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13 results for “Turbinaria”
MCR LTER: Coral Reef: Turbinaria CHN from a spatially explicit sampling campaign in lagoons of Moorea, French Polynesia
Nutrients are important for ecosystem structure and community dynamics. To quantify time-integrated patterns of nutrient regimes in tropical lagoon ecosystems, concentrations of nitrogen, hydrogen, and carbon were measured from tissues of the macroalga Turbinaria ornata collected in lagoons around Moorea, French Polynesia in 2016, 2017, and annually starting in 2019. These sampling periods initially corresponded with distinct seasonal shifts in rainfall and wave forcing and later focused on the rainy season. Results showed that N enrichment was highest nearshore in fringing reef habitats, as well as in bays and at reef passes.
MCR LTER: Coral Reef Resilience: Turbinaria Alternate State Experiment
These data describe the density of Turbinaria ornata stipes from experimentally manipulated 1 m X 1 m plots on the forereef and naturally occurring 1 m X 1 m patches on the fringing reefs. In this pilot experiment Turbinaria were transplanted from the fringing reef to the forereef at 10 m depth to test whether it persists upon establishment. This material is based upon work supported by the U.S. National Science Foundation under Grant No. OCE 16-37396 (and earlier awards) as well as a generous gift from the Gordon and Betty Moore Foundation. Research was completed under permits issued by the French Polynesian Government (Délégation à la Recherche) and the Haut-commissariat de la République en Polynésie Francaise (DTRT) (Protocole d'Accueil 2005-2018). This work represents a contribution of the Moorea Coral Reef (MCR) LTER Site.
Depth-dependent microskeletal features modify light harvesting in Turbinaria reniformis corals
Open the record for dataset details and reuse information.
Raman data for "Mechanisms and seasonal drivers of calcification in the temperate coral Turbinaria reniformis at its latitudinal limits"
<p>This file contains all the Raman data and code for "Mechanisms and seasonal drivers of calcification in the temperate coral <em>Turbinaria reniformis</em> at its latitudinal limits" by Ross et al. in Proceedings of the Royal Society B. Run the file, "run.R" in R to reproduce the analysis.</p> <p>Please see the published paper for methods and details: http://rspb.royalsocietypublishing.org/content/285/1879/20180215</p>
Fig. 1 in Spirornatas A-C from brown alga Turbinaria ornata: Anti-hypertensive spiroketals attenuate angiotensin-I converting enzyme
Fig. 1. Structural representation of 6,6-spiroketal compounds spirornatas A-C isolated from the thallus structure of the marine macroalga Turbinaria ornata.
Fig. 3 in Spirornatas A-C from brown alga Turbinaria ornata: Anti-hypertensive spiroketals attenuate angiotensin-I converting enzyme
Fig. 3. Molecular docking interactions of spirornata A and standard antihypertensive agent captopril with ACE-I. Nearer view of molecular binding interfaces of spirornata A (A) and captopril (B) in the catalytic domain (together with WPD loop) of ACE-I. The dotted lines designated the H-bonding connections with the active site of ACE-I. The studied compounds were drawn in ACD/ChemSketch, and saved as MDL-molfiles (ver-2000), which were changed to PDB layout using Open Babel (GUI ver-2.4.1.) software. The macromolecule was assigned for polar hydrogens with added kollman charge of +7.75. The grid box was built by the method of hit and miss, wherein grid box for ACE-I was taken as x = 57, y = 42, z = 38 (54 Å, 33 Å, 55 Å). The binding site was additionally corroborated by keeping the zinc ion in the optimized protein file. Cygwin-I terminal was applied to run the docking algorithm, and after autodocking experiment, RMSD (Root-Mean-Square Deviation) was evaluated, and Cygwin-II was used for further optimization.
