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Structure of Porriolide, a New Metabolite from Alternaria porri

Bioscience, biotechnology, and biochemistry, 1993, Vol.57 (2), p.334-335

1993

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Protein engineering of CYP105s for their industrial uses

Biochimica et biophysica acta. Proteins and proteomics, 2018-01, Vol.1866 (1), p.23-31

2018

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Production of an active form of vitamin D 2 by genetically engineered CYP105A1

Biochemical and biophysical research communications, 2017-04, Vol.486 (2), p.336-341

2017

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Production of an active form of vitamin D2 by genetically engineered CYP105A1

Biochemical and biophysical research communications, 2017-04, Vol.486 (2), p.336-341

2017

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Interpretation of the potential response of PVC membrane ion-selective electrodes based on the mixed potential theory

Journal of electroanalytical chemistry (Lausanne, Switzerland), 2012-03, Vol.668, p.107-112

2012

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Bioconversion of vitamin D to its active form by bacterial or mammalian cytochrome P450

Biochimica et biophysica acta, 2011, Vol.1814 (1), p.249-256

2011

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Structure-Based Design of a Highly Active Vitamin D Hydroxylase from Streptomyces griseolus CYP105A1

Biochemistry (Easton), 2008-11, Vol.47 (46), p.11964-11972

2008

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Crystal Structure of CYP105A1 (P450SU-1) in Complex with 1α,25-Dihydroxyvitamin D 3

Biochemistry (Easton), 2008-04, Vol.47 (13), p.4017-4027

2008

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Crystal Structure of CYP105A1 (P450SU-1) in Complex with 1α,25-Dihydroxyvitamin D3

Biochemistry (Easton), 2008-04, Vol.47 (13), p.4017-4027

2008

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Application of the Mixed-Potential Theory to the Interpretation of the Potential Response of a PVC Membrane Ion-Selective Electrode for Desipramine

Analytical Sciences, 2012/05/10, Vol.28(6), pp.565-570

2012

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Three-step hydroxylation of vitamin D3 by a genetically engineered CYP105A1: enzymes and catalysis

The FEBS journal, 2010-10, Vol.277 (19), p.3999-4009

2010

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Three‐step hydroxylation of vitamin D3 by a genetically engineered CYP105A1

The FEBS journal, 2010-10, Vol.277 (19), p.3999-4009

2010

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Three‐step hydroxylation of vitamin D 3 by a genetically engineered CYP105A1: Enzymes and catalysis

The FEBS journal, 2010-10, Vol.277 (19), p.3999-4009

2010

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Crystal structure of CYP105A1 (P450SU-1) in complex with 1alpha,25-dihydroxyvitamin D3

Biochemistry (Easton), 2008-04, Vol.47 (13), p.4017

2008

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Crystal Structure of CYP105A1 (P450SU-1) in Complex with 1 alpha ,25-Dihydroxyvitamin D sub(3)

Biochemistry (Easton), 2008-01, Vol.47 (13), p.4017-4027

2008

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3P099 Crystal structure of cytochrome P450SU-1 (CYP105A1) reveals the mechanism of two-step activation of vitamin D_3(Hemeproteins,Poster Presentations)

Seibutsu Butsuri, 2007/11/20, Vol.47(supplement), pp.S227

2007

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Structure of Porriolide, a New Metabolite from Alternaria porri

Protein engineering of CYP105s for their industrial uses

Production of an active form of vitamin D 2 by genetically engineered CYP105A1

Production of an active form of vitamin D2 by genetically engineered CYP105A1

Interpretation of the potential response of PVC membrane ion-selective electrodes based on the mixed potential theory

Bioconversion of vitamin D to its active form by bacterial or mammalian cytochrome P450

Structure-Based Design of a Highly Active Vitamin D Hydroxylase from Streptomyces griseolus CYP105A1

Crystal Structure of CYP105A1 (P450SU-1) in Complex with 1α,25-Dihydroxyvitamin D 3

Crystal Structure of CYP105A1 (P450SU-1) in Complex with 1α,25-Dihydroxyvitamin D3

Application of the Mixed-Potential Theory to the Interpretation of the Potential Response of a PVC Membrane Ion-Selective Electrode for Desipramine

Three-step hydroxylation of vitamin D3 by a genetically engineered CYP105A1: enzymes and catalysis

Three‐step hydroxylation of vitamin D3 by a genetically engineered CYP105A1

Three‐step hydroxylation of vitamin D 3 by a genetically engineered CYP105A1: Enzymes and catalysis

Crystal structure of CYP105A1 (P450SU-1) in complex with 1alpha,25-dihydroxyvitamin D3

Crystal Structure of CYP105A1 (P450SU-1) in Complex with 1 alpha ,25-Dihydroxyvitamin D sub(3)

3P099 Crystal structure of cytochrome P450SU-1 (CYP105A1) reveals the mechanism of two-step activation of vitamin D_3(Hemeproteins,Poster Presentations)

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