ArticleThe Journal of biological chemistry2014
Formation of amyloid fibers by monomeric light chain variable domains.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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Who cites it
28 citing papers in PubMed, 56 citations in OpenAlex.
- Small Molecule Stabilization of Diverse Amyloidogenic Immunoglobulin Light Chains Revealed by Hydrogen-Deuterium Exchange Mass Spectrometry.Journal of molecular biology · 2026Article
- Cryo-EM structures of light chain fibrils from abdominal fat biopsies of multiple myeloma patients.Nature communications · 2026Article
- Biopsy-resolved cryo-EM structures of amyloid fibrils provide molecular insights into AL amyloidosis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Small molecule stabilization of diverse amyloidogenic immunoglobulin light chains revealed by hydrogen-deuterium exchange mass spectrometry.bioRxiv : the preprint server for biology · 2026Article
- SAAINT-DB: a comprehensive structural antibody database for antibody modeling and design.Acta pharmacologica Sinica · 2025Article
- In vitro and in vivo disease models of cardiac amyloidosis: progress, pitfalls, and potential.Cardiovascular research · 2025Review
- Structural, Biophysical, and Computational Studies of a Murine Light Chain Dimer.Molecules (Basel, Switzerland) · 2024Article
- Re-Engineering Therapeutic Anti-Aβ Monoclonal Antibody to Target Amyloid Light Chain.International journal of molecular sciences · 2024Article
- A constant domain mutation in a patient-derived antibody light chain reveals principles of AL amyloidosis.Communications biology · 2023Article
- The Protein Network in Subcutaneous Fat Biopsies from Patients with AL Amyloidosis: More Than Diagnosis?Cells · 2023Article
- Donor-strand exchange drives assembly of the TasA scaffold in Bacillus subtilis biofilms.Nature communications · 2022Article
- Protease-sensitive regions in amyloid light chains: what a common pattern of fragmentation across organs suggests about aggregation.The FEBS journal · 2022Article
- Understanding AL amyloidosis with a little help fromFrontiers in immunology · 2022Review
- A Conservative Point Mutation in a Dynamic Antigen-binding Loop of Human Immunoglobulin λ6 Light Chain Promotes Pathologic Amyloid Formation.Journal of molecular biology · 2021Article
- Mass spectrometry characterization of light chain fragmentation sites in cardiac AL amyloidosis: insights into the timing of proteolysis.The Journal of biological chemistry · 2020Article
- Structural basis for the stabilization of amyloidogenic immunoglobulin light chains by hydantoins.Bioorganic & medicinal chemistry letters · 2020Article
- Site-Specific Interactions with Copper Promote Amyloid Fibril Formation for λ6aJL2-R24G.ACS omega · 2020Article
- Fatal amyloid formation in a patient's antibody light chain is caused by a single point mutation.eLife · 2020Article
- Article
- Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis.Nature communications · 2019Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Systemic light chain amyloidosis is a lethal disease characterized by excess immunoglobulin light chains and light chain fragments composed of variable domains, which aggregate into amyloid fibers. These fibers accumulate and damage organs. Some light chains induce formation of amyloid fibers, whereas others do not, making it unclear what distinguishes amyloid formers from non-formers. One mechanism by which sequence variation may reduce propensity to form amyloid fibers is by shifting the equilibrium toward an amyloid-resistant quaternary structure. Here we identify the monomeric form of the Mcg immunoglobulin light chain variable domain as the quaternary unit required for amyloid fiber assembly. Dimers of Mcg variable domains remain stable and soluble, yet become prone to assemble into amyloid fibers upon disassociation into monomers.
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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.