ArticleBiomolecules2020
FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts.
Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 61 citations in OpenAlex.
- S-Doped Carbon Dot Treatment Alters RNA Processing, Translation, and Protein Degradation Pathways in HeLa Cells.Current issues in molecular biology · 2026Article
- Covalent immobilization of Lepidium draba peroxidase on chitosan-coated magnetic nanoparticles and its application in glucose biosensing.Scientific reports · 2026Article
- Preparation of Self-Assembled Human Serum Albumin Nanoparticles Decorated with Trastuzumab as a Paclitaxel Delivery System.Micromachines · 2025Article
- Structural Instability of Human Serum Albumin during Microparticles Synthesis.ACS applied bio materials · 2025Article
- Bovine Serum Albumin-Trypsin Sponges for Enhanced Enzymatic Stability and Protein Digestion Efficiency.ACS applied bio materials · 2025Article
- Protein Corona as a Result of Interaction of Protein Molecules with Inorganic Nanoparticles.International journal of molecular sciences · 2025Review
- Infrared Spectral Patterns of Thyroglobulin Bearing Thyroiditogenic Epitopes.The protein journal · 2025Article
- Effect of a SARS-CoV-2 Protein Fragment on the Amyloidogenic Propensity of Human Islet Amyloid Polypeptide.ACS chemical neuroscience · 2024Article
- Prediction of Protein Targets in Ovarian Cancer Using a Ru-Complex and Carbon Dot Drug Delivery Therapeutic Nanosystems: A Bioinformatics and µ-FTIR Spectroscopy Approach.Pharmaceutics · 2024Article
- Toward Tunable Protein-Driven Hydrogel Lens.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Article
- Acetic Acid Enables Precise Tailoring of the Mechanical Behavior of Protein-Based Hydrogels.Nano letters · 2022Article
- Various Simulated Body Fluids Lead to Significant Differences in Collagen Tissue Engineering Scaffolds.Materials (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The effect of neutral salts on protein conformation was first analyzed by Hofmeister in 1888, however, even today this phenomenon is not completely understood. To clarify this effect, we studied changes in the secondary structure of two proteins: human serum albumin with predominantly α-helical structure and porcine pancreas β-trypsin with the typical β-structural arrangement in aqueous solutions of neutral salts (KSCN, KCl, (NH
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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.