation of protective effects of fractions isolated from Herniaria incana (HIhfr) and Herniaria polygama (HPfr) on the oxidative stress-induced modification of human fibrinogen structure. The figure contains an electrophoretic pattern of fibrinogen samples separated on gradient SDS-PAGE gel (4–20%) under the reducing conditions. Exposure of fibrinogen to ONOO resulted in the formation of high molecular weight protein aggregates (HMW), mainly derived from its Aα-chain and detectable over the fibrinogen pattern. The Herniaria fractions partly reduced these oxidative modifications to fibrinogen molecule; n = 3.

Fig. 7 in Determination of phenolic profiles of Herniaria polygama and Herniaria incana fractions and their in vitro antioxidant and anti-inflammatory effects

Fig. 7. Anti-inflammatory actions of the examined fractions isolated from Herniaria incana (HIhfr) and Herniaria polygama (HPfr) in the concanavalin A-stimulated PBMCs. Effects of the examined plant fractions were evaluated based on measurements of IL-2 (panel A) and TNF-α (panel B) secretion into the cell culture medium. The samples were assayed using the ELISA kits; *p <0.05, **p <0.01, ***p <0.001; n = 4.

Fig. 2 in Volatile phenolics: A comprehensive review of the anti-infective properties of an important class of essential oil constituents

Fig. 2. World map showing the publications of the different countries involved in scholarly publication of the anti-infective properties of volatile phenolics (1985–2019) as retrieved from the Scopus database.

Fig. 1 in Volatile phenolics: A comprehensive review of the anti-infective properties of an important class of essential oil constituents

Fig. 1. The number of publications retrieved from Scopus database in 35 years dealing with anti-infective properties of VP's (n = 2310 publications).