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脚注^ ; .mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation.cs-ja1 q,.mw-parser-output .citation.cs-ja2 q{quotes:"「""」""『""』"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free a,.mw-parser-output .citation .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited a,.mw-parser-output .id-lock-registration a,.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription a,.mw-parser-output .citation .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:#d33}.mw-parser-output .cs1-visible-error{color:#d33}.mw-parser-output .cs1-maint{display:none;color:#3a3;margin-left:0.3em}.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}Granier T, Langlois d'Estaintot B, Gallois B, Chevalier JM, Precigoux G, Santambrogio P, Arosio P (January 2003). "Structural description of the active sites of mouse L-chain ferritin at 1.2 A resolution". Journal of Biological Inorganic Chemistry. 8 (1?2): 105?11. doi:10.1007/s00775-002-0389-4. PMID 12459904。
^ PDB: 1r03​; Langlois d'Estaintot B, Santambrogio P, Granier T, Gallois B, Chevalier JM, Precigoux G, Levi S, Arosio P (July 2004). "Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala". Journal of Molecular Biology. 340 (2): 277?93. doi:10.1016/j.jmb.2004.04.036. PMID 15201052。
^Iron Use and Storage in the Body: Ferritin and Molecular Representations, Rachel Casiday and Regina Frey, Department of Chemistry, Washington University, St. Louis.
^ Wang W, Knovich MA, Coffman LG, Torti FM, Torti SV (August 2010). "Serum ferritin: Past, present and future". Biochimica et Biophysica Acta. 1800 (8): 760?9. doi:10.1016/j.bbagen.2010.03.011. PMC 2893236. PMID 20304033。
^ a b c Theil, Elizabeth C. (2012). “Ferritin protein nanocages?the story”. Nanotechnology Perceptions 8: 7?16. doi:10.4024/N03TH12A.ntp.08.01. 
^ Torti FM, Torti SV (May 2002). "Regulation of ferritin genes and protein". Blood. 99 (10): 3505?16. doi:10.1182/blood.V99.10.3505. PMID 11986201。
^ a b c d e f Theil EC (1987). "Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms". Annual Review of Biochemistry. 56 (1): 289?315. doi:10.1146/annurev.bi.56.070187.001445. PMID 3304136。
^ De Zoysa M, Lee J (September 2007). "Two ferritin subunits from disk abalone (Haliotis discus discus): cloning, characterization and expression analysis". Fish & Shellfish Immunology. 23 (3): 624?35. doi:10.1016/j.fsi.2007.01.013. PMID 17442591。
^FERRITIN STRUCTURE AND ITS BIOMEDICAL IMPLICATIONS
^ a b c d e f g h Andrews SC, Arosio P, Bottke W, Briat JF, von Darl M, Harrison PM, Laulhere JP, Levi S, Lobreaux S, Yewdall SJ (1992). "Structure, function, and evolution of ferritins". Journal of Inorganic Biochemistry. 47 (3?4): 161?74. doi:10.1016/0162-0134(92)84062-R. PMID 1431878。
^ a b “検査部/輸血部インフォメーション”. 岡山大学. 2017年10月15日閲覧。
^ Zhang Y, Meng Q, Jiang T, Wang H, Xie L, Zhang R (May 2003). "A novel ferritin subunit involved in shell formation from the pearl oyster (Pinctada fucata)". Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology. 135 (1): 43?54. doi:10.1016/S1096-4959(03)00050-2. PMID 12781972。
^ Levi S, Corsi B, Bosisio M, Invernizzi R, Volz A, Sanford D, Arosio P, Drysdale J (July 2001). "A human mitochondrial ferritin encoded by an intronless gene". The Journal of Biological Chemistry. 276 (27): 24437?40. doi:10.1074/jbc.C100141200. PMID 11323407。
^ Seckback J (1982). "Ferreting out the secrets of plant ferritin - A review". Journal of Plant Nutrition. 5 (4?7): 369?394. doi:10.1080/01904168209362966。
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^ Jackson DJ, Worheide G, Degnan BM (2007). "Dynamic expression of ancient and novel molluscan shell genes during ecological transitions". BMC Evolutionary Biology. 7: 160. doi:10.1186/1471-2148-7-160. PMC 2034539. PMID 17845714。
^ Yano M, Nagai K, Morimoto K, Miyamoto H (June 2006). "Shematrin: a family of glycine-rich structural proteins in the shell of the pearl oyster Pinctada fucata". Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology. 144 (2): 254?62. doi:10.1016/j.cbpb.2006.03.004. PMID 16626988。
^ Kyung-Suk K, Webb J, Macey D (1986). "Properties and role of ferritin in the hemolymph of the chiton Clavarizona hirtosa". Biochimica et Biophysica Acta (BBA) - General Subjects. 884 (3): 387?394. doi:10.1016/0304-4165(86)90188-1。
^ Zhang, Y., Mikhael, M., Xu, D., Li, Y., Soe-Lin, S., Ning, B., ... & Ponka, P. (2010). Lysosomal proteolysis is the primary degradation pathway for cytosolic ferritin and cytosolic ferritin degradation is necessary for iron exit. Antioxidants & redox signaling, 13(7), 999-1009.
^ a b c Honarmand Ebrahimi K, Hagedoorn PL, Hagen WR (January 2015). "Unity in the biochemistry of the iron-storage proteins ferritin and bacterioferritin". Chemical Reviews. 115 (1): 295?326. doi:10.1021/cr5004908. PMID 25418839。
^ a b Honarmand Ebrahimi K, Bill E, Hagedoorn PL, Hagen WR (November 2012). "The catalytic center of ferritin regulates iron storage via Fe(II)-Fe(III) displacement". Nature Chemical Biology. 8 (11): 941?8. doi:10.1038/nchembio.1071. PMID 23001032。
^ Watt RK (March 2013). "A unified model for ferritin iron loading by the catalytic center: implications for controlling "free iron" during oxidative stress". Chembiochem. 14 (4): 415?9. doi:10.1002/cbic.201200783. PMID 23404831。
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