ArticleBiophysical chemistry2008
Salts enhance both protein stability and amyloid formation of an immunoglobulin light chain.
Article in Biophysical chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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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Who cites it
31 citing papers in PubMed, 55 citations in OpenAlex.
- Quantitative Analysis of Amyloid Fibril Nucleation by Linking Folding and Nucleation Pathways Using a Robust Ultrasonic Assay.ACS omega · 2026Article
- An Optimized Protocol for High-Quality AFM Imaging of Amyloid Fibrils.Bio-protocol · 2025Article
- Biophysical characterization of human-cell-expressed, full-length κI O18/O8, AL-09, λ6a, and Wil immunoglobulin light chains.Biochimica et biophysica acta. Proteins and proteomics · 2024Article
- Early events in light chain aggregation at physiological pH reveal new insights on assembly, stability, and aggregate dissociation.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2021Article
- Understanding Mesangial Pathobiology in AL-Amyloidosis and Monoclonal Ig Light Chain Deposition Disease.Kidney international reports · 2020Review
- Mechanistic Insights into the Early Events in the Aggregation of Immunoglobulin Light Chains.Biochemistry · 2019Article
- Stabilization of amyloidogenic immunoglobulin light chains by small molecules.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Assays for Light Chain Amyloidosis Formation and Cytotoxicity.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Immunoglobulin light chain amyloid aggregation.Chemical communications (Cambridge, England) · 2018Review
- Differences in Protein Concentration Dependence for Nucleation and Elongation in Light Chain Amyloid Formation.Biochemistry · 2017Article
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- Recruitment of Light Chains by Homologous and Heterologous Fibrils Shows Distinctive Kinetic and Conformational Specificity.Biochemistry · 2016Article
- Mutations can cause light chains to be too stable or too unstable to form amyloid fibrils.Protein science : a publication of the Protein Society · 2015Article
- Differential effects on light chain amyloid formation depend on mutations and type of glycosaminoglycans.The Journal of biological chemistry · 2015Article
- Kinetic control in protein folding for light chain amyloidosis and the differential effects of somatic mutations.Journal of molecular biology · 2014Article
- Thermal stability threshold for amyloid formation in light chain amyloidosis.International journal of molecular sciences · 2013Article
- Thermal stability of lysozyme as a function of ion concentration: a reappraisal of the relationship between the Hofmeister series and protein stability.Protein science : a publication of the Protein Society · 2013Article
- Microcin amyloid fibrils A are reservoir of toxic oligomeric species.The Journal of biological chemistry · 2012Article
- In vitro aggregation behavior of a non-amyloidogenic λ light chain dimer deriving from U266 multiple myeloma cells.PloS one · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Amyloid fibrils are associated with sulfated glycosaminoglycans in the extracellular matrix. The presence of sulfated glycosaminoglycans is known to promote amyloid formation in vitro and in vivo, with the sulfate groups playing a role in this process. In order to understand the role that sulfate plays in amyloid formation, we have studied the effect of salts from the Hofmeister series on the protein structure, stability and amyloid formation of an amyloidogenic light chain protein, AL-12. We have been able to show for the first time a direct correlation between protein stability and amyloid formation enhancement by salts from the Hofmeister series, where SO(4)(2-) conferred the most protein stability and enhancement of amyloid formation. Our study emphasizes the importance of the effect of ions in the protein bound water properties and downplays the role of specific interactions between the protein and ions.
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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.