User:Brianna Barnes/Sandbox 1
From Proteopedia
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== Background == | == Background == | ||
- | + | Discovered in 1937 by French scientist Laufberger, ferritin was first detected in horse spleen and a few years later in humans (7). Ferritin is a protein that is responsible for iron storage and iron homeostasis, as well as various physiologic and pathological processes in prokaryotes and eukaryotes. Iron homeostasis is essential to maintaining life because iron can be toxic to DNA and proteins if not properly regulated. If there is an overload of iron, reactive oxygen species can be produced, lipid peroxidation can occur, and there can be damage to DNA. Typically, ferritin presents as a cytosolic protein, but there are also mitochondrial and nuclear forms that have recently been discovered. The most common measurement of ferritin is collected from serum ferritin, which is ferritin stored in red blood cells. Many variations of ferritin exist, as it is presumed that evolutionary adaptations were made in order to allow certain organisms to survive. | |
== Structure == | == Structure == | ||
Revision as of 19:41, 28 April 2022
Ferritin
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644