Results 161 to 170 of about 17,575 (209)
Selenoprotein P expression in glioblastoma as a regulator of ferroptosis sensitivity: preservation of GPX4 via the cycling-selenium storage. [PDF]
Zheng X +10 more
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Selenoprotein-p and insulin resistance in children and adolescents with obesity.
Elbarky A +6 more
europepmc +1 more source
Selenoprotein P, peroxiredoxin-5, renalase, and total antioxidant status in patients with suspected obstructive sleep apnea. [PDF]
Czerwińska K +8 more
europepmc +1 more source
Strong associations of serum selenoprotein P with all-cause mortality and mortality due to cancer, cardiovascular, respiratory and gastrointestinal diseases in older German adults. [PDF]
Schöttker B +5 more
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Selenoprotein P receptor from rat
Biochimica et Biophysica Acta (BBA) - Biomembranes, 1989Radioreceptor assay technology was used to show the presence in the rat of a receptor that binds selenoprotein P, a selenocysteine-containing rat plasma protein. 75Se-labeled selenoprotein P bound to testis, kidney, and liver membranes. The binding was specific in that increasing amounts of partially-fractionated rat plasma specifically displaced the ...
B, Gomez, A L, Tappel
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Some properties of selenoprotein P
Biological Trace Element Research, 1992Selenoprotein P is a newly characterized selenoprotein. It is the first protein described to contain multiple selenocysteines. It is secreted by the liver into the plasma and turns over rapidly. Its concentration is sensitive to the selenium status of the animal. Its function is unknown.
R F, Burk, K E, Hill
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Elevated Selenoprotein P Levels in Thalassemia Major Patients
Archives of Medical Research, 2022Previous studies have measured selenium levels and glutathione peroxidase 3 (GPX3) activity in patients with thalassemia major (TM). However, Selenoprotein P (SEPP), which is responsible for the storage and transport of selenium, has not been studied in thalassemia patients.
Gunel Talibova +3 more
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Cellular and Molecular Life Sciences, 2000
Selenoprotein P (SeP) is an extracellular, monomeric glycoprotein containing up to 10 selenocysteine residues in the polypeptide chain. It is ubiquitously expressed in mammalian tissues, and in human plasma it accounts for at least 40% of the total selenium concentration. SeP binds to heparin and cell membranes, and is associated with endothelial cells.
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Selenoprotein P (SeP) is an extracellular, monomeric glycoprotein containing up to 10 selenocysteine residues in the polypeptide chain. It is ubiquitously expressed in mammalian tissues, and in human plasma it accounts for at least 40% of the total selenium concentration. SeP binds to heparin and cell membranes, and is associated with endothelial cells.
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