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Fig. 8 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases

Fig. 8. HPLC chromatogram of the mogrol standard and Agrobacterium-mediated transient expression of fruit harbouring pTRV-SgCPRs and pTRV-0 at 24 h after agroinfiltration.

Fig. 9 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases

Fig. 9. (A) Mogrol content in the S. grosvenorii fruit harbouring PBI121, PBI121-SgCPR1, and PBI121-SgCPR2. (B) MIIE content in the S. grosvenorii fruit harbouring PBI121, PBI121-SgCPR1, and PBI121-SgCPR2. (C) MIII content in the S. grosvenorii fruit harbouring PBI121, PBI121-SgCPR1, and PBI121-SgCPR2. (D) Accumulation of mogrol in the S. grosvenorii fruit harbouring pTRV, pTRV-SgCPR1, and pTRV-SgCPR2. (E) Accumulation of MII in the S. grosvenorii fruit harbouring pTRV, pTRV- SgCPR1, and pTRV-SgCPR2. (F) Accumulation of MIII in the S. grosvenorii fruit harbouring pTRV, pTRV-SgCPR1, and pTRV-SgCPR2. The values are the mean ± SD of three independent biological replicates.

Fig. 7 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases

Fig. 7. HPLC chromatogram of the mogrol standard and Agrobacterium-mediated transient expression of fruit harbouring PBI121-SgCPRs and PBI121 at 24 h after agroinfiltration.

Fig. 2 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases

Fig. 2. (A) Cloning of full-length and specific fragments of the SgCPR1 and SgCPR2 genes from S. grosvenorii cDNA. M, marker (2000 bp). The fulllength SgCPR1 and SgCPR2 genes are shown in red brackets, whereas the blue arrow indicates the specific fragments of the SgCPR1 and SgCPR2 genes. (B) Vector map of PBI121. (C) Construction of PBI12- SgCPR recombinant plasmids with the GUS marker and CaMV35S promoter. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 5 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases

Fig. 5. qRT-PCR analysis of SgCPR1 and SgCPR2 in fruit after infiltration (at t = 0 h). Relative expression levels were normalized to t = 0 h. (A) Relative transcript levels of SgCPR1 in fruit harbouring PBI121- SgCPR1 and PBI121. (B) SgCPR2 gene expression levels in fruit harbouring PBI121 and PBI121-SgCPR2. (C) Relative expression levels of SgCPR1 in fruit harbouring pTRV-SgCPR1 and pTRV-0. (D) Expression levels of SgCPR2 in fruit harbouring pTRV-SgCPR2 and pTRV-0. The relative expression levels normalized to the level of the SgUBQ gene. All the data are shown as means±SDs. * indicates significant differences at p <0.05 (LSD test).

Fig. 3 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases

Fig. 3. (A) Selective nucleotide sequences for VIGS in S. grosvenorii, which were inserted into EcoRI and BamHI. (B) pTRV2-SgCPR recombinant plasmid construction.

Fig. 1 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases

Fig. 1. The mogroside biosynthetic pathway in S. grosvenorii. The blue box on the left shows the generation of mogrol, which is a unique nonglycosylated tetra-hydroxycucurbitane in S. grosvenorii. The red box on the right represents a series of glycosylation reactions. The enzyme names are abbreviated as follows: SgSQE, squalene epoxidase; SgCS, cucurbitadienol synthase; SgEPH, epoxide hydrolase; SgCYP450, cytochrome P450 monooxygenase; SgCPR, NADPHcytochrome P450 reductase; SgUGT, UDP-glucosyltransferase. Among these, the candidate SgCPRs are highlighted in red. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 6 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases

Fig. 6. Accumulation of MIII and MIIE. (A) Total ion chromatograms of ten standard mixtures determined by LC-MS/MS. Among these, the retention times of MIII and MIIE were 10.01 and 12.09 min, respectively. (B) Extracted ion chromatograms of the sample. The red arrow indicates the Q1/Q3 mass chromatograms of MIII, which are in the red box. The Q1/Q3 mass chromatograms of MIIE are shown in the blue box, as indicated by the blue arrow. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 4 in Development of an efficient transient expression system for Siraitia grosvenorii fruit and functional characterization of two NADPH-cytochrome P450 reductases

Fig. 4. Histochemical GUS assay of transient expression in S. grosvenorii. GUS expression was detected in fruit but not in CK or leaves.

