ArticleProtein science : a publication of the Protein Society2014
Solution structure of lysine-free (K0) ubiquitin.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- The Molecular Toolbox for Linkage Type-Specific Analysis of Ubiquitin Signaling.Chembiochem : a European journal of chemical biology · 2025Review
- Electrostatic and steric effects underlie acetylation-induced changes in ubiquitin structure and function.Nature communications · 2022Article
- Ubiquitination status does not affect Vps34 degradation.Genes & diseases · 2020Article
- A negative feedback mechanism links UBC gene expression to ubiquitin levels by affecting RNA splicing rather than transcription.Scientific reports · 2019Article
- Linkage via K27 Bestows Ubiquitin Chains with Unique Properties among Polyubiquitins.Structure (London, England : 1993) · 2016Article
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Authors and funding
3 authors.
Funding
Abstract
Lysine-free ubiquitin (K0-Ub) is commonly used to study the ubiquitin-signaling pathway, where it is assumed to have the same structure and function as wild-type ubiquitin (wt-Ub). However, the K0-Ub (15) N heteronuclear single quantum correlation NMR spectrum differs significantly from wt-Ub and the melting temperature is depressed by 19°C, raising the question of the structural integrity and equivalence to wt-Ub. The three-dimensional structure of K0-Ub was determined by solution NMR, using chemical shift and residual dipolar coupling data. K0-Ub adopts the same backbone structure as wt-Ub, and all significant chemical shifts can be related to interactions impacted by the K to R mutations.
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Registered trials
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