Iron is by far the most widespread and essential transition metal, possessing crucial biological functions for living systems. Despite chemical advantages, iron biology has forced organisms to face with some issues: ferric iron insolubility and ferrous-driven formation of toxic radicals. For these reasons, acquisition and transport of iron constitutes a formidable challenge for cells and organisms, which need to maintain adequate iron concentrations within a narrow range, allowing biological processes without triggering toxic effects. Higher organisms have evolved extracellular carrier proteins to acquire, transport and manage iron. In recent years, a renewed interest in iron biology has highlighted the role of iron-proteins dysregulation i...
Lactoferrin (LF) is an iron-binding glycoprotein that is composed of the transferrin family and is p...
Lactoferin (La) is an 80-kDa iron-binding glykoprotein. It shares a high degree of homology at amino...
Biotecnología Aplicada, Vol. 18, No. 1, March 2001, pp. 1-9 Iron and Transferrin. Research and Ther...
Human lactoferrin (hLf), an iron-binding multifunctional cationic glycoprotein secreted by exocrine ...
Brain iron accumulation is common in patients with Parkinson's disease (PD). Iron chelators have bee...
Lactoferrin (Lf), a cationic glycoprotein able to chelate two ferric irons per molecule, is synthesi...
Several lines of evidence indicate that alterations in iron metabolism and/or immune-mediated pathop...
Lactoferrin (Lf), a cationic glycoprotein able to chelate two ferric irons per molecule, is synthesi...
Iron balance is tightly linked to inflammation and it has been demonstrated that many proteins invol...
Over 2 billion people in both developing as well as developed countries - over 30% of the world's po...
Lactoferrin (Lf) is a biologically important molecule, that accomplishes a number of useful function...
In the last 20 years, several new genes and proteins involved in iron metabolism in eukaryotes, part...
Much progress has been achieved to elucidate the function of lactoferrin (LTF), an iron-binding glyc...
Lactoferrin is a non-haem iron binding glycoprotein present in virtually all mammalian body fluids, ...
Lactoferrin is a multi-functional protein found in the secretions of mammals. The antimicrobial acti...
Lactoferrin (LF) is an iron-binding glycoprotein that is composed of the transferrin family and is p...
Lactoferin (La) is an 80-kDa iron-binding glykoprotein. It shares a high degree of homology at amino...
Biotecnología Aplicada, Vol. 18, No. 1, March 2001, pp. 1-9 Iron and Transferrin. Research and Ther...
Human lactoferrin (hLf), an iron-binding multifunctional cationic glycoprotein secreted by exocrine ...
Brain iron accumulation is common in patients with Parkinson's disease (PD). Iron chelators have bee...
Lactoferrin (Lf), a cationic glycoprotein able to chelate two ferric irons per molecule, is synthesi...
Several lines of evidence indicate that alterations in iron metabolism and/or immune-mediated pathop...
Lactoferrin (Lf), a cationic glycoprotein able to chelate two ferric irons per molecule, is synthesi...
Iron balance is tightly linked to inflammation and it has been demonstrated that many proteins invol...
Over 2 billion people in both developing as well as developed countries - over 30% of the world's po...
Lactoferrin (Lf) is a biologically important molecule, that accomplishes a number of useful function...
In the last 20 years, several new genes and proteins involved in iron metabolism in eukaryotes, part...
Much progress has been achieved to elucidate the function of lactoferrin (LTF), an iron-binding glyc...
Lactoferrin is a non-haem iron binding glycoprotein present in virtually all mammalian body fluids, ...
Lactoferrin is a multi-functional protein found in the secretions of mammals. The antimicrobial acti...
Lactoferrin (LF) is an iron-binding glycoprotein that is composed of the transferrin family and is p...
Lactoferin (La) is an 80-kDa iron-binding glykoprotein. It shares a high degree of homology at amino...
Biotecnología Aplicada, Vol. 18, No. 1, March 2001, pp. 1-9 Iron and Transferrin. Research and Ther...