Fig. 2 in Spirornatas A-C from brown alga Turbinaria ornata: Anti-hypertensive spiroketals attenuate angiotensin-I converting enzyme
Fig. 2. (A–C) Key1H–1H COSY and HMBC correlations of spirornatas A-C.1H–1H COSY correlations are depicted with bold-face bonds and the HMBCs as doublebarbed arrows. (D–F) NOESY correlations (designated as single-barbed arrows) of spirornatas A-C. (G–I) Computer-generated models of spirornatas A-C (correlations are depicted with double-sided arrows), respectively using MM2 force-field calculations.
Fig. 2 in Conoidecyclics A-C from marine macroalga Turbinaria conoides: Newly described natural macrolides with prospective bioactive properties
Fig. 2. (A1-C1) 1H–1H COSY (bold-face bonds), selected HMBCs (double-barbed arrows), (A2-C2) NOE (colored arrows) correlations of conoidecyclics A-C isolated from T. conoides and (A3-C3) computer-generated models using MM2 force field calculations were displayed.
Fig. 5 in Conoidecyclics A-C from marine macroalga Turbinaria conoides: Newly described natural macrolides with prospective bioactive properties
Fig. 5. (A1-A2) Representative hydrogen binding interactions between conoidecyclic C and the amino acyl residues in the catalytic sites of COX-2; (A3-A4) Representative hydrogen binding interactions between conoidecyclic C and the amino acyl residues in the catalytic sites of 5-LOX; (A5-A6) Representative hydrogen binding interactions between conoidecyclic C and the amino acyl residues in the catalytic sites of PTP-1B; (A7-A8) Representative hydrogen binding interactions between conoidecyclic C and the amino acyl residues in the catalytic sites of ACE as obtained from in silico molecular docking analysis.
Fig. 3 in Conoidecyclics A-C from marine macroalga Turbinaria conoides: Newly described natural macrolides with prospective bioactive properties
Fig. 3. (A1-A2) Representative hydrogen binding interactions between conoidecyclic A and the amino acyl residues in the catalytic sites of COX-2; (A3-A4) Representative hydrogen binding interactions between conoidecyclic A and the amino acyl residues in the catalytic sites of 5-LOX; (A5-A6) Representative hydrogen binding interactions between conoidecyclic A and the amino acyl residues in the catalytic sites of PTP-1B; (A7-A8) Representative hydrogen binding interactions between conoidecyclic A and the amino acyl residues in the catalytic sites of ACE as obtained from in silico molecular docking analysis.
Fig. 1 in Conoidecyclics A-C from marine macroalga Turbinaria conoides: Newly described natural macrolides with prospective bioactive properties
Fig. 1. Structural representations of conoidecyclics A-C purified from the solvent extract of T. conoides. The thallus structure (leaf-like) of T. conoides was illustrated.
Fig. 4 in Conoidecyclics A-C from marine macroalga Turbinaria conoides: Newly described natural macrolides with prospective bioactive properties
Fig. 4. (A1-A2) Representative hydrogen binding interactions between conoidecyclic B and the amino acyl residues in the catalytic sites of COX-2; (A3-A4) Representative hydrogen binding interactions between conoidecyclic B and the amino acyl residues in the catalytic sites of 5-LOX; (A5-A6) Representative hydrogen binding interactions between conoidecyclic B and the amino acyl residues in the catalytic sites of PTP-1B; (A7-A8) Representative hydrogen binding interactions between conoidecyclic B and the amino acyl residues in the catalytic sites of ACE as obtained from in silico molecular docking analysis.
Fig. 6 in Conoidecyclics A-C from marine macroalga Turbinaria conoides: Newly described natural macrolides with prospective bioactive properties
Fig. 6. Kinetic studies of the pharmacologic response with regard to inhibition mode of ACE-I (A–C), PTP-1B (D–F) and 5-LOX (G–I), respectively to the studied conoidecyclics A-C. Representation of Dixon plots for conoidecyclics A-C, for the determination of the inhibition constant Ki. The Ki value was determined from the negative X-axis value at the point of the intersection of the four lines. The data were expressed as the mean reciprocal of initial velocity for triplicates (n = 3) at each substrate concentration. Different concentrations of isolated compounds were used, and the inhibitory potentials were expressed in mM.
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