Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds - Test2 - elhamkhani - TriplyDB

Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds

Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds

http://www.wikidata.org/entity/Q24630644

about

NMR Meets Tau: Insights into Its Function and Pathology The role of macropinocytosis in the propagation of protein aggregation associated with neurodegenerative diseases Connecting the dots between tau dysfunction and neurodegeneration Prion-like properties of Tau protein: the importance of extracellular Tau as a therapeutic target The dendritic hypothesis for Alzheimer's disease pathophysiology.Macropinocytosis Exploitation by Cancers and Cancer Therapeutics Tau physiology and pathomechanisms in frontotemporal lobar degeneration Spreading of pathology in neurodegenerative diseases: a focus on human studies Legal but lethal: functional protein aggregation at the verge of toxicity Heparin inhibits melanosome uptake and inflammatory response coupled with phagocytosis through blocking PI3k/Akt and MEK/ERK signaling pathways in human epidermal keratinocytes Intrastriatal injection of pre-formed mouse α-synuclein fibrils into rats triggers α-synuclein pathology and bilateral nigrostriatal degeneration Propagation of tau pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies.Data in support of the identification of neuronal and astrocyte proteins interacting with extracellularly applied oligomeric and fibrillar α-synuclein assemblies by mass spectrometry Glial contributions to neurodegeneration in tauopathies.Roles of tau protein in health and disease.Enhanced neuroinvasion by smaller, soluble prions.Heparin binding confers prion stability and impairs its aggregation.Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing α-synuclein oligomeric species toxicity RGTA® or ReGeneraTing Agents mimic heparan sulfate in regenerative medicine: from concept to curing patients Single mutations in tau modulate the populations of fibril conformers through seed selection.Enhancing astrocytic lysosome biogenesis facilitates Aβ clearance and attenuates amyloid plaque pathogenesis Neuronal heparan sulfates promote amyloid pathology by modulating brain amyloid-β clearance and aggregation in Alzheimer's disease.Unraveling the mechanism of cell death induced by chemical fibrils.Proteopathic tau seeding predicts tauopathy in vivo.Impairment of glymphatic pathway function promotes tau pathology after traumatic brain injury.New roles of glycosaminoglycans in α-synuclein aggregation in a cellular model of Parkinson disease.Templated misfolding of Tau by prion-like seeding along neuronal connections impairs neuronal network function and associated behavioral outcomes in Tau transgenic mice.Tau Trimers Are the Minimal Propagation Unit Spontaneously Internalized to Seed Intracellular Aggregation.Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain.Transgenic over-expression of mammalian heparanase delays prion disease onset and progression.Neuronal-Targeted TFEB Accelerates Lysosomal Degradation of APP, Reducing Aβ Generation and Amyloid Plaque Pathogenesis.Distinct Therapeutic Mechanisms of Tau Antibodies: Promoting Microglial Clearance Versus Blocking Neuronal Uptake.Modulation of Glycosaminoglycans Affects PrPSc Metabolism but Does Not Block PrPSc Uptake.α-synuclein assemblies sequester neuronal α3-Na+/K+-ATPase and impair Na+ gradient Neuronal uptake and propagation of a rare phosphorylated high-molecular-weight tau derived from Alzheimer's disease brain.Distinct C9orf72-Associated Dipeptide Repeat Structures Correlate with Neuronal Toxicity.SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation.Targeting protein aggregation for the treatment of degenerative diseases Tau Hyperphosphorylation and Oxidative Stress, a Critical Vicious Circle in Neurodegenerative Tauopathies?Bent out of shape: α-Synuclein misfolding and the convergence of pathogenic pathways in Parkinson's disease.

P2860

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P2860

Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds

http://www.wikidata.org/entity/Q24630644

description

2013 nî lūn-bûn

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2013 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի հուլիսին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Heparan sulfate proteoglycans ...... of specific proteopathic seeds

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Heparan sulfate proteoglycans ...... of specific proteopathic seeds

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Heparan sulfate proteoglycans ...... of specific proteopathic seeds

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Heparan sulfate proteoglycans ...... of specific proteopathic seeds

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Heparan sulfate proteoglycans ...... of specific proteopathic seeds

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Heparan sulfate proteoglycans ...... of specific proteopathic seeds

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Heparan sulfate proteoglycans ...... of specific proteopathic seeds

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Heparan sulfate proteoglycans ...... of specific proteopathic seeds

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PNAS.1301440110

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Proceedings of the National Academy of Sciences of the United States of America

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Heparan sulfate proteoglycans ...... of specific proteopathic seeds

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P2093

Devika P Bagchi

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Dulce Papy-Garcia

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Jayne Marasa

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Marc I Diamond

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Mei Li

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Mohand O Ouidja

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Najla Kfoury

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Paul T Kotzbauer

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Rachel Jacks

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Sarah L DeVos

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P2860

Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells

α-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells.

Transmission and spreading of tauopathy in transgenic mouse brain

Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein

Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates

Neuropathological stageing of Alzheimer-related changes

Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans

Interaction of HIV-1 Tat protein with heparin. Role of the backbone structure, sulfation, and size

HIV-1 Tat protein exits from cells via a leaderless secretory pathway and binds to extracellular matrix-associated heparan sulfate proteoglycans through its basic region

Uptake of HIV-1 tat protein mediated by low-density lipoprotein receptor-related protein disrupts the neuronal metabolic balance of the receptor ligands

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10.1073/PNAS.1301440110

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33

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110

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Frances M Brodsky

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Brandon B Holmes

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2013-07-29T00:00:00Z

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253339706

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23898162

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