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A novel murine protein with no effect on iron homoeostasis is homologous with transferrin and is the putative inhibitor of carbonic anhydrase

Biochemical journal, 2007-08, Vol.406 (1), p.85-95

2007

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Recombinant Expression and Functional Characterization of Human Hephaestin: A Multicopper Oxidase with Ferroxidase Activity

Biochemistry (Easton), 2005-11, Vol.44 (45), p.14725-14731

2005

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Mutational Analysis of C-Lobe Ligands of Human Serum Transferrin: Insights into the Mechanism of Iron Release

Biochemistry (Easton), 2005-06, Vol.44 (22), p.8013-8021

2005

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Two High-Resolution Crystal Structures of the Recombinant N-Lobe of Human Transferrin Reveal a Structural Change Implicated in Iron Release

Biochemistry (Easton), 1998-06, Vol.37 (22), p.7919-7928

1998

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Dual Role of Lys206−Lys296 Interaction in Human Transferrin N-Lobe: Iron-Release Trigger and Anion-Binding Site

Biochemistry (Easton), 1999-07, Vol.38 (30), p.9704-9711

1999

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Kinetic Studies on the Removal of Iron and Aluminum from Recombinant and Site-Directed Mutant N-Lobe Half Transferrins

Biochemistry (Easton), 1998-10, Vol.37 (40), p.14157-14166

1998

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A loop in the N-lobe of human serum transferrin is critical for binding to the transferrin receptor as revealed by mutagenesis, isothermal titration calorimetry, and epitope mapping

Journal of molecular recognition, 2009-11, Vol.22 (6), p.521-529

2009

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Analysis of γ-Carboxyglutamic Acid Content of Protein, Urine, and Plasma by Capillary Electrophoresis and Laser-Induced Fluorescence

Analytical chemistry (Washington), 1999-04, Vol.71 (8), p.1633-1637

1999

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Mutagenic, electrochemical, and crystallographic investigation of the cytochrome b5 oxidation-reduction equilibrium: involvement of asparagine-57, serine-64, and heme propionate-7

Biochemistry (Easton), 1990-06, Vol.29 (23), p.5500-5508

1990

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Ligand Variation in the Transferrin Family: The Crystal Structure of the H249Q Mutant of the Human Transferrin N-lobe As a Model for Iron Binding in Insect Transferrins

Biochemistry (Easton), 2001-10, Vol.40 (39), p.11670-11675

2001

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Crystal Structures and Iron Release Properties of Mutants (K206A and K296A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin

Biochemistry (Easton), 2001-02, Vol.40 (6), p.1616-1623

2001

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Mutations at the Histidine 249 Ligand Profoundly Alter the Spectral and Iron-Binding Properties of Human Serum Transferrin N-Lobe

Biochemistry (Easton), 2000-02, Vol.39 (6), p.1205-1210

2000

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Expression of glycosylated and nonglycosylated human transferrin in mammalian cells. Characterization of the recombinant proteins with comparison to three commercially available transferrins

Biochemistry (Easton), 1993-05, Vol.32 (20), p.5472-5479

1993

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Receptor recognition sites reside in both lobes of human serum transferrin

Biochemical journal, 1997-08, Vol.326 ( Pt 1) (1), p.77-85

1997

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Expression of the amino-terminal half-molecule of human serum transferrin in cultured cells and characterization of the recombinant protein

Biochemistry (Easton), 1990-02, Vol.29 (6), p.1654-1660

1990

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X-ray Crystallography and Mass Spectroscopy Reveal that the N-lobe of Human Transferrin Expressed in Pichia pastoris Is Folded Correctly but Is Glycosylated on Serine-32

Biochemistry (Easton), 1999-02, Vol.38 (8), p.2535-2541

1999

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Characterization of wild-type and an active-site mutant in Escherichia coli of short-chain acyl-CoA dehydrogenase from Megasphaera elsdenii

Biochemistry (Easton), 1993-10, Vol.32 (40), p.10736-10742

1993

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Characterization of bovine prothrombin mRNA and its translation product

Biochemistry (Easton), 1984-04, Vol.23 (8), p.1626-1634

1984

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Expression, purification, and characterization of authentic monoferric and apo-human serum transferrins

Protein expression and purification, 2004-08, Vol.36 (2), p.318-326

2004

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Interlobe Communication in 13C-Methionine-Labeled Human Transferrin

