S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration

By T. Uehara, Tomohiro Nakamura, Dongdong Yao, Z. Shi, Z. Gu, Yuliang Ma, E. Masliah, Y. Nomura, S. Lipton. Nature, 2006

899 citations recorded by the source corpus.

Subfields: Cell Biology, Clinical Biochemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/7a340df24763b52f7b27a65fa6619e6d2a2380b9

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In Cell Biology

1. R. Kaufman
2. G. Hotamışlıgil
3. J. Malhotra
4. Min Ni
5. Kezhong Zhang
6. John Calvin Reed
7. Inki Kim
8. W. Xu

In Clinical Biochemistry

1. G. Hotamışlıgil

In Molecular Biology

1. G. Hotamışlıgil
2. Ling-Yun Wu
3. Jun Ding
4. Yan Xu
5. R. Kaufman
6. Kuo-Chen Chou
7. Kezhong Zhang
8. J. Malhotra

Citations in the corpus

• A role for motoneuron subtype–selective ER stress in disease manifestations of FALS mice (2009, background): “PDI disruption can further be brought about by NO-mediated nitrosylatio”
• The eIF2α kinases: their structures and functions (2013, neutral): “NO has also been described to compromise ER protein folding capacity through S-nitrosylation of a key ER chaperone, protein disulphide isomerase [189].”
• ER chaperones in mammalian development and human diseases (2007, background): “and thapsigargin which is an inhibitor of ER Ca-ATPase [55].”
• Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Cycle or a Double-Edged Sword? (2007, positive): “Uehara and co-workers (143) elegantly demonstrated that NO-mediated S - nitrosylation of protein disulfide isomerase (PDI) inhibits PDI function, leads to dysregulated protein folding within the ER, elicits ER stress, and initiates neuronal cell death.”
• Nitric oxide in the central nervous system: neuroprotection versus neurotoxicity (2007, background): “Another target for NO-induced neurotoxicity is protein-disulphide isomerase ( PDI ), which catalyses thiol-disulphide exchange, thereby promoting the formation of disulphide bonds and protein rearrangemen”
• Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities (2008, background): “One of the underlying causes of protein unfolding in the ER identified in the context of neurodegeneration and brain ischaemia is nitrosylation of PDI, which inhibits protein disulphide-bond formatio”
• Endoplasmic Reticulum Stress and the Inflammatory Basis of Metabolic Disease (2010, positive): “Finally, recent studies suggest that nitric oxide (NO) generation could also be related to ER stress (Uehara et al., 2006).”
• From endoplasmic-reticulum stress to the inflammatory response (2008, background): “It has also been shown to modify the active site of PDI, thereby interfering with disulphide-bond formation and resulting in the accumulation of misfolded proteins in the E”
• iSNO-PseAAC: Predict Cysteine S-Nitrosylation Sites in Proteins by Incorporating Position Specific Amino Acid Propensity into Pseudo Amino Acid Composition (2013, background): “Meanwhile, increasing evidences have indicated that SNO also plays an important role in various major diseases [5], such as cancer [6], Parkinson’s [7,8], Alzheimer’s [9], and Amyotrophic Lateral Sclerosis (ALS) [10].”
• Excitotoxicity and stroke: identifying novel targets for neuroprotection. (2014, positive): “In contrast to its role in the stimulation of neuronal death signaling, S-nitrosylation of protein–disulphide isomerase inhibits its neuroprotective activity in neurons subjected to NMDAR stimulation (Uehara et al., 2006), and S-nitrosylation of src homology-2 domain-containing”
• Cellular Stress Responses: Cell Survival and Cell Death (2010, background): “[160] T.”