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Investigation of the Mechanism of Iron Release from the C-Lobe of Human Serum Transferrin: Mutational Analysis of the Role of a pH Sensitive Triad

Biochemistry (Easton), 2003-04, Vol.42 (13), p.3701-3707

2003

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Structure-Based Mutagenesis Reveals Critical Residues in the Transferrin Receptor Participating in the Mechanism of pH-Induced Release of Iron from Human Serum Transferrin

Biochemistry (Easton), 2012-03, Vol.51 (10), p.2113-2121

2012

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Ionic Residues of Human Serum Transferrin Affect Binding to the Transferrin Receptor and Iron Release

Biochemistry (Easton), 2012-01, Vol.51 (2), p.686-694

2012

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Intrinsic Fluorescence Reports a Global Conformational Change in the N-Lobe of Human Serum Transferrin following Iron Release

Biochemistry (Easton), 2007-09, Vol.46 (37), p.10603-10611

2007

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Inequivalent Contribution of the Five Tryptophan Residues in the C-Lobe of Human Serum Transferrin to the Fluorescence Increase when Iron is Released

Biochemistry (Easton), 2009-04, Vol.48 (13), p.2858-2867

2009

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Effect of Glycosylation on the Function of a Soluble, Recombinant Form of the Transferrin Receptor

Biochemistry (Easton), 2006-05, Vol.45 (21), p.6663-6673

2006

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Ligand-Induced Conformational Change in Transferrins: Crystal Structure of the Open Form of the N-Terminal Half-Molecule of Human Transferrin

Biochemistry (Easton), 1998-10, Vol.37 (40), p.13978-13986

1998

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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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Structural and Functional Consequences of the Substitution of Glycine 65 with Arginine in the N-Lobe of Human Transferrin

Biochemistry (Easton), 2009-03, Vol.48 (9), p.1945-1953

2009

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Differential Effect of a His Tag at the N- and C-Termini: Functional Studies with Recombinant Human Serum Transferrin

Biochemistry (Easton), 2002-07, Vol.41 (30), p.9448-9454

2002

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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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Engineering the Primary Substrate Specificity of Streptomyces griseus Trypsin

Biochemistry (Easton), 2003-08, Vol.42 (30), p.9060-9066

2003

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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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Inequivalence of the Two Tyrosine Ligands in the N-Lobe of Human Serum Transferrin

Biochemistry (Easton), 1997-12, Vol.36 (48), p.14853-14860

1997

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Composition of pH-Sensitive Triad in C-Lobe of Human Serum Transferrin. Comparison to Sequences of Ovotransferrin and Lactoferrin Provides Insight into Functional Differences in Iron Release

Biochemistry (Easton), 2005-11, Vol.44 (47), p.15451-15460

2005

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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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Conversion of Trypsin into a Na+-Activated Enzyme

Biochemistry (Easton), 2006-03, Vol.45 (9), p.2987-2993

2006

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Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin

Biochemistry (Easton), 1983-04, Vol.22 (9), p.2087-2097

1983

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A Kinetically Active Site in the C-Lobe of Human Transferrin

Biochemistry (Easton), 1997-09, Vol.36 (36), p.11036-11043

1997

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Structural and functional consequences of the substitution of glycine 65 by arginine in the N-lobe of human transferrin

Biochemistry (Easton), 2009-03, Vol.48 (9), p.1945-1953

2009

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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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Mutation of the Iron Ligand His 249 to Glu in the N-Lobe of Human Transferrin Abolishes the Dilysine “Trigger” but Does Not Significantly Affect Iron Release

Biochemistry (Easton), 2000-02, Vol.39 (6), p.1211-1216

2000

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Investigation of the Mechanism of Iron Release from the C-Lobe of Human Serum Transferrin: Mutational Analysis of the Role of a pH Sensitive Triad

Structure-Based Mutagenesis Reveals Critical Residues in the Transferrin Receptor Participating in the Mechanism of pH-Induced Release of Iron from Human Serum Transferrin

Ionic Residues of Human Serum Transferrin Affect Binding to the Transferrin Receptor and Iron Release

Intrinsic Fluorescence Reports a Global Conformational Change in the N-Lobe of Human Serum Transferrin following Iron Release

Inequivalent Contribution of the Five Tryptophan Residues in the C-Lobe of Human Serum Transferrin to the Fluorescence Increase when Iron is Released

Effect of Glycosylation on the Function of a Soluble, Recombinant Form of the Transferrin Receptor

Ligand-Induced Conformational Change in Transferrins: Crystal Structure of the Open Form of the N-Terminal Half-Molecule of Human Transferrin

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

Structural and Functional Consequences of the Substitution of Glycine 65 with Arginine in the N-Lobe of Human Transferrin

Differential Effect of a His Tag at the N- and C-Termini: Functional Studies with Recombinant Human Serum Transferrin

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

Engineering the Primary Substrate Specificity of Streptomyces griseus Trypsin

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

Inequivalence of the Two Tyrosine Ligands in the N-Lobe of Human Serum Transferrin

Composition of pH-Sensitive Triad in C-Lobe of Human Serum Transferrin. Comparison to Sequences of Ovotransferrin and Lactoferrin Provides Insight into Functional Differences in Iron Release

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

Conversion of Trypsin into a Na+-Activated Enzyme

Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin

A Kinetically Active Site in the C-Lobe of Human Transferrin

Structural and functional consequences of the substitution of glycine 65 by arginine in the N-lobe of human transferrin

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

Mutation of the Iron Ligand His 249 to Glu in the N-Lobe of Human Transferrin Abolishes the Dilysine “Trigger” but Does Not Significantly Affect Iron Release

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