@article{edde814fede5401aba17e045885c539a,
title = "Good and bad of Cu/Zn-superoxide dismutase controlled by metal ions and disulfide bonds",
abstract = "Cu/Zn-superoxide dismutase (SOD1) is a metalloenzyme that catalyzes the disproportionation of superoxide. This review summarizes intracellular processes for metal binding and disulfide formation in SOD1, both of which are essential to stabilization of the protein structure as well as its enzymatic function. Also, failure of those processes as a possible cause of a neurodegenerative disease through protein misfolding will be described.",
keywords = "Metalloprotein, Neurodegenerative disease, Protein folding",
author = "Yoshiaki Furukawa",
note = "Funding Information: This work was supported by Grants-in-Aid 19H05765 for Scientific Research on Innovative Areas from the Ministry of Education, Culture, Sports, Science and Technology of Japan and also supported by Grants-in-Aid for Programs for the Advancement of Research in Core Projects under Keio University{\textquoteright}s Longevity Initiative and for the Advancement of Next Generation Research Projects from Keio University. Publisher Copyright: {\textcopyright} 2021 The Chemical Society of Japan.",
year = "2021",
doi = "10.1246/CL.200770",
language = "English",
volume = "50",
pages = "331--341",
journal = "Chemistry Letters",
issn = "0366-7022",
publisher = "Chemical Society of Japan",
number = "2",
}