ArticleScientific reports2013
Role of mutations in the cellular internalization of amyloidogenic light chains into cardiomyocytes.
Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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
23 citing papers in PubMed, 40 citations in OpenAlex.
- Immunoglobulin Kappa Light Chain Produced by Cardiomyocytes and Participates in Maintaining Intercalated Disc Integrity.MedComm · 2026Article
- In vitro and in vivo disease models of cardiac amyloidosis: progress, pitfalls, and potential.Cardiovascular research · 2025Review
- Serum and Tissue Light-Chains as Disease Biomarkers in AL Amyloidosis.International journal of molecular sciences · 2025Review
- 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
- Understanding AL amyloidosis with a little help fromFrontiers in immunology · 2022Review
- Future Perspectives.Hematology/oncology clinics of North America · 2020Review
- Understanding Mesangial Pathobiology in AL-Amyloidosis and Monoclonal Ig Light Chain Deposition Disease.Kidney international reports · 2020Review
- Light chain amyloidosis induced inflammatory changes in cardiomyocytes and adipose-derived mesenchymal stromal cells.Leukemia · 2020Article
- Macrophage-Mediated Phagocytosis and Dissolution of Amyloid-Like Fibrils in Mice, Monitored by Optical Imaging.The American journal of pathology · 2019Article
- Immunoglobulin light chain amyloid aggregation.Chemical communications (Cambridge, England) · 2018Review
- 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
- Solid-state NMR chemical shift assignments for AL-09 VBiomolecular NMR assignments · 2017Article
- Immunoglobulin Light Chains Form an Extensive and Highly Ordered Fibril Involving the N- and C-Termini.ACS omega · 2017Article
- Differences in Protein Concentration Dependence for Nucleation and Elongation in Light Chain Amyloid Formation.Biochemistry · 2017Article
- Cell Damage in Light Chain Amyloidosis: FIBRIL INTERNALIZATION, TOXICITY AND CELL-MEDIATED SEEDING.The Journal of biological chemistry · 2016Article
- Viewing Extrinsic Proteotoxic Stress Through the Lens of Amyloid Cardiomyopathy.Physiology (Bethesda, Md.) · 2016Review
- Monosialoganglioside-Containing Nanoliposomes Restore Endothelial Function Impaired by AL Amyloidosis Light Chain Proteins.Journal of the American Heart Association · 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
- Pathophysiology and treatment of cardiac amyloidosis.Nature reviews. Cardiology · 2015Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Light chain (AL) amyloidosis is characterized by the misfolding of immunoglobulin light chains, accumulating as amyloid fibrils in vital organs. Multiple reports have indicated that amyloidogenic light chains internalize into a variety of cell types, but these studies used urine-derived proteins without indicating any protein sequence information. As a result, the role of somatic mutations in amyloidogenic protein internalization has not been yet studied. We characterized the internalization of AL-09, an AL amyloidosis protein into mouse cardiomyocytes. We also characterized the internalization of the germline protein κI O18/O8, devoid of somatic mutations, and three AL-09 restorative mutations (I34N, Q42K, and H87Y) previously characterized for their role in protein structure, stability, and amyloid formation kinetics. All proteins shared a common internalization pathway into lysosomal compartments. The proteins caused different degrees of lysosomal expansion. Oregon green (OG) labeled AL-09 showed the most rapid internalization, while OG-Q42K presented the slowest rate of internalization.
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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.