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Incorporation of an Active Site Inhibitor in Factor VIIa Alters the Affinity for Tissue Factor

The Journal of biological chemistry, 1997-05, Vol.272 (18), p.11863-11868

1997

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Directed Evolution of a Thermostable Esterase

Proceedings of the National Academy of Sciences - PNAS, 1998-10, Vol.95 (22), p.12809-12813

1998

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Isomerase and Chaperone Activity of Prolyl Isomerase in the Folding of Carbonic Anhydrase

Science (American Association for the Advancement of Science), 1992-10, Vol.258 (5081), p.466-468

1992

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Exclusion of known protease-activated receptors in factor VIIa-induced signal transduction

Thrombosis and haemostasis, 2000-04, Vol.83 (4), p.571-576

2000

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Structural Mapping of an Aggregation Nucleation Site in a Molten Globule Intermediate

The Journal of biological chemistry, 1999-11, Vol.274 (46), p.32897-32903

1999

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Structural changes in factor VIIa induced by Ca2+ and tissue factor studied using circular dichroism spectroscopy

Protein science, 1996-08, Vol.5 (8), p.1531-1540

1996

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Probing Inhibitor-Induced Conformational Changes along the Interface between Tissue Factor and Factor VIIa

Biochemistry (Easton), 2001-08, Vol.40 (31), p.9324-9328

2001

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Trafficking of Endogenous Immunoglobulins by Endothelial Cells at the Blood-Brain Barrier

Scientific reports, 2016-05, Vol.6 (1), p.25658-25658, Article 25658

2016

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Binding of Zn2+ to a Ca2+ loop allosterically attenuates the activity of factor VIIa and reduces its affinity for tissue factor

Protein science, 2000-05, Vol.9 (5), p.859-866

2000

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Factor VIIa-induced p44/42 Mitogen-activated Protein Kinase Activation Requires the Proteolytic Activity of Factor VIIa and Is Independent of the Tissue Factor Cytoplasmic Domain

The Journal of biological chemistry, 1999-07, Vol.274 (30), p.21349-21354

1999

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Contribution of tryptophan residues to the CD spectrum of the extracellular domain of human tissue factor: application in folding studies and prediction of secondary structure

European journal of biochemistry, 2001-02, Vol.268 (4), p.1118-1128

2001

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A comparative CD study of carbonic anhydrase isoenzymes with different number of tryptophans: Impact on calculation of secondary structure content

Protein science, 1996-12, Vol.5 (12), p.2479-2484

1996

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Probing the interface between factor Xa and tissue factor in the quaternary complex tissue factor–factor VIIa–factor Xa–tissue factor pathway inhibitor

European journal of biochemistry, 2003-06, Vol.270 (12), p.2576-2582

2003

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Cis-trans isomerization is rate-determining in the reactivation of denatured human carbonic anhydrase II as evidenced by proline isomerase

FEBS letters, 1992-01, Vol.296 (1), p.90-94

1992

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Characterization of a folding intermediate of human carbonic anhydrase II: probing local mobility by electron paramagnetic resonance

Biophysical journal, 1995-07, Vol.69 (1), p.202-213

1995

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Properties of Spin and Fluorescent Labels at a Receptor-Ligand Interface

Biophysical journal, 1999-10, Vol.77 (4), p.2237-2250

1999

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Folding around the C-terminus of human carbonic anhydrase II Kinetic characterization by use of a chemically reactive SH-group introduced by protein engineering

FEBS letters, 1991-09, Vol.289 (1), p.117-122

1991

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Adsorption to silica nanoparticles of human carbonic anhydrase II and truncated forms induce a molten-globule-like structure

FEBS letters, 1997-02, Vol.402 (1), p.67-72

1997

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Contribution of Individual Tryptophan Residues to the Fluorescence Spectrum of Native and Denatured Forms of Human Carbonic Anhydrase II

Biochemistry (Easton), 1995, Vol.34 (3), p.1011-1021

1995

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Characterization of folding intermediates of human carbonic anhydrase II : probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis

