Wild type and P301L mutant Tau promote neuro-inflammation and α-Synuclein accumulation in lentiviral gene delivery models. - Wikidata - wikimedia - TriplyDB

Wild type and P301L mutant Tau promote neuro-inflammation and α-Synuclein accumulation in lentiviral gene delivery models.

Wild type and P301L mutant Tau promote neuro-inflammation and α-Synuclein accumulation in lentiviral gene delivery models.

http://www.wikidata.org/entity/Q39994322

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Inflammation and α-synuclein's prion-like behavior in Parkinson's disease--is there a link?Alpha-synuclein and tau: teammates in neurodegeneration?Aging reduces glial uptake and promotes extracellular accumulation of Aβ from a lentiviral vector.Tyrosine Kinase Inhibition Regulates Early Systemic Immune Changes and Modulates the Neuroimmune Response in α-Synucleinopathy The role of telomerase protein TERT in Alzheimer's disease and in tau-related pathology in vitro.Gene Therapy Models of Alzheimer's Disease and Other Dementias.Decreased parkin solubility is associated with impairment of autophagy in the nigrostriatum of sporadic Parkinson's disease.A strategy for developing new treatment paradigms for neuropsychiatric and neurocognitive symptoms in Alzheimer's disease.Transgenic models of Alzheimer's disease: better utilization of existing models through viral transgenesis.Examining the mechanisms that link β-amyloid and α-synuclein pathologies.Fractalkine Mediates Communication between Pathogenic Proteins and Microglia: Implications of Anti-Inflammatory Treatments in Different Stages of Neurodegenerative Diseases.Interactions Between α-Synuclein and Tau Protein: Implications to Neurodegenerative Disorders.Polymeric alkylpyridinium salts permit intracellular delivery of human Tau in rat hippocampal neurons: requirement of Tau phosphorylation for functional deficits.Fractalkine signaling and Tau hyper-phosphorylation are associated with autophagic alterations in lentiviral Tau and Aβ1-42 gene transfer models.Tau deletion impairs intracellular β-amyloid-42 clearance and leads to more extracellular plaque deposition in gene transfer models.Fractalkine activates NRF2/NFE2L2 and heme oxygenase 1 to restrain tauopathy-induced microgliosis.Lentiviral delivery of the human wild-type tau protein mediates a slow and progressive neurodegenerative tau pathology in the rat brain.A Focus on the Beneficial Effects of Alpha Synuclein and a Re-appraisal of Synucleinopathies.Untangling Tau and Iron: Exploring the Interaction Between Iron and Tau in Neurodegeneration

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P2860

Wild type and P301L mutant Tau promote neuro-inflammation and α-Synuclein accumulation in lentiviral gene delivery models.

http://www.wikidata.org/entity/Q39994322

description

2011 nî lūn-bûn

@nan

2011年の論文

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2011年学术文章

@wuu

2011年学术文章

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2011年学术文章

@zh-hans

2011年学术文章

@zh-my

2011年学术文章

@zh-sg

2011年學術文章

@yue

2011年學術文章

@zh

2011年學術文章

@zh-hant

name

Wild type and P301L mutant Tau ...... ntiviral gene delivery models.

@en

Wild type and P301L mutant Tau ...... ntiviral gene delivery models.

@nl

type

label

Wild type and P301L mutant Tau ...... ntiviral gene delivery models.

@en

Wild type and P301L mutant Tau ...... ntiviral gene delivery models.

@nl

prefLabel

Wild type and P301L mutant Tau ...... ntiviral gene delivery models.

@en

Wild type and P301L mutant Tau ...... ntiviral gene delivery models.

@nl

P1433

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J.MCN.2011.09.002

P1433

Molecular and Cellular Neuroscience

P1476

Wild type and P301L mutant Tau ...... ntiviral gene delivery models.

@en

P2093

Alexander M Herman

http://www.w3.org/2001/XMLSchema#string

Charbel E-H Moussa

http://www.w3.org/2001/XMLSchema#string

G William Rebeck

http://www.w3.org/2001/XMLSchema#string

Preeti J Khandelwal

http://www.w3.org/2001/XMLSchema#string

Sonya B Dumanis

http://www.w3.org/2001/XMLSchema#string

P2860

Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3beta (GSK3beta) plays a critical role in regulating tau's ability to bind and stabilize microtubules

Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model

Overexpression of the human NFM subunit in transgenic mice modifies the level of endogenous NFL and the phosphorylation state of NFH subunits

Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments

Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease

Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology

Neurodegenerative tauopathies

Molecular pathways of neurodegeneration in Parkinson's disease

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44-53

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scholarly article

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10.1016/J.MCN.2011.09.002

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1

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21945393

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3246111

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