Immunochemical characterization on pathological oligomers of mutant Cu/Zn-superoxide dismutase in amyotrophic lateral sclerosis
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- 作者：Eiichi Tokuda ; Itsuki Anzai ; Takao Nomura ; Keisuke Toichi…
- 关键词：Amyotrophic lateral sclerosis ; Cu/Zn ; superoxide dismutase ; Protein misfolding ; Disulfide bond
- 刊名：Molecular Neurodegeneration
- 出版年：2017
- 出版时间：December 2017
- 年：2017
- 卷：12
- 期：1
- 全文大小：4550KB
- 刊物主题：Neurosciences; Neurology; Molecular Medicine;
- 出版者：BioMed Central
- ISSN：1750-1326
- 卷排序：12
文摘
BackgroundDominant mutations in Cu/Zn-superoxide dismutase (SOD1) gene cause a familial form of amyotrophic lateral sclerosis (SOD1-ALS) with accumulation of misfolded SOD1 proteins as intracellular inclusions in spinal motor neurons. Oligomerization of SOD1 via abnormal disulfide crosslinks has been proposed as one of the misfolding pathways occurring in mutant SOD1; however, the pathological relevance of such oligomerization in the SOD1-ALS cases still remains obscure.