The lore of the RINGs: substrate recognition and catalysis by ubiquitin ligases.

By Peter Jackson, A. G. Eldridge, E. Freed, Laura Furstenthal, Jerry Y. Hsu, Brett K. Kaiser, Julie D. R. Reimann. Trends in Cell Biology, 2000

686 citations recorded by the source corpus.

Subfields: Epidemiology, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/52f18cee0d3fdc99f0446cf96d2e5f79285c55ec

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In Epidemiology

1. A. Goldberg
2. S. Lecker
3. W. Mitch
4. Aaron Ciechanover
5. M. Glickman

In Molecular Biology

1. A. Goldberg
2. S. Lecker
3. Aaron Ciechanover
4. W. Mitch
5. Graciana Diez-Roux
6. Y. Nakatani
7. M. Glickman
8. J. Sawada

In Oncology

1. A. Goldberg
2. Aaron Ciechanover
3. M. Glickman

Citations in the corpus

• MAX1 and MAX2 control shoot lateral branching in Arabidopsis. (2002, background): “Members of this protein family function as subunits of the multiprotein SCF-type E3 ligases that polyubiquitinate proteins and thus target them for degradation by the 26S proteasome (Patton et al., 1998; Jackson et al., 2000).”
• Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. (2006, background): “(homologous to E6-AP carboxy-terminus) domains or RING fingers (22).”
• Control of Mammalian Circadian Rhythm by CKIε-Regulated Proteasome-Mediated PER2 Degradation (2005, background): “In order for a protein destined for degradation by the 26S proteasome to be polyubiquitinated, it must first be recognized by an E3 ubiquitin ligase (18).”
• The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. (2003, methodology): “…similar complexes (Figureis uncertain, we measured ubiquitin-polymerizing activity using Uba1 E1 and UbcH5 E2 enzymes, which func- 4B), indicating that the mutation in the CSN5 metallopro- tease motif does not disrupt the CSN complex.tion with other cullin family members (Jackson et al., 2000).”
• TRIM/RBCC, a novel class of ‘single protein RING finger’ E3 ubiquitin ligases (2005, background): “The E3 ubiquitin ligases are divided into three distinct classes based on the catalytic domain mediating ubiquitin transfer: HECT (Homologous to E6AP Carboxy Terminus)-, U-box- and RING finger-containing E3s.”
• The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. (2002, background): “Most E2s interact with several E3s (Fig.”