ArticleBiophysical chemistry2015
Thermodynamic and fibril formation studies of full length immunoglobulin light chain AL-09 and its germline protein using scan rate dependent thermal unfolding.
Article in Biophysical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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Who cites it
31 citing papers in PubMed.
- Small Molecule Stabilization of Diverse Amyloidogenic Immunoglobulin Light Chains Revealed by Hydrogen-Deuterium Exchange Mass Spectrometry.Journal of molecular biology · 2026Article
- Multiple Myeloma Concomitant with AL Amyloidosis: Histopathological Aspects of the Common Plasma Cell Spectrum.International journal of molecular sciences · 2026Article
- Small molecule stabilization of diverse amyloidogenic immunoglobulin light chains revealed by hydrogen-deuterium exchange mass spectrometry.bioRxiv : the preprint server for biology · 2026Article
- Clone-specific residue changes at multiple positions are associated with amyloid formation by antibody light chains.Frontiers in immunology · 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
- Widespread amyloidogenicity potential of multiple myeloma patient-derived immunoglobulin light chains.BMC biology · 2023Article
- An N-glycosylation hotspot in immunoglobulin κ light chains is associated with AL amyloidosis.Leukemia · 2022Article
- Cu(II) Binding Increases the Soluble Toxicity of Amyloidogenic Light Chains.International journal of molecular sciences · 2022Article
- Article
- Dissection of the amyloid formation pathway in AL amyloidosis.Nature communications · 2021Article
- Barriers to Small Molecule Drug Discovery for Systemic Amyloidosis.Molecules (Basel, Switzerland) · 2021Article
- Discovery of Potent Coumarin-Based Kinetic Stabilizers of Amyloidogenic Immunoglobulin Light Chains Using Structure-Based Design.Journal of medicinal chemistry · 2021Article
- A kinetic coupling between protein unfolding and aggregation controls time-dependent solubility of the human myeloma antibody light chain.Protein science : a publication of the Protein Society · 2020Article
- Understanding Mesangial Pathobiology in AL-Amyloidosis and Monoclonal Ig Light Chain Deposition Disease.Kidney international reports · 2020Review
- Structural basis for the stabilization of amyloidogenic immunoglobulin light chains by hydantoins.Bioorganic & medicinal chemistry letters · 2020Article
- Fatal amyloid formation in a patient's antibody light chain is caused by a single point mutation.eLife · 2020Article
- Article
- The Role of Protein Thermodynamics and Primary Structure in Fibrillogenesis of Variable Domains from Immunoglobulin Light Chains.Journal of the American Chemical Society · 2019Article
- Stabilization of amyloidogenic immunoglobulin light chains by small molecules.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Identification of two principal amyloid-driving segments in variable domains of Ig light chains in systemic light-chain amyloidosis.The Journal of biological chemistry · 2018Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Light chain (AL) amyloidosis is a fatal disease where monoclonal immunoglobulin light chains deposit as insoluble amyloid fibrils. For many years it has been considered that AL amyloid deposits are formed primarily by the variable domain, while its constant domain has been considered not to be amyloidogenic. However recent studies identify full length (FL) light chains as part of the amyloid deposits. In this report, we compare the stabilities and amyloidogenic properties of two light chains, an amyloid-associated protein AL-09 FL, and its germline protein κ I O18/O8 FL (IGKV 1-33). We demonstrate that the thermal unfolding for both proteins is irreversible and scan rate dependent, with similar stability parameters compared to their VL counterparts. In addition, the constant domain seems to modulate their amyloidogenic properties and affect the morphology of the amyloid fibrils. These results allow us to understand the role of the kappa constant domain in AL amyloidosis.
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