Loss of presenilin function enhances tau phosphorylation and aggregation in mice

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2051-5960

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Loss of presenilin function enhances tau phosphorylation and aggregation in mice ; volume:9 ; number:1 ; day:30 ; month:9 ; year:2021 ; pages:1-20 ; date:12.2021
Acta Neuropathologica Communications ; 9, Heft 1 (30.9.2021), 1-20, 12.2021

Creator: Soto-Faguás, Carlos M.
Sanchez-Molina, Paula
Saura, Carlos A.

Contributor: SpringerLink (Online service)

DOI: 10.1186/s40478-021-01259-7

URN: urn:nbn:de:101:1-2021121905505803234751

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

Last update: 15.08.2025, 7:33 AM CEST

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Soto-Faguás, Carlos M.
Sanchez-Molina, Paula
Saura, Carlos A.
SpringerLink (Online service)

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Loss of presenilin function enhances tau phosphorylation and aggregation in mice

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Other Objects (12)

TYK2 regulates tau levels, phosphorylation and aggregation in a tauopathy mouse model

Ischemic axonal injury up-regulates MARK4 in cortical neurons and primes tau phosphorylation and aggregation

Tau aggregation following subcortical hemorrhage

Tumor suppressor PTEN affects tau phosphorylation: deficiency in the phosphatase activity of PTEN increases aggregation of an FTDP-17 mutant Tau

Tau binding protein CAPON induces tau aggregation and neurodegeneration

USP10 deubiquitinates Tau, mediating its aggregation

Tau Ser208 phosphorylation promotes aggregation and reveals neuropathologic diversity in Alzheimer’s disease and other tauopathies

Tau protein liquid–liquid phase separation can initiate tau aggregation

Abeta is prerequisite, but insufficient to cause tau phosphorylation in vivo: tau phosphorylation in APP mice by diabetes

Phosphorylation regulates tau’s phase separation behavior and interactions with chromatin

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Author Correction: Tau binding protein CAPON induces tau aggregation and neurodegeneration

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Tumor suppressor PTEN affects tau phosphorylation: deficiency in the phosphatase activity of PTEN increases aggregation of an FTDP-17 mutant Tau

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Tau Ser208 phosphorylation promotes aggregation and reveals neuropathologic diversity in Alzheimer’s disease and other tauopathies

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Abeta is prerequisite, but insufficient to cause tau phosphorylation in vivo: tau phosphorylation in APP mice by diabetes

Phosphorylation regulates tau’s phase separation behavior and interactions with chromatin

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Author Correction: Tau binding protein CAPON induces tau aggregation and neurodegeneration

TYK2 regulates tau levels, phosphorylation and aggregation in a tauopathy mouse model

Ischemic axonal injury up-regulates MARK4 in cortical neurons and primes tau phosphorylation and aggregation

Tau aggregation following subcortical hemorrhage

Tumor suppressor PTEN affects tau phosphorylation: deficiency in the phosphatase activity of PTEN increases aggregation of an FTDP-17 mutant Tau

Tau binding protein CAPON induces tau aggregation and neurodegeneration

USP10 deubiquitinates Tau, mediating its aggregation

Tau Ser208 phosphorylation promotes aggregation and reveals neuropathologic diversity in Alzheimer’s disease and other tauopathies

Tau protein liquid–liquid phase separation can initiate tau aggregation

Abeta is prerequisite, but insufficient to cause tau phosphorylation in vivo: tau phosphorylation in APP mice by diabetes

Phosphorylation regulates tau’s phase separation behavior and interactions with chromatin

Suppressing Tau Aggregation and Toxicity by an Anti-Aggregant Tau Fragment

Author Correction: Tau binding protein CAPON induces tau aggregation and neurodegeneration

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