ReviewBiophysical reviews2013
Application and use of differential scanning calorimetry in studies of thermal fluctuation associated with amyloid fibril formation.
Review in Biophysical reviews, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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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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
6 citing papers in PubMed, 20 citations in OpenAlex.
- Thermally Stressed Solid-State Stability of Semaglutide: Understanding the Influence of Temperature on Protein Content, Secondary Structure, Phase Transition, and Chemical Degradation.Pharmaceutical research · 2026Article
- Formation and Physicochemical Properties of Freeze-Dried Amyloid-Like Fibrils From Pinto Bean Protein: Amyloid-Like Fibrils From Pinto Bean Protein.International journal of analytical chemistry · 2024Article
- Peptide Inhibitors of Insulin Fibrillation: Current and Future Challenges.International journal of molecular sciences · 2023Review
- Modification of the structural stability of human serum albumin in rheumatoid arthritis.PloS one · 2023Article
- Measurement of amyloid formation by turbidity assay-seeing through the cloud.Biophysical reviews · 2016Review
- Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aggregation of proteins into amyloid fibrils is a topic that has attracted great interest because the process is associated with the pathology of numerous human diseases. Despite considerable progress in the elucidation of the structure of amyloid fibrils and the kinetic mechanism of their formation, knowledge on the thermodynamic aspects underlying the formation and stability of amyloid fibrils is limited. In this review, we summarize recent calorimetric studies of amyloid fibril formation, with the goal of obtaining a better understanding of the causal factors that thermally induce proteins to aggregate into amyloid fibrils. Calorimetric data show that differential scanning calorimetry is a useful technique to study the causative factors that thermally trigger the conversion to the amyloid structure and highlight the physics related to the thermal fluctuation of proteins during this conversion.
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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.