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A folding pattern that is stable to thermal cycling is achieved by long term storage of recombinant human beta-casein with four extra N-terminals amino-acid residues at -20 degrees C

Archives of biochemistry and biophysics, 2006-10, Vol.454 (1), p.55-58

2006

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The International Study to Predict Optimized Treatment in Depression (iSPOT-D): Outcomes from the acute phase of antidepressant treatment

Journal of psychiatric research, 2015-02, Vol.61, p.1-12

2015

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The effect of conserved residue charge reversal on the folding of recombinant non-phosphorylated human β-casein

Archives of biochemistry and biophysics, 2003-11, Vol.419 (2), p.244-250

2003

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Comparison of native and recombinant non-phosphorylated human β-casein: further evidence for a unique β-casein folding pattern

Archives of biochemistry and biophysics, 2003-07, Vol.415 (2), p.213-220

2003

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Reconstituted micelle formation using reduced, carboxymethylated bovine kappa-casein and human beta-casein

The protein journal, 2006-07, Vol.25 (5), p.352-360

2006

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Colloidal calcium phosphate in the reconstituted milk micelle may direct wild-type recombinant human beta-casein to fold like the native protein

The protein journal, 2005-08, Vol.24 (6), p.379-384

2005

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The Effect of C-Terminal Deletion on the Folding and Self-association of Recombinant Non-phosphorylated Human ß-Casein

The Protein Journal, 2004-11, Vol.23 (8), p.509-517

2004

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The formation of casein micelles reconstituted with Ca+2 and added inorganic phosphate is influenced by the non-phosphorylated form of human beta-casein

The protein journal, 2005-05, Vol.24 (4), p.227-232

2005

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The effect of C-terminal deletion on the folding and self-association of recombinant non-phosphorylated human beta-casein

The protein journal, 2004-11, Vol.23 (8), p.509

2004

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A folding pattern that is stable to thermal cycling is achieved by long term storage of recombinant human β-casein with four extra N-terminals amino-acid residues at −20 °C

Archives of biochemistry and biophysics, 2006-10, Vol.454 (1), p.55-58

2006

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Interactions of doubly phosphorylated human β‐casein with native and reduced, carboxymethylated bovine κ‐casein leading to micelle formation: Role of inorganic phosphate

The FASEB journal, 2006-03, Vol.20 (4), p.A617-A617

2006

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Colloidal Calcium Phosphate in the Reconstituted Milk Micelle May Direct Wild-type Recombinant Human [beta]-Casein to Fold Like the Native Protein

The Protein Journal, 2005-08, Vol.24 (6), p.379

2005

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The Formation of Casein Micelles Reconstituted with Ca+2 and Added Inorganic Phosphate is Influenced by the Non-phosphorylated Form of Human [beta]-Casein

The Protein Journal, 2005-05, Vol.24 (4), p.227

2005

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Association of Mixtures of the Two Major Forms of β-Casein from Human Milk

Journal of dairy science, 2001-10, Vol.84 (10), p.2163-2169

2001

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Reconstituted Micelle Formation Using Reduced, Carboxymethylated Bovine [kappa]-Casein and Human [beta]-Casein

The Protein Journal, 2006-07, Vol.25 (5), p.352

2006

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Thermal Cycling Aids Folding of a Recombinant Human β-Casein with Four Extra N-Terminal Amino Acid Residues

Archives of biochemistry and biophysics, 2000-11, Vol.383 (2), p.215-224

2000

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Monomer Characterization and Studies of Self-Association of the Major β-Casein of Human Milk

Journal of dairy science, 1997-08, Vol.80 (8), p.1554-1560

1997

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Structural Studies on Casein Micelles of Human Milk: Dissociation of β-Casein of Different Phosphorylation Levels Induced by Cooling and Ethylenediaminetetraacetate

Journal of dairy science, 1997-04, Vol.80 (4), p.628-633

1997

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The pH-dependent Dissociation of β-Casein from Human Milk Micelles: Role of Electrostatic Interactions

