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Resolution of Michaelis Complex, Acylation, and Conformational Change Steps in the Reactions of the Serpin, Plasminogen Activator Inhibitor-1, with Tissue Plasminogen Activator and Trypsin

Biochemistry (Easton), 2001-10, Vol.40 (39), p.11742-11756

2001

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Kinetic Characterization of dUTPase from Escherichia coli

The Journal of biological chemistry, 1996-09, Vol.271 (39), p.24010-24016

1996

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Partitioning of Serpin-Proteinase Reactions between Stable Inhibition and Substrate Cleavage Is Regulated by the Rate of Serpin Reactive Center Loop Insertion into β-Sheet A

The Journal of biological chemistry, 2000-02, Vol.275 (8), p.5839-5844

2000

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Serpin-Protease Complexes Are Trapped as Stable Acyl-Enzyme Intermediates (∗)

The Journal of biological chemistry, 1995-10, Vol.270 (43), p.25309-25312

1995

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Accelerated Conversion of Human Plasminogen Activator Inhibitor-1 to Its Latent Form by Antibody Binding

The Journal of biological chemistry, 1999-06, Vol.274 (25), p.17511-17517

1999

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Inhibitory Mechanism of Serpins: Loop Insertion Forces Acylation of Plasminogen Activator by Plasminogen Activator Inhibitor-1

Biochemistry (Easton), 1998-11, Vol.37 (44), p.15491-15502

1998

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The acid stabilization of plasminogen activator inhibitor-1 depends on protonation of a single group that affects loop insertion into beta-sheet A

The Journal of biological chemistry, 1995-11, Vol.270 (46), p.27942-27947

1995

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dUTPase from the retrovirus equine infectious anemia virus: specificity, turnover and inhibition

FEBS letters, 1997-09, Vol.414 (2), p.271-274

1997

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A fluorescent probe study of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism

The Journal of biological chemistry, 1995-03, Vol.270 (10), p.5395

1995

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Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin family. Contribution of a covalent interaction to the binding energy of serpin-proteinase complexes

The Journal of biological chemistry, 1995-12, Vol.270 (50), p.30007-30017

1995

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Mutation of the Highly Conserved Tryptophan in the Serpin Breach Region Alters the Inhibitory Mechanism of Plasminogen Activator Inhibitor-1

Biochemistry (Easton), 2003-10, Vol.42 (42), p.12260-12272

2003

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A double role for a strictly conserved serine: further insights into the dUTPase catalytic mechanism (Poster Presentations)

33rd FEBS Congress and 11th IUBMB Conference,Athens, Greece,2008-06-28 - 2008-07-03, 2008, Vol.275 (Suppl. 1), p.165

2008

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Purification of human plasminogen activator inhibitor (PAI-1) from Escherichia coli and separation of its active and latent forms by hydrophobic interaction chromatography

Fibrinolysis, 1995-07, Vol.9 (4), p.215-221

1995

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Effect of ph on coenzyme binding to liver alcohol dehydrogenase [horse]

European journal of biochemistry, 1979-10, Vol.100 (1), p.115-123

1979

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Stereochemistry of colchicinoids. Enantiomeric stability and binding to tubulin of desacetamidocolchicine and desacetamidoisocolchicine

Bioorganic chemistry, 1991, Vol.19 (1), p.53-65

1991

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Mechanism of 1,3‐bisphosphoglycerate transfer from phosphoglycerate kinase to glyceraldehyde‐3‐phosphate dehydrogenase

European journal of biochemistry, 1989-12, Vol.186 (1‐2), p.265-272

1989

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Evidence that 1,3‐bisphosphoglycerate dissociation from phosphoglycerate kinase is an intrinsically rapid reaction step

European journal of biochemistry, 1989-12, Vol.186 (1‐2), p.261-264

1989

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Unified Mechanism for Proton‐Transfer Reactions Affecting the Catalytic Activity of Liver Alcohol Dehydrogenase

European journal of biochemistry, 1980-02, Vol.103 (3), p.565-575

1980

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Mechanism of glyceraldehyde‐3‐phosphate transfer from aldolase to glyceraldehyde‐3‐phosphate dehydrogenase

