D F Lewis

发表

Molecular modelling and quantitative structure-activity relationship studies on the interaction of omeprazole with cytochrome P450 isozymes.

D. Lewis, B. Lake, B G Lake, 1998, Toxicology.

An assessment of human liver-derived in vitro systems to predict the in vivo metabolism and clearance of almokalant.

R J Edwards, A R Boobis, K J Hoffmann, 2001, Drug metabolism and disposition: the biological fate of chemicals.

Structural determinants of cytochrome P450 substrate specificity, binding affinity and catalytic rate.

M H Tarbit, D. Lewis, M. Tarbit, 1998, Chemico-biological interactions.

A combined COMPACT and HazardExpert study of 40 chemicals for which information on mutagenicity and carcinogenicity is known, including the results of human epidemiological studies

C. Ioannides, D. Parke, C Ioannides, 1998, Human and Experimental Toxicology.

Molecular modelling of mammalian CYP2B isoforms and their interaction with substrates, inhibitors and redox partners.

D. Lewis, B. Lake, B G Lake, 1997, Xenobiotica; the fate of foreign compounds in biological systems.

Quantitative Structure-Activity Relationships (QSARs) Within Substrates of Human Cytochromes P450 Involved in Drug Metabolism

M. Dickins, D F Lewis, M Dickins, 2001, Drug metabolism and drug interactions.

Interaction of a series of nitriles with the alcohol-inducible isoform of P450: computer analysis of structure-activity relationships.

D. Lewis, C. Ioannides, D. Parke, 1994, Xenobiotica; the fate of foreign compounds in biological systems.

Structural characteristics of human P450s involved in drug metabolism: QSARs and lipophilicity profiles.

D. Lewis, D F Lewis, D.F.V. Lewis, 2000, Toxicology.

The CYP2 family: models, mutants and interactions.

D. Lewis, D F Lewis, 1998, Xenobiotica; the fate of foreign compounds in biological systems.

Molecular modelling of the human cytochrome P450 isoform CYP2A6 and investigations of CYP2A substrate selectivity.

M H Tarbit, D. Lewis, B. Lake, 1999, Toxicology.

Comparison between rodent carcinogenicity test results of 44 chemicals and a number of predictive systems.

D. Lewis, D F Lewis, 1994, Regulatory toxicology and pharmacology : RTP.

On the recognition of mammalian microsomal cytochrome P450 substrates and their characteristics: towards the prediction of human p450 substrate specificity and metabolism.

D. Lewis, D F Lewis, 2000, Biochemical pharmacology.

Molecular modelling of CYP2E1 enzymes from rat, mouse and man: an explanation for species differences in butadiene metabolism and potential carcinogenicity, and rationalization of CYP2E substrate specificity.

D. Lewis, D. Parke, M. Bird, 1997, Toxicology.

Quantitative structure-activity relationships and COMPACT analysis of a series of food mutagens.

D. Lewis, C. Ioannides, D. Parke, 1995, Food additives and contaminants.

Molecular dimensions of the substrate binding site of cytochrome P-448.

D. Lewis, C. Ioannides, D. Parke, 1986, Biochemical pharmacology.

Validation of a novel molecular orbital approach (COMPACT) for the prospective safety evaluation of chemicals, by comparison with rodent carcinogenicity and Salmonella mutagenicity data evaluated by the U.S. NCI/NTP.

D. Lewis, C. Ioannides, D. Parke, 1993, Mutation research.

Molecular modelling of CYP2B6, the human CYP2B isoform, by homology with the substrate-bound CYP102 crystal structure: evaluation of CYP2B6 substrate characteristics, the cytochrome b5 binding site and comparisons with CYP2B1 and CYP2B4.

M H Tarbit, D. Lewis, B. Lake, 1999, Xenobiotica; the fate of foreign compounds in biological systems.

Molecular modelling of cytochrome CYP1A1: a putative access channel explains differences in induction potency between the isomers benzo(a)pyrene and benzo(e)pyrene, and 2- and 4-acetylaminofluorene.

D. Lewis, C. Ioannides, D. Parke, 1994, Toxicology letters.

Molecular modelling of human CYP2E1 by homology with the CYP102 haemoprotein domain: investigation of the interactions of substrates and inhibitors within the putative active site of the human CYP2E1 isoform.

M H Tarbit, D. Lewis, B. Lake, 2000, Xenobiotica; the fate of foreign compounds in biological systems.

Molecular modelling of CYP3A4 from an alignment with CYP102: identification of key interactions between putative active site residues and CYP3A-specific chemicals.

M H Tarbit, D. Lewis, M. Tarbit, 1996, Xenobiotica; the fate of foreign compounds in biological systems.

Molecular modelling of lanosterol 14 alpha-demethylase (CYP51) from Saccharomyces cerevisiae via homology with CYP102, a unique bacterial cytochrome P450 isoform: quantitative structure-activity relationships (QSARs) within two related series of antifungal azole derivatives.

M H Tarbit, D. Lewis, M. Tarbit, 1999, Journal of enzyme inhibition.

Molecular modelling of CYP1A subfamily members based on an alignment with CYP102: rationalization of CYP1A substrate specificity in terms of active site amino acid residues.

D. Lewis, B. Lake, B G Lake, 1996, Xenobiotica; the fate of foreign compounds in biological systems.

Molecular modelling of human CYP2C subfamily enzymes CYP2C9 and CYP2C19: rationalization of substrate specificity and site-directed mutagenesis experiments in the CYP2C subfamily.

M H Tarbit, D. Lewis, R. Weaver, 1998, Xenobiotica; the fate of foreign compounds in biological systems.

Further evaluation of COMPACT, the molecular orbital approach for the prospective safety evaluation of chemicals.

D. Parke, C Ioannides, D V Parke, 1998, Mutation research.

Molecular modelling of cytochrome P4502D6 (CYP2D6) based on an alignment with CYP102: structural studies on specific CYP2D6 substrate metabolism.

M H Tarbit, D. Lewis, M. Tarbit, 1997, Xenobiotica; the fate of foreign compounds in biological systems.