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415 results for “diterpenoid”
Fig. 10 in Diverse diterpenoids with α-glucosidase and β-glucuronidase inhibitory activities from Euphorbia milii
Fig. 10. The dose-dependent inhibition curves of inhibitors on PNPG-hydrolyzing activity of α-glucosidase (A) and EcGUS (B). All data were expressed as mean ± SD of triplicate reactions.
Fig. 8 in Highly oxygenated isoryanodane diterpenoids from the leaves of Cinnamomum cassia and their immunomodulatory activities
Fig. 8. Effects of 1, 2, 6, and 10 on ConA-induced T-cells proliferation (A) and effects of 1, 2, 6, and 10–12 on LPS-induced B-cells proliferation (B), mean ± SD of three replicates are shown.
Fig. 5 in Highly oxygenated isoryanodane diterpenoids from the leaves of Cinnamomum cassia and their immunomodulatory activities
Fig. 5. Linear correlation plots (A) and the relative errors (B) between the experimental and calculated 13C NMR chemical shifts of 4a 4d.
Fig. 7. The relative errors between the experimental and calculated 13C in Highly oxygenated isoryanodane diterpenoids from the leaves of Cinnamomum cassia and their immunomodulatory activities
Fig. 7. The relative errors between the experimental and calculated 13C NMR chemical shifts of 5 and 6.
Fig. 4 in Highly oxygenated isoryanodane diterpenoids from the leaves of Cinnamomum cassia and their immunomodulatory activities
Fig. 4. Linear correlation plots (A) and the relative errors (B) between the experimental and calculated 13C NMR chemical shifts of (8R*)-3a and (8S*)-3b.
Fig. 2. Key 1 H– 1 H in Pimarane, abietane, and labdane diterpenoids from Euphorbia pekinensis Rupr. and their anti-tumor activities
Fig. 2. Key 1 H– 1 H COSY (red bold lines) and HMBC (blue→) of compounds 5 (a1) and 16 (a2), NOSEY correlation (blue→) of compounds 5 (b1) and 16 (b2), The ORTEP drawing of compounds 5 (c1) and 16 (c2). (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Fig. 3. Key 1H–1H in Pimarane, abietane, and labdane diterpenoids from Euphorbia pekinensis Rupr. and their anti-tumor activities
Fig. 3. Key 1H–1H COSY (red bold lines) and HMBC (blue→) of compound 9 (a), NOSEY correlation (blue→) of compound 9 (b), The ORTEP drawing of compound 9 (c). (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Fig. 4. Key 1H–1H in Pimarane, abietane, and labdane diterpenoids from Euphorbia pekinensis Rupr. and their anti-tumor activities
Fig. 4. Key 1H–1H COSY (red bold lines) and HMBC (blue→) correlation of compounds 11 (a), 12 (b), 13 (c), and 15 (d). (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Fig. 2 in Serrulatane diterpenoids from the leaves of Eremophila glabra and their potential as antihyperglycemic drug leads
Fig. 2. Structures of previously unreported serrulatane-type diterpenoids isolated from leaves of E. glabra. The full chemical names of the compounds 5a, 5c, 7, 8a, 8b, 10b, and 13c are found in the main text.
Fig. 4 in Serrulatane diterpenoids from the leaves of Eremophila glabra and their potential as antihyperglycemic drug leads
Fig. 4. Experimental and calculated electronic circular dichroism spectra of serrulatane-type diterpenoids. A. Experimental ECD of compounds in group A (5a, 5b, 5c, 6, 8b, 9, 11 and 13c). B. Experimental ECD of compounds in group B (8a and 12b). C. Experimental ECD of compounds in group B (7 and 10b). D. Calculated ECD of (1R,4S,11S)-5a model compared to the experimental ECD of 5a. E. Calculated ECD of (1R,4S,11S)-8a model compared to the experimental ECD of 8a. F. Calculated ECD of (1S,2R,4S,11S)-7 model compared to the experimental ECD of 7a.