European journal of biochemistry, 1988-03, Vol.172 (2), p.427-431

1988

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Kinetics of coenzyme binding to liver alcohol dehydrogenase in the pH range 10–12

European journal of biochemistry, 1987-07, Vol.166 (1), p.167-172

1987

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Kinetic Transients in the Reduction of Aldehydes Catalysed by Liver Alcohol Dehydrogenase

European journal of biochemistry, 1976-10, Vol.69 (1), p.279-287

1976

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Effect of pH on the process of ternary-complex interconversion in the liver-alcohol-dehydrogenase reaction [horse]

European journal of biochemistry, 1978-06, Vol.87 (2), p.417-427

1978

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Catalytic significance of binary enzyme‐aldehyde complexes in the liver alcohol dehydrogenase reaction

European journal of biochemistry, 1984-03, Vol.139 (3), p.519-527

1984

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Synergism between Coenzyme and Aldehyde Binding to Liver Alcohol Dehydrogenase

European journal of biochemistry, 1983-07, Vol.133 (3), p.651-655

1983

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Effect of pH on the binding of decanoate and trifluoroethanol to liver alcohol dehydrogenase [horse]

European journal of biochemistry, 1980-02, Vol.103 (3), p.557-564

1980

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Resolution of Michaelis Complex, Acylation, and Conformational Change Steps in the Reactions of the Serpin, Plasminogen Activator Inhibitor-1, with Tissue Plasminogen Activator and Trypsin

Kinetic Characterization of dUTPase from Escherichia coli

Partitioning of Serpin-Proteinase Reactions between Stable Inhibition and Substrate Cleavage Is Regulated by the Rate of Serpin Reactive Center Loop Insertion into β-Sheet A

Serpin-Protease Complexes Are Trapped as Stable Acyl-Enzyme Intermediates (∗)

Accelerated Conversion of Human Plasminogen Activator Inhibitor-1 to Its Latent Form by Antibody Binding

Inhibitory Mechanism of Serpins: Loop Insertion Forces Acylation of Plasminogen Activator by Plasminogen Activator Inhibitor-1

The acid stabilization of plasminogen activator inhibitor-1 depends on protonation of a single group that affects loop insertion into beta-sheet A

dUTPase from the retrovirus equine infectious anemia virus: specificity, turnover and inhibition

A fluorescent probe study of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism

Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin family. Contribution of a covalent interaction to the binding energy of serpin-proteinase complexes

Mutation of the Highly Conserved Tryptophan in the Serpin Breach Region Alters the Inhibitory Mechanism of Plasminogen Activator Inhibitor-1

A double role for a strictly conserved serine: further insights into the dUTPase catalytic mechanism (Poster Presentations)

Purification of human plasminogen activator inhibitor (PAI-1) from Escherichia coli and separation of its active and latent forms by hydrophobic interaction chromatography

Effect of ph on coenzyme binding to liver alcohol dehydrogenase [horse]

Stereochemistry of colchicinoids. Enantiomeric stability and binding to tubulin of desacetamidocolchicine and desacetamidoisocolchicine

Mechanism of 1,3‐bisphosphoglycerate transfer from phosphoglycerate kinase to glyceraldehyde‐3‐phosphate dehydrogenase

Evidence that 1,3‐bisphosphoglycerate dissociation from phosphoglycerate kinase is an intrinsically rapid reaction step

Unified Mechanism for Proton‐Transfer Reactions Affecting the Catalytic Activity of Liver Alcohol Dehydrogenase

Mechanism of glyceraldehyde‐3‐phosphate transfer from aldolase to glyceraldehyde‐3‐phosphate dehydrogenase

Kinetics of coenzyme binding to liver alcohol dehydrogenase in the pH range 10–12

Kinetic Transients in the Reduction of Aldehydes Catalysed by Liver Alcohol Dehydrogenase

Effect of pH on the process of ternary-complex interconversion in the liver-alcohol-dehydrogenase reaction [horse]

Catalytic significance of binary enzyme‐aldehyde complexes in the liver alcohol dehydrogenase reaction

Synergism between Coenzyme and Aldehyde Binding to Liver Alcohol Dehydrogenase

Effect of pH on the binding of decanoate and trifluoroethanol to liver alcohol dehydrogenase [horse]

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