ArticleRSC advances2022
Denaturation of proteins: electrostatic effects
Article in RSC advances, 2022. 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
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
5 citing papers in PubMed, 11 citations in OpenAlex.
- Electrochemical differentiation of native-denatured hemoglobin using a same-metal PCB-based three-electrode system.RSC advances · 2026Article
- Interaction of Lysozyme with Sulfated β-Cyclodextrin: Dissecting Salt and Hydration Contributions.Molecules (Basel, Switzerland) · 2026Article
- Measuring the Thermal Unfolding of Lysozyme: A Critical Comparison of Differential Scanning Fluorimetry and Differential Scanning Calorimetry.ChemistryOpen · 2025Article
- Driving Forces in the Formation of Biocondensates of Highly Charged Proteins: A Thermodynamic Analysis of the Binary Complex Formation.Biomolecules · 2024Article
- Correlation between Water Characteristics and Gel Strength in the Gel Formation of Golden Pompano Surimi Induced by Dense Phase Carbon Dioxide.Foods (Basel, Switzerland) · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The unfolding transition of proteins in aqueous solution containing various salts or uncharged solutes is a classical subject of biophysics. In many cases, this transition is a well-defined two-stage equilibrium process which can be described by a free energy of transition Δ
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.