Tenuigenin attenuates α-synuclein-induced cytotoxicity by down-regulating polo-like kinase 3. (Q39147084)

23710708

9 September 2017

title

Tenuigenin attenuates α-synuclein-induced cytotoxicity by down-regulating polo-like kinase 3. (English)

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9 September 2017

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Glenda Halliday

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author name string

Jin-Xia Zhou

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Hao-Bo Zhang

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Yi He

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Yan Zheng

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John P Anderson

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Wei-Ping Gai

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Zhi-Gang Liang

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Yong Wang

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Xin-Miao Ren

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Qi Wang

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Xiao-Li Gong

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Jian Yang

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Xuan Wang

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Xiao-Min Wang

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publication date

27 May 2013

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23710708

CNS Neuroscience & Therapeutics

9 September 2017

published in

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volume

19

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issue

9

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page(s)

688-694

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BT-11 is effective for enhancing cognitive functions in the elderly humans

14 May 2020

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Effects of BT-11 on memory in healthy humans

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BT-11 improves stress-induced memory impairments through increment of glucose utilization and total neural cell adhesion molecule levels in rat brains

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Tenuigenin treatment decreases secretion of the Alzheimer's disease amyloid beta-protein in cultured cells

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Tenuifolin, an extract derived from tenuigenin, inhibits amyloid-beta secretion in vitro.

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Polygalae radix inhibits toxin-induced neuronal death in the Parkinson's disease models

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Neuroprotective effects of tenuigenin in a SH-SY5Y cell model with 6-OHDA-induced injury

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Characterization of anti-neurodegenerative effects of Polygala tenuifolia in Abeta(25-35)-treated cortical neurons

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In vivo alpha-synuclein overexpression in rodents: a useful model of Parkinson's disease?

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Viral vector-mediated overexpression of α-synuclein as a progressive model of Parkinson's disease

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Alpha-synuclein locus duplication as a cause of familial Parkinson's disease

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alpha-Synuclein locus triplication causes Parkinson's disease

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The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia

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Rescuing defective vesicular trafficking protects against alpha-synuclein toxicity in cellular and animal models of Parkinson's disease

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Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form

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Function and dysfunction of α-synuclein: probing conformational changes and aggregation by single molecule fluorescence

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Brain alpha-synuclein accumulation in multiple system atrophy, Parkinson's disease and progressive supranuclear palsy: a comparative investigation

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Phenotypic variation in a large Swedish pedigree due to SNCA duplication and triplication

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α-Synuclein posttranslational modification and alternative splicing as a trigger for neurodegeneration

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Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson's disease pathogenesis and therapies

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Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease

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α-Synuclein phosphorylation as a therapeutic target in Parkinson's disease

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Polo-like kinase 2 (PLK2) phosphorylates alpha-synuclein at serine 129 in central nervous system

21 January 2018

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Phosphorylation of synucleins by members of the Polo-like kinase family

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Specificity and regulation of casein kinase-mediated phosphorylation of alpha-synuclein

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Synucleins are a novel class of substrates for G protein-coupled receptor kinases

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Alpha-synuclein aggregation and Ser-129 phosphorylation-dependent cell death in oligodendroglial cells.

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Changes in the solubility and phosphorylation of α-synuclein over the course of Parkinson's disease.

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Characterization of kinases involved in the phosphorylation of aggregated α-synuclein

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Aggregates assembled from overexpression of wild-type alpha-synuclein are not toxic to human neuronal cells

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Dopamine-dependent neurotoxicity of alpha-synuclein: a mechanism for selective neurodegeneration in Parkinson disease

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The role of alpha-synuclein in both neuroprotection and neurodegeneration

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Biochemical increase in phosphorylated alpha-synuclein precedes histopathology of Lewy-type synucleinopathies

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Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease

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Authentically phosphorylated α-synuclein at Ser129 accelerates neurodegeneration in a rat model of familial Parkinson's disease.

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Alpha-synuclein S129 phosphorylation mutants do not alter nigrostriatal toxicity in a rat model of Parkinson disease

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Familial Mutants of α-Synuclein with Increased Neurotoxicity Have a Destabilized Conformation

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Phosphorylation does not prompt, nor prevent, the formation of alpha-synuclein toxic species in a rat model of Parkinson's disease

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1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23710708

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Tenuigenin protects dopaminergic neurons from inflammation-mediated damage induced by the lipopolysaccharide

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23710708

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Changes in properties of serine 129 phosphorylated α-synuclein with progression of Lewy-type histopathology in human brains

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23710708

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1111/CNS.12124

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=PMCID:PMC6493467&resulttype=core&format=json

14 May 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=PMCID:PMC6493467&resulttype=core&format=json

14 May 2020

23710708

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=PMCID:PMC6493467&resulttype=core&format=json