Ferritin - Wikipedia
网页In human ferritin, introns are present between amino acid residues 14 and 15, 34 and 35, and 82 and 83; in addition, there are one to two hundred untranslated bases at either end of the combined exons. [8] The tyrosine residue at amino acid position 27 is thought to be associated with biomineralization. [9]
Ferritin self-assembly, structure, function, and biotechnological ...
网页2023年1月1日 · Human H-ferritin active center consists of six amino acids: Glu-61, Glu-62, His-65, Glu-107, Gln-141, and Glu-27 [81], [132] (Fig. 6 A). Ferrous ions Fe 2+ enter the protein through 3-fold channels, interacting with conservative acidic amino acids [132] (they act as temporary sites for ion landing), and then move along other amino acid residues ...
Chemistry and Biology of Ferritin - PMC - National Center for ...
网页Ferritin operates as a fundamental iron storage protein in cells forming multimeric assemblies with crystalline iron cores. We discuss the latest findings on ferritin structure and activity and its link to cell metabolism and ferroptosis.
Ferritin: The Protein Nanocage and Iron Biomineral in Health and …
网页2013年11月4日 · Ferritin catalytic sites are generally in the middle of each subunit with metal ligands from each of the 4 α helices in the bundle; exceptions occur in a few mini-ferritins 15. The amino acids at the active sites are similar among animals, plants, and microorganism, but not identical (Table 1).
Ferritin microheterogeneity, subunit composition, functional, and ...
网页2023年11月14日 · The H-subunit of chicken ferritin has a 93% amino acid sequence identity to the human ferritin H-subunit, and chicken liver ferritin (CLF) is similar in composition to human mitochondrial...
Ferritin for the Clinician - PMC - National Center for …
网页Ferritin, an iron storage protein, is the primary iron storage mechanism and is critical to iron homeostasis. Ferritin makes iron available for critical cellular processes while protecting lipids, DNA, and proteins from the potentially toxic effects of iron.
Newly uncovered biochemical and functional aspects of ferritin
网页2023年7月13日 · Human ferritin is a 24-subunit, 480-kDa, 12-nm globular protein with a hollow center cavity. 8 Cytosolic ferritin is composed of ferritin heavy chain (FTH) and ferritin light chain (FTL). The human FTH gene and FTL gene are located on chromosomes 11q12.3 and 19q13.33, and encode 183 amino acids (molecular weight of 21 kDa) and 175 amino acids ...
Self-Assembly of Ferritin: Structure, Biological Function ... - Springer
网页2019年11月12日 · Ferritin is a ubiquitous multi-subunit iron storage protein formed by 24 polypeptide chains that self-assemble into a hollow, roughly spherical protein cage. Ferritin has external and internal diameters of approximately 12 nm and 8 nm, respectively. Functionally, ferritin performs iron sequestration and is highly conserved in evolution.
Biochemistry of mammalian ferritins in the regulation of cellular …
网页2020年9月17日 · Ferritin, an iron-storage protein, regulates cellular iron metabolism and oxidative stress. The ferritin structure is characterized as a spherical cage, inside which large amounts of iron are deposited in a safe, compact and bioavailable form.
New Insights into the Role of Ferritin in Iron Homeostasis and ...
网页2021年1月28日 · Ferritin is an iron storage protein which stores iron in a redox inactive form. It is synthesized in response to high cellular iron levels and is degraded to release iron when iron demand is increased. Ferritin synthesis is controlled at translational level, transcriptional level and post-transcriptional level.
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