Function and regulation of cullin–RING ubiquitin ligases

By M. Petroski, R. Deshaies. Nature reviews. Molecular cell biology, 2005

2,187 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/b947d751cb77a61f8bcc475e6c906c51ca0d2376

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. Masayuki Yamamoto
2. Johannes C. Walter
3. J. Hayes
4. A. Weissman
5. L. An
6. H. Feng
7. C. Joazeiro
8. R. Deshaies

In Epidemiology

1. J. Harper
2. J. Hayes
3. A. Weissman
4. C. Joazeiro
5. R. Deshaies

In Molecular Biology

1. Masayuki Yamamoto
2. J. Hayes
3. D. Glass
4. K. I. Tong
5. A. Kong
6. Wenge Li
7. Michael T. McMahon
8. Zhaoyu Jin

Citations in the corpus

• A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1. (2006, background): “Together, these CRLs may assemble more than 200 distinct E3s.”
• HIV-1 accessory proteins--ensuring viral survival in a hostile environment. (2008, background): “Proteasome-Mediated Degradation: A Frequent Viral Target A recurring theme throughout this review is the use of protein degradation, and in particular cullin-RING finger ubiquitin ligases (Petroski and Deshaies, 2005), to avert the action of host proteins that interfere with HIV-1 replication.”
• Molecular Mechanisms of Nrf2-Mediated Antioxidant Response (2009, background): “To date, 7 Cullin proteins have been cloned [60].”
• The E3 Ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle. (2007, background): “Both MuRF1 and MAFbx encode E3 ubiquitin ligases, a large family of proteins that mediate the ubiquitination of distinct protein substrates (Petroski and Deshaies, 2005; Winston et al., 1999; Yamao, 1999).”
• The General Transcription Machinery and General Cofactors (2006, background): “Undoubtedly, the counteracting activity between Ctk1-FCP1 and TFIIH-Ssu72 on CTD phosphorylation must play an important role in initiation, elongation, termination, and transcription-coupled mRNA processing.”
• Genome-Wide and Functional Annotation of Human E3 Ubiquitin Ligases Identifies MULAN, a Mitochondrial E3 that Regulates the Organelle's Dynamics and Signaling (2008, background): “In particular, the RNF proteins Rbx1/2 add great diversity to E3s by forming SCF and SCF-like complexes with alternative substrate-recognition subunits, often characterized by the additional presence of an F box, SOCS box, DDB1 or BTB domain [2,3].”
• HECT and RING finger families of E3 ubiquitin ligases at a glance (2012, background): “Multi-subunit RING domains are exemplified by the cullin RING ligase (CRL) superfamily (Hua and Vierstra, 2011; Petroski and Deshaies, 2005), which includes the SCF complex, consisting of S-phase kinaseassociated protein 1 (SKP1), cullin and F-box protein, and the more elaborate anaphasepromoting…”
• Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease (2015, neutral): “The substrate receptor β-TrCP is an F-box-containing protein, which uses its C-terminal WD40 protein–protein interaction domain to bind substrates and its F-box motif to bind to the SCF E3 ubiquitin ligase complex [289].”