Biochemistry (Easton), 1996-06, Vol.35 (24), p.7635-7642

1996

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Spectral and metal-binding properties of three single-point tryptophan mutants of the human transferrin N-lobe

Biochemical journal, 2001-03, Vol.354 (Pt 2), p.423-429

2001

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Characterization of the bovine prothrombin gene

Biochemistry (Easton), 1985-11, Vol.24 (24), p.6854-6861

1985

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Three-dimensional structure of lactoferrin. Implications for function, including comparisons with transferrin

Advances in experimental medicine and biology, 1998, Vol.443, p.1

1998

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Association of the two lobes of ovotransferrin is a prerequisite for receptor recognition. Studies with recombinant ovotransferrins

Biochemical journal, 1996-10, Vol.319 ( Pt 2) (2), p.361-368

1996

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Partial Characterization of Vertebrate Prothrombin cDNAs: Amplification and Sequence Analysis of the B Chain of Thrombin from Nine Different Species

Proceedings of the National Academy of Sciences - PNAS, 1992-04, Vol.89 (7), p.2779-2783

1992

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A novel murine protein with no effect on iron homoeostasis is homologous with transferrin and is the putative inhibitor of carbonic anhydrase

Recombinant Expression and Functional Characterization of Human Hephaestin: A Multicopper Oxidase with Ferroxidase Activity

Mutational Analysis of C-Lobe Ligands of Human Serum Transferrin: Insights into the Mechanism of Iron Release

Two High-Resolution Crystal Structures of the Recombinant N-Lobe of Human Transferrin Reveal a Structural Change Implicated in Iron Release

Dual Role of Lys206−Lys296 Interaction in Human Transferrin N-Lobe: Iron-Release Trigger and Anion-Binding Site

Kinetic Studies on the Removal of Iron and Aluminum from Recombinant and Site-Directed Mutant N-Lobe Half Transferrins

A loop in the N-lobe of human serum transferrin is critical for binding to the transferrin receptor as revealed by mutagenesis, isothermal titration calorimetry, and epitope mapping

Analysis of γ-Carboxyglutamic Acid Content of Protein, Urine, and Plasma by Capillary Electrophoresis and Laser-Induced Fluorescence

Mutagenic, electrochemical, and crystallographic investigation of the cytochrome b5 oxidation-reduction equilibrium: involvement of asparagine-57, serine-64, and heme propionate-7

Ligand Variation in the Transferrin Family: The Crystal Structure of the H249Q Mutant of the Human Transferrin N-lobe As a Model for Iron Binding in Insect Transferrins

Crystal Structures and Iron Release Properties of Mutants (K206A and K296A) That Abolish the Dilysine Interaction in the N-Lobe of Human Transferrin

Mutations at the Histidine 249 Ligand Profoundly Alter the Spectral and Iron-Binding Properties of Human Serum Transferrin N-Lobe

Expression of glycosylated and nonglycosylated human transferrin in mammalian cells. Characterization of the recombinant proteins with comparison to three commercially available transferrins

Receptor recognition sites reside in both lobes of human serum transferrin

Expression of the amino-terminal half-molecule of human serum transferrin in cultured cells and characterization of the recombinant protein

X-ray Crystallography and Mass Spectroscopy Reveal that the N-lobe of Human Transferrin Expressed in Pichia pastoris Is Folded Correctly but Is Glycosylated on Serine-32

Characterization of wild-type and an active-site mutant in Escherichia coli of short-chain acyl-CoA dehydrogenase from Megasphaera elsdenii

Characterization of bovine prothrombin mRNA and its translation product

Expression, purification, and characterization of authentic monoferric and apo-human serum transferrins

Interlobe Communication in 13C-Methionine-Labeled Human Transferrin

Spectral and metal-binding properties of three single-point tryptophan mutants of the human transferrin N-lobe

Characterization of the bovine prothrombin gene

Three-dimensional structure of lactoferrin. Implications for function, including comparisons with transferrin

Association of the two lobes of ovotransferrin is a prerequisite for receptor recognition. Studies with recombinant ovotransferrins

Partial Characterization of Vertebrate Prothrombin cDNAs: Amplification and Sequence Analysis of the B Chain of Thrombin from Nine Different Species

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