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Examining the interactions of Galahad™ compound with viruses to develop a novel inactivated influenza A virus vaccine

Heliyon, 2022-07, Vol.8 (7), p.e09887-e09887, Article e09887

2022

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Antithrombin III Phenylalanines 122 and 121 Contribute to Its High Affinity for Heparin and Its Conformational Activation

The Journal of biological chemistry, 2003-05, Vol.278 (18), p.15941-15950

2003

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Saturation Mutagenesis of the Antithrombin Reactive Center Loop P14 Residue Supports a Three-step Mechanism of Heparin Allosteric Activation Involving Intermediate and Fully Activated States

The Journal of biological chemistry, 2015-11, Vol.290 (47), p.28020-28036

2015

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Specificity of the Basic Side Chains of Lys114, Lys125, and Arg129 of Antithrombin in Heparin Binding

Biochemistry (Easton), 2002-10, Vol.41 (41), p.12369-12376

2002

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Importance of Lysine 125 for Heparin Binding and Activation of Antithrombin

Biochemistry (Easton), 2002-04, Vol.41 (15), p.4779-4788

2002

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Roles of N-Terminal Region Residues Lys11, Arg13, and Arg24 of Antithrombin in Heparin Recognition and in Promotion and Stabilization of the Heparin-Induced Conformational Change

Biochemistry (Easton), 2004-01, Vol.43 (3), p.675-683

2004

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Elimination of P1 Arginine 393 Interaction with Underlying Glutamic Acid 255 Partially Activates Antithrombin III for Thrombin Inhibition but Not Factor Xa Inhibition

The Journal of biological chemistry, 2002-07, Vol.277 (27), p.24460-24465

2002

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Disruption of a Tight Cluster Surrounding Tyrosine 131 in the Native Conformation of Antithrombin III Activates It for Factor Xa Inhibition

The Journal of biological chemistry, 2006-10, Vol.281 (42), p.31668-31676

2006

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Identification of Critical Molecular Interactions Mediating Heparin Activation of Antithrombin: Implications for the Design of Improved Heparin Anticoagulants

Trends in Cardiovascular Medicine, 2002-07, Vol.12 (5), p.198-205

2002

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Lysine 114 of Antithrombin Is of Crucial Importance for the Affinity and Kinetics of Heparin Pentasaccharide Binding

The Journal of biological chemistry, 2001-11, Vol.276 (47), p.43809-43817

2001

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The Oligosaccharide Side Chain on Asn-135 of α-Antithrombin, Absent in β-Antithrombin, Decreases the Heparin Affinity of the Inhibitor by Affecting the Heparin-Induced Conformational Change

Biochemistry (Easton), 1997-06, Vol.36 (22), p.6682-6691

1997

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The Antithrombin P1 Residue Is Important for Target Proteinase Specificity but Not for Heparin Activation of the Serpin. Characterization of P1 Antithrombin Variants with Altered Proteinase Specificity but Normal Heparin Activation

Biochemistry (Easton), 2001-06, Vol.40 (22), p.6670-6679

2001

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Disruption of a Tight Cluster Surrounding Tyrosine 131 in the Native Conformation of Antithrombin III Activates It for Factor Xa Inhibition

The Journal of biological chemistry, 2006-10, Vol.281 (42), p.31668-31676

2006

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Role of Arginine 129 in Heparin Binding and Activation of Antithrombin

The Journal of biological chemistry, 2000-06, Vol.275 (25), p.18976-18984

2000

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The Role of Arg46 and Arg47 of Antithrombin in Heparin Binding

Biochemistry (Easton), 1999-08, Vol.38 (31), p.10196-10204

1999

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The Region of Antithrombin Interacting with Full-Length Heparin Chains Outside the High-Affinity Pentasaccharide Sequence Extends to Lys136 but Not to Lys139

Biochemistry (Easton), 2000-07, Vol.39 (29), p.8512-8518

2000

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Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the .beta.-antithrombin III isoform with enhanced heparin affinity

Biochemistry (Easton), 1995-07, Vol.34 (26), p.8433-8440

1995

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Examining the interactions of Galahad™ compound with viruses to develop a novel inactivated influenza A virus vaccine

