S-nitrosylated protein disulfide isomerase contributes to mutant SOD1 aggregates in amyotrophic lateral sclerosis-Reference-Cited by-同舟云学术

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S-nitrosylated protein disulfide isomerase contributes to mutant SOD1 aggregates in amyotrophic lateral sclerosis

Published:2012-11-01 Issue:1 Volume:124 Page:45-58
ISSN:0022-3042
Container-title:Journal of Neurochemistry
language:en
Short-container-title:J. Neurochem.

Author:

Chen Xueping¹²,Zhang Xiaosha¹,Li Chen¹,Guan Teng¹,Shang Huifang²,Cui Liying³,Li Xin-Min⁴,Kong Jiming¹

Affiliation:

1. Department of Human Anatomy and Cell Science; University of Manitoba; Winnipeg Manitoba Canada

2. Department of Neurology, West China Hospital; Sichuan University; Chengdu China

3. Department of Neurology; Beijing Union Hospital; Beijing China

4. Department of Psychiatry, Faculty of Medicine; University of Manitoba; Winnipeg Manitoba Canada

Publisher

Wiley

Subject

Cellular and Molecular Neuroscience,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/jnc.12046/fullpdf

Reference73 articles.

1. Mutant SOD1 from spinal cord of G93A rats is destabilized and binds to inner mitochondrial membrane;Ahtoniemi;Neurobiol. Dis.,2008

2. Inducible nitric oxide synthase up-regulation in a transgenic mouse model of familial amyotrophic lateral sclerosis;Almer;J. Neurochem.,1999

3. Proteasome activation and nNOS down-regulation in neuroblastoma cells expressing a Cu, Zn superoxide dismutase mutant involved in familial ALS;Aquilano;J. Neurochem.,2003

4. Inactivation of cytochrome c oxidase by mutant SOD1s in mouse motoneuronal NSC-34 cells is independent from copper availability but is because of nitric oxide;Arciello;J. Neurochem.,2010

5. The unusually stable quaternary structure of human Cu, Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status;Arnesano;J. Biol. Chem.,2004

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