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A synthetic peptide with the putative iron binding motif of amyloid precursor protein (APP) does not catalytically oxidize ironThe amyloid precursor protein (APP) does not have a ferroxidase site in its E2 domainFerritin couples iron and fatty acid metabolismThe sedimentation properties of ferritins. New insights and analysis of methods of nanoparticle preparation.An iron-binding protein, Dpr, from Streptococcus mutans prevents iron-dependent hydroxyl radical formation in vitro.Inhibition and stimulation of formation of the ferroxidase center and the iron core in Pyrococcus furiosus ferritin.A versatile microparticle-based immunoaggregation assay for macromolecular biomarker detection and quantification.Functionality of the three-site ferroxidase center of Escherichia coli bacterial ferritin (EcFtnA).Identification of the ferroxidase centre of Escherichia coli bacterioferritinIncorporation of iron by the unusual dodecameric ferritin from Listeria innocua.Catalysis of iron core formation in Pyrococcus furiosus ferritin.Ferroxidase activity of ferritin: effects of pH, buffer and Fe(II) and Fe(III) concentrations on Fe(II) autoxidation and ferroxidation.Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua.Iron incorporation into ferritins: evidence for the transfer of monomeric Fe(III) between ferritin molecules and for the formation of an unusual mineral in the ferritin of Escherichia coli.Defining the roles of the threefold channels in iron uptake, iron oxidation and iron-core formation in ferritin: a study aided by site-directed mutagenesis.Iron (II) oxidation and early intermediates of iron-core formation in recombinant human H-chain ferritin.A comparative Mössbauer study of the mineral cores of human H-chain ferritin employing dioxygen and hydrogen peroxide as iron oxidants.Evidence that the specificity of iron incorporation into homopolymers of human ferritin L- and H-chains is conferred by the nucleation and ferroxidase centres.Evidence that residues exposed on the three-fold channels have active roles in the mechanism of ferritin iron incorporation.
P2860
Q21134149-CA22BD90-3430-40BD-9EF3-19985539F11DQ21559570-B8F30E80-B9DF-4031-8792-11D98874D89BQ27677460-3075A782-B2CB-4CF8-85A0-99093084A1CDQ34065934-137E82F4-CD53-436C-A0DA-38BAC6BE6B08Q34311689-786C2D50-1B71-44F5-AA68-03D1821B2BE0Q34332999-E39AA51A-AFAD-4C97-9BCE-5050F09832F2Q35557014-DE9886C0-E614-41FD-A310-540BDBD04718Q37633306-952D5345-A689-41CA-91F8-AAF563C0FCBEQ38288531-A69082E8-E97C-4C2C-BCE1-32BC79AE1AD1Q41843967-697A0EAD-D956-49B1-85E0-EFBA9C0718B9Q41895434-5E25C78A-F994-4CB2-A163-943C6E5EEBBFQ42047968-8F747DA8-2097-462C-9E93-6377FBBCB83DQ42108734-6983C033-21DA-44FE-A49B-D71ADADEB84FQ42142539-AEE0CA19-B1BC-40E0-ABCF-3D80E5CBA732Q42161104-EC687F44-0784-47F6-B3E9-D4B2791CC2F1Q42161108-F7CF6D11-F644-42CB-AC50-FD1BE42611FBQ42871053-4DC54FF6-F716-43F6-A461-3AAAE6C01C54Q42980931-3B8E8211-7173-4812-B355-1C02AB8F2E36Q42983006-65EB7B42-7F14-4B80-B6BF-C5D4C1187478
P2860
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh-hant
name
Ferroxidase kinetics of horse spleen apoferritin.
@en
Ferroxidase kinetics of horse spleen apoferritin.
@nl
type
label
Ferroxidase kinetics of horse spleen apoferritin.
@en
Ferroxidase kinetics of horse spleen apoferritin.
@nl
prefLabel
Ferroxidase kinetics of horse spleen apoferritin.
@en
Ferroxidase kinetics of horse spleen apoferritin.
@nl
P1476
Ferroxidase kinetics of horse spleen apoferritin.
@en
P2093
P304
25160-25166
P407
P577
1992-12-01T00:00:00Z