Phosphorylation of synucleins by members of the Polo-like kinase family. - Wikidata - wikimedia - TriplyDB

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

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

http://www.wikidata.org/entity/Q33514979

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Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model Polo-like kinase 2 regulates selective autophagic α-synuclein clearance and suppresses its toxicity in vivo The benefits of humanized yeast models to study Parkinson's disease Phosphorylation modulates clearance of alpha-synuclein inclusions in a yeast model of Parkinson's disease Impaired c-Fos and polo-like kinase 2 induction in the limbic system of fear-conditioned α-synuclein transgenic mice Selective and brain-permeable polo-like kinase-2 (Plk-2) inhibitors that reduce α-synuclein phosphorylation in rat brain Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications The phosphorylation of α-synuclein: development and implication for the mechanism and therapy of the Parkinson's disease Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions Assessing the subcellular dynamics of alpha-synuclein using photoactivation microscopy.Metformin lowers Ser-129 phosphorylated α-synuclein levels via mTOR-dependent protein phosphatase 2A activation.Parkinson's disease-implicated kinases in the brain; insights into disease pathogenesis.Polo-like kinase 2 activates an antioxidant pathway to promote the survival of cells with mitochondrial dysfunction.The novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of α-synuclein, and enhances its secretion and nuclear localization in cells.α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer Parkin depletion delays motor decline dose-dependently without overtly affecting neuropathology in α-synuclein transgenic mice.Evaluating the relationship between amyloid-β and α-synuclein phosphorylated at Ser129 in dementia with Lewy bodies and Parkinson's disease.SMG1 identified as a regulator of Parkinson's disease-associated alpha-synuclein through siRNA screening.Parkinson disease mutant E46K enhances α-synuclein phosphorylation in mammalian cell lines, in yeast, and in vivo Identification of the PLK2-dependent phosphopeptidome by quantitative proteomics [corrected].Biochemical increase in phosphorylated alpha-synuclein precedes histopathology of Lewy-type synucleinopathies Characterization of kinases involved in the phosphorylation of aggregated α-synuclein.The Interplay between Alpha-Synuclein Clearance and Spreading Interaction between Neuromelanin and Alpha-Synuclein in Parkinson's Disease.Polo-Like Kinase 3 Appears Dispensable for Normal Retinal Development Despite Robust Embryonic Expression.Increased α-synuclein phosphorylation and nitration in the aging primate substantia nigra.Emerging neurotoxic mechanisms in environmental factors-induced neurodegeneration.Alterations in axonal transport motor proteins in sporadic and experimental Parkinson's disease.A novel multiplex assay for simultaneous quantification of total and S129 phosphorylated human alpha-synuclein.O-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson's disease Characterization of semisynthetic and naturally Nα-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein.Polo-like kinase 2 acting as a promoter in human tumor cells with an abundance of TAp73.α-Synuclein disrupts stress signaling by inhibiting polo-like kinase Cdc5/Plk2 PLK2 phosphorylates and inhibits enriched TAp73 in human osteosarcoma cells Effects of Serine 129 Phosphorylation on α-Synuclein Aggregation, Membrane Association, and Internalization.Serine 129 phosphorylation of membrane-associated α-synuclein modulates dopamine transporter function in a G protein-coupled receptor kinase-dependent manner.Age- and brain region-dependent α-synuclein oligomerization is attributed to alterations in intrinsic enzymes regulating α-synuclein phosphorylation in aging monkey brains.Changes in properties of serine 129 phosphorylated α-synuclein with progression of Lewy-type histopathology in human brains.

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P2860

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

http://www.wikidata.org/entity/Q33514979

description

2009 nî lūn-bûn

@nan

2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

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2009年論文

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2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

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name

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

@ast

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

@en

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

@nl

type

label

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

@ast

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

@en

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

@nl

prefLabel

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

@ast

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

@en

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

@nl

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JBC.M109.081950

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Journal of Biological Chemistry

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

@en

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Abid Oueslati

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Ahmed Boucharaba

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Diana Olschewski

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Guowei Yin

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Harald Hirling

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Heinrich Schell

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Katerina E Paleologou

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Margot Fournier

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Martial K Mbefo

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Philipp J Kahle

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P2860

Polo-like kinase 3 is required for entry into S phase

Polo-like kinase-2 is required for centriole duplication in mammalian cells

Cdc25C phosphorylation on serine 191 by Plk3 promotes its nuclear translocation

The polo-like protein kinases Fnk and Snk associate with a Ca(2+)- and integrin-binding protein and are regulated dynamically with synaptic plasticity

Misfolded proteinase K-resistant hyperphosphorylated alpha-synuclein in aged transgenic mice with locomotor deterioration and in human alpha-synucleinopathies

The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex

alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies

Modulation of receptor cycling by neuron-enriched endosomal protein of 21 kD

Role of Plk2 (Snk) in mouse development and cell proliferation

The Sak polo-box comprises a structural domain sufficient for mitotic subcellular localization

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2807-2822

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10.1074/JBC.M109.081950

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4

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285

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Markus Zweckstetter

Eliezer Masliah

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2009-11-04T00:00:00Z

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38067381

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19889641

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phosphorylation

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2807335

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