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The Productive Conformation of Arachidonic Acid Bound to Prostaglandin Synthase

Science (American Association for the Advancement of Science), 2000-09, Vol.289 (5486), p.1933-1937

2000

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Structure of Eicosapentaenoic and Linoleic Acids in the Cyclooxygenase Site of Prostaglandin Endoperoxide H Synthase-1

The Journal of biological chemistry, 2001-10, Vol.276 (40), p.37547-37555

2001

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Interactions of fatty acids, nonsteroidal anti-inflammatory drugs, and coxibs with the catalytic and allosteric subunits of cyclooxygenases-1 and -2

The Journal of biological chemistry, 2019-02, Vol.294 (5), p.1697-1705

2019

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The co‐crystal structure of unliganded bovine α‐thrombin and prethrombin‐2: Movement of the Tyr‐Pro‐Pro‐Trp segment and active site residues upon ligand binding

Protein science, 1997-07, Vol.6 (7), p.1438-1448

1997

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The structure of a complex of bovine alpha-thrombin and recombinant hirudin at 2.8-A resolution

The Journal of biological chemistry, 1992-09, Vol.267 (25), p.17670-17678

1992

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New insights into the regulation of the blood clotting cascade derived from the X-ray crystal structure of bovine meizothrombin des F1 in complex with PPACK

Structure (London), 1997-12, Vol.5 (12), p.1681-1693

1997

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The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9-angstrom resolution

The Journal of biological chemistry, 1995-03, Vol.270 (13), p.7077-7087

1995

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Prostaglandin endoperoxide H synthase-1: the functions of cyclooxygenase active site residues in the binding, positioning, and oxygenation of arachidonic acid

The Journal of biological chemistry, 2001-03, Vol.276 (13), p.10347

2001

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Bovine Thrombin Complexed with an Uncleavable Analog of Residues 7−19 of Fibrinogen Aα: Geometry of the Catalytic Triad and Interactions of the P1‘, P2‘, and P3‘ Substrate Residues

Biochemistry (Easton), 1996-10, Vol.35 (40), p.13030-13039

1996

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The amino-terminal residues in the crystal structure of connective tissue activating peptide-III (des10) block the ELR chemotactic sequence

Journal of molecular biology, 1997-02, Vol.266 (2), p.367-380

1997

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Coordinated productive and unproductive substrate binding in the COX-2 homodimer

Acta crystallographica. Section A, Foundations of crystallography, 2011-08, Vol.67 (a1), p.C424-C424

2011

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The structures of prostaglandin endoperoxide H synthases-1 and -2

Prostaglandins & other lipid mediators, 2002-08, Vol.68, p.129-152

2002

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The structure of a complex of bovine alpha -thrombin and recombinant hirudin at 2.8-angstrom resolution

The Journal of biological chemistry, 1992-09, Vol.267 (25), p.17670-17678

1992

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Mutational and X-ray Crystallographic Analysis of the Interaction of Dihomo-γ-linolenic Acid with Prostaglandin Endoperoxide H Synthases

The Journal of biological chemistry, 2001-03, Vol.276 (13), p.10358-10365

2001

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The Formation of Stable Fatty Acid Substrate Complexes in Prostaglandin H2 Synthase-1

Archives of biochemistry and biophysics, 2000-08, Vol.380 (1), p.39-45

2000

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The Crystal Structure of Recombinant Human Neutrophil-activating Peptide-2 (M6L) at 1.9-Å Resolution (∗)

The Journal of biological chemistry, 1995-03, Vol.270 (13), p.7077-7087

1995

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Structure of a Bovine Thrombin-Hirudin51−65 Complex Determined by a Combination of Molecular Replacement and Graphics. Incorporation of Known Structural Information in Molecular Replacement

Acta crystallographica. Section D, Biological crystallography., 1996-05, Vol.52 (3), p.453-464

1996

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Mutational and x-ray crystallographic analysis of the interaction of dihomo-y-linolenic acid with prostaglandin endoperoxide H synthases

The Journal of biological chemistry, 2003-03, Vol.276 (13 ; Mar. 30, 2003)

2003

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The formation of stable fatty acid substrate complexes in prostaglandin H(2) synthase-1

Archives of biochemistry and biophysics, 2000-08, Vol.380 (1), p.39-45

2000

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Crystal structure of fibrinogen-Aalpha peptide 1-23 (F8Y) bound to bovine thrombin explains why the mutation of Phe-8 to tyrosine strongly inhibits normal cleavage at Arg-16

