ArticleFEBS open bio2015
Ubiquitin is a versatile scaffold protein for the generation of molecules with de novo binding and advantageous drug-like properties.
Article in FEBS open bio, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- An edge β-strand mutation turns ubiquitin into a pore-forming amyloid.Protein science : a publication of the Protein Society · 2026Article
- Clinical value of free ubiquitin in the identification of diabetic nephropathy in patients with type 2 diabetes mellitus and preliminary exploration of its protective effect.BMC nephrology · 2025Article
- Efficient Design of AffilinInternational journal of molecular sciences · 2025Article
- Almost 50 Years of Monomeric Extracellular Ubiquitin (eUb).Pharmaceuticals (Basel, Switzerland) · 2024Review
- Electrochemical sensing of blood proteins for mild traumatic brain injury (mTBI) diagnostics and prognostics: towards a point-of-care application.RSC advances · 2021Review
- Extracellular ubiquitin inhibits the apoptosis of hepatoma cells via the involvement of macrophages.Translational cancer research · 2020Article
- Sequencing Analysis and Identification of the Primary Peptide Component of the Dialyzable Leukocyte Extract "Transferon Oral": The Starting Point to Understand Its Mechanism of Action.Frontiers in pharmacology · 2020Article
- Identification and Characterization of Mutations in Ubiquitin Required for Non-covalent Dimer Formation.Structure (London, England : 1993) · 2019Article
- Emerging drug development technologies targeting ubiquitination for cancer therapeutics.Pharmacology & therapeutics · 2019Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the search for effective therapeutic strategies, protein-based biologicals are under intense development. While monoclonal antibodies represent the majority of these drugs, other innovative approaches are exploring the use of scaffold proteins for the creation of binding molecules with tailor-made properties. Ubiquitin is especially suited for this strategy due to several key characteristics. Ubiquitin is a natural serum protein, 100% conserved across the mammalian class and possesses high thermal, structural and proteolytic stability. Because of its small size and lack of posttranslational modifications, it can be easily produced in Escherichia coli. In this work we provide evidence that ubiquitin is safe as tested experimentally in vivo. In contrast to previously published results, we show that, in our hands, ubiquitin does not act as a functional ligand of the chemokine receptor CXCR4. Cellular assays based on different signaling pathways of the receptor were conducted with the natural agonist SDF-1 as a benchmark. In none of the assays could a response to ubiquitin treatment be elicited. Furthermore, intravenous application to mice at high concentrations did not induce any detectable effect on cytokine levels or hematological parameters.
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Registered trials
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.