Tau tubulin kinase 2 is required to initiate mammalian ciliogenesis

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2046-2530

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Tau tubulin kinase 2 is required to initiate mammalian ciliogenesis ; volume:1 ; number:1 ; day:16 ; month:11 ; year:2012 ; pages:1 ; date:11.2012
Cilia ; 1, Heft 1 (16.11.2012), 1, 11.2012

Creator: Goetz, S.

Contributor: Anderson, KV
SpringerLink (Online service)

DOI: 10.1186/2046-2530-1-S1-O18

URN: urn:nbn:de:1111-2016072640829

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:54 AM CEST

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Goetz, S.
Anderson, KV
SpringerLink (Online service)

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Tau protein liquid–liquid phase separation can initiate tau aggregation

Expanded Conformations of Monomeric Tau Initiate Its Amyloidogenesis **

Modulation of tau tubulin kinases (TTBK1 and TTBK2) impacts ciliogenesis

Einfluss des Nukleotidstatus von Tubulin auf die Tau-Mikrotubuli-Interaktion

The force required to remove tubulin from the microtubule lattice by pulling on its α-tubulin C-terminal tail

Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges

Mapping of ESE-1 subdomains required to initiate mammary epithelial cell transformation via a cytoplasmic mechanism

Antisense oligonucleotide-based targeting of Tau-tubulin kinase 1 prevents hippocampal accumulation of phosphorylated tau in PS19 tauopathy mice

Hochschulschrift

Reversible tau phosphorylation and neuronal plasticity in mammalian hibernation

The GTPase domain of gamma-tubulin is required for normal mitochondrial function and spatial organization

Hochschulschrift

Untersuchungen zur Primärstruktur von β-Tubulin [Beta-Tubulin] aus Schweinehirn

Tau protein liquid–liquid phase separation can initiate tau aggregation

Expanded Conformations of Monomeric Tau Initiate Its Amyloidogenesis **

Modulation of tau tubulin kinases (TTBK1 and TTBK2) impacts ciliogenesis

Einfluss des Nukleotidstatus von Tubulin auf die Tau-Mikrotubuli-Interaktion

The force required to remove tubulin from the microtubule lattice by pulling on its α-tubulin C-terminal tail

Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges

Mapping of ESE-1 subdomains required to initiate mammary epithelial cell transformation via a cytoplasmic mechanism

Antisense oligonucleotide-based targeting of Tau-tubulin kinase 1 prevents hippocampal accumulation of phosphorylated tau in PS19 tauopathy mice

Hochschulschrift

Reversible tau phosphorylation and neuronal plasticity in mammalian hibernation

The GTPase domain of gamma-tubulin is required for normal mitochondrial function and spatial organization

Hochschulschrift

Untersuchungen zur Primärstruktur von β-Tubulin [Beta-Tubulin] aus Schweinehirn

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Tau tubulin kinase 2 is required to initiate mammalian ciliogenesis

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Other Objects (12)

Tau protein liquid–liquid phase separation can initiate tau aggregation

Expanded Conformations of Monomeric Tau Initiate Its Amyloidogenesis **

Expanded Conformations of Monomeric Tau Initiate Its Amyloidogenesis **

Modulation of tau tubulin kinases (TTBK1 and TTBK2) impacts ciliogenesis

Einfluss des Nukleotidstatus von Tubulin auf die Tau-Mikrotubuli-Interaktion

The force required to remove tubulin from the microtubule lattice by pulling on its α-tubulin C-terminal tail

Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges

Mapping of ESE-1 subdomains required to initiate mammary epithelial cell transformation via a cytoplasmic mechanism

Antisense oligonucleotide-based targeting of Tau-tubulin kinase 1 prevents hippocampal accumulation of phosphorylated tau in PS19 tauopathy mice

Reversible tau phosphorylation and neuronal plasticity in mammalian hibernation

The GTPase domain of gamma-tubulin is required for normal mitochondrial function and spatial organization

Untersuchungen zur Primärstruktur von β-Tubulin [Beta-Tubulin] aus Schweinehirn

Tau protein liquid–liquid phase separation can initiate tau aggregation

Expanded Conformations of Monomeric Tau Initiate Its Amyloidogenesis **

Expanded Conformations of Monomeric Tau Initiate Its Amyloidogenesis **

Modulation of tau tubulin kinases (TTBK1 and TTBK2) impacts ciliogenesis

Einfluss des Nukleotidstatus von Tubulin auf die Tau-Mikrotubuli-Interaktion

The force required to remove tubulin from the microtubule lattice by pulling on its α-tubulin C-terminal tail

Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges

Mapping of ESE-1 subdomains required to initiate mammary epithelial cell transformation via a cytoplasmic mechanism

Antisense oligonucleotide-based targeting of Tau-tubulin kinase 1 prevents hippocampal accumulation of phosphorylated tau in PS19 tauopathy mice

Reversible tau phosphorylation and neuronal plasticity in mammalian hibernation

The GTPase domain of gamma-tubulin is required for normal mitochondrial function and spatial organization

Untersuchungen zur Primärstruktur von β-Tubulin [Beta-Tubulin] aus Schweinehirn

Tau protein liquid–liquid phase separation can initiate tau aggregation

Expanded Conformations of Monomeric Tau Initiate Its Amyloidogenesis **

Expanded Conformations of Monomeric Tau Initiate Its Amyloidogenesis **

Modulation of tau tubulin kinases (TTBK1 and TTBK2) impacts ciliogenesis

Einfluss des Nukleotidstatus von Tubulin auf die Tau-Mikrotubuli-Interaktion

The force required to remove tubulin from the microtubule lattice by pulling on its α-tubulin C-terminal tail

Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges

Mapping of ESE-1 subdomains required to initiate mammary epithelial cell transformation via a cytoplasmic mechanism

Antisense oligonucleotide-based targeting of Tau-tubulin kinase 1 prevents hippocampal accumulation of phosphorylated tau in PS19 tauopathy mice

Reversible tau phosphorylation and neuronal plasticity in mammalian hibernation

The GTPase domain of gamma-tubulin is required for normal mitochondrial function and spatial organization

Untersuchungen zur Primärstruktur von β-Tubulin [Beta-Tubulin] aus Schweinehirn

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