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Discovery of a Long-Acting, Peripherally Selective Inhibitor of Catechol-O-methyltransferase

Journal of medicinal chemistry, 2010-04, Vol.53 (8), p.3396-3411

2010

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Pharmacokinetics, Pharmacodynamics and Tolerability of Opicapone, a Novel Catechol-O-Methyltransferase Inhibitor, in Healthy Subjects: Prediction of Slow Enzyme–Inhibitor Complex Dissociation of a Short-Living and Very Long-Acting Inhibitor

Clinical pharmacokinetics, 2013-02, Vol.52 (2), p.139-151

2013

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Inactivation Mechanism of the Fatty Acid Amide Hydrolase Inhibitor BIA 10‐2474

Chembiochem : a European journal of chemical biology, 2022-10, Vol.23 (20), p.e202200166-n/a

2022

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Opicapone: a short lived and very long acting novel catechol‐O‐methyltransferase inhibitor following multiple dose administration in healthy subjects

British journal of clinical pharmacology, 2013-11, Vol.76 (5), p.763-775

2013

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Discovery of a Potent, Long‐Acting, and CNS‐Active Inhibitor (BIA 10‐2474) of Fatty Acid Amide Hydrolase

ChemMedChem, 2018-10, Vol.13 (20), p.2177-2188

2018

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Synthesis, Biological Evaluation, and Molecular Modeling Studies of a Novel, Peripherally Selective Inhibitor of Catechol-O-methyltransferase

Journal of medicinal chemistry, 2004-12, Vol.47 (25), p.6207-6217

2004

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Computation of the binding affinities of catechol-O-methyltransferase inhibitors: Multisubstate relative free energy calculations

Journal of computational chemistry, 2012-04, Vol.33 (9), p.970-986

2012

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BiGGER: A new (soft) docking algorithm for predicting protein interactions

Proteins, structure, function, and bioinformatics, 2000-06, Vol.39 (4), p.372-384

2000

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Modeling protein complexes with BiGGER

Proteins, structure, function, and bioinformatics, 2003-07, Vol.52 (1), p.19-23

2003

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Synechocystis ferredoxin/ferredoxin-NADP +-reductase/NADP + complex: Structural model obtained by NMR-restrained docking

FEBS letters, 2005-08, Vol.579 (21), p.4585-4590

2005

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Catechol‐O‐methyltransferase and Its Inhibitors in Parkinson's Disease

CNS drug reviews, 2007-09, Vol.13 (3), p.352-379

2007

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Structure of the Tetraheme Cytochrome from Desulfovibrio desulfuricans ATCC 27774: X-ray Diffraction and Electron Paramagnetic Resonance Studies

Biochemistry (Easton), 1995-10, Vol.34 (39), p.12830-12841

1995

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Structural Model of the Fe-Hydrogenase/Cytochromec 553 Complex Combining Transverse Relaxation-optimized Spectroscopy Experiments and Soft Docking Calculations

The Journal of biological chemistry, 2000-07, Vol.275 (30), p.23204-23210

2000

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CHAPTER 4 - Catechol‐O‐Methyl‐Transferase Inhibitors: Present Problems and Relevance of the New Ones

Emerging Drugs and Targets for Parkinson's Disease, 2013, p.83-109

2013

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Modelling the Electron-Transfer Complex Between Aldehyde Oxidoreductase and Flavodoxin

European Journal of Inorganic Chemistry, 2006-10, Vol.2006 (19), p.3835-3840

2006

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A novel approach for assessing macromolecular complexes combining soft-docking calculations with NMR data

Protein science, 2001-10, Vol.10 (10), p.2131-2137

2001

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Heteronuclear NMR and Soft Docking: An Experimental Approach for a Structural Model of the Cytochrome c553−Ferredoxin Complex

Biochemistry (Easton), 2000-03, Vol.39 (10), p.2530-2537

2000

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Structural model of the Fe-hydrogenase/cytochrome c553 complex combining transverse relaxation-optimized spectroscopy experiments and soft docking calculations

The Journal of biological chemistry, 2000-07, Vol.275 (30), p.23204-23210

2000

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A novel approach for assesing macromolecular complexes combining soft‐docking calculations with NMR data

Protein science, 2001-10, Vol.10 (10), p.2131-2137

2001

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Structural Model of the Fe-Hydrogenase/Cytochromec553 Complex Combining Transverse Relaxation-optimized Spectroscopy Experiments and Soft Docking Calculations

