Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3. - Test2 - elhamkhani - TriplyDB

Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3.

Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3.

http://www.wikidata.org/entity/Q41015843

about

Single cell imaging and quantification of TDP-43 and α-synuclein intercellular propagation.Exploring Braak's Hypothesis of Parkinson's Disease.α-Synuclein Amyloids Hijack Prion Protein to Gain Cell Entry, Facilitate Cell-to-Cell Spreading and Block Prion Replication.Impaired endo-lysosomal membrane integrity accelerates the seeding progression of α-synuclein aggregates.The cellular prion protein (PrPC) as neuronal receptor for α-synuclein.Internalization, axonal transport and release of fibrillar forms of alpha-synuclein.Extracellular Vesicles: Unique Intercellular Delivery Vehicles.Selective neuronal vulnerability in Parkinson disease.The Contribution of α-Synuclein Spreading to Parkinson's Disease Synaptopathy.Alpha-synuclein and iron: two keys unlocking Parkinson's disease.Designer protein disaggregases to counter neurodegenerative disease.Potential Modes of Intercellular α-Synuclein Transmission.LAG3 (CD223) as a cancer immunotherapy target.Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism.TMEM230: How does it fit in the etiology and pathogenesis of Parkinson's disease?Alpha-Synuclein to the Rescue: Immune Cell Recruitment by Alpha-Synuclein during Gastrointestinal Infection.T cells from patients with Parkinson's disease recognize α-synuclein peptides.Involvement of Cellular Prion Protein in α-Synuclein Transport in Neurons.Progress toward an integrated understanding of Parkinson's disease.Protein arginylation targets alpha synuclein, facilitates normal brain health, and prevents neurodegeneration Novel animal model defines genetic contributions for neuron-to-neuron transfer of α-synuclein.Selective imaging of internalized proteopathic α-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies.LRRK2 Antisense Oligonucleotides Ameliorate α-Synuclein Inclusion Formation in a Parkinson's Disease Mouse Model.Production of Monoclonal Antibodies to Pathologic β-sheet Oligomeric Conformers in Neurodegenerative Diseases.In vivo models of alpha-synuclein transmission and propagation.Vertebrate food products as a potential source of prion-like α-synuclein.Intercellular transfer of pathogenic α-synuclein by extracellular vesicles is induced by the lipid peroxidation product 4-hydroxynonenal.Alpha-synuclein oligomers: a new hope.Phosphorylated exogenous alpha-synuclein fibrils exacerbate pathology and induce neuronal dysfunction in mice.Mini-review on initiatives to interfere with the propagation and clearance of alpha-synuclein in Parkinson's disease.c-Abl and Parkinson's Disease: Mechanisms and Therapeutic Potential.GBA1 deficiency negatively affects physiological α-synuclein tetramers and related multimers.α-Synuclein accumulation and GBA deficiency due to L444P GBA mutation contributes to MPTP-induced parkinsonism.A network-based meta-analysis for characterizing the genetic landscape of human aging.Parkinson's Disease Is Not Simply a Prion Disorder.Induction of alpha-synuclein pathology in the enteric nervous system of the rat and non-human primate results in gastrointestinal dysmotility and transient CNS pathology.Critical appraisal of pathology transmission in the α-synuclein fibril model of Lewy body disorders.Prying into the Prion Hypothesis for Parkinson's Disease.Inflammatory CNS disease caused by immune checkpoint inhibitors: status and perspectives.Milestones of Parkinson's Disease Research: 200 Years of History and Beyond.

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P2860

Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3.

http://www.wikidata.org/entity/Q41015843

description

2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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name

Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3.

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type

label

Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3.

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prefLabel

Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3.

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SCIENCE.AAH3374

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Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3

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Chen Qi

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Creg J Workman

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Dario A A Vignali

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Donghoon Kim

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George Essien Umanah

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Han Seok Ko

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Ho Chul Kang

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Hyejin Park

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James A Keiler

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Jianmin Zhang

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P2860

Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers

Alpha-synuclein and polyunsaturated fatty acids promote clathrin-mediated endocytosis and synaptic vesicle recycling

EEA1, an early endosome-associated protein. EEA1 is a conserved alpha-helical peripheral membrane protein flanked by cysteine "fingers" and contains a calmodulin-binding IQ motif

Characterization of the major histocompatibility complex class II binding site on LAG-3 protein

Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds

Functional requirement for class I MHC in CNS development and plasticity

Endosome maturation

Self-propagation of pathogenic protein aggregates in neurodegenerative diseases

Neurodegenerative diseases: expanding the prion concept

Subcellular fractionation and localization studies reveal a direct interaction of the fragile X mental retardation protein (FMRP) with nucleolin

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scholarly article

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10.1126/SCIENCE.AAH3374

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6307

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353

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Nikhil Panicker

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2016-09-01T00:00:00Z

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27708076

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5510615

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