Institution
Hokkaido University
Education•Sapporo, Hokkaidô, Japan•
About: Hokkaido University is a education organization based out in Sapporo, Hokkaidô, Japan. It is known for research contribution in the topics: Catalysis & Population. The organization has 53925 authors who have published 115403 publications receiving 2651647 citations. The organization is also known as: Hokudai & Hokkaidō daigaku.
Topics: Catalysis, Population, Gene, Virus, Oxide
Papers published on a yearly basis
Papers
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Tehran University of Medical Sciences1, Alexandria University2, Mayo Clinic3, Innsbruck Medical University4, King Saud University5, Aga Khan University6, Aga Khan University Hospital7, Mahidol University8, Ankara University9, Chang Gung University10, University of Coimbra11, Peking Union Medical College12, University of Baghdad13, Athens Regional Medical Center14, Jordan Hospital15, Hokkaido University16, University of Lisbon17, Peking University18
TL;DR: Behçet's disease (BD) is a chronic, relapsing, inflammatory vascular disease with no pathognomonic test.
Abstract: Objective
Behcet's disease (BD) is a chronic, relapsing, inflammatory vascular disease with no pathognomonic test. Low sensitivity of the currently applied International Study Group (ISG) clinical diagnostic criteria led to their reassessment.
Methods
An International Team for the Revision of the International Criteria for BD (from 27 countries) submitted data from 2556 clinically diagnosed BD patients and 1163 controls with BD-mimicking diseases or presenting at least one major BD sign. These were randomly divided into training and validation sets. Logistic regression, ‘leave-one-country-out’ cross-validation and clinical judgement were employed to develop new International Criteria for BD (ICBD) with the training data. Existing and new criteria were tested for their performance in the validation set.
Results
For the ICBD, ocular lesions, oral aphthosis and genital aphthosis are each assigned 2 points, while skin lesions, central nervous system involvement and vascular manifestations 1 point each. The pathergy test, when used, was assigned 1 point. A patient scoring ≥4 points is classified as having BD. In the training set, 93.9% sensitivity and 92.1% specificity were assessed compared with 81.2% sensitivity and 95.9% specificity for the ISG criteria. In the validation set, ICBD demonstrated an unbiased estimate of sensitivity of 94.8% (95% CI: 93.4–95.9%), considerably higher than that of the ISG criteria (85.0%). Specificity (90.5%, 95% CI: 87.9–92.8%) was lower than that of the ISG-criteria (96.0%), yet still reasonably high. For countries with at least 90%-of-cases and controls having a pathergy test, adding 1 point for pathergy test increased the estimate of sensitivity from 95.5% to 98.5%, while barely reducing specificity from 92.1% to 91.6%.
Conclusion
The new proposed criteria derived from multinational data exhibits much improved sensitivity over the ISG criteria while maintaining reasonable specificity. It is proposed that the ICBD criteria to be adopted both as a guide for diagnosis and classification of BD.
854 citations
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TL;DR: It is shown that PDI is S-nitrosylated, a reaction transferring a nitric oxide group to a critical cysteine thiol to affect protein function, which prevents neurotoxicity associated with ER stress and protein misfolding in neurodegenerative disorders.
Abstract: Stress proteins located in the cytosol or endoplasmic reticulum (ER) maintain cell homeostasis and afford tolerance to severe insults. In neurodegenerative diseases, several chaperones ameliorate the accumulation of misfolded proteins triggered by oxidative or nitrosative stress, or of mutated gene products. Although severe ER stress can induce apoptosis, the ER withstands relatively mild insults through the expression of stress proteins or chaperones such as glucose-regulated protein (GRP) and protein-disulphide isomerase (PDI), which assist in the maturation and transport of unfolded secretory proteins. PDI catalyses thiol-disulphide exchange, thus facilitating disulphide bond formation and rearrangement reactions. PDI has two domains that function as independent active sites with homology to the small, redox-active protein thioredoxin. During neurodegenerative disorders and cerebral ischaemia, the accumulation of immature and denatured proteins results in ER dysfunction, but the upregulation of PDI represents an adaptive response to protect neuronal cells. Here we show, in brains manifesting sporadic Parkinson's or Alzheimer's disease, that PDI is S-nitrosylated, a reaction transferring a nitric oxide (NO) group to a critical cysteine thiol to affect protein function. NO-induced S-nitrosylation of PDI inhibits its enzymatic activity, leads to the accumulation of polyubiquitinated proteins, and activates the unfolded protein response. S-nitrosylation also abrogates PDI-mediated attenuation of neuronal cell death triggered by ER stress, misfolded proteins or proteasome inhibition. Thus, PDI prevents neurotoxicity associated with ER stress and protein misfolding, but NO blocks this protective effect in neurodegenerative disorders through the S-nitrosylation of PDI.
850 citations
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TL;DR: It was shown that fe(III) is effectively masked by fluoride, and the pH of the solution to be masked should be below 2.5 in order to prevent acceleration by the fluoride of aerial oxidation of Fe(II).
849 citations
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847 citations
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TL;DR: Results clearly showed thatDJ‐1 has a role in the antioxidative stress reaction and that mutations of DJ‐1 lead to cell death, which is observed in PD.
Abstract: Deletion and point (L166P) mutations of DJ-1 have recently been shown to be responsible for the onset of familial Parkinson's disease (PD, PARK7). The aim of this study was to determine the role of DJ-1 in PD. We first found that DJ-1 eliminated hydrogen peroxide in vitro by oxidizing itself. We then found that DJ-1 knockdown by short interfering RNA rendered SH-SY5Y neuroblastoma cells susceptible to hydrogen peroxide-, MPP+- or 6-hydroxydopamine-induced cell death and that cells harbouring mutant forms of DJ-1, including L166P, became susceptible to death in parallel with the loss of oxidized forms of DJ-1. These results clearly showed that DJ-1 has a role in the antioxidative stress reaction and that mutations of DJ-1 lead to cell death, which is observed in PD.
841 citations
Authors
Showing all 54156 results
Name | H-index | Papers | Citations |
---|---|---|---|
Shizuo Akira | 261 | 1308 | 320561 |
Yi Cui | 220 | 1015 | 199725 |
John F. Hartwig | 145 | 714 | 66472 |
Yoshihiro Kawaoka | 139 | 883 | 75087 |
David Y. Graham | 138 | 1047 | 80886 |
Takashi Kadowaki | 137 | 873 | 89729 |
Kazunari Domen | 130 | 908 | 77964 |
Susumu Kitagawa | 125 | 809 | 69594 |
Toshikazu Nakamura | 121 | 732 | 51374 |
Toshio Hirano | 120 | 401 | 55721 |
Li-Jun Wan | 113 | 639 | 52128 |
Wenbin Lin | 113 | 474 | 56786 |
Xiaoming Li | 113 | 1932 | 72445 |
Jinhua Ye | 112 | 658 | 49496 |
Terence Tao | 111 | 606 | 94316 |