Structural Basis for Chaperone‐Independent Ubiquitination of Tau Protein by Its E3 Ligase CHIP-Reference-Cited by-同舟云学术

Structural Basis for Chaperone‐Independent Ubiquitination of Tau Protein by Its E3 Ligase CHIP

Published:2022-02-18 Issue:15 Volume:61 Page:
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew Chem Int Ed

Author:

Munari Francesca¹,Mollica Luca²,Valente Carlo²,Parolini Francesca¹,Kachoie Elham Ataie¹,Arrigoni Giorgio³⁴,D'Onofrio Mariapina¹,Capaldi Stefano¹,Assfalg Michael¹^ORCID

Affiliation:

1. Department of Biotechnology University of Verona Strada Le Grazie 15 37134 Verona Italy

2. Department of Medical Biotechnology and Translational Medicine University of Milan Milan Italy

3. Department of Biomedical Sciences University of Padova Padova Italy

4. Proteomics Center University of Padova and Azienda Ospedaliera di Padova Padova Italy

Publisher

Wiley

Subject

General Chemistry,Catalysis

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.202112374

Reference46 articles.

1. The proteostasis network and its decline in ageing

2. The emerging complexity of protein ubiquitination

3. Reading the ubiquitin postal code

4. Polyubiquitin chains: polymeric protein signals

5. Targeting of substrates to the 26S proteasome

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1. Phosphorylation of tau at a single residue inhibits binding to the E3 ubiquitin ligase, CHIP;Nature Communications;2024-09-12

2. Involvement of ubiquitination in Alzheimer’s disease;Frontiers in Neurology;2024-09-05

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5. Site‐Specific Ubiquitination of Tau Amyloids Promoted by the E3 Ligase CHIP;Angewandte Chemie;2023-11-10