ArticleEuropean biophysics journal : EBJ2017
Maleimido-proxyl as an EPR spin label for the evaluation of conformational changes of albumin.
Article in European biophysics journal : EBJ, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Mapping of TEMPO‑, PROXYL‑, and Phosphoryl-Functionalized Spin Probes into Biointerface Fatty Acid Recognition Sites of BSA.ACS omega · 2026Article
- Quantifying Ligand-to-Protein Distances in Complex Environments Using IntermolecularChembiochem : a European journal of chemical biology · 2026Article
- Article
- Human Serum Albumin Loaded with Fatty Acids Reveals Complex Protein-Ligand Thermodynamics and Boleadora-Type Solution Dynamics Leading to Gelation.The journal of physical chemistry. B · 2025Article
- Stable Nitroxide as Diagnostic Tools for Monitoring of Oxidative Stress and Hypoalbuminemia in the Context of COVID-19.International journal of molecular sciences · 2024Review
- Molecular Serum Albumin Unmask Nanobio Properties of Molecular Graphenes in Shungite Carbon Nanoparticles.International journal of molecular sciences · 2024Article
- Spin-Label Electron Paramagnetic Resonance Spectroscopy Reveals Effects of Wastewater Filter Membrane Coated with Titanium Dioxide Nanoparticles on Bovine Serum Albumin.Molecules (Basel, Switzerland) · 2023Article
- Direct Application of 3-Maleimido-PROXYL for Proving Hypoalbuminemia in Cases of SARS-CoV-2 Infection: The Potential Diagnostic Method of Determining Albumin Instability and Oxidized Protein Level in Severe COVID-19.International journal of molecular sciences · 2023Article
- Protein-Caged Nanoparticles: A Promising Nanomedicine Against Cancer.Chonnam medical journal · 2023Review
- Site-Directed Spin Labeling EPR Spectroscopy for Determination of Albumin Structural Damage and Hypoalbuminemia in Critical COVID-19.Antioxidants (Basel, Switzerland) · 2022Article
- Paramagnetic NMR in drug discovery.Journal of biomolecular NMR · 2020Review
- Protein modification by thiolactone homocysteine chemistry: a multifunctionalized human serum albumin theranostic.RSC medicinal chemistry · 2020Article
- Redox properties and human serum albumin binding of nitro-oleic acid.Redox biology · 2019Article
- Regional Biophysics Conference - RBC2016.European biophysics journal : EBJ · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Albumin is the most abundant plasma protein and as such has been the subject of many studies using a variety of techniques. One of them, capable of monitoring the conformational changes and the binding capacity of proteins, is electron paramagnetic resonance spectroscopy (EPR) spin labeling. To date, albumin has been investigated using a number of different spin labels, mostly spin-labeled fatty acids (SLFAs). However, albumin can bind up to seven equivalents of fatty acids, making it difficult to determine which parts of the molecule undergo conformational changes. To obtain information from a specific site on a protein, spin labels that bind to free cysteine residues may be used. In this work, the applicability of such a label, 3-maleimido proxyl (5-MSL), was evaluated for monitoring conformational changes of bovine serum albumin (BSA) at different temperatures and pH values. Also, the effect of ethanol, reactive oxygen species (hydrogen peroxide and superoxide radical), and the binding of ligands specific for albumin, namely fatty acids, and several drugs were evaluated. The results indicate that the labeling of albumin at its free cysteine residue (Cys-34) using 5-MSL may successfully be used for the detection of conformational changes, even in the case of the subtle alterations induced by ligand binding.
Indexed as
Identifiers
What OpenQuestion holds
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.