Heliyon, 2022-07, Vol.8 (7)

2022

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Examining the interactions of Galahad™ compound with viruses to develop a novel inactivated influenza A virus vaccine

Heliyon, 2022-07, Vol.8 (7)

2022

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The sequence of human serum albumin cDNA and its expression in E. coli

Nucleic acids research, 1981-11, Vol.9 (22), p.6103-6114

1981

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Specific protein synthesis in cellular differentiation

Developmental biology, 1986-09, Vol.117 (1), p.215-225

1986

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Thrombin-Antithrombin System

Trauma Induced Coagulopathy, p.15-29

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Structures and models of native serpins

Protein engineering, 1990-12, Vol.4 (2), p.107-108

BOCK, S. C

1990

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Specific protein synthesis in cellular differentiation: VI. Temporal expression of chorion gene families in Bombyx mori strain C108

Developmental biology, 1986, Vol.117 (1), p.215-225

1986

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Two-dimensional electrophoresis of small-molecular-weight proteins

Analytical biochemistry, 1979-10, Vol.99 (1), p.33-40

1979

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Examining the interactions of Galahad™ compound with viruses to develop a novel inactivated influenza A virus vaccine

Antithrombin III Phenylalanines 122 and 121 Contribute to Its High Affinity for Heparin and Its Conformational Activation

Saturation Mutagenesis of the Antithrombin Reactive Center Loop P14 Residue Supports a Three-step Mechanism of Heparin Allosteric Activation Involving Intermediate and Fully Activated States

Specificity of the Basic Side Chains of Lys114, Lys125, and Arg129 of Antithrombin in Heparin Binding

Importance of Lysine 125 for Heparin Binding and Activation of Antithrombin

Roles of N-Terminal Region Residues Lys11, Arg13, and Arg24 of Antithrombin in Heparin Recognition and in Promotion and Stabilization of the Heparin-Induced Conformational Change

Elimination of P1 Arginine 393 Interaction with Underlying Glutamic Acid 255 Partially Activates Antithrombin III for Thrombin Inhibition but Not Factor Xa Inhibition

Disruption of a Tight Cluster Surrounding Tyrosine 131 in the Native Conformation of Antithrombin III Activates It for Factor Xa Inhibition

Identification of Critical Molecular Interactions Mediating Heparin Activation of Antithrombin: Implications for the Design of Improved Heparin Anticoagulants

Lysine 114 of Antithrombin Is of Crucial Importance for the Affinity and Kinetics of Heparin Pentasaccharide Binding

The Oligosaccharide Side Chain on Asn-135 of α-Antithrombin, Absent in β-Antithrombin, Decreases the Heparin Affinity of the Inhibitor by Affecting the Heparin-Induced Conformational Change

The Antithrombin P1 Residue Is Important for Target Proteinase Specificity but Not for Heparin Activation of the Serpin. Characterization of P1 Antithrombin Variants with Altered Proteinase Specificity but Normal Heparin Activation

Disruption of a Tight Cluster Surrounding Tyrosine 131 in the Native Conformation of Antithrombin III Activates It for Factor Xa Inhibition

Role of Arginine 129 in Heparin Binding and Activation of Antithrombin

The Role of Arg46 and Arg47 of Antithrombin in Heparin Binding

The Region of Antithrombin Interacting with Full-Length Heparin Chains Outside the High-Affinity Pentasaccharide Sequence Extends to Lys136 but Not to Lys139

Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the .beta.-antithrombin III isoform with enhanced heparin affinity

Examining the interactions of Galahad™ compound with viruses to develop a novel inactivated influenza A virus vaccine

Examining the interactions of Galahad™ compound with viruses to develop a novel inactivated influenza A virus vaccine

The sequence of human serum albumin cDNA and its expression in E. coli

Specific protein synthesis in cellular differentiation

Thrombin-Antithrombin System

Structures and models of native serpins

Specific protein synthesis in cellular differentiation: VI. Temporal expression of chorion gene families in Bombyx mori strain C108

Two-dimensional electrophoresis of small-molecular-weight proteins

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