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Thiol−Disulfide Exchange between Glutaredoxin and Glutathione

Biochemistry (Easton), 2010-02, Vol.49 (4), p.810-820

2010

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A CBM20 low-affinity starch-binding domain from glucan, water dikinase

FEBS letters, 2009-04, Vol.583 (7), p.1159-1163

2009

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Exact Analysis of Competition Ligand Binding by Displacement Isothermal Titration Calorimetry

Analytical biochemistry, 2000-01, Vol.277 (2), p.260-266

Sigurskjold, Bent W.

2000

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Small Angle X-ray Studies Reveal That Aspergillus niger Glucoamylase Has a Defined Extended Conformation and Can Form Dimers in Solution

The Journal of biological chemistry, 2008-05, Vol.283 (21), p.14772-14780

2008

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Thermodynamics of Ligand Binding to Acyl-Coenzyme A Binding Protein Studied by Titration Calorimetry

Biochemistry (Easton), 1996-11, Vol.35 (45), p.14118-14126

1996

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Starch-binding domains in the CBM45 family - low-affinity domains from glucan, water dikinase and α-amylase involved in plastidial starch metabolism

The FEBS journal, 2011-04, Vol.278 (7), p.1175-1185

2011

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Two Secondary Carbohydrate Binding Sites on the Surface of Barley α-Amylase 1 Have Distinct Functions and Display Synergy in Hydrolysis of Starch Granules

Biochemistry (Easton), 2009-08, Vol.48 (32), p.7686-7697

2009

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Recognition of Peptides by Cyclodextrin Trimers

European Journal of Organic Chemistry, 2011-09, Vol.2011 (27), p.5279-5290

2011

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Stability and Function of Interdomain Linker Variants of Glucoamylase 1 from Aspergillus niger

Biochemistry (Easton), 2001-08, Vol.40 (31), p.9336-9346

2001

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The Structure of a Mixed GluR2 Ligand-binding Core Dimer in Complex with ( S)-Glutamate and the Antagonist ( S)-NS1209

Journal of molecular biology, 2006-04, Vol.357 (4), p.1184-1201

2006

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Molecular Recognition of a Salmonella Trisaccharide Epitope by Monoclonal Antibody Se155-4

Biochemistry (Easton), 1994-05, Vol.33 (17), p.5172-5182

1994

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Ligand Binding and Thermostability of Different Allosteric States of the Insulin Zinc−Hexamer

Biochemistry (Easton), 2006-03, Vol.45 (12), p.4014-4024

2006

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Development of prolactin receptor antagonists with reduced pH-dependence of receptor binding

Journal of molecular recognition, 2011-07, Vol.24 (4), p.533-547

2011

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Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes

The Journal of biological chemistry, 2005-01, Vol.280 (4), p.3051-3059

2005

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Kinetics and Energetics of the Binding between Barley α-Amylase/Subtilisin Inhibitor and Barley α-Amylase 2 Analyzed by Surface Plasmon Resonance and Isothermal Titration Calorimetry

Biochemistry (Easton), 2003-02, Vol.42 (6), p.1478-1487

2003

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Crystal Structure of the Ig1 Domain of the Neural Cell Adhesion Molecule NCAM2 Displays Domain Swapping

Journal of molecular biology, 2008-10, Vol.382 (5), p.1113-1120

2008

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Probing the combining site of an anti-carbohydrate antibody by saturation-mutagenesis: Role of the heavy-chain CDR3 residues

Biochemistry (Easton), 1993-02, Vol.32 (4), p.1180-1187

1993

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Thermodynamics of Reversible and Irreversible Unfolding and Domain Interactions of Glucoamylase from Aspergillus niger Studied by Differential Scanning and Isothermal Titration Calorimetry

Biochemistry (Easton), 1999-05, Vol.38 (19), p.6300-6310

1999

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Thermodynamics of Inhibitor Binding to the Catalytic Site of Glucoamylase from Aspergillus niger Determined by Displacement Titration Calorimetry

Biochemistry (Easton), 1994-08, Vol.33 (33), p.10191-10199

1994

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Steady‐state kinetics of the glutaminase reaction of CTP synthase from Lactococcus lactis: The role of the allosteric activator GTP in coupling between glutamine hydrolysis and CTP synthesis

European journal of biochemistry, 2002-10, Vol.269 (19), p.4772-4779

2002

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Thermodynamics of Binding of Heterobidentate Ligands Consisting of Spacer-Connected Acarbose and β-Cyclodextrin to the Catalytic and Starch-Binding Domains of Glucoamylase from Aspergillus niger Shows That the Catalytic and Starch-Binding Sites Are in Close Proximity in Space

