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  6. Keywords
  7. Topics
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We are analyzing https://link.springer.com/article/10.1007/s00401-014-1268-0.

Title:
Amyloidogenic α-synuclein seeds do not invariably induce rapid, widespread pathology in mice | Acta Neuropathologica
Description:
In order to further evaluate the parameters whereby intracerebral administration of recombinant α-synuclein (αS) induces pathological phenotypes in mice, we conducted a series of studies where αS fibrils were injected into the brains of M83 (A53T) and M47 (E46K) αS transgenic (Tg) mice, and non-transgenic (nTg) mice. Using multiple markers to assess αS inclusion formation, we find that injected fibrillar human αS induced widespread cerebral αS inclusion formation in the M83 Tg mice, but in both nTg and M47 Tg mice, induced αS inclusion pathology is largely restricted to the site of injection. Furthermore, mouse αS fibrils injected into nTg mice brains also resulted in inclusion pathology restricted to the site of injection with no evidence for spread. We find no compelling evidence for extensive spread of αS pathology within white matter tracts, and we attribute previous reports of white matter tract spreading to cross-reactivity of the αS pSer129/81A antibody with phosphorylated neurofilament subunit L. These studies suggest that, with the exception of the M83 Tg mice which appear to be uniquely susceptible to induction of inclusion pathology by exogenous forms of αS, there are significant barriers in mice to widespread induction of αS pathology following intracerebral administration of amyloidogenic αS.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Education
  • Science
  • Business & Finance

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month


Based on our best estimate, this website will receive around 5,000,019 visitors per month in the current month.
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How Does Link.springer.com Make Money? {💸}

We see no obvious way the site makes money.

The purpose of some websites isn't monetary gain; they're meant to inform, educate, or foster collaboration. Everyone has unique reasons for building websites. This could be an example. Link.springer.com has a revenue plan, but it's either invisible or we haven't found it.

Keywords {🔍}

pubmed, scholar, google, cas, alphasynuclein, disease, central, parkinsons, giasson, mice, lee, pathology, supplementary, material, human, lewy, tiff, trojanowski, article, neuropathol, neurol, neurosci, acta, αsynuclein, brain, biol, exp, protein, zhang, transgenic, research, body, mutation, waxman, thomas, pathological, formation, neurodegenerative, neurodegeneration, neuron, nat, mol, cell, neurons, induce, golde, fibrils, inclusion, neurofilament, access,

Topics {✒️}

wild-type alpha-synuclein proteins lewy body-related alpha-synucleinopathy neurofilament-beta-galactosidase fusion protein neuron-released oligomeric alpha-synuclein amyloidogenic α-synuclein seeds month download article/chapter unique exon-intron organization amyloidogenic recombinant alpha-synuclein alpha-synuclein fibrils include fibrillar alpha-synuclein inclusions pathological alpha-synuclein initiates alpha-synuclein aggregate morphology alpha-synuclein locus triplication selectively detect alpha-synuclein alpha-synuclein gene identified cns alpha-synuclein pathology αs pser129/81a antibody alpha-synuclein dysfunction potentiate volpicelli-daley la phosphorylated alpha-synuclein histopathology alpha-synuclein alters toll alpha-synuclein missense mutation high-efficiency cellular model alpha-synuclein secondary structure g51d alpha-synuclein mutation recombinant α-synuclein waxman ea mutant alpha-synuclein linked central nervous system alpha-synuclein dependent activation alpha-synuclein seeds α-synuclein pathology human alpha-synuclein alpha-synuclein strains human neurofilament gene casein kinase-mediated phosphorylation aggregated alpha-synuclein alpha-synuclein pathology alpha-synuclein linked severe movement disorder pathological alpha-synuclein mice lacking neurofilaments full article pdf invariably induce rapid privacy choices/manage cookies early-onset parkinson disease luk kc gomez-esteban jc alpha-synuclein release alpha-synuclein permutations

Questions {❓}

  • Kiely AP, Asi YT, Kara E, Limousin P, Ling H, Lewis P, Proukakis C, Quinn N, Lees AJ, Hardy J, Revesz T, Houlden H, Holton JL (2013) Alpha-synucleinopathy associated with G51D SNCA mutation: a link between Parkinson’s disease and multiple system atrophy?

Schema {🗺️}

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      headline:Amyloidogenic α-synuclein seeds do not invariably induce rapid, widespread pathology in mice
      description:In order to further evaluate the parameters whereby intracerebral administration of recombinant α-synuclein (αS) induces pathological phenotypes in mice, we conducted a series of studies where αS fibrils were injected into the brains of M83 (A53T) and M47 (E46K) αS transgenic (Tg) mice, and non-transgenic (nTg) mice. Using multiple markers to assess αS inclusion formation, we find that injected fibrillar human αS induced widespread cerebral αS inclusion formation in the M83 Tg mice, but in both nTg and M47 Tg mice, induced αS inclusion pathology is largely restricted to the site of injection. Furthermore, mouse αS fibrils injected into nTg mice brains also resulted in inclusion pathology restricted to the site of injection with no evidence for spread. We find no compelling evidence for extensive spread of αS pathology within white matter tracts, and we attribute previous reports of white matter tract spreading to cross-reactivity of the αS pSer129/81A antibody with phosphorylated neurofilament subunit L. These studies suggest that, with the exception of the M83 Tg mice which appear to be uniquely susceptible to induction of inclusion pathology by exogenous forms of αS, there are significant barriers in mice to widespread induction of αS pathology following intracerebral administration of amyloidogenic αS.
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      name:Department of Neuroscience, Center for Translational Research in Neurodegenerative Disease and McKnight Brain Institute, College of Medicine University of Florida, Gainesville, USA
      name:Department of Laboratory Medicine and Pathobiology, Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Canada
      name:Department of Neuroscience, Center for Translational Research in Neurodegenerative Disease and McKnight Brain Institute, College of Medicine University of Florida, Gainesville, USA
      name:Department of Neuroscience, Center for Translational Research in Neurodegenerative Disease and McKnight Brain Institute, College of Medicine University of Florida, Gainesville, USA
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