The HSP40 family chaperone isoform DNAJB6b prevents neuronal cells from tau aggregation

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: 1 Online-Ressource.

Language: Englisch

Bibliographic citation: The HSP40 family chaperone isoform DNAJB6b prevents neuronal cells from tau aggregation ; volume:21 ; number:1 ; day:18 ; month:12 ; year:2023 ; pages:1-17 ; date:12.2023
BMC biology ; 21, Heft 1 (18.12.2023), 1-17, 12.2023

Creator: Chang, Ya-Lan
Yang, Chan-Chih
Huang, Yun-Yu
Chen, Yi-An
Yang, Chia-Wei
Liao, Chia-Yu
Li, Hsun
Wu, Ching-Shyi
Lin, Chin-Hsien
Teng, Shu-Chun

Contributor: SpringerLink (Online service)

DOI: 10.1186/s12915-023-01798-6

URN: urn:nbn:de:101:1-2024030221102494254521

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

Last update: 14.08.2025, 10:46 AM CEST

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Associated

Chang, Ya-Lan
Yang, Chan-Chih
Huang, Yun-Yu
Chen, Yi-An
Yang, Chia-Wei
Liao, Chia-Yu
Li, Hsun
Wu, Ching-Shyi
Lin, Chin-Hsien
Teng, Shu-Chun
SpringerLink (Online service)

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The HSP40 family chaperone isoform DNAJB6b prevents neuronal cells from tau aggregation

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Other Objects (12)

Tau aggregation following subcortical hemorrhage

Disruption of tubulin-alpha4a polyglutamylation prevents aggregation of hyper-phosphorylated tau and microglia activation in mice

Tau binding protein CAPON induces tau aggregation and neurodegeneration

USP10 deubiquitinates Tau, mediating its aggregation

Tau protein liquid–liquid phase separation can initiate tau aggregation

Chemical chaperone suppresses the antibody aggregation in CHO cell culture

A novel D-amino acid peptide with therapeutic potential (ISAD1) inhibits aggregation of neurotoxic disease-relevant mutant Tau and prevents Tau toxicity in vitro

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

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

Molecular Mechanisms of Tau Protein Aggregation Inhibition

NUB1 modulation of GSK3β reduces tau aggregation

Chemical chaperone 4-phenylbutyrate prevents endoplasmic reticulum stress induced by T17M rhodopsin

Tau aggregation following subcortical hemorrhage

Disruption of tubulin-alpha4a polyglutamylation prevents aggregation of hyper-phosphorylated tau and microglia activation in mice

Tau binding protein CAPON induces tau aggregation and neurodegeneration

USP10 deubiquitinates Tau, mediating its aggregation

Tau protein liquid–liquid phase separation can initiate tau aggregation

Chemical chaperone suppresses the antibody aggregation in CHO cell culture

A novel D-amino acid peptide with therapeutic potential (ISAD1) inhibits aggregation of neurotoxic disease-relevant mutant Tau and prevents Tau toxicity in vitro

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

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

Molecular Mechanisms of Tau Protein Aggregation Inhibition

NUB1 modulation of GSK3β reduces tau aggregation

Chemical chaperone 4-phenylbutyrate prevents endoplasmic reticulum stress induced by T17M rhodopsin

Tau aggregation following subcortical hemorrhage

Disruption of tubulin-alpha4a polyglutamylation prevents aggregation of hyper-phosphorylated tau and microglia activation in mice

Tau binding protein CAPON induces tau aggregation and neurodegeneration

USP10 deubiquitinates Tau, mediating its aggregation

Tau protein liquid–liquid phase separation can initiate tau aggregation

Chemical chaperone suppresses the antibody aggregation in CHO cell culture

A novel D-amino acid peptide with therapeutic potential (ISAD1) inhibits aggregation of neurotoxic disease-relevant mutant Tau and prevents Tau toxicity in vitro

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

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

Molecular Mechanisms of Tau Protein Aggregation Inhibition

NUB1 modulation of GSK3β reduces tau aggregation

Chemical chaperone 4-phenylbutyrate prevents endoplasmic reticulum stress induced by T17M rhodopsin

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