Why do cellular proteins linked to K63-polyubiquitin chains not associate with proteasomes?
出版年份 2013 全文链接
标题
Why do cellular proteins linked to K63-polyubiquitin chains not associate with proteasomes?
作者
关键词
-
出版物
EMBO JOURNAL
Volume 32, Issue 4, Pages 552-565
出版商
Wiley
发表日期
2013-01-11
DOI
10.1038/emboj.2012.354
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response
- (2012) Laura R Butler et al. EMBO JOURNAL
- Polyubiquitin Linkage Profiles in Three Models of Proteolytic Stress Suggest the Etiology of Alzheimer Disease
- (2011) Eric B. Dammer et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- HRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradation
- (2011) Marian L. Burr et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- How Ubiquitin Functions with ESCRTs
- (2011) S. Brookhart Shields et al. TRAFFIC
- VHS domains of ESCRT-0 cooperate in high-avidity binding to polyubiquitinated cargo
- (2010) Xuefeng Ren et al. EMBO JOURNAL
- ATP-Dependent Steps in the Binding of Ubiquitin Conjugates to the 26S Proteasome that Commit to Degradation
- (2010) Andreas Peth et al. MOLECULAR CELL
- Enhancement of proteasome activity by a small-molecule inhibitor of USP14
- (2010) Byung-Hoon Lee et al. NATURE
- Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome
- (2009) Daniel Finley Annual Review of Biochemistry
- Isolation of Mammalian 26S Proteasomes and p97/VCP Complexes Using the Ubiquitin-like Domain from HHR23B Reveals Novel Proteasome-Associated Proteins†
- (2009) Henrike C. Besche et al. BIOCHEMISTRY
- Quantitative Proteomics Reveals the Function of Unconventional Ubiquitin Chains in Proteasomal Degradation
- (2009) Ping Xu et al. CELL
- Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome
- (2009) Yasushi Saeki et al. EMBO JOURNAL
- K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1
- (2009) Eric M Cooper et al. EMBO JOURNAL
- S5a promotes protein degradation by blocking synthesis of nondegradable forked ubiquitin chains
- (2009) Hyoung Tae Kim et al. EMBO JOURNAL
- The Lysine 48 and Lysine 63 Ubiquitin Conjugates Are Processed Differently by the 26 S Proteasome
- (2009) Andrew D. Jacobson et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Ubiquitinated Proteins Activate the Proteasome by Binding to Usp14/Ubp6, which Causes 20S Gate Opening
- (2009) Andreas Peth et al. MOLECULAR CELL
- Principles of ubiquitin and SUMO modifications in DNA repair
- (2009) Steven Bergink et al. NATURE
- Viral avoidance and exploitation of the ubiquitin system
- (2009) Felix Randow et al. NATURE CELL BIOLOGY
- Hybrid Structural Model of the Complete Human ESCRT-0 Complex
- (2009) Xuefeng Ren et al. STRUCTURE
- Ubiquitin Chain Editing Revealed by Polyubiquitin Linkage-Specific Antibodies
- (2008) Kim Newton et al. CELL
- Atypical ubiquitin chains: new molecular signals. ‘Protein Modifications: Beyond the Usual Suspects’ Review Series
- (2008) Fumiyo Ikeda et al. EMBO REPORTS
- The trafficking and regulation of membrane receptors by the RING-CH ubiquitin E3 ligases
- (2008) James A. Nathan et al. EXPERIMENTAL CELL RESEARCH
- 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
- (2008) K. Cadwell et al. JOURNAL OF VIROLOGY
- Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction
- (2008) Patrick Schreiner et al. NATURE
- Proteasome subunit Rpn13 is a novel ubiquitin receptor
- (2008) Koraljka Husnjak et al. NATURE
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