Age-dependent dopamine transporter dysfunction and Serine129 phospho-α-synuclein overload in G2019S LRRK2 mice

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2051-5960

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Age-dependent dopamine transporter dysfunction and Serine129 phospho-α-synuclein overload in G2019S LRRK2 mice ; volume:5 ; number:1 ; day:14 ; month:3 ; year:2017 ; pages:1-17 ; date:12.2017
Acta Neuropathologica Communications ; 5, Heft 1 (14.3.2017), 1-17, 12.2017

Keyword: Harnwege
Lymphsystem
Sekretion
Drüse
Endokrinium
Blutbildendes Gewebe

Creator: Longo, Francesco

Contributor: Mercatelli, Daniela
Novello, Salvatore
Arcuri, Ludovico
Brugnoli, Alberto
Vincenzi, Fabrizio
Russo, Isabella
Berti, Giulia
Mabrouk, Omar S.
Kennedy, Robert T.
Shimshek, Derya R.
Varani, Katia
Bubacco, Luigi
Greggio, Elisa
Morari, Michele
SpringerLink (Online service)

DOI: 10.1186/s40478-017-0426-8

URN: urn:nbn:de:1111-201704037677

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:54 AM CEST

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Associated

Longo, Francesco
Mercatelli, Daniela
Novello, Salvatore
Arcuri, Ludovico
Brugnoli, Alberto
Vincenzi, Fabrizio
Russo, Isabella
Berti, Giulia
Mabrouk, Omar S.
Kennedy, Robert T.
Shimshek, Derya R.
Varani, Katia
Bubacco, Luigi
Greggio, Elisa
Morari, Michele
SpringerLink (Online service)

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Age-dependent dopamine transporter dysfunction and Serine129 phospho-α-synuclein overload in G2019S LRRK2 mice

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Other Objects (12)

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LRRK2 interactions with α-synuclein in Parkinson’s disease brains and in cell models

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Macroautophagy deficiency mediates age-dependent neurodegeneration through a phospho-tau pathway

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LRRK2 activity does not dramatically alter α-synuclein pathology in primary neurons

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Parkinson’s Disease–Associated LRRK2 Interferes with Astrocyte-Mediated Alpha-Synuclein Clearance

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Inhibition of LRRK2 kinase activity promotes anterograde axonal transport and presynaptic targeting of α-synuclein

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Parkinson-causing mutations in LRRK2 impair the physiological tetramerization of endogenous α-synuclein in human neurons

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LRRK2 activity does not dramatically alter α-synuclein pathology in primary neurons

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