Results 61 to 70 of about 34,396 (232)
Iron is the fourth most common element in the earth's crust and the most abundant transition metal in the human body. It is an essential element required for growth and survival. Maintaining the correct iron balance is crucial for health. All living organisms evolved sophisticated mechanisms to maintain appropriate iron levels in their cells and within
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Background: Hepcidin-25 is a 25 amino acid hepatokine and a key regulator of iron metabolism related to iron deficiency anemia. Recent studies have suggested that an elevated hepcidin level is correlated with low energy availability.
Shinsuke Nirengi +9 more
doaj +1 more source
Hemojuvelin-Neogenin Interaction Is Required for Bone Morphogenic Protein-4-induced Hepcidin Expression [PDF]
Hemojuvelin (HJV) is a glycosylphosphatidylinositol-linked protein and binds both bone morphogenic proteins (BMPs) and neogenin. Cellular HJV acts as a BMP co-receptor to enhance the transcription of hepcidin, a key iron regulatory hormone secreted ...
An-Sheng Zhang +44 more
core +4 more sources
A tincture of hepcidin cures all: the potential for hepcidin therapeutics [PDF]
Iron overload as a result of blood transfusions and excessive intestinal iron absorption can be a complication of chronic anemias such as β-thalassemia. Inappropriately low levels of hepcidin, a negative regulator of iron absorption and recycling, underlie the pathophysiology of the intestinal hyperabsorption. In this issue of the JCI, Gardenghi et al.
Thomas B, Bartnikas, Mark D, Fleming
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Proteinvermittelte Kupfer‐Redoxregulation: Rolle von Disulfidbrücken und allosterischer Modulation
Copper binding triggers structural changes that expose a reactive disulphide bridge, enabling intrinsic Cu(II) reduction in folded proteins. SAXS, XAS, and QM/MM simulations reveal how globular proteins such as HSA and SOD1 employ disulphide‐mediated dynamics to modulate site accessibility and control copper redox chemistry.
Rebecca Sternke‐Hoffmann +9 more
wiley +1 more source
Hepatic heparan sulfate is a master regulator of hepcidin expression and iron homeostasis in human hepatocytes and mice. [PDF]
Hepcidin is a liver-derived peptide hormone that controls systemic iron homeostasis. Its expression is regulated by the bone morphogenetic protein 6 (BMP6)/SMAD1/5/8 pathway and by the proinflammatory cytokine interleukin 6 (IL6).
Anower-E-Khuda, Ferdous +8 more
core
Copper binding triggers structural changes that expose a reactive disulphide bridge, enabling intrinsic Cu(II) reduction in folded proteins. SAXS, XAS, and QM/MM simulations reveal how globular proteins such as HSA and SOD1 employ disulphide‐mediated dynamics to modulate site accessibility and control copper redox chemistry.
Rebecca Sternke‐Hoffmann +9 more
wiley +1 more source
A two‐stage transcriptomic filter comparing rHuEPO, exercise and altitude responses reduced 153 candidate genes to 50 that were unaffected by physiological stimuli. These retained transcripts offer focused biomarker leads to strengthen antidoping detection of rHuEPO.
Daria Obratov +4 more
wiley +1 more source
Elevated circulating hepcidin levels have been reported in patients with pulmonary artery hypertension (PAH). Hepcidin has been shown to promote proliferation of human pulmonary artery smooth muscle cells (PASMCs) in vitro, suggesting a potential role in
Theo Issitt +12 more
doaj +1 more source
Hepcidin is the key mediator of renal anemia, and reliable measurement of serum hepcidin levels has been made possible by the ProteinChip system. We therefore investigated the iron status and serum hepcidin levels of peritoneal dialysis (PD) patients who
Aya Eguchi +7 more
doaj +1 more source

