ArticleBiomacromolecules2022
Macromolecular and Solution Properties of the Recombinant Fusion Protein HUG.
Article in Biomacromolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Predominance of Biliverdin over Bilirubin in Human Seminal Plasma.Biomolecules · 2026Article
- The HELP-UnaG Fusion Protein as a Bilirubin Biosensor: From Theory to Mature Technological Development.Molecules (Basel, Switzerland) · 2025Review
- Standardized lab-scale production of the recombinant fusion protein HUG for the nanoscale analysis of bilirubin.MethodsX · 2024Article
- Combined fluorometric analysis of biliverdin and bilirubin by the recombinant protein HUG.MethodsX · 2024Article
- Genetic Functionalization of Protein-Based Biomaterials via Protein Fusions.Biomacromolecules · 2024Review
- A Versatile Elastin-Like Carrier for Bioactive Antimicrobial Peptide Production and Delivery.Macromolecular bioscience · 2024Article
- Nanoscale Bilirubin Analysis in Translational Research and Precision Medicine by the Recombinant Protein HUG.International journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The recombinant fusion protein HELP-UnaG (HUG) is a bifunctional product that exhibits human elastin-like polypeptide (HELP)-specific thermal behavior, defined as a reverse phase transition, and UnaG-specific bilirubin-dependent fluorescence emission. HUG provides an interesting model to understand how its two domains influence each other's properties. Turbidimetric, calorimetric, and light scattering measurements were used to determine different parameters for the reverse temperature transition and coacervation behavior. This shows that the UnaG domain has a measurable but limited effect on the thermal properties of HELP. Although the HELP domain decreased the affinity of UnaG for bilirubin, HUG retained the property of displacing bilirubin from bovine serum albumin and thus remains one of the strongest bilirubin-binding proteins known to date. These data demonstrate that HELP can be used to create new bifunctional fusion products that pave the way for expanded technological applications.
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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.