Fig. 1 in Serrulatane diterpenoids from the leaves of Eremophila glabra and their potential as antihyperglycemic drug leads
Fig. 1. Dual high-resolution α-glucosidase/PTP1B inhibition profile of the crude extract of E. glabra leaf resin. The analytical-scale HPLC profile recorded at 254 nm is shown at the top with isolated fractions/compounds marked by numbers. The corresponding high-resolution α-glucosidase (red) and PTP1B (green) inhibition profiles are shown below. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 3 in Serrulatane diterpenoids from the leaves of Eremophila glabra and their potential as antihyperglycemic drug leads
Fig. 3. Key COSY (bold), HMBC (black, H to C), and ROESY (red) correlations used for structure elucidation of the previously unreported serrulatane-type diterpenoids isolated from E. glabra. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 7 in Thirteen cyathane diterpenoids with acetylcholinesterase inhibitory effects from the fungus Cyathus africanus
Fig. 7. The binding modes of 9 (A), 10 (B) and 11 (C) with human AChE (PDB ID: 4M0F). Hydrogen bond interactions were depicted with red dotted lines in Å. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
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.
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.
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. 1 in Antifeedant, cytotoxic, and anti-inflammatory neo-clerodane diterpenoids in the peltate glandular trichomes and fresh leaves of Ajuga forrestii
Fig. 1. Morphology and laser microdissection of the peltate glandular trichomes (GTs) of A. forrestii. (A) An A. forrestii plant growing in its natural habitat. (B) An A. forrestii plant blooming. (C) Peltate GTs on the leaf surface. (D) Intact peltate GTs before dissection. (E) The remaining leaf tissue after dissection of a peltate GT. (F) Peltate GTs collected in the cap of a centrifuge tube. (G) Other leaf tissues (LTs) without glandular trichomes before dissection. (H) The remaining leaf tissue after dissection of the LTs. (I) LTs collected in the cap of a centrifuge tube. Panels (C-I) are micrographs.
Fig. 2 in Antifeedant, cytotoxic, and anti-inflammatory neo-clerodane diterpenoids in the peltate glandular trichomes and fresh leaves of Ajuga forrestii
Fig. 2. Chemical structures of compounds 1–14 identified in the peltate GTs and whole leaves of A. forrestii.
Fig. 4 in Diterpenoid alkaloids from Delphinium forrestii var. viride and their anti-inflammation activity
Fig. 4. Effect of compounds 1–15 on LPS-induced production of NO. Dexamethasone (Dex) was used as the positive control.
Fig. 8. Forrestline F suppressed LPSinduced inflammatory activity through Nrf2 in Diterpenoid alkaloids from Delphinium forrestii var. viride and their anti-inflammation activity
Fig. 8. Forrestline F suppressed LPSinduced inflammatory activity through Nrf2 pathways and promoted the LPSinduced nuclear translocation of Nrf2. (A–B) The cells were exposed to forrestline F (5, 10, 20 μM) for 3 h and cultured with LPS for 24 h, except for the control group. The protein expression of Keap-1/Nrf2 pathway was determined by western blotting and the quantifications of protein expression were performed by Image J. (C) The inhibitory effect of forrestline F (20 μM) on the nuclear translocation of Nrf2 induced by LPS via confocal laser scanning microscopy, in conjunction with nuclear DAPI stain (scale bar: 50 μM). The values are presented as mean ± SD of three independent experiments, n = 3. ###p <0.001, vs. the control group; ***p <0.001, vs. LPS-stimulated group.
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Allen Brain Atlas
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Annotated Behaviour and Observability Dataset (ABODe)
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DANDI Archive for NWB datasets
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International Brain Laboratory public data
The International Brain Laboratory public data releases expose standardized mouse decision-making experiments, including Neuropixels recordings, widefield calcium imaging, behavior, and session metadata accessed through the ONE API.
OpenNeuro
OpenNeuro is a free, open platform for sharing neuroimaging datasets, with public search, dataset pages, and download paths for web, S3, DataLad, and the OpenNeuro CLI.