Ligand characterization of CYP4B1 isoforms modified for high-level expression in Escherichia coli and HepG2 cells.

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Ligand characterization of CYP4B1 isoforms modified for high-level expression in Escherichia coli and HepG2 cells.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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Ligand characterization of CYP ...... herichia coli and HepG2 cells.

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Ligand characterization of CYP ...... herichia coli and HepG2 cells.

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Ligand characterization of CYP ...... herichia coli and HepG2 cells.

@en

Ligand characterization of CYP ...... herichia coli and HepG2 cells.

@nl

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Ligand characterization of CYP ...... herichia coli and HepG2 cells.

@en

Ligand characterization of CYP ...... herichia coli and HepG2 cells.

@nl

P1476

Ligand characterization of CYP ...... cherichia coli and HepG2 cells

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P2093

Allan E Rettie

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Constanze Wiek

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Helmut Hanenberg

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John P Kowalski

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Katharina Roellecke

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Stephanie Mielke

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Veselin H Gyurov

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P2860

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Covalent linkage of prosthetic heme to CYP4 family P450 enzymes

Progress and problems with the use of suicide genes for targeted cancer therapy

CYP4 enzymes as potential drug targets: focus on enzyme multiplicity, inducers and inhibitors, and therapeutic modulation of 20-hydroxyeicosatetraenoic acid (20-HETE) synthase and fatty acid ω-hydroxylase activities

CYP4B1 activates 4-ipomeanol in rat lung

THE CARBON MONOXIDE-BINDING PIGMENT OF LIVER MICROSOMES. II. SOLUBILIZATION, PURIFICATION, AND PROPERTIES

Pharmacogenetics of cytochromes P450.

Evaluation of methods for estimating the dissociation constant of tight binding enzyme inhibitors.

Enhanced bacterial expression of several mammalian cytochrome P450s by codon optimization and chaperone coexpression

P304

205-216

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P31

scholarly article

P356

10.1093/PROTEIN/GZW075

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P433

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P478

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P50

Marco Girhard

Vera D Jäger

P577

2017-03-01T00:00:00Z

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P698

28073960

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P932

5421619

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