Why do cellular proteins linked to K63-polyubiquitin chains not associate with proteasomes?-Reference-Cited by-同舟云学术

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Why do cellular proteins linked to K63-polyubiquitin chains not associate with proteasomes?

Published:2013-01-11 Issue:4 Volume:32 Page:552-565
ISSN:0261-4189
Container-title:The EMBO Journal
language:
Short-container-title:EMBO J

Author:

Nathan James A,Tae Kim Hyoung,Ting Lily,Gygi Steven P,Goldberg Alfred L

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Reference53 articles.

1. Principles of ubiquitin and SUMO modifications in DNA repair

2. Isolation of Mammalian 26S Proteasomes and p97/VCP Complexes Using the Ubiquitin-like Domain from HHR23B Reveals Novel Proteasome-Associated Proteins

3. HRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradation

4. The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response

5. The Specificities of Kaposi's Sarcoma-Associated Herpesvirus-Encoded E3 Ubiquitin Ligases Are Determined by the Positions of Lysine or Cysteine Residues within the Intracytoplasmic Domains of Their Targets

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1. Phase separation of polyubiquitinated proteins in UBQLN2 condensates controls substrate fate;Proceedings of the National Academy of Sciences;2024-08-09

2. The lowdown on breakdown: Open questions in plant proteolysis;The Plant Cell;2024-07-09

3. VCP/p97-associated proteins are binders and debranching enzymes of K48–K63-branched ubiquitin chains;Nature Structural & Molecular Biology;2024-07-08

4. Localized K63 ubiquitin signaling is regulated by VCP/p97 during oxidative stress;2024-06-21

5. The USP12/46 deubiquitinases protect integrins from ESCRT-mediated lysosomal degradation;2024-05-17

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