Biochemistry (Easton), 1993-01, Vol.32 (1), p.224-231

1993

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Spin and Fluorescent Probing of the Binding Interface between Tissue Factor and Factor VIIa at Multiple Sites

Biophysical journal, 2001-10, Vol.81 (4), p.2357-2369

2001

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Site-directed fluorescence probing to dissect the calcium-dependent association between soluble tissue factor and factor VIIa domains

Biochimica et biophysica acta, 2003-05, Vol.1648 (1), p.12-16

2003

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Conformational Stability of Factor VIIa: Biophysical Studies of Thermal and Guanidine Hydrochloride-Induced Denaturation

Biochemistry (Easton), 1998-05, Vol.37 (20), p.7203-7212

1998

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Formation of Local Native-like Tertiary Structures in the Slow Refolding Reaction of Human Carbonic Anhydrase II as Monitored by Circular Dichroism on Tryptophan Mutants

Biochemistry (Easton), 1997-04, Vol.36 (15), p.4623-4630

1997

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Sequential coagulation factor VIIa domain binding to tissue factor

Biochemical and biophysical research communications, 2005-12, Vol.337 (4), p.1276-1282

2005

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Incorporation of an Active Site Inhibitor in Factor VIIa Alters the Affinity for Tissue Factor

Directed Evolution of a Thermostable Esterase

Isomerase and Chaperone Activity of Prolyl Isomerase in the Folding of Carbonic Anhydrase

Exclusion of known protease-activated receptors in factor VIIa-induced signal transduction

Structural Mapping of an Aggregation Nucleation Site in a Molten Globule Intermediate

Structural changes in factor VIIa induced by Ca2+ and tissue factor studied using circular dichroism spectroscopy

Probing Inhibitor-Induced Conformational Changes along the Interface between Tissue Factor and Factor VIIa

Trafficking of Endogenous Immunoglobulins by Endothelial Cells at the Blood-Brain Barrier

Binding of Zn2+ to a Ca2+ loop allosterically attenuates the activity of factor VIIa and reduces its affinity for tissue factor

Factor VIIa-induced p44/42 Mitogen-activated Protein Kinase Activation Requires the Proteolytic Activity of Factor VIIa and Is Independent of the Tissue Factor Cytoplasmic Domain

Contribution of tryptophan residues to the CD spectrum of the extracellular domain of human tissue factor: application in folding studies and prediction of secondary structure

A comparative CD study of carbonic anhydrase isoenzymes with different number of tryptophans: Impact on calculation of secondary structure content

Probing the interface between factor Xa and tissue factor in the quaternary complex tissue factor–factor VIIa–factor Xa–tissue factor pathway inhibitor

Cis-trans isomerization is rate-determining in the reactivation of denatured human carbonic anhydrase II as evidenced by proline isomerase

Characterization of a folding intermediate of human carbonic anhydrase II: probing local mobility by electron paramagnetic resonance

Properties of Spin and Fluorescent Labels at a Receptor-Ligand Interface

Folding around the C-terminus of human carbonic anhydrase II Kinetic characterization by use of a chemically reactive SH-group introduced by protein engineering

Adsorption to silica nanoparticles of human carbonic anhydrase II and truncated forms induce a molten-globule-like structure

Contribution of Individual Tryptophan Residues to the Fluorescence Spectrum of Native and Denatured Forms of Human Carbonic Anhydrase II

Characterization of folding intermediates of human carbonic anhydrase II : probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis

Spin and Fluorescent Probing of the Binding Interface between Tissue Factor and Factor VIIa at Multiple Sites

Site-directed fluorescence probing to dissect the calcium-dependent association between soluble tissue factor and factor VIIa domains

Conformational Stability of Factor VIIa: Biophysical Studies of Thermal and Guanidine Hydrochloride-Induced Denaturation

Formation of Local Native-like Tertiary Structures in the Slow Refolding Reaction of Human Carbonic Anhydrase II as Monitored by Circular Dichroism on Tryptophan Mutants

Sequential coagulation factor VIIa domain binding to tissue factor

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