S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration (Q28242222)

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Tomohiro Nakamura

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Dongdong Yao

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Zhong-Qing Shi

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Zezong Gu

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Yuliang Ma

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Yasuyuki Nomura

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Stuart A Lipton

Setting the standards: quality control in the secretory pathway

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language of work or name

English

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publication date

25 May 2006

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published in

Nature

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volume

441

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issue

7092

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page(s)

513-7

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cites work

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Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death

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An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin

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Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin

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Identification of the protein disulfide isomerase family member PDIp in experimental Parkinson's disease and Lewy body pathology

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Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69.

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Characterization of the S-denitrosation activity of protein disulfide isomerase

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Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity

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Protein S-nitrosylation: a physiological signal for neuronal nitric oxide

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Chronic systemic pesticide exposure reproduces features of Parkinson's disease

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S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function

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