about
FutA2 is a ferric binding protein from Synechocystis PCC 6803Iron and bismuth bound human serum transferrin reveals a partially-opened conformation in the N-lobe"Anion clamp" allows flexible protein to impose coordination geometry on metal ionsLactoferrin from Milk: Nutraceutical and Pharmacological PropertiesDealing with iron: common structural principles in proteins that transport iron and heme.Competitive binding of bismuth to transferrin and albumin in aqueous solution and in blood plasma.Studying Lactoferrin N-Glycosylation.Lactoferrin and transferrin: functional variations on a common structural framework.The influence of the synergistic anion on iron chelation by ferric binding protein, a bacterial transferrin.The crystal structure of iron-free human serum transferrin provides insight into inter-lobe communication and receptor binding.Structure and domain dynamics of human lactoferrin in solution and the influence of Fe(III)-ion ligand bindingImmunomodulatory effects of lactoferrinReceptor recognition of transferrin bound to lanthanides and actinides: a discriminating step in cellular acquisition of f-block metals.Lactoferrin and cancer disease prevention.The Antifungal Activity of Lactoferrin and Its Derived Peptides: Mechanisms of Action and Synergy with Drugs against Fungal Pathogens.A structural perspective on lactoferrin function.The impact of iron on the bleaching efficacy of hydrogen peroxide in liquid whey systems.Mutations at nonliganding residues Tyr-85 and Glu-83 in the N-lobe of human serum transferrin. Functional second shell effects.Lactoferrin: A Natural Glycoprotein Involved in Iron and Inflammatory Homeostasis.The low pKa value of iron-binding ligand Tyr188 and its implication in iron release and anion binding of human transferrin.UV Raman evidence of a tyrosine in apo-human serum transferrin with a low pK(a) that is elevated upon binding of sulphate.Mapping of stereoselective recognition sites on human serum transferrin by capillary electrophoresis and molecular modelling.Synergistic anion and metal binding to the ferric ion-binding protein from Neisseria gonorrhoeae.Lactoferrin: Structure, function, denaturation and digestion.Binding of oxo-Cu2 clusters to ferric ion-binding protein A from Neisseria gonorrhoeae: a structural insight.Human apo-lactoferrin as a physiological mimetic of hypoxia stabilizes hypoxia-inducible factor-1 alpha.Lactoferrin potentially facilitates glucose regulation and enhances the incretin effect.Anion-mediated iron release from transferrins. The kinetic and mechanistic model for N-lobe of ovotransferrin.
P2860
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P2860
description
wetenschappelijk artikel
@nl
наукова стаття, опублікована в 1994
@uk
name
Structure and Reactivity of Transferrins
@en
Structure and Reactivity of Transferrins
@nl
type
label
Structure and Reactivity of Transferrins
@en
Structure and Reactivity of Transferrins
@nl
prefLabel
Structure and Reactivity of Transferrins
@en
Structure and Reactivity of Transferrins
@nl
P1476
Structure and Reactivity of Transferrins
@en
P2093
E.N. Baker
P304
P356
10.1016/S0898-8838(08)60176-2
P577
1994-01-01T00:00:00Z