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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page(s)

513-7

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issue

7092

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cites work

1 reference

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Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls

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Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals

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Misfolded proteins, endoplasmic reticulum stress and neurodegeneration

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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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Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese

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Protein disulfide isomerase

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Protein aggregation after transient cerebral ischemia.

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Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death

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Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death

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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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A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds.

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Redox signaling: nitrosylation and related target interactions of nitric oxide

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

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7 January 2021

Characterization of the S-denitrosation activity of protein disulfide isomerase

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7 January 2021

S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death

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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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7 January 2021

Chronic systemic pesticide exposure reproduces features of Parkinson's disease

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7 January 2021

Novel function of PS2V: change in conformation of tau proteins

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Apoptosis and necrosis: two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures

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Nitric oxide mediates glutamate neurotoxicity in primary cortical cultures

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Excitatory amino acids as a final common pathway for neurologic disorders.

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S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding

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7 January 2021

Pael-R is accumulated in Lewy bodies of Parkinson's disease.

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7 January 2021

Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease.

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7 January 2021

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

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https://api.crossref.org/works/10.1038%2FNATURE04782

7 January 2021

Identifiers

DOI

10.1038/NATURE04782

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Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

2532257

1006704546

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2532257

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference