ReviewBiophysical reviews2018
Salt-induced formations of partially folded intermediates and amyloid fibrils suggests a common underlying mechanism.
Review in Biophysical reviews, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Tied to Work: Topologically Knotted SPOUT Methyltransferases and UCH Deubiquitinases in Cellular Biochemistry.Journal of cellular biochemistry · 2026Review
- Dental plaque biofilm transforms host-derived βBiofilm · 2025Article
- Investigation of the Effect of NaCl Concentrations on the Formation of Amyloid Fibrils During the Cooking of Wheat Noodles.Foods (Basel, Switzerland) · 2025Article
- Unraveling the Effects of Hexametaphosphate: Insights into Trypsin Aggregation and Structural Reversal.ACS omega · 2024Article
- Investigating the Effects of NaCl on the Formation of AFs from Gluten in Cooked Wheat Noodles.International journal of molecular sciences · 2023Article
- Amyloid-Based Albumin Hydrogels.Advanced healthcare materials · 2023Article
- Mechanisms of polyphosphate-induced amyloid fibril formation triggered by breakdown of supersaturation.Biophysics and physicobiology · 2023Article
- Multivariate effects of pH, salt, and ZnCommunications chemistry · 2022Article
- Insights into Cerebral Amyloid Angiopathy Type 1 and Type 2 from Comparisons of the Fibrillar Assembly and Stability of the Aβ40-Iowa and Aβ40-Dutch Peptides.Biochemistry · 2022Article
- Nicking and fragmentation are responsible for α-lactalbumin amyloid fibril formation at acidic pH and elevated temperature.Protein science : a publication of the Protein Society · 2021Article
- Polyphenol-solubility alters amyloid fibril formation of α-synuclein.Protein science : a publication of the Protein Society · 2021Article
- The protein-surfactant stoichiometry governs the conformational switching and amyloid nucleation kinetics of tau K18.European biophysics journal : EBJ · 2020Article
- Exploration of Insulin Amyloid Polymorphism Using Raman Spectroscopy and Imaging.Biophysical journal · 2020Article
- FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts.Biomolecules · 2020Article
- Using protein engineering to understand and modulate aggregation.Current opinion in structural biology · 2020Review
- Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanism.Current research in structural biology · 2020Article
- Possible mechanisms of polyphosphate-induced amyloid fibril formation of βProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Foreword to 'Multiscale structural biology: biophysical principles and mechanisms underlying the action of bio-nanomachines', a special issue in Honour of Fumio Arisaka's 70th birthday.Biophysical reviews · 2018Article
- Cu/Zn-superoxide dismutase forms fibrillar hydrogels in a pH-dependent manner via a water-rich extended intermediate state.PloS one · 2018Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fibrils are misfolded forms of proteins and are involved in various diseases. They have been studied extensively with the aim to obtain a comprehensive understanding of protein folding and misfolding and to use this knowledge to develop therapeutic strategies against the associated diseases. Salt conditions are important factors determining the formation and stability of amyloid fibrils. In the 1990s, salt effects were studied extensively to understand the conformational stability of acid-denatured proteins, and the results of these studies revealed the role of electrostatic repulsion in forming the compact intermediate states. In this review, we compare the effects of salts on the compact intermediate states with those on the formation of amyloid fibrils under acidic conditions. The results argue that both protein folding and misfolding are driven by the same forces, although the resultant conformations are distinct because they are monomeric and multimeric reactions, respectively.
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