title: |
Loss-Of HSPB8 leads to prolonged stress granules disassembly via impaired CASA-complex
ultimately causing FUS-aggregation |
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contributing persons: |
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contributing corporate bodies: |
Universität Rostock[Grad-verleihende Institution] |
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38329-6 |
Universitätsmedizin Rostock[Grad-verleihende Institution] |
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1029510660 |
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abstract: |
Our research sheds light on the collaborative functioning of various chaperone systems
within the proteostasis network. Molecular chaperones, including HSP70, and HSP40,
and co-chaperones like HSC70, HSP90, and CHIP, are vital in protein quality control
and degradation. Dysregulation within these systems, observed in HSPB8 knockout neurons,
indicates impaired mechanisms for maintaining cellular proteostasis. This deficiency
renders cells vulnerable to stress, resulting in detrimental effects on cellular survival.
[English] |
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document type: |
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institution: |
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language: |
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subject class (DDC): |
610 Medical sciences Medicine |
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extent: |
1 Online-Ressource (140 Seiten)
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publication / production: |
Rostock
Rostock: Universität Rostock
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18.09.2023
(normalised date: 2023) |
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statement of responsibility: |
vorgelegt von Kanza Saleem |
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identifiers: |
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access condition: |
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license/rights statement: |
all rights reserved This work may only be used under the terms of the German Copyright Law (Urheberrechtsgesetz). |
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RosDok id: |
rosdok_disshab_0000003168 |
created / modified: |
01.07.2024 / 02.07.2024
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metadata license: |
The metadata of this document was dedicated to the public domain (CC0 1.0 Universal Public Domain Dedication). |