Journal of dairy science, 1998-12, Vol.81 (12), p.3149-3153

1998

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Stability ofEscherichia coliAlanyl-tRNA Synthetase Quaternary Structure under Increased Pressure

Archives of biochemistry and biophysics, 1997-10, Vol.346 (2), p.322-323

1997

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Stability of Escherichia coli alanyl-tRNA synthetase quaternary structure under increased pressure

Archives of biochemistry and biophysics, 1997-10, Vol.346 (2), p.322-323

1997

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κ-Casein and β-Caseins in Human-Milk Micelles: Structural Studies

Archives of biochemistry and biophysics, 1994-11, Vol.314 (2), p.329-336

1994

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Interaction Properties of Singly Phosphorylated Human β-Casein: Similarities with Other Phosphorylation Levels

Journal of dairy science, 1994-02, Vol.77 (2), p.405-412

1994

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Further Characterization ofEscherichia coliAlanyl–tRNA Synthetase

Archives of biochemistry and biophysics, 1996-04, Vol.328 (2), p.295-301

1996

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Further characterization of Escherichia coli alanyl-tRNA synthetase

Archives of biochemistry and biophysics, 1996-04, Vol.328 (2), p.295-301

1996

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A folding pattern that is stable to thermal cycling is achieved by long term storage of recombinant human beta-casein with four extra N-terminals amino-acid residues at -20 degrees C

The International Study to Predict Optimized Treatment in Depression (iSPOT-D): Outcomes from the acute phase of antidepressant treatment

The effect of conserved residue charge reversal on the folding of recombinant non-phosphorylated human β-casein

Comparison of native and recombinant non-phosphorylated human β-casein: further evidence for a unique β-casein folding pattern

Reconstituted micelle formation using reduced, carboxymethylated bovine kappa-casein and human beta-casein

Colloidal calcium phosphate in the reconstituted milk micelle may direct wild-type recombinant human beta-casein to fold like the native protein

The Effect of C-Terminal Deletion on the Folding and Self-association of Recombinant Non-phosphorylated Human ß-Casein

The formation of casein micelles reconstituted with Ca+2 and added inorganic phosphate is influenced by the non-phosphorylated form of human beta-casein

The effect of C-terminal deletion on the folding and self-association of recombinant non-phosphorylated human beta-casein

A folding pattern that is stable to thermal cycling is achieved by long term storage of recombinant human β-casein with four extra N-terminals amino-acid residues at −20 °C

Interactions of doubly phosphorylated human β‐casein with native and reduced, carboxymethylated bovine κ‐casein leading to micelle formation: Role of inorganic phosphate

Colloidal Calcium Phosphate in the Reconstituted Milk Micelle May Direct Wild-type Recombinant Human [beta]-Casein to Fold Like the Native Protein

The Formation of Casein Micelles Reconstituted with Ca+2 and Added Inorganic Phosphate is Influenced by the Non-phosphorylated Form of Human [beta]-Casein

Association of Mixtures of the Two Major Forms of β-Casein from Human Milk

Reconstituted Micelle Formation Using Reduced, Carboxymethylated Bovine [kappa]-Casein and Human [beta]-Casein

Thermal Cycling Aids Folding of a Recombinant Human β-Casein with Four Extra N-Terminal Amino Acid Residues

Monomer Characterization and Studies of Self-Association of the Major β-Casein of Human Milk

Structural Studies on Casein Micelles of Human Milk: Dissociation of β-Casein of Different Phosphorylation Levels Induced by Cooling and Ethylenediaminetetraacetate

The pH-dependent Dissociation of β-Casein from Human Milk Micelles: Role of Electrostatic Interactions

Stability ofEscherichia coliAlanyl-tRNA Synthetase Quaternary Structure under Increased Pressure

Stability of Escherichia coli alanyl-tRNA synthetase quaternary structure under increased pressure

κ-Casein and β-Caseins in Human-Milk Micelles: Structural Studies

Interaction Properties of Singly Phosphorylated Human β-Casein: Similarities with Other Phosphorylation Levels

Further Characterization ofEscherichia coliAlanyl–tRNA Synthetase

Further characterization of Escherichia coli alanyl-tRNA synthetase

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