ArticleThe Journal of biological chemistry2012
Tyrosine residues mediate fibril formation in a dynamic light chain dimer interface.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 26 citations in OpenAlex.
- Targeted biologics for TNBC: Advances in nanobodies, antibodies, peptides, and aptamers.Molecular therapy. Oncology · 2026Review
- Substituent-Based Modulation of Self-Assembly and Immunogenicity of Amphipathic Peptides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Self-Assembly of a Novel Pentapeptide into Hydrogelated Dendritic Architecture: Synthesis, Properties, Molecular Docking and Prospective Applications.Gels (Basel, Switzerland) · 2024Article
- Molecular Mechanism of Pathogenesis and Treatment Strategies for AL Amyloidosis.International journal of molecular sciences · 2022Review
- 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
- Mechanistic Insights into the Early Events in the Aggregation of Immunoglobulin Light Chains.Biochemistry · 2019Article
- Assays for Light Chain Amyloidosis Formation and Cytotoxicity.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Mesenchymal stromal cells protect human cardiomyocytes from amyloid fibril damage.Cytotherapy · 2017Article
- Concurrent structural and biophysical traits link with immunoglobulin light chains amyloid propensity.Scientific reports · 2017Article
- Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study.Scientific reports · 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
- Cell Damage in Light Chain Amyloidosis: FIBRIL INTERNALIZATION, TOXICITY AND CELL-MEDIATED SEEDING.The Journal of biological chemistry · 2016Article
- 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
- Intrinsically disordered and aggregation prone regions underlie β-aggregation in S100 proteins.PloS one · 2013Article
- Molecular mechanism of amyloidogenic mutations in hypervariable regions of antibody light chains.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Light chain amyloidosis is an incurable protein misfolding disease where monoclonal immunoglobulin light chains misfold and deposit as amyloid fibrils, causing organ failure and death. Previously, we determined that amyloidogenic light chains AL-09 and AL-103 do not form fibrils at pH 10 (tyrosine pK(a)). There are three tyrosine residues (32, 91, and 96) clustered in the dimer interface, interacting differently in the two light chain proteins due to their two different dimer conformations. These tyrosines may be ionized at pH 10, causing repulsion and inhibiting fibril formation. Here, we characterize single and double Tyr-to-Phe mutations in AL-09 and AL-103. All AL-09 Tyr-to-Phe mutants form fibrils at pH 10, whereas none of the AL-103 mutants form fibrils at pH 10. NMR studies suggest that although both AL-09 and AL-103 present conformational heterogeneity, only AL-09 favors dimer conformations where tyrosine residues mediate crucial interactions for amyloid formation.
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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.