ArticleAmyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis2008
Biochemical and aggregation analysis of Bence Jones proteins from different light chain diseases.
Article in Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 45 citations in OpenAlex.
- Role of the mechanisms for antibody repertoire diversification in monoclonal light chain deposition disorders: when a friend becomes foe.Frontiers in immunology · 2023Review
- Review
- Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans.Journal of visualized experiments : JoVE · 2021Article
- Understanding Mesangial Pathobiology in AL-Amyloidosis and Monoclonal Ig Light Chain Deposition Disease.Kidney international reports · 2020Review
- The CDR1 and Other Regions of Immunoglobulin Light Chains are Hot Spots for Amyloid Aggregation.Scientific reports · 2019Article
- Sustained and Prolonged Delivery of Protein Therapeutics from Two-Dimensional Nanosilicates.ACS applied materials & interfaces · 2019Article
- The FLC dimer with lambda type may false-migrate to the position of "albumin" band by urine protein electrophoresis on Sebia agarose gel-based detection system.Journal of clinical laboratory analysis · 2019Article
- Immunoglobulin light chain amyloid aggregation.Chemical communications (Cambridge, England) · 2018Review
- Structure and energetic basis of overrepresented λ light chain in systemic light chain amyloidosis patients.Biochimica et biophysica acta. Molecular basis of disease · 2018Article
- Kinetic stability and sequence/structure studies of urine-derived Bence-Jones proteins from multiple myeloma and light chain amyloidosis patients.Biophysical chemistry · 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
- The Kinetic Stability of a Full-Length Antibody Light Chain Dimer Determines whether Endoproteolysis Can Release Amyloidogenic Variable Domains.Journal of molecular biology · 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
- Site-directed mutagenesis reveals regions implicated in the stability and fiber formation of human λ3r light chains.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
- Systemic amyloidoses.Annual review of biochemistry · 2013Review
- Tyrosine residues mediate fibril formation in a dynamic light chain dimer interface.The Journal of biological chemistry · 2012Article
- Differences in immunoglobulin light chain species found in urinary exosomes in light chain amyloidosis (Al).PloS one · 2012Article
- Amyloid formation in light chain amyloidosis.Current topics in medicinal chemistry · 2012Review
- In vitro aggregation behavior of a non-amyloidogenic λ light chain dimer deriving from U266 multiple myeloma cells.PloS one · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Deposition of immunoglobulin light chains is a result of clonal proliferation of monoclonal plasma cells that secrete free immunoglobulin light chains, also called Bence Jones proteins (BJP). These BJP are present in circulation in large amounts and excreted in urine in various light chain diseases such as light chain amyloidosis (AL), light chain deposition disease (LCDD) and multiple myeloma (MM). BJP from patients with AL, LCDD and MM were purified from their urine and studies were performed to determine their secondary structure, thermodynamic stability and aggregate formation kinetics. Our results show that LCDD and MM proteins have the lowest free energy of folding while all proteins show similar melting temperatures. Incubation of the BJP at their melting temperature produced morphologically different aggregates: amyloid fibrils from the AL proteins, amorphous aggregates from the LCDD proteins and large spherical species from the MM proteins. The aggregates formed under in vitro conditions suggested that the various proteins derived from patients with different light chain diseases might follow different aggregation pathways.
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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.