ArticleProtein science : a publication of the Protein Society2021
Quantitative analyses for effects of neddylation on CRL2
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Neddylation relieves cytoskeletal tension to permit primary cilia formation during mouse decidualization.Cell communication and signaling : CCS · 2026Article
- E3 ubiquitin ligases in signaling, disease, and therapeutics.Trends in biochemical sciences · 2025Review
- MLN4924 Suppresses Acute Myeloid Leukemia Progression by LINC01128-Driven Epigenetic Reactivation of TRIM58.Drug design, development and therapy · 2025Article
- Mechanism of degrader-targeted protein ubiquitinability.Science advances · 2024Article
- CAND1 inhibits Cullin-2-RING ubiquitin ligases for enhanced substrate specificity.Nature structural & molecular biology · 2024Article
- Review: A silent concert in developing plants: Dynamic assembly of cullin-RING ubiquitin ligases.Plant science : an international journal of experimental plant biology · 2023Review
- E3 ligase autoinhibition by C-degron mimicry maintains C-degron substrate fidelity.Molecular cell · 2023Article
- A review on cullin neddylation and strategies to identify its inhibitors for cancer therapy.3 Biotech · 2022Article
- Roles of Cullin-RING Ubiquitin Ligases in Cardiovascular Diseases.Biomolecules · 2022Review
- Determining the Effects of Neddylation on Cullin-RING Ligase-Dependent Protein Ubiquitination.Current protocols · 2022Article
- Potassium Effects on NCC Are Attenuated during Inhibition of Cullin E3-Ubiquitin Ligases.Cells · 2021Article
- Quantitative analyses for effects of neddylation on CRL2Protein science : a publication of the Protein Society · 2021Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Through catalyzing the ubiquitination of key regulatory proteins, cullin-RING ubiquitin ligases (CRLs) play essential biological roles and their activities are controlled by multiple mechanisms including neddylation, the conjugation of NEDD8 to cullins. Upon neddylation, a CRL, such as the CUL1-based CRL1, undergoes conformational changes that accelerate substrate ubiquitination. Given the structural diversity across subfamilies of CRLs and their substrates, to what extent neddylation modulates the activity of individual CRLs remains to be evaluated. Here, through reconstituting the CRL2 ubiquitination reaction in vitro, we showed that neddylation promotes CRL2
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.