The Journal of biological chemistry, 2000-07, Vol.275 (30), p.23204-23210

2000

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Heteronuclear NMR and Soft Docking: An Experimental Approach for a Structural Model of the Cytochrome c 553−Ferredoxin Complex

Biochemistry (Easton), 2000-03, Vol.39 (10), p.2530-2537

2000

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[12] Ferredoxins

Methods in Enzymology, 1994, Vol.243, p.165-188

1994

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Evidence for a Ternary Complex Formed between Flavodoxin and Cytochrome c3: 1H-NMR and Molecular Modeling Studies

Biochemistry (Easton), 1994-05, Vol.33 (21), p.6394-6407

1994

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Two‐dimensional 1 H NMR studies on Desulfovibrio gigas ferredoxins. Assignment of the iron‐sulfur cluster cysteinyl ligand protons

Magnetic resonance in chemistry, 1993-12, Vol.31 (13)

1993

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Two-dimensional 1H NMR studies on Desulfovibrio gigas ferredoxins. Assignment of the iron-sulfur cluster cysteinyl ligand protons

Magnetic resonance in chemistry, 1993-12, Vol.31 (13), p.S59-S67

1993

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Discovery of a Long-Acting, Peripherally Selective Inhibitor of Catechol-O-methyltransferase

Pharmacokinetics, Pharmacodynamics and Tolerability of Opicapone, a Novel Catechol-O-Methyltransferase Inhibitor, in Healthy Subjects: Prediction of Slow Enzyme–Inhibitor Complex Dissociation of a Short-Living and Very Long-Acting Inhibitor

Inactivation Mechanism of the Fatty Acid Amide Hydrolase Inhibitor BIA 10‐2474

Opicapone: a short lived and very long acting novel catechol‐O‐methyltransferase inhibitor following multiple dose administration in healthy subjects

Discovery of a Potent, Long‐Acting, and CNS‐Active Inhibitor (BIA 10‐2474) of Fatty Acid Amide Hydrolase

Synthesis, Biological Evaluation, and Molecular Modeling Studies of a Novel, Peripherally Selective Inhibitor of Catechol-O-methyltransferase

Computation of the binding affinities of catechol-O-methyltransferase inhibitors: Multisubstate relative free energy calculations

BiGGER: A new (soft) docking algorithm for predicting protein interactions

Modeling protein complexes with BiGGER

Synechocystis ferredoxin/ferredoxin-NADP +-reductase/NADP + complex: Structural model obtained by NMR-restrained docking

Catechol‐O‐methyltransferase and Its Inhibitors in Parkinson's Disease

Structure of the Tetraheme Cytochrome from Desulfovibrio desulfuricans ATCC 27774: X-ray Diffraction and Electron Paramagnetic Resonance Studies

Structural Model of the Fe-Hydrogenase/Cytochromec 553 Complex Combining Transverse Relaxation-optimized Spectroscopy Experiments and Soft Docking Calculations

CHAPTER 4 - Catechol‐O‐Methyl‐Transferase Inhibitors: Present Problems and Relevance of the New Ones

Modelling the Electron-Transfer Complex Between Aldehyde Oxidoreductase and Flavodoxin

A novel approach for assessing macromolecular complexes combining soft-docking calculations with NMR data

Heteronuclear NMR and Soft Docking: An Experimental Approach for a Structural Model of the Cytochrome c553−Ferredoxin Complex

Structural model of the Fe-hydrogenase/cytochrome c553 complex combining transverse relaxation-optimized spectroscopy experiments and soft docking calculations

A novel approach for assesing macromolecular complexes combining soft‐docking calculations with NMR data

Structural Model of the Fe-Hydrogenase/Cytochromec553 Complex Combining Transverse Relaxation-optimized Spectroscopy Experiments and Soft Docking Calculations

Heteronuclear NMR and Soft Docking: An Experimental Approach for a Structural Model of the Cytochrome c 553−Ferredoxin Complex

[12] Ferredoxins

Evidence for a Ternary Complex Formed between Flavodoxin and Cytochrome c3: 1H-NMR and Molecular Modeling Studies

Two‐dimensional 1 H NMR studies on Desulfovibrio gigas ferredoxins. Assignment of the iron‐sulfur cluster cysteinyl ligand protons

Two-dimensional 1H NMR studies on Desulfovibrio gigas ferredoxins. Assignment of the iron-sulfur cluster cysteinyl ligand protons

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