ArticleFEBS letters2017
Identification of primary and secondary UBA footprints on the surface of ubiquitin in cell-mimicking crowded solution.
Article in FEBS letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- Biomolecular phase separation through the lens of sodium-23 NMR.Protein science : a publication of the Protein Society · 2021Article
- Semisynthetic Modification of Tau Protein with Di-Ubiquitin Chains for Aggregation Studies.International journal of molecular sciences · 2020Article
- Survival analysis of genome-wide profiles coupled with Connectivity Map database mining to identify potential therapeutic targets for cholangiocarcinoma.Oncology reports · 2018Article
- Protein shape modulates crowding effects.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Crowding in Cellular Environments at an Atomistic Level from Computer Simulations.The journal of physical chemistry. B · 2017Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Despite significant advancements in our understanding of ubiquitin-mediated signaling, the influence of the intracellular environment on the formation of transient ubiquitin-partner complexes remains poorly explored. In our work, we introduce macromolecular crowding as a first level of complexity toward the imitation of a cellular environment in the study of such interactions. Using NMR spectroscopy, we find that the stereospecific complex of ubiquitin and the ubiquitin-associated domain (UBA) is minimally perturbed by the crowding agent Ficoll. However, in addition to the primary canonical recognition patch on ubiquitin, secondary patches are identified, indicating that in cell-mimicking crowded solution, UBA contacts ubiquitin at multiple sites.
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Registered trials
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