Structure and spatial conformation of the iron-binding sites of transferrins.
about
Pseudomonas and neutrophil products modify transferrin and lactoferrin to create conditions that favor hydroxyl radical formation.Protease-cleaved iron-transferrin augments oxidant-mediated endothelial cell injury via hydroxyl radical formation.Identification of altered plasma proteins by proteomic study in valvular heart diseases and the potential clinical significanceThe role of transferrin in the mechanism of cellular iron uptake.An overview of iron metabolism at a molecular level.Protease cleavage of iron-transferrin augments pyocyanin-mediated endothelial cell injury via promotion of hydroxyl radical formation.A transferrinlike (hemiferrin) mRNA is expressed in the germ cells of rat testis.Interaction of transferrin and its iron-binding fragments with heparin.Copper binding and release by immobilized transferrin: a new approach to heavy metal removal and recovery.
P2860
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P2860
Structure and spatial conformation of the iron-binding sites of transferrins.
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
@zh-cn
name
Structure and spatial conformation of the iron-binding sites of transferrins.
@en
Structure and spatial conformation of the iron-binding sites of transferrins.
@nl
type
label
Structure and spatial conformation of the iron-binding sites of transferrins.
@en
Structure and spatial conformation of the iron-binding sites of transferrins.
@nl
prefLabel
Structure and spatial conformation of the iron-binding sites of transferrins.
@en
Structure and spatial conformation of the iron-binding sites of transferrins.
@nl
P2093
P1433
P1476
Structure and spatial conformation of the iron-binding sites of transferrins.
@en
P2093
P304
P356
10.1016/0300-9084(88)90184-8
P577
1988-09-01T00:00:00Z