insightii software package docking (Molecular Simulations Inc)
90
Structured Review
Molecular Simulations Inc
insightii software package docking
Insightii Software Package Docking, supplied by Molecular Simulations Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/docking+simulation+software/insightii+software+package+docking/pm12490624-146-6-16
Average 90 stars, based on 1 article reviews
Insightii Software Package Docking, supplied by Molecular Simulations Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/docking+simulation+software/insightii+software+package+docking/pm12490624-146-6-16
Average 90 stars, based on 1 article reviews
insightii software package docking - by Bioz Stars,
2026-10
90/100 stars
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Construct:Article Title: Analysis of differential substrate selectivities of CYP2B6 and CYP2E1 by site-directed mutagenesis and molecular modeling. Article Snippet: Human CYP2B6 and CYP2E1 were used to investigate the extent to which differential substrate selectivities between cytochrome P450 subfamilies reflect differences in active-site residues as opposed to distinct arrangement of the backbone of the enzymes.. Reciprocal CYP2B6 and CYP2E1 mutants at active-site positions 103, 209, 294, 363, 367, and 477 (numbering according to CYP2B6) were characterized using the CYP2B6-selective substrate 7-ethoxy-4-trifluoromethylcoumarin, the CYP2E1-selective substrate p-nitrophenol, and the common substrates 7-ethoxycoumarin, 7-butoxycoumarin, and arachidonic acid.. This report is the first to study the active site of CYP2E1 by systematic site-directed mutagenesis. Software:Article Title: Analysis of differential substrate selectivities of CYP2B6 and CYP2E1 by site-directed mutagenesis and molecular modeling. Article Snippet: Human CYP2B6 and CYP2E1 were used to investigate the extent to which differential substrate selectivities between cytochrome P450 subfamilies reflect differences in active-site residues as opposed to distinct arrangement of the backbone of the enzymes.. Reciprocal CYP2B6 and CYP2E1 mutants at active-site positions 103, 209, 294, 363, 367, and 477 (numbering according to CYP2B6) were characterized using the CYP2B6-selective substrate 7-ethoxy-4-trifluoromethylcoumarin, the CYP2E1-selective substrate p-nitrophenol, and the common substrates 7-ethoxycoumarin, 7-butoxycoumarin, and arachidonic acid.. This report is the first to study the active site of CYP2E1 by systematic site-directed mutagenesis. |