Biochemistry (Easton), 1998-07, Vol.37 (29), p.10446-10452

1998

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Physicochemical characterisation of the two active site mutants Trp(52)-->Phe and Asp(55)-->Val of glucoamylase from Aspergillus niger

Biochimica et biophysica acta, 2002-12, Vol.1601 (2), p.163

2002

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Structures of dCTP Deaminase from Escherichia coli with Bound Substrate and Product

The Journal of biological chemistry, 2005-01, Vol.280 (4), p.3051-3059

2005

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The Plasminogen Binding Site of the C-Type Lectin Tetranectin Is Located in the Carbohydrate Recognition Domain, and Binding Is Sensitive to Both Calcium and Lysine

The Journal of biological chemistry, 1998-10, Vol.273 (44), p.29241-29246

1998

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Tetranectin-Binding Site on Plasminogen Kringle 4 Involves the Lysine-Binding Pocket and at Least One Additional Amino Acid Residue

Biochemistry (Easton), 2000-06, Vol.39 (25), p.7414-7419

2000

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Thiol−Disulfide Exchange between Glutaredoxin and Glutathione

A CBM20 low-affinity starch-binding domain from glucan, water dikinase

Exact Analysis of Competition Ligand Binding by Displacement Isothermal Titration Calorimetry

Small Angle X-ray Studies Reveal That Aspergillus niger Glucoamylase Has a Defined Extended Conformation and Can Form Dimers in Solution

Thermodynamics of Ligand Binding to Acyl-Coenzyme A Binding Protein Studied by Titration Calorimetry

Starch-binding domains in the CBM45 family - low-affinity domains from glucan, water dikinase and α-amylase involved in plastidial starch metabolism

Two Secondary Carbohydrate Binding Sites on the Surface of Barley α-Amylase 1 Have Distinct Functions and Display Synergy in Hydrolysis of Starch Granules

Recognition of Peptides by Cyclodextrin Trimers

Stability and Function of Interdomain Linker Variants of Glucoamylase 1 from Aspergillus niger

The Structure of a Mixed GluR2 Ligand-binding Core Dimer in Complex with ( S)-Glutamate and the Antagonist ( S)-NS1209

Molecular Recognition of a Salmonella Trisaccharide Epitope by Monoclonal Antibody Se155-4

Ligand Binding and Thermostability of Different Allosteric States of the Insulin Zinc−Hexamer

Development of prolactin receptor antagonists with reduced pH-dependence of receptor binding

Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes

Kinetics and Energetics of the Binding between Barley α-Amylase/Subtilisin Inhibitor and Barley α-Amylase 2 Analyzed by Surface Plasmon Resonance and Isothermal Titration Calorimetry

Crystal Structure of the Ig1 Domain of the Neural Cell Adhesion Molecule NCAM2 Displays Domain Swapping

Probing the combining site of an anti-carbohydrate antibody by saturation-mutagenesis: Role of the heavy-chain CDR3 residues

Thermodynamics of Reversible and Irreversible Unfolding and Domain Interactions of Glucoamylase from Aspergillus niger Studied by Differential Scanning and Isothermal Titration Calorimetry

Thermodynamics of Inhibitor Binding to the Catalytic Site of Glucoamylase from Aspergillus niger Determined by Displacement Titration Calorimetry

Steady‐state kinetics of the glutaminase reaction of CTP synthase from Lactococcus lactis: The role of the allosteric activator GTP in coupling between glutamine hydrolysis and CTP synthesis

Thermodynamics of Binding of Heterobidentate Ligands Consisting of Spacer-Connected Acarbose and β-Cyclodextrin to the Catalytic and Starch-Binding Domains of Glucoamylase from Aspergillus niger Shows That the Catalytic and Starch-Binding Sites Are in Close Proximity in Space

Physicochemical characterisation of the two active site mutants Trp(52)-->Phe and Asp(55)-->Val of glucoamylase from Aspergillus niger

Structures of dCTP Deaminase from Escherichia coli with Bound Substrate and Product

The Plasminogen Binding Site of the C-Type Lectin Tetranectin Is Located in the Carbohydrate Recognition Domain, and Binding Is Sensitive to Both Calcium and Lysine

Tetranectin-Binding Site on Plasminogen Kringle 4 Involves the Lysine-Binding Pocket and at Least One Additional Amino Acid Residue

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