Biochemical journal, 1997-09, Vol.326 ( Pt 3) (Pt 3), p.815-822

1997

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Crystal structure of fibrinogen-A α peptide 1–23 (F8Y) bound to bovine thrombin explains why the mutation of Phe-8 to tyrosine strongly inhibits normal cleavage at Arg-16

Biochemical journal, 1997-09, Vol.326 (3), p.815-822

1997

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Fatty acid binding to cyclooxygenases

International Congress series, 2002-11, Vol.1233, p.283-289

2002

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CTAP-IIIdes10: implications of amino terminal residues on chemotactic activity and receptor activation

Acta crystallographica. Section A, Foundations of crystallography, 1996-08, Vol.52 (a1), p.C236-C237

1996

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Structure of a Bovine Thrombin–Hirudin 51−65 Complex Determined by a Combination of Molecular Replacement and Graphics. Incorporation of Known Structural Information in Molecular Replacement

Acta crystallographica. Section D, Biological crystallography., 1996-05, Vol.52 (3), p.453-464

1996

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The structure of des-F1-meizothrombin: the nature and location of kringle-thrombin and kringle-kringle interactions

Acta crystallographica. Section A, Foundations of crystallography, 1993-08, Vol.49 (s1), p.c159-c159

1993

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The Productive Conformation of Arachidonic Acid Bound to Prostaglandin Synthase

Structure of Eicosapentaenoic and Linoleic Acids in the Cyclooxygenase Site of Prostaglandin Endoperoxide H Synthase-1

Interactions of fatty acids, nonsteroidal anti-inflammatory drugs, and coxibs with the catalytic and allosteric subunits of cyclooxygenases-1 and -2

The co‐crystal structure of unliganded bovine α‐thrombin and prethrombin‐2: Movement of the Tyr‐Pro‐Pro‐Trp segment and active site residues upon ligand binding

The structure of a complex of bovine alpha-thrombin and recombinant hirudin at 2.8-A resolution

New insights into the regulation of the blood clotting cascade derived from the X-ray crystal structure of bovine meizothrombin des F1 in complex with PPACK

The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9-angstrom resolution

Prostaglandin endoperoxide H synthase-1: the functions of cyclooxygenase active site residues in the binding, positioning, and oxygenation of arachidonic acid

Bovine Thrombin Complexed with an Uncleavable Analog of Residues 7−19 of Fibrinogen Aα: Geometry of the Catalytic Triad and Interactions of the P1‘, P2‘, and P3‘ Substrate Residues

The amino-terminal residues in the crystal structure of connective tissue activating peptide-III (des10) block the ELR chemotactic sequence

Coordinated productive and unproductive substrate binding in the COX-2 homodimer

The structures of prostaglandin endoperoxide H synthases-1 and -2

The structure of a complex of bovine alpha -thrombin and recombinant hirudin at 2.8-angstrom resolution

Mutational and X-ray Crystallographic Analysis of the Interaction of Dihomo-γ-linolenic Acid with Prostaglandin Endoperoxide H Synthases

The Formation of Stable Fatty Acid Substrate Complexes in Prostaglandin H2 Synthase-1

The Crystal Structure of Recombinant Human Neutrophil-activating Peptide-2 (M6L) at 1.9-Å Resolution (∗)

Structure of a Bovine Thrombin-Hirudin51−65 Complex Determined by a Combination of Molecular Replacement and Graphics. Incorporation of Known Structural Information in Molecular Replacement

Mutational and x-ray crystallographic analysis of the interaction of dihomo-y-linolenic acid with prostaglandin endoperoxide H synthases

The formation of stable fatty acid substrate complexes in prostaglandin H(2) synthase-1

Crystal structure of fibrinogen-Aalpha peptide 1-23 (F8Y) bound to bovine thrombin explains why the mutation of Phe-8 to tyrosine strongly inhibits normal cleavage at Arg-16

Crystal structure of fibrinogen-A α peptide 1–23 (F8Y) bound to bovine thrombin explains why the mutation of Phe-8 to tyrosine strongly inhibits normal cleavage at Arg-16

Fatty acid binding to cyclooxygenases

CTAP-IIIdes10: implications of amino terminal residues on chemotactic activity and receptor activation

Structure of a Bovine Thrombin–Hirudin 51−65 Complex Determined by a Combination of Molecular Replacement and Graphics. Incorporation of Known Structural Information in Molecular Replacement

The structure of des-F1-meizothrombin: the nature and location of kringle-thrombin and kringle-kringle interactions

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