Fig. 6 in Cytochrome P450 catalyses the 29-carboxyl group formation of celastrol

Fig. 6. Molecular docking and mutagenesis assay of TwCYP712K1 from T. wilfordii. (a) Molecular docking of TwCYP712K1 with friedelin and the amino acid residues in the active site that were selected for mutagenesis. Friedelin (yellow); haem (green with red and blue). (b) The active site of TwCYP712K1 is shown as a cartoon and surface model. (c) The production of 29- hydroxyfriedelan-3-one in yeast harbour TwCYP712K1 or its mutants. (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 Cytochrome P450 catalyses the 29-carboxyl group formation of celastrol

Fig. 5. The role of TwCYP712K1 in celastrol biosynthesis. (a) Network of differentially expressed CYP450s and TwOSC involved in the biosynthesis of celastrol. Transcripts are represented by circles and metabolites by squares and edges are drawn when the linear correlation coefficient is> 0.7 in that tissues. The size of each circle represents the amount of expression of the gene. The pie chart shows the ratio of gene accumulation expression in different tissues. Colour key: the root was represented by purple, the stem periderm by orange, leaves by green, the stem vascular bundle by blue and flowers by red. (b) Relative expression of TwCYP712K1 in RNAi suspension cells and control suspension cells. (c) Relative expression of TwCYP712K1 in the overexpression suspension cells and control suspension cells. (d) Celastrol content in the RNAi suspension cells, overexpression suspension cells and their control suspension cells. Student's t-test was used to test for significant differences in gene expression levels and celastrol levels between the control group and experimental group. The data represent the average ± SD of at least three independent lines of suspension cells. CK, control group; OE, overexpression group; and RI, RNA interference group. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 4 in Cytochrome P450 catalyses the 29-carboxyl group formation of celastrol

Fig. 4. Gas chromatography-mass spectrometry (GC-MS) analysis of the products in yeast strains harbouring TwCYP712K1 from T. wilfordii. (a) Gas chromatographymass spectrometry (GC-MS) analysis of the products in yeast strains harbouring TwCYP712K1 from T. wilfordii. Peak 1, friedelin; Peak 2, 29-hydroxyfriedelan-3-one; Peak 4, polpunonic acid. (b) The reaction catalysed by TwCYP712K1. TIC, Total Ion Chromatography; EIC, Extracted Ion Chromatogram.

Fig. 3 in Cytochrome P450 catalyses the 29-carboxyl group formation of celastrol

Fig. 3. Phylogenetic tree of candidate P450s from T. wilfordii. The maximum-likelihood method was used to construct this tree with 1000 replicate bootstrap supports.

Fig. 2 in Cytochrome P450 catalyses the 29-carboxyl group formation of celastrol

Fig. 2. Hierarchical clustering of RNA-Seq expression data and heat map depicting the expression profile of candidate P450 genes. (a) The gene expression of candidate P450 genes in different tissues of T. wilfordii. (b) The gene expression of candidate P450 genes in MeJA-induced suspension cells of T. wilfordii. Colour key: candidate CYP72 family genes (blue), candidate CYP450 genes showing specific expression in the root and induced by MeJA (red), and other candidate CYP450 genes with high expression levels in the root and TwOSC1-3 (black). RX, root xylem; RP, root phloem; RB, root periderm; PS, stem vascular bundle; SB, stem periderm; F, Flowers; and L, Leaves. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 1 in Cytochrome P450 catalyses the 29-carboxyl group formation of celastrol

Fig. 1. The proposed carboxyl group formation of celastrol at the C-29 position and carboxyl group formation of β-amyrin at C-30 position by other cytochrome P450s. The red dashed arrows indicate one or multiple proposed step reactions, and the black solid arrow indicates a biosynthetic reaction catalysed by known CYP450 genes. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

closedIPD-NOFeb 2026View details →

Cytochrome P450 Inhibition to Decrease Dosage of Dasatinib for Chronic Myelogenous Leukemia

ClinicalTrials.gov study NCT05638763. IPD Sharing: NO. Countries: 1. Publications: 3.

restrictedIPD-UNDECIDEDFeb 2026View details →

Evaluation of the Potential for Cytochrome P450 3A4 Inhibition by F901318 Using Oral Midazolam as a Probe

ClinicalTrials.gov study NCT02680808. IPD Sharing: UNDECIDED. Countries: 1. Publications: 0.

controlledIPD-YESFeb 2026View details →

A Study to Investigate Safety, Tolerability, and Pharmacokinetics (PK) of VH4524184 and the Potential for Changes in Cytochrome P450 3A (CYP3A) Activity

ClinicalTrials.gov study NCT05631704. IPD Sharing: YES. Countries: 1. Publications: 1.

restrictedIPD-UNDECIDEDFeb 2026View details →

Study to Evaluate the Effect of Cytochrome P450 (CYP) 3A Inhibition and Induction on the Pharmacokinetics of CC-220 in Healthy Subjects

ClinicalTrials.gov study NCT02820935. IPD Sharing: Not stated. Countries: 1. Publications: 1.