Activation of the macroautophagic system in scrapie-infected experimental animals and human genetic prion diseases
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Overexpression of PLK3 Mediates the Degradation of Abnormal Prion Proteins Dependent on Chaperone-Mediated AutophagyDownregulation of the Repressor Element 1-Silencing Transcription Factor (REST) Is Associated with Akt-mTOR and Wnt-β-Catenin Signaling in Prion Diseases Models.The Functional Role of Prion Protein (PrPC) on Autophagy.Strain-Dependent Effect of Macroautophagy on Abnormally Folded Prion Protein Degradation in Infected Neuronal Cells.Cellular prion protein (PrP(C)) and its role in stress responses.Human prion protein-induced autophagy flux governs neuron cell damage in primary neuron cells.Activation of the AMPK-ULK1 pathway plays an important role in autophagy during prion infection.Prion-mediated neurodegeneration is associated with early impairment of the ubiquitin-proteasome systemGADD45A inhibits autophagy by regulating the interaction between BECN1 and PIK3C3.The Autophagy-Lysosomal Pathway in Neurodegeneration: A TFEB PerspectiveSynaptic dysfunction in prion diseases: a trafficking problem?De novo prion aggregates trigger autophagy in skeletal muscle.Regulation of proteasomes in prion disease.Remarkable reductions of PAKs in the brain tissues of scrapie-infected rodent possibly linked closely with neuron loss.Analyses of the similarity and difference of global gene expression profiles in cortex regions of three neurodegenerative diseases: sporadic Creutzfeldt-Jakob disease (sCJD), fatal familial insomnia (FFI), and Alzheimer's disease (AD).Increased expression of p62/SQSTM1 in prion diseases and its association with pathogenic prion protein.FBXW7-Induced MTOR Degradation Forces Autophagy to Counteract Persistent Prion Infection.Significant reduction of the GLUT3 level, but not GLUT1 level, was observed in the brain tissues of several scrapie experimental animals and scrapie-infected cell lines.Overexpression of p62/SQSTM1 promotes the degradations of abnormally accumulated PrP mutants in cytoplasm and relieves the associated cytotoxicities via autophagy-lysosome-dependent way.Lysosomal Quality Control in Prion Diseases.Increases of Galectin-1 and its S-nitrosylated form in the Brain Tissues of Scrapie-Infected Rodent Models and Human Prion Diseases.What Is Our Current Understanding of PrPSc-Associated Neurotoxicity and Its Molecular Underpinnings?Abnormally upregulated αB-crystallin was highly coincidental with the astrogliosis in the brains of scrapie-infected hamsters and human patients with prion diseases.
P2860
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P2860
Activation of the macroautophagic system in scrapie-infected experimental animals and human genetic prion diseases
description
2012 nî lūn-bûn
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2012年の論文
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2012年学术文章
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2012年学术文章
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2012年学术文章
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2012年学术文章
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2012年学术文章
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2012年學術文章
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2012年學術文章
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name
Activation of the macroautopha ...... d human genetic prion diseases
@ast
Activation of the macroautopha ...... d human genetic prion diseases
@en
type
label
Activation of the macroautopha ...... d human genetic prion diseases
@ast
Activation of the macroautopha ...... d human genetic prion diseases
@en
prefLabel
Activation of the macroautopha ...... d human genetic prion diseases
@ast
Activation of the macroautopha ...... d human genetic prion diseases
@en
P2093
P2860
P356
P1433
P1476
Activation of the macroautopha ...... d human genetic prion diseases
@en
P2093
Wu-Ling Xie
Xiao-Ping Dong
P2860
P304
P356
10.4161/AUTO.21482
P50
P577
2012-08-09T00:00:00Z