Characterization of antibodies that selectively detect alpha-synuclein in pathological inclusions.
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Propagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies.Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic miceIntramuscular injection of α-synuclein induces CNS α-synuclein pathology and a rapid-onset motor phenotype in transgenic mice.Intrastriatal injection of α-synuclein can lead to widespread synucleinopathy independent of neuroanatomic connectivity.DJ-1 deficient mice demonstrate similar vulnerability to pathogenic Ala53Thr human alpha-syn toxicity.Extensive enteric nervous system abnormalities in mice transgenic for artificial chromosomes containing Parkinson disease-associated alpha-synuclein gene mutations precede central nervous system changes.Abrogation of α-synuclein-mediated dopaminergic neurodegeneration in LRRK2-deficient rats.The glycolytic enzyme, GPI, is a functionally conserved modifier of dopaminergic neurodegeneration in Parkinson's models.Mitochondrial inhibitor 3-nitroproprionic acid enhances oxidative modification of alpha-synuclein in a transgenic mouse model of multiple system atrophyA novel, high-efficiency cellular model of fibrillar alpha-synuclein inclusions and the examination of mutations that inhibit amyloid formationAugmentation of phenotype in a transgenic Parkinson mouse heterozygous for a Gaucher mutationE46K human alpha-synuclein transgenic mice develop Lewy-like and tau pathology associated with age-dependent, detrimental motor impairmentStudies of protein aggregation in A53T α-synuclein transgenic, Tg2576 transgenic, and P246L presenilin-1 knock-in cross bred mice.Characterization of kinases involved in the phosphorylation of aggregated α-synuclein.Studies of lipopolysaccharide effects on the induction of α-synuclein pathology by exogenous fibrils in transgenic mice.Soluble α-synuclein is a novel modulator of Alzheimer's disease pathophysiology.Amyloidogenic α-synuclein seeds do not invariably induce rapid, widespread pathology in mice.Molecular mechanisms of alpha-synuclein neurodegeneration.Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synucleinRobust Central Nervous System Pathology in Transgenic Mice following Peripheral Injection of α-Synuclein Fibrils.Neuropathology of sporadic Parkinson's disease: evaluation and changes of concepts.An antibody with high reactivity for disease-associated α-synuclein reveals extensive brain pathology.Review: Spreading the word: precise animal models and validated methods are vital when evaluating prion-like behaviour of alpha-synuclein.Robust cytoplasmic accumulation of phosphorylated TDP-43 in transgenic models of tauopathy.Viral expression of ALS-linked ubiquilin-2 mutants causes inclusion pathology and behavioral deficits in mice.A novel panel of α-synuclein antibodies reveal distinctive staining profiles in synucleinopathies.Molecular and Biological Compatibility with Host Alpha-Synuclein Influences Fibril Pathogenicity.The ER retention protein RER1 promotes alpha-synuclein degradation via the proteasome.Progression of alpha-synuclein pathology in multiple system atrophy of the cerebellar type.Brain alpha-synuclein accumulation in multiple system atrophy, Parkinson's disease and progressive supranuclear palsy: a comparative investigation.Dopamine induces soluble α-synuclein oligomers and nigrostriatal degeneration.Lewy body extracts from Parkinson disease brains trigger α-synuclein pathology and neurodegeneration in mice and monkeys.Reversible Conformational Conversion of α-Synuclein into Toxic Assemblies by Glucosylceramide.Glucocerebrosidase haploinsufficiency in A53T α-synuclein mice impacts disease onset and course.Comparison of the in vivo induction and transmission of α-synuclein pathology by mutant α-synuclein fibril seeds in transgenic mice.Proteolysis of α-synuclein fibrils in the lysosomal pathway limits induction of inclusion pathology.Induction of the Immunoproteasome Subunit Lmp7 Links Proteostasis and Immunity in α-Synuclein Aggregation Disorders.
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Characterization of antibodies that selectively detect alpha-synuclein in pathological inclusions.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 15 April 2008
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Characterization of antibodies ...... in in pathological inclusions.
@en
Characterization of antibodies ...... in in pathological inclusions.
@nl
type
label
Characterization of antibodies ...... in in pathological inclusions.
@en
Characterization of antibodies ...... in in pathological inclusions.
@nl
prefLabel
Characterization of antibodies ...... in in pathological inclusions.
@en
Characterization of antibodies ...... in in pathological inclusions.
@nl
P2093
P2860
P1476
Characterization of antibodies ...... in in pathological inclusions.
@en
P2093
Benoit I Giasson
Elisa A Waxman
John E Duda
P2860
P2888
P356
10.1007/S00401-008-0375-1
P577
2008-04-15T00:00:00Z