Protein disulfide isomerase regulates endoplasmic reticulum stress and the apoptotic process during prion infection and PrP mutant-induced cytotoxicity.
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The Unfolded Protein Response and the Role of Protein Disulfide Isomerase in NeurodegenerationProtein disulfide isomerases in neurodegeneration: from disease mechanisms to biomedical applicationsNeurodegeneration and unfolded-protein response in mice expressing a membrane-tethered flexible tail of PrPProtein Disulfide Isomerase Superfamily in Disease and the Regulation of ApoptosisQuantitative proteomics reveals the effect of protein glycosylation in soybean root under flooding stress.Protective effects of transforming growth factor β2 in intestinal epithelial cells by regulation of proteins associated with stress and endotoxin responses.Proapoptotic activities of protein disulfide isomerase (PDI) and PDIA3 protein, a role of the Bcl-2 protein Bak.Novel roles for protein disulphide isomerase in disease states: a double edged sword?Interplay of endoplasmic reticulum stress and autophagy in neurodegenerative disorders.Endoplasmic reticulum stress: its role in disease and novel prospects for therapy.The role of s-nitrosylation and s-glutathionylation of protein disulphide isomerase in protein misfolding and neurodegeneration.Remarkable reductions of PAKs in the brain tissues of scrapie-infected rodent possibly linked closely with neuron loss.Proteomic Analyses for the Global S-Nitrosylated Proteins in the Brain Tissues of Different Human Prion Diseases.The Protein-disulfide Isomerase ERp57 Regulates the Steady-state Levels of the Prion Protein.Overexpression of p62/SQSTM1 promotes the degradations of abnormally accumulated PrP mutants in cytoplasm and relieves the associated cytotoxicities via autophagy-lysosome-dependent way.Infection of prions and treatment of PrP106-126 alter the endogenous status of protein 14-3-3 and trigger the mitochondrial apoptosis possibly via activating Bax pathway.Aberrant Alterations of Mitochondrial Factors Drp1 and Opa1 in the Brains of Scrapie Experiment Rodents.Differential proteomic analysis of replanted Rehmannia glutinosa roots by iTRAQ reveals molecular mechanisms for formation of replant disease.Emerging roles of protein disulfide isomerase in cancer.Treadmill exercise represses neuronal cell death and inflammation during Aβ-induced ER stress by regulating unfolded protein response in aged presenilin 2 mutant mice.Abnormally upregulated αB-crystallin was highly coincidental with the astrogliosis in the brains of scrapie-infected hamsters and human patients with prion diseases.Potential effect of S-nitrosylated protein disulfide isomerase on mutant SOD1 aggregation and neuronal cell death in amyotrophic lateral sclerosis.The effect of Tmem135 overexpression on the mouse heart
P2860
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P2860
Protein disulfide isomerase regulates endoplasmic reticulum stress and the apoptotic process during prion infection and PrP mutant-induced cytotoxicity.
description
2012 nî lūn-bûn
@nan
2012 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Protein disulfide isomerase re ...... P mutant-induced cytotoxicity.
@ast
Protein disulfide isomerase re ...... P mutant-induced cytotoxicity.
@en
Protein disulfide isomerase re ...... P mutant-induced cytotoxicity.
@nl
type
label
Protein disulfide isomerase re ...... P mutant-induced cytotoxicity.
@ast
Protein disulfide isomerase re ...... P mutant-induced cytotoxicity.
@en
Protein disulfide isomerase re ...... P mutant-induced cytotoxicity.
@nl
prefLabel
Protein disulfide isomerase re ...... P mutant-induced cytotoxicity.
@ast
Protein disulfide isomerase re ...... P mutant-induced cytotoxicity.
@en
Protein disulfide isomerase re ...... P mutant-induced cytotoxicity.
@nl
P2093
P2860
P921
P1433
P1476
Protein disulfide isomerase re ...... P mutant-induced cytotoxicity.
@en
P2093
Bao-Yun Zhang
Shao-Bin Wang
Wu-Ling Xie
Xiao-Ping Dong
P2860
P304
P356
10.1371/JOURNAL.PONE.0038221
P407
P577
2012-06-07T00:00:00Z