A model for human cytochrome P450 2D6 based on homology modeling and NMR studies of substrate binding.
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Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolutionCrystal structure of human cytochrome P450 2D6Structures of Cytochrome P450 2B4 Complexed with the Antiplatelet Drugs Ticlopidine and Clopidogrel,Structure-Guided Directed Evolution of Highly Selective P450-Based Magnetic Resonance Imaging Sensors for Dopamine and SerotoninInfluence of phenylalanine-481 substitutions on the catalytic activity of cytochrome P450 2D6Human NADPH-P450 oxidoreductase modulates the level of cytochrome P450 CYP2D6 holoprotein via haem oxygenase-dependent and -independent pathwaysComparative protein structure modeling using ModellerProtein structure modeling in the proteomics era.Comparative Protein Structure Modeling Using MODELLERStructural features of cytochromes P450 and ligands that affect drug metabolism as revealed by X-ray crystallography and NMR.Engineering of a water-soluble plant cytochrome P450, CYP73A1, and NMR-based orientation of natural and alternate substrates in the active site.Chemical proteomics from a nuclear magnetic resonance spectroscopy perspective.Quantitative structure-activity relationships (QSARs) within substrates of human cytochromes P450 involved in drug metabolism.New insights into the structural characteristics and functional relevance of the human cytochrome P450 2D6 enzyme.Rate-limiting steps in cytochrome P450 catalysis.Molecular evolution of the CYP2D subfamily in primates: purifying selection on substrate recognition sites without the frequent or long-tract gene conversionNMR in pharmacokinetic and pharmacodynamic profiling.Insights into drug metabolism by cytochromes P450 from modelling studies of CYP2D6-drug interactions.Computational prediction of human drug metabolism.Modeling kinetics of subcellular disposition of chemicals.Quantitation of human cytochrome P450 2D6 protein with immunoblot and mass spectrometry analysis.Pharmacovigilance: effects of herbal components on human drugs interactions involving cytochrome P450Conformational plasticity and structure/function relationships in cytochromes P450.Computational modeling of P450s for toxicity prediction.Directed evolution of cytochrome P450 enzymes for biocatalysis: exploiting the catalytic versatility of enzymes with relaxed substrate specificity.Substrate proton to heme distances in CYP2C9 allelic variants and alterations by the heterotropic activator, dapsone.Comparative Protein Structure Modeling Using MODELLER.Modeling the active sites of cytochrome P450s and glutathione S-transferases, two of the most important biotransformation enzymes.Engineering microsomal cytochrome P450 2C5 to be a soluble, monomeric enzyme. Mutations that alter aggregation, phospholipid dependence of catalysis, and membrane binding.Determinants of the substrate specificity of human cytochrome P-450 CYP2D6: design and construction of a mutant with testosterone hydroxylase activity.Ile115Leu mutation in the SRS1 region of an insect cytochrome P450 (CYP6B1) compromises substrate turnover via changes in a predicted product release channel.Evidence that serine 304 is not a key ligand-binding residue in the active site of cytochrome P450 2D6.Diversity in mechanisms of substrate oxidation by cytochrome P450 2D6. Lack of an allosteric role of NADPH-cytochrome P450 reductase in catalytic regioselectivity.Oxidation of methoxyphenethylamines by cytochrome P450 2D6. Analysis of rate-limiting steps.Impact of incorporating the 2C5 crystal structure into comparative models of cytochrome P450 2D6.Residues glutamate 216 and aspartate 301 are key determinants of substrate specificity and product regioselectivity in cytochrome P450 2D6.Comparative Protein Structure Modeling Using MODELLER.Isolation and characterization of the CYP2D6 gene in Felidae with comparison to other mammals.AmineDB: large scale docking of amines with CYP2D6 and scoring for druglike properties--towards defining the scope of the chemical defense against foreign amines in humans.Control of the stereo-selectivity of styrene epoxidation by cytochrome P450 BM3 using structure-based mutagenesis
P2860
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P2860
A model for human cytochrome P450 2D6 based on homology modeling and NMR studies of substrate binding.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
A model for human cytochrome P ...... studies of substrate binding.
@en
type
label
A model for human cytochrome P ...... studies of substrate binding.
@en
prefLabel
A model for human cytochrome P ...... studies of substrate binding.
@en
P2093
P356
P1433
P1476
A model for human cytochrome P ...... studies of substrate binding.
@en
P2093
Primrose WU
Roberts GC
Sutcliffe MJ
P304
P356
10.1021/BI952742O
P407
P577
1996-04-01T00:00:00Z