taxonID	type	format	identifier	references	title	description	created	creator	contributor	publisher	audience	source	license	rightsHolder	datasetID
03FB8795FF82BD495E50B9D7E2201FC8.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8258132/files/figure.png	https://doi.org/10.5281/zenodo.8258132	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.	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.	2021-11-30	Chakraborty, Kajal;Dhara, Shubhajit		Zenodo	biologists	Chakraborty, Kajal;Dhara, Shubhajit			
03FB8795FF82BD495E50B9D7E2201FC8.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8258126/files/figure.png	https://doi.org/10.5281/zenodo.8258126	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. 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.	2021-11-30	Chakraborty, Kajal;Dhara, Shubhajit		Zenodo	biologists	Chakraborty, Kajal;Dhara, Shubhajit			
03FB8795FF82BD495E50B9D7E2201FC8.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8258128/files/figure.png	https://doi.org/10.5281/zenodo.8258128	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. 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.	2021-11-30	Chakraborty, Kajal;Dhara, Shubhajit		Zenodo	biologists	Chakraborty, Kajal;Dhara, Shubhajit			
03FB8795FF82BD495E50B9D7E2201FC8.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8258130/files/figure.png	https://doi.org/10.5281/zenodo.8258130	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. 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.	2021-11-30	Chakraborty, Kajal;Dhara, Shubhajit		Zenodo	biologists	Chakraborty, Kajal;Dhara, Shubhajit			
