ArticleInternational journal of molecular sciences2013
Thermal stability threshold for amyloid formation in light chain amyloidosis.
Article in International journal of molecular sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 28 citations in OpenAlex.
- Tracking reduction-induced molecular changes in pathological free light chains by SV-AUC.European biophysics journal : EBJ · 2025Article
- Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots.International journal of molecular sciences · 2024Article
- Role of the mechanisms for antibody repertoire diversification in monoclonal light chain deposition disorders: when a friend becomes foe.Frontiers in immunology · 2023Review
- Review
- Silver Nanoparticles as a Tool for the Study of Spontaneous Aggregation of Immunoglobulin Monoclonal Free Light Chains.International journal of molecular sciences · 2021Article
- Light chain amyloidosis induced inflammatory changes in cardiomyocytes and adipose-derived mesenchymal stromal cells.Leukemia · 2020Article
- Silver Nanoparticle-Based Assay for the Detection of Immunoglobulin Free Light Chains.Materials (Basel, Switzerland) · 2019Article
- Immunoglobulin light chain amyloid aggregation.Chemical communications (Cambridge, England) · 2018Review
- A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation.Redox biology · 2018Article
- Isolation and purification of recombinant immunoglobulin light chain variable domains from the periplasmic space of Escherichia coli.PloS one · 2018Article
- Mesenchymal stromal cells protect human cardiomyocytes from amyloid fibril damage.Cytotherapy · 2017Article
- Aggregation of Full-length Immunoglobulin Light Chains from Systemic Light Chain Amyloidosis (AL) Patients Is Remodeled by Epigallocatechin-3-gallate.The Journal of biological chemistry · 2017Article
- Differences in Protein Concentration Dependence for Nucleation and Elongation in Light Chain Amyloid Formation.Biochemistry · 2017Article
- Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains.Scientific reports · 2017Article
- Article
- Cell Damage in Light Chain Amyloidosis: FIBRIL INTERNALIZATION, TOXICITY AND CELL-MEDIATED SEEDING.The Journal of biological chemistry · 2016Article
- In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study.Scientific reports · 2016Article
- Recruitment of Light Chains by Homologous and Heterologous Fibrils Shows Distinctive Kinetic and Conformational Specificity.Biochemistry · 2016Article
- Thermodynamic and fibril formation studies of full length immunoglobulin light chain AL-09 and its germline protein using scan rate dependent thermal unfolding.Biophysical chemistry · 2015Article
- 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
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Light chain (AL) amyloidosis is a devastating disease characterized by amyloid deposits formed by immunoglobulin light chains. Current available treatments involve conventional chemotherapy and autologous stem cell transplant. We have recently concluded a phase III trial comparing these two treatments. AL amyloidosis patients who achieve hematological complete response (CR) do not necessarily achieve organ response regardless of the treatment they received. In order to investigate the possible correlation between amyloid formation kinetics and organ response, we selected AL amyloidosis patients from the trial with kidney involvement and CR after treatment. Six patients were selected and their monoclonal immunoglobulin light chains were characterized. The proteins showed differences in their stability and their kinetics of amyloid formation. A correlation was detected at pH 7.4, showing that less stable proteins are more likely to form amyloid fibrils. AL-T03 is too unstable to form amyloid fibrils at pH 7.4. This protein was found in the only patient in the study that had organ response, suggesting that partially folded species are required for amyloid formation to occur in AL amyloidosis.
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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.