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

to related objects

Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2373-8057

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Parkinson-causing mutations in LRRK2 impair the physiological tetramerization of endogenous α-synuclein in human neurons ; volume:8 ; number:1 ; day:16 ; month:9 ; year:2022 ; pages:1-10 ; date:12.2022
npj Parkinson's Disease ; 8, Heft 1 (16.9.2022), 1-10, 12.2022

Creator: Fonseca-Ornelas, Luis
Stricker, Jonathan M. S.
Soriano-Cruz, Stephanie
Weykopf, Beatrice
Dettmer, Ulf
Muratore, Christina R.
Scherzer, Clemens R.
Selkoe, Dennis J.

Contributor: SpringerLink (Online service)

DOI: 10.1038/s41531-022-00380-1

URN: urn:nbn:de:101:1-2022120309192443652506

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:20 AM CEST

Data provider

This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.

Show original at data provider

Associated

Fonseca-Ornelas, Luis
Stricker, Jonathan M. S.
Soriano-Cruz, Stephanie
Weykopf, Beatrice
Dettmer, Ulf
Muratore, Christina R.
Scherzer, Clemens R.
Selkoe, Dennis J.
SpringerLink (Online service)

Other Objects (12)

LRRK2 kinase regulates α-synuclein propagation via RAB35 phosphorylation

Leucine-rich repeat kinase 2 (LRRK2) regulates α-synuclein clearance in microglia

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

Pathological α-synuclein recruits LRRK2 expressing pro-inflammatory monocytes to the brain

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

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

α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice

Functionalization of α-synuclein fibrils

LRRK2 inhibition does not impart protection from α-synuclein pathology and neuron death in non-transgenic mice

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein

Long-term inhibition of mutant LRRK2 hyper-kinase activity reduced mouse brain α-synuclein oligomers without adverse effects

LRRK2 kinase regulates α-synuclein propagation via RAB35 phosphorylation

Leucine-rich repeat kinase 2 (LRRK2) regulates α-synuclein clearance in microglia

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

Pathological α-synuclein recruits LRRK2 expressing pro-inflammatory monocytes to the brain

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

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

α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice

Functionalization of α-synuclein fibrils

LRRK2 inhibition does not impart protection from α-synuclein pathology and neuron death in non-transgenic mice

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein

Long-term inhibition of mutant LRRK2 hyper-kinase activity reduced mouse brain α-synuclein oligomers without adverse effects

LRRK2 kinase regulates α-synuclein propagation via RAB35 phosphorylation

Leucine-rich repeat kinase 2 (LRRK2) regulates α-synuclein clearance in microglia

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

Pathological α-synuclein recruits LRRK2 expressing pro-inflammatory monocytes to the brain

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

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

α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice

Functionalization of α-synuclein fibrils

LRRK2 inhibition does not impart protection from α-synuclein pathology and neuron death in non-transgenic mice

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein

Long-term inhibition of mutant LRRK2 hyper-kinase activity reduced mouse brain α-synuclein oligomers without adverse effects

Cultural heritage institutions wishing to register will find more information here.

Fields marked * need to be filled in.

Username*

Please enter your username

Email*

Please enter your email address

Please do not fill this field

First name

Last name

Password*

Please enter your password

Confirm password*

Please enter the same password

I have read the terms of use and the privacy policy for the collection of personal data and accept them. *

This field is required.

I would like to subscribe to the newsletter of the Deutsche Digitale Bibliothek. See newsletter subscription info.

Account created

Your "My DDB" account has been successfully created. Before you can log in to your account, you must click the confirmation link in the message we just sent to the email address you provided.

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

Object Details

References and Relationships

Contributors, Places and Time

Further information

Data provider

Associated

Other Objects (12)

LRRK2 kinase regulates α-synuclein propagation via RAB35 phosphorylation

Leucine-rich repeat kinase 2 (LRRK2) regulates α-synuclein clearance in microglia

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

Pathological α-synuclein recruits LRRK2 expressing pro-inflammatory monocytes to the brain

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

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

α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice

Functionalization of α-synuclein fibrils

LRRK2 inhibition does not impart protection from α-synuclein pathology and neuron death in non-transgenic mice

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein

Long-term inhibition of mutant LRRK2 hyper-kinase activity reduced mouse brain α-synuclein oligomers without adverse effects

LRRK2 kinase regulates α-synuclein propagation via RAB35 phosphorylation

Leucine-rich repeat kinase 2 (LRRK2) regulates α-synuclein clearance in microglia

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

Pathological α-synuclein recruits LRRK2 expressing pro-inflammatory monocytes to the brain

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

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

α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice

Functionalization of α-synuclein fibrils

LRRK2 inhibition does not impart protection from α-synuclein pathology and neuron death in non-transgenic mice

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein

Long-term inhibition of mutant LRRK2 hyper-kinase activity reduced mouse brain α-synuclein oligomers without adverse effects

LRRK2 kinase regulates α-synuclein propagation via RAB35 phosphorylation

Leucine-rich repeat kinase 2 (LRRK2) regulates α-synuclein clearance in microglia

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

Pathological α-synuclein recruits LRRK2 expressing pro-inflammatory monocytes to the brain

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

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

α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice

Functionalization of α-synuclein fibrils

LRRK2 inhibition does not impart protection from α-synuclein pathology and neuron death in non-transgenic mice

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein

Long-term inhibition of mutant LRRK2 hyper-kinase activity reduced mouse brain α-synuclein oligomers without adverse effects

Related objects

Reset password