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

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2051-5960

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity ; volume:5 ; number:1 ; day:10 ; month:1 ; year:2017 ; pages:1-15 ; date:12.2017
Acta Neuropathologica Communications ; 5, Heft 1 (10.1.2017), 1-15, 12.2017

Keyword: Hirnkrankheit
Neuropsychiatrie
Nervenkrankheit

Creator: Ysselstein, Daniel

Contributor: Dehay, Benjamin
Costantino, Isabel M.
McCabe, George P.
Frosch, Matthew P.
George, Julia M.
Bezard, Erwan
Rochet, Jean-Christophe
SpringerLink (Online service)

DOI: 10.1186/s40478-016-0403-7

URN: urn:nbn:de:1111-2017020812006

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:49 AM CEST

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Ysselstein, Daniel
Dehay, Benjamin
Costantino, Isabel M.
McCabe, George P.
Frosch, Matthew P.
George, Julia M.
Bezard, Erwan
Rochet, Jean-Christophe
SpringerLink (Online service)

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Functionalization of α-synuclein fibrils

Hyperosmotic stress induces cell-dependent aggregation of α-synuclein

Pharmacological inhibition of α-synuclein aggregation within liquid condensates

Decreased Water Mobility Contributes To Increased α‐Synuclein Aggregation **

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

Upregulating β-hexosaminidase activity in rodents prevents α-synuclein lipid associations and protects dopaminergic neurons from α-synuclein-mediated neurotoxicity

Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein

Hochschulschrift

Structural features and environmental conditions regulating α-synuclein [alpha-synuclein] aggregation

Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation

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

Functionalization of α-synuclein fibrils

Hyperosmotic stress induces cell-dependent aggregation of α-synuclein

Pharmacological inhibition of α-synuclein aggregation within liquid condensates

Decreased Water Mobility Contributes To Increased α‐Synuclein Aggregation **

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

Upregulating β-hexosaminidase activity in rodents prevents α-synuclein lipid associations and protects dopaminergic neurons from α-synuclein-mediated neurotoxicity

Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein

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

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Other Objects (12)

Structural features and environmental conditions regulating α-synuclein [alpha-synuclein] aggregation

Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation

Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation

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

Functionalization of α-synuclein fibrils

Hyperosmotic stress induces cell-dependent aggregation of α-synuclein

Pharmacological inhibition of α-synuclein aggregation within liquid condensates

Decreased Water Mobility Contributes To Increased α‐Synuclein Aggregation **

Decreased Water Mobility Contributes To Increased α‐Synuclein Aggregation **

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

Upregulating β-hexosaminidase activity in rodents prevents α-synuclein lipid associations and protects dopaminergic neurons from α-synuclein-mediated neurotoxicity

Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein

Structural features and environmental conditions regulating α-synuclein [alpha-synuclein] aggregation

Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation

Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation

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

Functionalization of α-synuclein fibrils

Hyperosmotic stress induces cell-dependent aggregation of α-synuclein

Pharmacological inhibition of α-synuclein aggregation within liquid condensates

Decreased Water Mobility Contributes To Increased α‐Synuclein Aggregation **

Decreased Water Mobility Contributes To Increased α‐Synuclein Aggregation **

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

Upregulating β-hexosaminidase activity in rodents prevents α-synuclein lipid associations and protects dopaminergic neurons from α-synuclein-mediated neurotoxicity

Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein

Structural features and environmental conditions regulating α-synuclein [alpha-synuclein] aggregation

Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation

Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation

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

Functionalization of α-synuclein fibrils

Hyperosmotic stress induces cell-dependent aggregation of α-synuclein

Pharmacological inhibition of α-synuclein aggregation within liquid condensates

Decreased Water Mobility Contributes To Increased α‐Synuclein Aggregation **

Decreased Water Mobility Contributes To Increased α‐Synuclein Aggregation **

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

Upregulating β-hexosaminidase activity in rodents prevents α-synuclein lipid associations and protects dopaminergic neurons from α-synuclein-mediated neurotoxicity

Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein

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