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http://hub.abes.fr/acs/periodical/bichaw/1993/volume_32/issue_36/101021bi00087a015/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1994/volume_33/issue_12/101021bi00178a026/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1995/volume_34/issue_24/101021bi00024a008/authorship/5
http://hub.abes.fr/bmj/periodical/jmedgenet/2004/volume_41/issue_6/B3598D6B61937CBEE053120B220A90C5/authorship/11
http://hub.abes.fr/acs/periodical/bichaw/2003/volume_42/issue_10/101021bi027357v/authorship/3
http://hub.abes.fr/bmj/periodical/gutjnl/2002/volume_50/issue_3/B356B02520F03CE9E053120B220A6533/authorship/7
http://hub.abes.fr/oup/periodical/jbchem/2006/volume_139/issue_5/101093jbmvj101/authorship/4
http://hub.abes.fr/oup/periodical/proeng/1998/volume_11/issue_5/101093protein115377/authorship/3
http://hub.abes.fr/oup/periodical/proeng/2004/volume_17/issue_1/101093proteingzh011/authorship/6
http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_11/101021ja044355k/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/2000/volume_39/issue_27/101021bi992036d/authorship/8
http://hub.abes.fr/acs/periodical/bichaw/1998/volume_37/issue_27/101021bi973128a/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/2006/volume_45/issue_10/101021bi052443r/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/2004/volume_43/issue_14/101021bi0498813/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/2008/volume_130/issue_52/101021ja8054035/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_37/101021bi020215g/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/2001/volume_40/issue_36/101021bi011052j/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1999/volume_38/issue_13/101021bi982690d/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1989/volume_28/issue_12/101021bi00438a040/authorship/6
http://hub.abes.fr/acs/periodical/bichaw/1982/volume_21/issue_10/101021bi00539a004/authorship/3
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Ferroxidase kinetics of human liver apoferritin, recombinant H-chain apoferritin, and site-directed mutants
Tyrosyl radical formation during the oxidative deposition of iron in human apoferritin
Structural heterogeneity and subunit composition of horse ferritins
Multiple Pathways for Mineral Core Formation in Mammalian Apoferritin. TheRole of Hydrogen Peroxide
Distinct stability of recombinant L and H subunits of human ferritin: calorimetric and ANS binding studies.
Antiferritin Single-Chain Fv Fragment Is a Functional Protein with Properties of aPartially Structured State: Comparison with the Completely Folded VL Domain
The Putative “Nucleation Site” in Human H-Chain Ferritin Is Not Required forMineralization of the Iron Core
Ferrous Ion Binding to Recombinant Human H-Chain Ferritin. An IsothermalTitration Calorimetry Study
Mutations of Ferritin H Chain C-Terminus Produced by Nucleotide Insertions Have Altered Stability and Functional Properties
Fusion of the antiferritin antibody VL domain to barnase results in enhanced solubility and altered pH stability
Origin of the Unusual Kinetics of Iron Deposition in HumanH-Chain Ferritin
Reaction Paths of Iron Oxidation and Hydrolysis in Horse Spleen and RecombinantHuman Ferritins
Is Hydrogen Peroxide Produced during Iron(II) Oxidation in MammalianApoferritins?
Iron(II) and Hydrogen Peroxide Detoxification by Human H-Chain Ferritin. AnEPR Spin-Trapping Study
Redox Reactivity of Animal Apoferritins and Apoheteropolymers Assembled fromRecombinant Heavy and Light Human Chain Ferritins
Facilitated Diffusion of Iron(II) and Dioxygen Substrates into Human H-Chain Ferritin. A Fluorescence and Absorbance Study Employing the Ferroxidase Center Substitution Y34W
Identification of the EPR-Active Iron-Nitrosyl Complexes in Mammalian Ferritins
Expression and structural and functional properties of human ferritin L-chain from Escherichia coli
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